UniProtKB - Q14676 (MDC1_HUMAN)
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- BLAST>sp|Q14676|MDC1_HUMAN Mediator of DNA damage checkpoint protein 1 OS=Homo sapiens OX=9606 GN=MDC1 PE=1 SV=3 MEDTQAIDWDVEEEEETEQSSESLRCNVEPVGRLHIFSGAHGPEKDFPLHLGKNVVGRMP DCSVALPFPSISKQHAEIEILAWDKAPILRDCGSLNGTQILRPPKVLSPGVSHRLRDQEL ILFADLLCQYHRLDVSLPFVSRGPLTVEETPRVQGETQPQRLLLAEDSEEEVDFLSERRM VKKSRTTSSSVIVPESDEEGHSPVLGGLGPPFAFNLNSDTDVEEGQQPATEEASSAARRG ATVEAKQSEAEVVTEIQLEKDQPLVKERDNDTKVKRGAGNGVVPAGVILERSQPPGEDSD TDVDDDSRPPGRPAEVHLERAQPFGFIDSDTDAEEERIPATPVVIPMKKRKIFHGVGTRG PGAPGLAHLQESQAGSDTDVEEGKAPQAVPLEKSQASMVINSDTDDEEEVSAALTLAHLK ESQPAIWNRDAEEDMPQRVVLLQRSQTTTERDSDTDVEEEELPVENREAVLKDHTKIRAL VRAHSEKDQPPFGDSDDSVEADKSSPGIHLERSQASTTVDINTQVEKEVPPGSAIIHIKK HQVSVEGTNQTDVKAVGGPAKLLVVSLEEAWPLHGDCETDAEEGTSLTASVVADVRKSQL PAEGDAGAEWAAAVLKQERAHEVGAQGGPPVAQVEQDLPISRENLTDLVVDTDTLGESTQ PQREGAQVPTGREREQHVGGTKDSEDNYGDSEDLDLQATQCFLENQGLEAVQSMEDEPTQ AFMLTPPQELGPSHCSFQTTGTLDEPWEVLATQPFCLRESEDSETQPFDTHLEAYGPCLS PPRAIPGDQHPESPVHTEPMGIQGRGRQTVDKVMGIPKETAERVGPERGPLERETEKLLP ERQTDVTGEEELTKGKQDREQKQLLARDTQRQESDKNGESASPERDRESLKVEIETSEEI QEKQVQKQTLPSKAFEREVERPVANRECDPAELEEKVPKVILERDTQRGEPEGGSQDQKG QASSPTPEPGVGAGDLPGPTSAPVPSGSQSGGRGSPVSPRRHQKGLLNCKMPPAEKASRI RAAEKVSRGDQESPDACLPPTVPEAPAPPQKPLNSQSQKHLAPPPLLSPLLPSIKPTVRK TRQDGSQEAPEAPLSSELEPFHPKPKIRTRKSSRMTPFPATSAAPEPHPSTSTAQPVTPK PTSQATRSRTNRSSVKTPEPVVPTAPELQPSTSTDQPVTSEPTSQVTRGRKSRSSVKTPE TVVPTALELQPSTSTDRPVTSEPTSQATRGRKNRSSVKTPEPVVPTAPELQPSTSTDQPV TSEPTYQATRGRKNRSSVKTPEPVVPTAPELRPSTSTDRPVTPKPTSRTTRSRTNMSSVK TPETVVPTAPELQISTSTDQPVTPKPTSRTTRSRTNMSSVKNPESTVPIAPELPPSTSTE QPVTPEPTSRATRGRKNRSSGKTPETLVPTAPKLEPSTSTDQPVTPEPTSQATRGRTNRS SVKTPETVVPTAPELQPSTSTDQPVTPEPTSQATRGRTDRSSVKTPETVVPTAPELQASA STDQPVTSEPTSRTTRGRKNRSSVKTPETVVPAAPELQPSTSTDQPVTPEPTSRATRGRT NRSSVKTPESIVPIAPELQPSTSRNQLVTPEPTSRATRCRTNRSSVKTPEPVVPTAPEPH PTTSTDQPVTPKLTSRATRRKTNRSSVKTPKPVEPAASDLEPFTPTDQSVTPEAIAQGGQ SKTLRSSTVRAMPVPTTPEFQSPVTTDQPISPEPITQPSCIKRQRAAGNPGSLAAPIDHK PCSAPLEPKSQASRNQRWGAVRAAESLTAIPEPASPQLLETPIHASQIQKVEPAGRSRFT PELQPKASQSRKRSLATMDSPPHQKQPQRGEVSQKTVIIKEEEEDTAEKPGKEEDVVTPK PGKRKRDQAEEEPNRIPSRSLRRTKLNQESTAPKVLFTGVVDARGERAVLALGGSLAGSA AEASHLVTDRIRRTVKFLCALGRGIPILSLDWLHQSRKAGFFLPPDEYVVTDPEQEKNFG FSLQDALSRARERRLLEGYEIYVTPGVQPPPPQMGEIISCCGGTYLPSMPRSYKPQRVVI TCPQDFPHCSIPLRVGLPLLSPEFLLTGVLKQEAKPEAFVLSPLEMSST
- Align
Mediator of DNA damage checkpoint protein 1
MDC1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage."
Mochan T.A., Venere M., DiTullio R.A. Jr., Halazonetis T.D.
Cancer Res. 63:8586-8591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.9"NFBD1, a novel nuclear protein with signature motifs of FHA and BRCT, and an internal 41-amino acid repeat sequence, is an early participant in DNA damage response."
Shang Y.L., Bodero A.J., Chen P.-L.
J. Biol. Chem. 278:6323-6329(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.10"NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathways."
Xu X., Stern D.F.
J. Biol. Chem. 278:8795-8803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL CYCLE-DEPENDENT PHOSPHORYLATION, DOMAINS NLS1 AND NLS2. - Ref.11"NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage."
Peng A., Chen P.-L.
J. Biol. Chem. 278:8873-8876(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2. - Ref.12"Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control."
Lou Z., Chini C.C.S., Minter-Dykhouse K., Chen J.
J. Biol. Chem. 278:13599-13602(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND BARD1. - Ref.13"MDC1 is required for the intra-S-phase DNA damage checkpoint."
Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D., Bartek J., Jackson S.P.
Nature 421:952-956(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, MUTAGENESIS OF ARG-58. - Ref.14"MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways."
Lou Z., Minter-Dykhouse K., Wu X., Chen J.
Nature 421:957-961(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2, PHOSPHORYLATION BY ATM AND CHEK2, MUTAGENESIS OF ARG-58; SER-72; ASN-96; GLY-97 AND THR-98. - Ref.15"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX; ATM; FANCD2; H2AFX; SMC1A AND TP53BP1, PHOSPHORYLATION BY ATM. - Ref.17"Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention."
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S., Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.
EMBO J. 23:2674-2683(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH H2AFX. - Ref.18"MDC1 regulates DNA-PK autophosphorylation in response to DNA damage."
Lou Z., Chen B.P.-C., Asaithamby A., Minter-Dykhouse K., Chen D.J., Chen J.
J. Biol. Chem. 279:46359-46362(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PRKDC COMPLEX.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- FHA domain binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein C-terminus binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- double-strand break repair via nonhomologous end joining Source: Reactome
- intra-S DNA damage checkpoint Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Biological process | Cell cycle, DNA damage, DNA repair |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3108214. SUMOylation of DNA damage response and repair proteins. R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. R-HSA-5693571. Nonhomologous End-Joining (NHEJ). R-HSA-5693607. Processing of DNA double-strand break ends. R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes. R-HSA-69473. G2/M DNA damage checkpoint. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q14676. |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q14676. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Mediator of DNA damage checkpoint protein 1Alternative name(s): Nuclear factor with BRCT domains 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:MDC1 Synonyms:KIAA0170, NFBD1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000137337.14. |
Human Gene Nomenclature Database More...HGNCi | HGNC:21163. MDC1. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607593. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q14676. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 11 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage."
Mochan T.A., Venere M., DiTullio R.A. Jr., Halazonetis T.D.
Cancer Res. 63:8586-8591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.9"NFBD1, a novel nuclear protein with signature motifs of FHA and BRCT, and an internal 41-amino acid repeat sequence, is an early participant in DNA damage response."
Shang Y.L., Bodero A.J., Chen P.-L.
J. Biol. Chem. 278:6323-6329(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.10"NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathways."
Xu X., Stern D.F.
J. Biol. Chem. 278:8795-8803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL CYCLE-DEPENDENT PHOSPHORYLATION, DOMAINS NLS1 AND NLS2. - Ref.11"NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage."
Peng A., Chen P.-L.
J. Biol. Chem. 278:8873-8876(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2. - Ref.12"Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control."
Lou Z., Chini C.C.S., Minter-Dykhouse K., Chen J.
J. Biol. Chem. 278:13599-13602(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND BARD1. - Ref.13"MDC1 is required for the intra-S-phase DNA damage checkpoint."
Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D., Bartek J., Jackson S.P.
Nature 421:952-956(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, MUTAGENESIS OF ARG-58. - Ref.14"MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways."
Lou Z., Minter-Dykhouse K., Wu X., Chen J.
Nature 421:957-961(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2, PHOSPHORYLATION BY ATM AND CHEK2, MUTAGENESIS OF ARG-58; SER-72; ASN-96; GLY-97 AND THR-98. - Ref.15"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX; ATM; FANCD2; H2AFX; SMC1A AND TP53BP1, PHOSPHORYLATION BY ATM. - Ref.17"Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention."
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S., Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.
EMBO J. 23:2674-2683(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH H2AFX. - Ref.18"MDC1 regulates DNA-PK autophosphorylation in response to DNA damage."
Lou Z., Chen B.P.-C., Asaithamby A., Minter-Dykhouse K., Chen D.J., Chen J.
J. Biol. Chem. 279:46359-46362(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PRKDC COMPLEX. - Ref.29"CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response."
Becherel O.J., Jakob B., Cherry A.L., Gueven N., Fusser M., Kijas A.W., Peng C., Katyal S., McKinnon P.J., Chen J., Epe B., Smerdon S.J., Taucher-Scholz G., Lavin M.F.
Nucleic Acids Res. 38:1489-1503(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APTX.
- Nucleus 11 Publications
Other locations
- Chromosome By similarity
Note: Associated with chromatin. Relocalizes to discrete nuclear foci following DNA damage, this requires 'Ser-139' phosphorylation of H2AFX. Colocalizes with APTX at sites of DNA double-strand breaks.
Nucleus
- nuclear body Source: HPA
- nucleoplasm Source: HPA
- nucleus Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- chromosome Source: UniProtKB
- focal adhesion Source: HPA
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Chromosome, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 58 | R → A: Abrogates binding to the MRE11 complex and to CHEK2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 72 | S → A: Abrogates binding to CHEK2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 96 | N → A: Abrogates binding to CHEK2; when associated with A-97 and A-98. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 97 | G → A: Abrogates binding to CHEK2; when associated with A-96 and A-98. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 98 | T → A: Abrogates binding to CHEK2; when associated with A-96 and A-97. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1840 | K → R: Suppresses RNF4-mediated ubiquitination, accumulates at sites of DNA damage, defective homologous recombination. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 9656. |
Open Targets More...OpenTargetsi | ENSG00000137337. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134942837. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MDC1. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000096316 | 1 – 2089 | Mediator of DNA damage checkpoint protein 1Add BLAST | 2089 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 4 | Phosphothreonine; by ATM1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 108 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 146 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 168 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 176 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 299 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 301 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 329 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 331 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 372 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 376 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 378 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 394 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 397 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 402 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 404 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 411 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 449 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 453 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 455 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 485 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 495 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 498 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 504 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 505 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 513 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 523 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 590 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 616 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 616 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 780 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 793 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 812 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 955 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 998 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1033 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1068 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1086 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1157 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1198 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1235 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1239 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1280 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1302 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1399 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1400 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1402 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1403 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1413 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1413 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1425 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1466 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1548 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1564 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1567 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1589 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1604 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1608 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1630 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1664 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1671 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1681 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1697 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1702 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1711 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1740 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1775 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1790 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1800 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1820 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1840 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1840 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1858 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1943 | Omega-N-methylarginineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.13"MDC1 is required for the intra-S-phase DNA damage checkpoint."
Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D., Bartek J., Jackson S.P.
Nature 421:952-956(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, MUTAGENESIS OF ARG-58. - Ref.14"MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways."
Lou Z., Minter-Dykhouse K., Wu X., Chen J.
Nature 421:957-961(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2, PHOSPHORYLATION BY ATM AND CHEK2, MUTAGENESIS OF ARG-58; SER-72; ASN-96; GLY-97 AND THR-98. - Ref.15"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX; ATM; FANCD2; H2AFX; SMC1A AND TP53BP1, PHOSPHORYLATION BY ATM. - Ref.43"Structural mechanism of the phosphorylation-dependent dimerization of the MDC1 forkhead-associated domain."
Liu J., Luo S., Zhao H., Liao J., Li J., Yang C., Xu B., Stern D.F., Xu X., Ye K.
Nucleic Acids Res. 40:3898-3912(2012) [PubMed] [Europe PMC] [Abstract]
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.32"Sumoylation of MDC1 is important for proper DNA damage response."
Luo K., Zhang H., Wang L., Yuan J., Lou Z.
EMBO J. 31:3008-3019(2012) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-1840, UBIQUITINATION BY RNF4, MUTAGENESIS OF LYS-1840, INTERACTION WITH TP53BP1.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.32"Sumoylation of MDC1 is important for proper DNA damage response."
Luo K., Zhang H., Wang L., Yuan J., Lou Z.
EMBO J. 31:3008-3019(2012) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-1840, UBIQUITINATION BY RNF4, MUTAGENESIS OF LYS-1840, INTERACTION WITH TP53BP1.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q14676. |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q14676. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q14676. |
PeptideAtlas More...PeptideAtlasi | Q14676. |
PRoteomics IDEntifications database More...PRIDEi | Q14676. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q14676. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q14676. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q14676. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.10"NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathways."
Xu X., Stern D.F.
J. Biol. Chem. 278:8795-8803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL CYCLE-DEPENDENT PHOSPHORYLATION, DOMAINS NLS1 AND NLS2.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000137337. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q14676. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q14676. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA006915. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.11"NFBD1, like 53BP1, is an early and redundant transducer mediating Chk2 phosphorylation in response to DNA damage."
Peng A., Chen P.-L.
J. Biol. Chem. 278:8873-8876(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2. - Ref.12"Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control."
Lou Z., Chini C.C.S., Minter-Dykhouse K., Chen J.
J. Biol. Chem. 278:13599-13602(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND BARD1. - Ref.13"MDC1 is required for the intra-S-phase DNA damage checkpoint."
Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D., Bartek J., Jackson S.P.
Nature 421:952-956(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, MUTAGENESIS OF ARG-58. - Ref.14"MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways."
Lou Z., Minter-Dykhouse K., Wu X., Chen J.
Nature 421:957-961(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2, PHOSPHORYLATION BY ATM AND CHEK2, MUTAGENESIS OF ARG-58; SER-72; ASN-96; GLY-97 AND THR-98. - Ref.15"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE MRN COMPLEX; ATM; FANCD2; H2AFX; SMC1A AND TP53BP1, PHOSPHORYLATION BY ATM. - Ref.17"Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention."
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S., Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.
EMBO J. 23:2674-2683(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH H2AFX. - Ref.18"MDC1 regulates DNA-PK autophosphorylation in response to DNA damage."
Lou Z., Chen B.P.-C., Asaithamby A., Minter-Dykhouse K., Chen D.J., Chen J.
J. Biol. Chem. 279:46359-46362(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PRKDC COMPLEX. - Ref.22"Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase."
Kolas N.K., Chapman J.R., Nakada S., Ylanko J., Chahwan R., Sweeney F.D., Panier S., Mendez M., Wildenhain J., Thomson T.M., Pelletier L., Jackson S.P., Durocher D.
Science 318:1637-1640(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RNF8. - Ref.23"Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1."
Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.
Genes Dev. 22:587-600(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CEP164. - Ref.29"CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response."
Becherel O.J., Jakob B., Cherry A.L., Gueven N., Fusser M., Kijas A.W., Peng C., Katyal S., McKinnon P.J., Chen J., Epe B., Smerdon S.J., Taucher-Scholz G., Lavin M.F.
Nucleic Acids Res. 38:1489-1503(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APTX. - Ref.32"Sumoylation of MDC1 is important for proper DNA damage response."
Luo K., Zhang H., Wang L., Yuan J., Lou Z.
EMBO J. 31:3008-3019(2012) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-1840, UBIQUITINATION BY RNF4, MUTAGENESIS OF LYS-1840, INTERACTION WITH TP53BP1. - Ref.39"MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks."
Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P.
Cell 123:1213-1226(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 1883-2089 IN COMPLEX WITH PHOSPHORYLATED H2AFX. - Ref.40"Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail."
Lee M.S., Edwards R.A., Thede G.L., Glover J.N.M.
J. Biol. Chem. 280:32053-32056(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1891-2086, INTERACTION WITH PHOSPHORYLATED H2AFX. - Ref.41"Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1."
Campbell S.J., Edwards R.A., Glover J.N.
Structure 18:167-176(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1891-2089 IN COMPLEX WITH PHOSPHORYLATED HISTONE TETRAPEPTIDE.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
ATM | Q13315 | 2 | EBI-495644,EBI-495465 | |
H2AFX | P16104 | 21 | EBI-495644,EBI-494830 | |
NBN | O60934 | 32 | EBI-495644,EBI-494844 | |
nbs1 | O43070 | 2 | EBI-495644,EBI-2125045 | From Schizosaccharomyces pombe (strain 972 / ATCC 24843). |
NSD2 | O96028 | 3 | EBI-495644,EBI-2693298 | |
NSD2 | O96028-1 | 3 | EBI-495644,EBI-15910280 | |
RAD51 | Q06609 | 3 | EBI-495644,EBI-297202 | |
RNF8 | O76064 | 11 | EBI-495644,EBI-373337 | |
RNF8 | O76064-1 | 2 | EBI-495644,EBI-15964690 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- FHA domain binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein C-terminus binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115014. 198 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q14676. |
Database of interacting proteins More...DIPi | DIP-33603N. |
Protein interaction database and analysis system More...IntActi | Q14676. 25 interactors. |
Molecular INTeraction database More...MINTi | Q14676. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000365588. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 21 – 24 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 32 – 36 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 39 – 42 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 45 – 49 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 51 – 59 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 62 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 76 – 80 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 88 – 91 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 98 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 101 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 120 – 123 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 126 – 132 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1894 – 1897 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1903 – 1911 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1920 – 1922 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1924 – 1927 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1935 – 1943 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1951 – 1959 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1966 – 1968 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1973 – 1978 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1983 – 1992 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1995 – 1998 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2000 – 2003 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 2011 – 2020 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2024 – 2026 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2037 – 2040 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 2043 – 2048 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 2050 – 2055 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 2063 – 2071 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 2076 – 2079 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2ADO | X-ray | 1.45 | A/B | 1891-2086 | [»] | |
2AZM | X-ray | 2.41 | A/B | 1883-2089 | [»] | |
2ETX | X-ray | 1.33 | A/B | 1884-2089 | [»] | |
3K05 | X-ray | 1.33 | A/B | 1891-2089 | [»] | |
3UEO | X-ray | 2.60 | E/F | 325-336 | [»] | |
3UMZ | X-ray | 1.65 | A/B | 27-138 | [»] | |
3UN0 | X-ray | 2.30 | A/B | 26-138 | [»] | |
3UNM | X-ray | 1.80 | A/B | 27-138 | [»] | |
3UNN | X-ray | 1.70 | A | 27-138 | [»] | |
B | 1-8 | [»] | ||||
3UOT | X-ray | 1.80 | A/B | 19-138 | [»] | |
D/E | 1-10 | [»] | ||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q14676. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q14676. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q14676. |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 54 – 105 | FHAPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 52 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1892 – 1970 | BRCT 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 79 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1991 – 2082 | BRCT 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 92 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 150 | Interaction with CHEK2Add BLAST | 150 | |
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 2 – 220 | Interaction with the MRN complexAdd BLAST | 219 | |
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 145 – 568 | Required for nuclear localization (NLS1)Add BLAST | 424 | |
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1148 – 1610 | Interaction with the PRKDC complexAdd BLAST | 463 | |
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1698 – 2089 | Required for nuclear localization (NLS2)Add BLAST | 392 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1034 – 1469 | Pro-richAdd BLAST | 436 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.10"NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathways."
Xu X., Stern D.F.
J. Biol. Chem. 278:8795-8803(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL CYCLE-DEPENDENT PHOSPHORYLATION, DOMAINS NLS1 AND NLS2.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2043. Eukaryota. ENOG4111RPS. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00600000084454. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG080567. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q14676. |
KEGG Orthology (KO) More...KOi | K20780. |
Identification of Orthologs from Complete Genome Data More...OMAi | FPLYLGK. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0V3Z. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q14676. |
TreeFam database of animal gene trees More...TreeFami | TF329580. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00027. BRCT. 1 hit. cd00060. FHA. 1 hit. |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.10190. 2 hits. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001357. BRCT_dom. IPR036420. BRCT_dom_sf. IPR000253. FHA_dom. IPR008984. SMAD_FHA_dom_sf. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00498. FHA. 1 hit. PF16770. RTT107_BRCT_5. 1 hit. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00240. FHA. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49879. SSF49879. 1 hit. SSF52113. SSF52113. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50172. BRCT. 1 hit. PS50006. FHA_DOMAIN. 1 hit. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH
60 70 80 90 100
LGKNVVGRMP DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI
110 120 130 140 150
LRPPKVLSPG VSHRLRDQEL ILFADLLCQY HRLDVSLPFV SRGPLTVEET
160 170 180 190 200
PRVQGETQPQ RLLLAEDSEE EVDFLSERRM VKKSRTTSSS VIVPESDEEG
210 220 230 240 250
HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG ATVEAKQSEA
260 270 280 290 300
EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
310 320 330 340 350
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR
360 370 380 390 400
KIFHGVGTRG PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI
410 420 430 440 450
NSDTDDEEEV SAALTLAHLK ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE
460 470 480 490 500
RDSDTDVEEE ELPVENREAV LKDHTKIRAL VRAHSEKDQP PFGDSDDSVE
510 520 530 540 550
ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK HQVSVEGTNQ
560 570 580 590 600
TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
610 620 630 640 650
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV
660 670 680 690 700
DTDTLGESTQ PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ
710 720 730 740 750
CFLENQGLEA VQSMEDEPTQ AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL
760 770 780 790 800
ATQPFCLRES EDSETQPFDT HLEAYGPCLS PPRAIPGDQH PESPVHTEPM
810 820 830 840 850
GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP ERQTDVTGEE
860 870 880 890 900
ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI
910 920 930 940 950
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE
960 970 980 990 1000
PEGGSQDQKG QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR
1010 1020 1030 1040 1050
RHQKGLLNCK MPPAEKASRI RAAEKVSRGD QESPDACLPP TVPEAPAPPQ
1060 1070 1080 1090 1100
KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK TRQDGSQEAP EAPLSSELEP
1110 1120 1130 1140 1150
FHPKPKIRTR KSSRMTPFPA TSAAPEPHPS TSTAQPVTPK PTSQATRSRT
1160 1170 1180 1190 1200
NRSSVKTPEP VVPTAPELQP STSTDQPVTS EPTSQVTRGR KSRSSVKTPE
1210 1220 1230 1240 1250
TVVPTALELQ PSTSTDRPVT SEPTSQATRG RKNRSSVKTP EPVVPTAPEL
1260 1270 1280 1290 1300
QPSTSTDQPV TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LRPSTSTDRP
1310 1320 1330 1340 1350
VTPKPTSRTT RSRTNMSSVK TPETVVPTAP ELQISTSTDQ PVTPKPTSRT
1360 1370 1380 1390 1400
TRSRTNMSSV KNPESTVPIA PELPPSTSTE QPVTPEPTSR ATRGRKNRSS
1410 1420 1430 1440 1450
GKTPETLVPT APKLEPSTST DQPVTPEPTS QATRGRTNRS SVKTPETVVP
1460 1470 1480 1490 1500
TAPELQPSTS TDQPVTPEPT SQATRGRTDR SSVKTPETVV PTAPELQASA
1510 1520 1530 1540 1550
STDQPVTSEP TSRTTRGRKN RSSVKTPETV VPAAPELQPS TSTDQPVTPE
1560 1570 1580 1590 1600
PTSRATRGRT NRSSVKTPES IVPIAPELQP STSRNQLVTP EPTSRATRCR
1610 1620 1630 1640 1650
TNRSSVKTPE PVVPTAPEPH PTTSTDQPVT PKLTSRATRR KTNRSSVKTP
1660 1670 1680 1690 1700
KPVEPAASDL EPFTPTDQSV TPEAIAQGGQ SKTLRSSTVR AMPVPTTPEF
1710 1720 1730 1740 1750
QSPVTTDQPI SPEPITQPSC IKRQRAAGNP GSLAAPIDHK PCSAPLEPKS
1760 1770 1780 1790 1800
QASRNQRWGA VRAAESLTAI PEPASPQLLE TPIHASQIQK VEPAGRSRFT
1810 1820 1830 1840 1850
PELQPKASQS RKRSLATMDS PPHQKQPQRG EVSQKTVIIK EEEEDTAEKP
1860 1870 1880 1890 1900
GKEEDVVTPK PGKRKRDQAE EEPNRIPSRS LRRTKLNQES TAPKVLFTGV
1910 1920 1930 1940 1950
VDARGERAVL ALGGSLAGSA AEASHLVTDR IRRTVKFLCA LGRGIPILSL
1960 1970 1980 1990 2000
DWLHQSRKAG FFLPPDEYVV TDPEQEKNFG FSLQDALSRA RERRLLEGYE
2010 2020 2030 2040 2050
IYVTPGVQPP PPQMGEIISC CGGTYLPSMP RSYKPQRVVI TCPQDFPHCS
2060 2070 2080
IPLRVGLPLL SPEFLLTGVL KQEAKPEAFV LSPLEMSST
The sequence of this isoform differs from the canonical sequence as follows:
741-1004: Missing.
10 20 30 40 50
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH
60 70 80 90 100
LGKNVVGRMP DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI
110 120 130 140 150
LRPPKVLSPG VSHRLRDQEL ILFADLLCQY HRLDVSLPFV SRGPLTVEET
160 170 180 190 200
PRVQGETQPQ RLLLAEDSEE EVDFLSERRM VKKSRTTSSS VIVPESDEEG
210 220 230 240 250
HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG ATVEAKQSEA
260 270 280 290 300
EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
310 320 330 340 350
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR
360 370 380 390 400
KIFHGVGTRG PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI
410 420 430 440 450
NSDTDDEEEV SAALTLAHLK ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE
460 470 480 490 500
RDSDTDVEEE ELPVENREAV LKDHTKIRAL VRAHSEKDQP PFGDSDDSVE
510 520 530 540 550
ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK HQVSVEGTNQ
560 570 580 590 600
TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
610 620 630 640 650
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV
660 670 680 690 700
DTDTLGESTQ PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ
710 720 730 740 750
CFLENQGLEA VQSMEDEPTQ AFMLTPPQEL GPSHCSFQTT GLLNCKMPPA
760 770 780 790 800
EKASRIRAAE KVSRGDQESP DACLPPTVPE APAPPQKPLN SQSQKHLAPP
810 820 830 840 850
PLLSPLLPSI KPTVRKTRQD GSQEAPEAPL SSELEPFHPK PKIRTRKSSR
860 870 880 890 900
MTPFPATSAA PEPHPSTSTA QPVTPKPTSQ ATRSRTNRSS VKTPEPVVPT
910 920 930 940 950
APELQPSTST DQPVTSEPTS QVTRGRKSRS SVKTPETVVP TALELQPSTS
960 970 980 990 1000
TDRPVTSEPT SQATRGRKNR SSVKTPEPVV PTAPELQPST STDQPVTSEP
1010 1020 1030 1040 1050
TYQATRGRKN RSSVKTPEPV VPTAPELRPS TSTDRPVTPK PTSRTTRSRT
1060 1070 1080 1090 1100
NMSSVKTPET VVPTAPELQI STSTDQPVTP KPTSRTTRSR TNMSSVKNPE
1110 1120 1130 1140 1150
STVPIAPELP PSTSTEQPVT PEPTSRATRG RKNRSSGKTP ETLVPTAPKL
1160 1170 1180 1190 1200
EPSTSTDQPV TPEPTSQATR GRTNRSSVKT PETVVPTAPE LQPSTSTDQP
1210 1220 1230 1240 1250
VTPEPTSQAT RGRTDRSSVK TPETVVPTAP ELQASASTDQ PVTSEPTSRT
1260 1270 1280 1290 1300
TRGRKNRSSV KTPETVVPAA PELQPSTSTD QPVTPEPTSR ATRGRTNRSS
1310 1320 1330 1340 1350
VKTPESIVPI APELQPSTSR NQLVTPEPTS RATRCRTNRS SVKTPEPVVP
1360 1370 1380 1390 1400
TAPEPHPTTS TDQPVTPKLT SRATRRKTNR SSVKTPKPVE PAASDLEPFT
1410 1420 1430 1440 1450
PTDQSVTPEA IAQGGQSKTL RSSTVRAMPV PTTPEFQSPV TTDQPISPEP
1460 1470 1480 1490 1500
ITQPSCIKRQ RAAGNPGSLA APIDHKPCSA PLEPKSQASR NQRWGAVRAA
1510 1520 1530 1540 1550
ESLTAIPEPA SPQLLETPIH ASQIQKVEPA GRSRFTPELQ PKASQSRKRS
1560 1570 1580 1590 1600
LATMDSPPHQ KQPQRGEVSQ KTVIIKEEEE DTAEKPGKEE DVVTPKPGKR
1610 1620 1630 1640 1650
KRDQAEEEPN RIPSRSLRRT KLNQESTAPK VLFTGVVDAR GERAVLALGG
1660 1670 1680 1690 1700
SLAGSAAEAS HLVTDRIRRT VKFLCALGRG IPILSLDWLH QSRKAGFFLP
1710 1720 1730 1740 1750
PDEYVVTDPE QEKNFGFSLQ DALSRARERR LLEGYEIYVT PGVQPPPPQM
1760 1770 1780 1790 1800
GEIISCCGGT YLPSMPRSYK PQRVVITCPQ DFPHCSIPLR VGLPLLSPEF
1810 1820
LLTGVLKQEA KPEAFVLSPL EMSST
The sequence of this isoform differs from the canonical sequence as follows:
1124-1410: Missing.
10 20 30 40 50
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH
60 70 80 90 100
LGKNVVGRMP DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI
110 120 130 140 150
LRPPKVLSPG VSHRLRDQEL ILFADLLCQY HRLDVSLPFV SRGPLTVEET
160 170 180 190 200
PRVQGETQPQ RLLLAEDSEE EVDFLSERRM VKKSRTTSSS VIVPESDEEG
210 220 230 240 250
HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG ATVEAKQSEA
260 270 280 290 300
EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
310 320 330 340 350
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR
360 370 380 390 400
KIFHGVGTRG PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI
410 420 430 440 450
NSDTDDEEEV SAALTLAHLK ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE
460 470 480 490 500
RDSDTDVEEE ELPVENREAV LKDHTKIRAL VRAHSEKDQP PFGDSDDSVE
510 520 530 540 550
ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK HQVSVEGTNQ
560 570 580 590 600
TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
610 620 630 640 650
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV
660 670 680 690 700
DTDTLGESTQ PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ
710 720 730 740 750
CFLENQGLEA VQSMEDEPTQ AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL
760 770 780 790 800
ATQPFCLRES EDSETQPFDT HLEAYGPCLS PPRAIPGDQH PESPVHTEPM
810 820 830 840 850
GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP ERQTDVTGEE
860 870 880 890 900
ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI
910 920 930 940 950
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE
960 970 980 990 1000
PEGGSQDQKG QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR
1010 1020 1030 1040 1050
RHQKGLLNCK MPPAEKASRI RAAEKVSRGD QESPDACLPP TVPEAPAPPQ
1060 1070 1080 1090 1100
KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK TRQDGSQEAP EAPLSSELEP
1110 1120 1130 1140 1150
FHPKPKIRTR KSSRMTPFPA TSAAPKLEPS TSTDQPVTPE PTSQATRGRT
1160 1170 1180 1190 1200
NRSSVKTPET VVPTAPELQP STSTDQPVTP EPTSQATRGR TDRSSVKTPE
1210 1220 1230 1240 1250
TVVPTAPELQ ASASTDQPVT SEPTSRTTRG RKNRSSVKTP ETVVPAAPEL
1260 1270 1280 1290 1300
QPSTSTDQPV TPEPTSRATR GRTNRSSVKT PESIVPIAPE LQPSTSRNQL
1310 1320 1330 1340 1350
VTPEPTSRAT RCRTNRSSVK TPEPVVPTAP EPHPTTSTDQ PVTPKLTSRA
1360 1370 1380 1390 1400
TRRKTNRSSV KTPKPVEPAA SDLEPFTPTD QSVTPEAIAQ GGQSKTLRSS
1410 1420 1430 1440 1450
TVRAMPVPTT PEFQSPVTTD QPISPEPITQ PSCIKRQRAA GNPGSLAAPI
1460 1470 1480 1490 1500
DHKPCSAPLE PKSQASRNQR WGAVRAAESL TAIPEPASPQ LLETPIHASQ
1510 1520 1530 1540 1550
IQKVEPAGRS RFTPELQPKA SQSRKRSLAT MDSPPHQKQP QRGEVSQKTV
1560 1570 1580 1590 1600
IIKEEEEDTA EKPGKEEDVV TPKPGKRKRD QAEEEPNRIP SRSLRRTKLN
1610 1620 1630 1640 1650
QESTAPKVLF TGVVDARGER AVLALGGSLA GSAAEASHLV TDRIRRTVKF
1660 1670 1680 1690 1700
LCALGRGIPI LSLDWLHQSR KAGFFLPPDE YVVTDPEQEK NFGFSLQDAL
1710 1720 1730 1740 1750
SRARERRLLE GYEIYVTPGV QPPPPQMGEI ISCCGGTYLP SMPRSYKPQR
1760 1770 1780 1790 1800
VVITCPQDFP HCSIPLRVGL PLLSPEFLLT GVLKQEAKPE AFVLSPLEMS
ST
The sequence of this isoform differs from the canonical sequence as follows:
741-1004: Missing.
1029-1787: Missing.
10 20 30 40 50
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH
60 70 80 90 100
LGKNVVGRMP DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI
110 120 130 140 150
LRPPKVLSPG VSHRLRDQEL ILFADLLCQY HRLDVSLPFV SRGPLTVEET
160 170 180 190 200
PRVQGETQPQ RLLLAEDSEE EVDFLSERRM VKKSRTTSSS VIVPESDEEG
210 220 230 240 250
HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG ATVEAKQSEA
260 270 280 290 300
EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
310 320 330 340 350
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR
360 370 380 390 400
KIFHGVGTRG PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI
410 420 430 440 450
NSDTDDEEEV SAALTLAHLK ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE
460 470 480 490 500
RDSDTDVEEE ELPVENREAV LKDHTKIRAL VRAHSEKDQP PFGDSDDSVE
510 520 530 540 550
ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK HQVSVEGTNQ
560 570 580 590 600
TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
610 620 630 640 650
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV
660 670 680 690 700
DTDTLGESTQ PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ
710 720 730 740 750
CFLENQGLEA VQSMEDEPTQ AFMLTPPQEL GPSHCSFQTT GLLNCKMPPA
760 770 780 790 800
EKASRIRAAE KVSRIQKVEP AGRSRFTPEL QPKASQSRKR SLATMDSPPH
810 820 830 840 850
QKQPQRGEVS QKTVIIKEEE EDTAEKPGKE EDVVTPKPGK RKRDQAEEEP
860 870 880 890 900
NRIPSRSLRR TKLNQESTAP KVLFTGVVDA RGERAVLALG GSLAGSAAEA
910 920 930 940 950
SHLVTDRIRR TVKFLCALGR GIPILSLDWL HQSRKAGFFL PPDEYVVTDP
960 970 980 990 1000
EQEKNFGFSL QDALSRARER RLLEGYEIYV TPGVQPPPPQ MGEIISCCGG
1010 1020 1030 1040 1050
TYLPSMPRSY KPQRVVITCP QDFPHCSIPL RVGLPLLSPE FLLTGVLKQE
1060
AKPEAFVLSP LEMSST
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 638 | L → P in CAH18685 (PubMed:17974005).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 645 – 1326 | Missing in CAH18685 (PubMed:17974005).CuratedAdd BLAST | 682 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1005 | G → GS in BAB63322 (Ref. 3) Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1041 | T → A in BAA11487 (PubMed:8724849).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1041 | T → A in AAI52557 (PubMed:15489334).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1266 | Y → S in BAE78617 (PubMed:16702430).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1283 | P → T in BAE78617 (PubMed:16702430).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1533 | A → T in BAC54931 (PubMed:16702430).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1533 | A → T in BAF31266 (PubMed:16702430).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1536 | E → A in CAM25929 (PubMed:14574404).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1664 | T → S in BAE78617 (PubMed:16702430).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1668 | Q → R in CAH18685 (PubMed:17974005).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1734 | A → T in BAE78617 (PubMed:16702430).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1843 | E → K (PubMed:17974005).Curated | 1 | |
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 2048 | H → R (PubMed:17974005).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051160 | 179 | R → C. Corresponds to variant dbSNP:rs28986464Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022843 | 251 | E → K1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022844 | 268 | R → K2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022845 | 371 | E → K1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051161 | 386 | P → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_043922 | 536 | I → M2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022846 | 586 | S → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051162 | 917 | R → S. Corresponds to variant dbSNP:rs28986467Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051163 | 1100 | P → A. Corresponds to variant dbSNP:rs28994869Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051164 | 1112 | S → F. Corresponds to variant dbSNP:rs28987085Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051165 | 1180 | S → P1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022847 | 1509 | E → D2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022848 | 1540 | S → PCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_043923 | 1545 | Q → R6 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051166 | 1745 | P → R. Corresponds to variant dbSNP:rs28994871Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051167 | 1791 | V → E. Corresponds to variant dbSNP:rs28994873Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051168 | 1855 | D → E. Corresponds to variant dbSNP:rs28994874Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051169 | 1883 | R → Q. Corresponds to variant dbSNP:rs28994875Ensembl. | 1 | |
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051170 | 1904 | R → Q. Corresponds to variant dbSNP:rs28994876Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_014593 | 741 – 1004 | Missing in isoform 2 and isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 264 | |
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_034103 | 1029 – 1787 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 759 | |
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_034104 | 1124 – 1410 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 287 |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D79992 mRNA. Translation: BAA11487.2. Different initiation. CR749828 mRNA. Translation: CAH18685.1. Different termination. BA000025 Genomic DNA. Translation: BAB63322.1. AB088099 Genomic DNA. Translation: BAC54931.1. AB202097 Genomic DNA. Translation: BAE78617.1. AB103605 Genomic DNA. Translation: BAF31266.1. AL662848 Genomic DNA. Translation: CAI17440.1. AL662797 Genomic DNA. Translation: CAI18195.1. AL845353 Genomic DNA. Translation: CAI41890.2. AL845353 Genomic DNA. Translation: CAI41891.1. AL662848 Genomic DNA. Translation: CAM24847.1. AL662797 Genomic DNA. Translation: CAM25512.1. BX248307 Genomic DNA. Translation: CAM25928.1. BX248307 Genomic DNA. Translation: CAM25929.1. BX927283 Genomic DNA. Translation: CAQ06769.1. BX927283 Genomic DNA. Translation: CAQ06770.1. CR936878 Genomic DNA. Translation: CAQ06813.1. CR936878 Genomic DNA. Translation: CAQ06814.1. CR788240 Genomic DNA. Translation: CAQ07571.1. CR788240 Genomic DNA. Translation: CAQ07572.1. CR759873 Genomic DNA. Translation: CAQ08690.1. CR759873 Genomic DNA. Translation: CAQ08691.1. CH471081 Genomic DNA. Translation: EAX03321.1. BC110645 mRNA. Translation: AAI10646.1. BC152556 mRNA. Translation: AAI52557.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS34384.1. [Q14676-1] |
NCBI Reference Sequences More...RefSeqi | NP_055456.2. NM_014641.2. [Q14676-1] XP_005249551.1. XM_005249494.4. [Q14676-1] XP_011513303.1. XM_011515001.2. [Q14676-1] XP_011513305.1. XM_011515003.2. [Q14676-1] XP_016867008.1. XM_017011519.1. [Q14676-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.653495. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000376406; ENSP00000365588; ENSG00000137337. [Q14676-1] ENST00000383566; ENSP00000373060; ENSG00000206481. ENST00000420019; ENSP00000396484; ENSG00000224587. [Q14676-1] ENST00000420320; ENSP00000416511; ENSG00000225589. [Q14676-1] ENST00000427406; ENSP00000387429; ENSG00000234012. [Q14676-1] ENST00000435664; ENSP00000404318; ENSG00000231135. ENST00000440369; ENSP00000415212; ENSG00000228575. [Q14676-1] ENST00000449153; ENSP00000409167; ENSG00000237095. [Q14676-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9656. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9656. |
UCSC genome browser More...UCSCi | uc003nrg.5. human. [Q14676-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
---|---|---|---|---|---|---|---|
Q14676 | A0A1U9XBC1 A1Z5I7 A2AB05 UPI000387B5F4 UPI00006912BA UPI0000576773 | Homo sapiens (Human) | 2,089 | UniRef100_Q14676 | Cluster: Mediator of DNA damage checkpoint protein 1 | 7 |
Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
---|---|---|---|---|---|---|---|
Q14676 | A0A1U9XBC1 A1Z5I7 A2AB05 UPI000387B5F4 UPI00006912BA UPI0000576773 UPI000387C0C7 UPI000387B0E4 UPI00045E3FAF UPI00045E1BAB +23 | Homo sapiens (Human) Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus) Papio anubis (Olive baboon) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Pan troglodytes (Chimpanzee) Gorilla gorilla gorilla (Western lowland gorilla) Colobus angolensis palliatus (Peters' Angolan colobus) Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti) | 2,089 | UniRef90_Q14676 | Cluster: Mediator of DNA damage checkpoint protein 1 | 34 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D79992 mRNA. Translation: BAA11487.2. Different initiation. CR749828 mRNA. Translation: CAH18685.1. Different termination. BA000025 Genomic DNA. Translation: BAB63322.1. AB088099 Genomic DNA. Translation: BAC54931.1. AB202097 Genomic DNA. Translation: BAE78617.1. AB103605 Genomic DNA. Translation: BAF31266.1. AL662848 Genomic DNA. Translation: CAI17440.1. AL662797 Genomic DNA. Translation: CAI18195.1. AL845353 Genomic DNA. Translation: CAI41890.2. AL845353 Genomic DNA. Translation: CAI41891.1. AL662848 Genomic DNA. Translation: CAM24847.1. AL662797 Genomic DNA. Translation: CAM25512.1. BX248307 Genomic DNA. Translation: CAM25928.1. BX248307 Genomic DNA. Translation: CAM25929.1. BX927283 Genomic DNA. Translation: CAQ06769.1. BX927283 Genomic DNA. Translation: CAQ06770.1. CR936878 Genomic DNA. Translation: CAQ06813.1. CR936878 Genomic DNA. Translation: CAQ06814.1. CR788240 Genomic DNA. Translation: CAQ07571.1. CR788240 Genomic DNA. Translation: CAQ07572.1. CR759873 Genomic DNA. Translation: CAQ08690.1. CR759873 Genomic DNA. Translation: CAQ08691.1. CH471081 Genomic DNA. Translation: EAX03321.1. BC110645 mRNA. Translation: AAI10646.1. BC152556 mRNA. Translation: AAI52557.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS34384.1. [Q14676-1] |
NCBI Reference Sequences More...RefSeqi | NP_055456.2. NM_014641.2. [Q14676-1] XP_005249551.1. XM_005249494.4. [Q14676-1] XP_011513303.1. XM_011515001.2. [Q14676-1] XP_011513305.1. XM_011515003.2. [Q14676-1] XP_016867008.1. XM_017011519.1. [Q14676-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.653495. |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2ADO | X-ray | 1.45 | A/B | 1891-2086 | [»] | |
2AZM | X-ray | 2.41 | A/B | 1883-2089 | [»] | |
2ETX | X-ray | 1.33 | A/B | 1884-2089 | [»] | |
3K05 | X-ray | 1.33 | A/B | 1891-2089 | [»] | |
3UEO | X-ray | 2.60 | E/F | 325-336 | [»] | |
3UMZ | X-ray | 1.65 | A/B | 27-138 | [»] | |
3UN0 | X-ray | 2.30 | A/B | 26-138 | [»] | |
3UNM | X-ray | 1.80 | A/B | 27-138 | [»] | |
3UNN | X-ray | 1.70 | A | 27-138 | [»] | |
B | 1-8 | [»] | ||||
3UOT | X-ray | 1.80 | A/B | 19-138 | [»] | |
D/E | 1-10 | [»] | ||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q14676. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q14676. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115014. 198 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q14676. |
Database of interacting proteins More...DIPi | DIP-33603N. |
Protein interaction database and analysis system More...IntActi | Q14676. 25 interactors. |
Molecular INTeraction database More...MINTi | Q14676. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000365588. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q14676. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q14676. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q14676. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MDC1. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q14676. |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q14676. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q14676. |
PeptideAtlas More...PeptideAtlasi | Q14676. |
PRoteomics IDEntifications database More...PRIDEi | Q14676. |
Protocols and materials databases
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000376406; ENSP00000365588; ENSG00000137337. [Q14676-1] ENST00000383566; ENSP00000373060; ENSG00000206481. ENST00000420019; ENSP00000396484; ENSG00000224587. [Q14676-1] ENST00000420320; ENSP00000416511; ENSG00000225589. [Q14676-1] ENST00000427406; ENSP00000387429; ENSG00000234012. [Q14676-1] ENST00000435664; ENSP00000404318; ENSG00000231135. ENST00000440369; ENSP00000415212; ENSG00000228575. [Q14676-1] ENST00000449153; ENSP00000409167; ENSG00000237095. [Q14676-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9656. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9656. |
UCSC genome browser More...UCSCi | uc003nrg.5. human. [Q14676-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9656. |
DisGeNET More...DisGeNETi | 9656. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000137337.14. |
GeneCards: human genes, protein and diseases More...GeneCardsi | MDC1. |
Human Gene Nomenclature Database More...HGNCi | HGNC:21163. MDC1. |
Human Protein Atlas More...HPAi | HPA006915. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607593. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q14676. |
Open Targets More...OpenTargetsi | ENSG00000137337. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134942837. |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2043. Eukaryota. ENOG4111RPS. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00600000084454. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG080567. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q14676. |
KEGG Orthology (KO) More...KOi | K20780. |
Identification of Orthologs from Complete Genome Data More...OMAi | FPLYLGK. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0V3Z. |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q14676. |
TreeFam database of animal gene trees More...TreeFami | TF329580. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3108214. SUMOylation of DNA damage response and repair proteins. R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. R-HSA-5693571. Nonhomologous End-Joining (NHEJ). R-HSA-5693607. Processing of DNA double-strand break ends. R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes. R-HSA-69473. G2/M DNA damage checkpoint. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q14676. |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q14676. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MDC1. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q14676. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MDC1. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9656. |
Protein Ontology More...PROi | PR:Q14676. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000137337. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q14676. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q14676. HS. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00027. BRCT. 1 hit. cd00060. FHA. 1 hit. |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.10190. 2 hits. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001357. BRCT_dom. IPR036420. BRCT_dom_sf. IPR000253. FHA_dom. IPR008984. SMAD_FHA_dom_sf. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00498. FHA. 1 hit. PF16770. RTT107_BRCT_5. 1 hit. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00240. FHA. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF49879. SSF49879. 1 hit. SSF52113. SSF52113. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50172. BRCT. 1 hit. PS50006. FHA_DOMAIN. 1 hit. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | MDC1_HUMAN | |
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q14676Primary (citable) accession number: Q14676 Secondary accession number(s): A2AB04 , A2BF04, A2RRA8, A7YY86, B0S8A2, Q0EFC2, Q2L6H7, Q2TAZ4, Q5JP55, Q5JP56, Q5ST83, Q68CQ3, Q86Z06, Q96QC2 | |
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 5, 2005 |
Last sequence update: | July 5, 2005 | |
Last modified: | February 28, 2018 | |
This is version 180 of the entry and version 3 of the sequence. See complete history. | ||
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |