UniProtKB - Q96JM3 (CHAP1_HUMAN)
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>sp|Q96JM3|CHAP1_HUMAN Chromosome alignment-maintaining phosphoprotein 1 OS=Homo sapiens OX=9606 GN=CHAMP1 PE=1 SV=2 MEAFQELRKPSARLECDHCSFRGTDYENVQIHMGTIHPEFCDEMDAGGLGKMIFYQKSAK LFHCHKCFFTSKMYSNVYYHITSKHASPDKWNDKPKNQLNKETDPVKSPPLPEHQKIPCN SAEPKSIPALSMETQKLGSVLSPESPKPTPLTPLEPQKPGSVVSPELQTPLPSPEPSKPA SVSSPEPPKSVPVCESQKLAPVPSPEPQKPAPVSPESVKATLSNPKPQKQSHFPETLGPP SASSPESPVLAASPEPWGPSPAASPESRKSARTTSPEPRKPSPSESPEPWKPFPAVSPEP RRPAPAVSPGSWKPGPPGSPRPWKSNPSASSGPWKPAKPAPSVSPGPWKPIPSVSPGPWK PTPSVSSASWKSSSVSPSSWKSPPASPESWKSGPPELRKTAPTLSPEHWKAVPPVSPELR KPGPPLSPEIRSPAGSPELRKPSGSPDLWKLSPDQRKTSPASLDFPESQKSSRGGSPDLW KSSFFIEPQKPVFPETRKPGPSGPSESPKAASDIWKPVLSIDTEPRKPALFPEPAKTAPP ASPEARKRALFPEPRKHALFPELPKSALFSESQKAVELGDELQIDAIDDQKCDILVQEEL LASPKKLLEDTLFPSSKKLKKDNQESSDAELSSSEYIKTDLDAMDIKGQESSSDQEQVDV ESIDFSKENKMDMTSPEQSRNVLQFTEEKEAFISEEEIAKYMKRGKGKYYCKICCCRAMK KGAVLHHLVNKHNVHSPYKCTICGKAFLLESLLKNHVAAHGQSLLKCPRCNFESNFPRGF KKHLTHCQSRHNEEANKKLMEALEPPLEEQQIHelp videoAdd a publicationFeedback
Chromosome alignment-maintaining phosphoprotein 1
CHAMP1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<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.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 738 – 760 | C2H2-typePROSITE-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 | 23 |
<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
- metal ion binding Source: UniProtKB-KW
- nucleic acid binding Source: InterPro
GO - Biological processi
- attachment of mitotic spindle microtubules to kinetochore Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- protein localization to kinetochore Source: UniProtKBInferred from mutant phenotypei
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- protein localization to microtubule Source: UniProtKBInferred from mutant phenotypei
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- sister chromatid biorientation Source: UniProtKBInferred from mutant phenotypei
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
<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
Ligand | Metal-binding, Zinc |
<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: Chromosome alignment-maintaining phosphoprotein 1Alternative name(s): Zinc finger protein 828 |
<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:CHAMP1 Synonyms:C13orf8, CAMP, CHAMP, KIAA1802, ZNF828 |
<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 NCBI 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
Human Gene Nomenclature Database More...HGNCi | HGNC:20311 CHAMP1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 616327 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96JM3 |
<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 1 Publication
Manual assertion based on experiment ini
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- Nucleus 1 Publication
Cytoskeleton
- spindle 1 Publication
Manual assertion based on experiment ini
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- spindle 1 Publication
Other locations
- Chromosome 1 Publication
Manual assertion based on experiment ini
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- kinetochore 1 Publication
Manual assertion based on experiment ini
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- Chromosome 1 Publication
Cytoskeleton
- spindle Source: UniProtKB
<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
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- spindle Source: UniProtKB
<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
Nucleus
- nuclear body Source: HPA
- nucleoplasm Source: HPA
- nucleus Source: UniProtKBInferred from direct assayi
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Other locations
- cell Source: GOC
- condensed chromosome Source: UniProtKBInferred from direct assayi
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- condensed chromosome kinetochore Source: UniProtKBInferred from direct assayi
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
- cytoplasm Source: UniProtKB-KW
- Flemming body Source: HPA
Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, 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
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Mental retardation, autosomal dominant 40 (MRD40)2 PublicationsManual assertion based on experiment ini
- Ref.20"De novo mutations in CHAMP1 cause intellectual disability with severe speech impairment."
Hempel M., Cremer K., Ockeloen C.W., Lichtenbelt K.D., Herkert J.C., Denecke J., Haack T.B., Zink A.M., Becker J., Wohlleber E., Johannsen J., Alhaddad B., Pfundt R., Fuchs S., Wieczorek D., Strom T.M., van Gassen K.L., Kleefstra T. , Kubisch C., Engels H., Lessel D.
Am. J. Hum. Genet. 97:493-500(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN MRD40. - Ref.22"Large-scale discovery of novel genetic causes of developmental disorders."
Deciphering Developmental Disorders Study
Nature 519:223-228(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN MRD40.
Hempel M., Cremer K., Ockeloen C.W., Lichtenbelt K.D., Herkert J.C., Denecke J., Haack T.B., Zink A.M., Becker J., Wohlleber E., Johannsen J., Alhaddad B., Pfundt R., Fuchs S., Wieczorek D., Strom T.M., van Gassen K.L., Kleefstra T. , Kubisch C., Engels H., Lessel D.
Am. J. Hum. Genet. 97:493-500(2015) [PubMed] [Europe PMC] [Abstract]
Deciphering Developmental Disorders Study
Nature 519:223-228(2015) [PubMed] [Europe PMC] [Abstract]
Keywords - Diseasei
Mental retardationOrganism-specific databases
DisGeNET More...DisGeNETi | 283489 |
MalaCards human disease database More...MalaCardsi | CHAMP1 |
MIMi | 616579 phenotype |
Open Targets More...OpenTargetsi | ENSG00000198824 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 178469 Autosomal dominant non-syndromic intellectual disability |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA162410749 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | Q96JM3 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CHAMP1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 114149935 |
<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_0000248319 | 1 – 812 | Chromosome alignment-maintaining phosphoprotein 1Add BLAST | 812 |
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 | 1 | N-acetylmethionineCombined 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 | |
Modified residuei | 87 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 108 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 173 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 184 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 204 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 214 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 217 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 244 | 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 | |
Modified residuei | 247 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 253 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 264 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 275 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 282 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 286 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 297 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 308 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 319 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 344 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 355 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 376 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 382 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 386 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 403 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 405 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 416 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 427 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 432 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 436 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 443 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 445 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 452 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 458 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 459 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 462 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 472 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 476 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 490 | N6-acetyllysine; alternateCombined sources 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">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, 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 | 490 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
Modified residuei | 507 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 512 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 542 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Cross-linki | 565 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
Modified residuei | 572 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 603 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Cross-linki | 606 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
Modified residuei | 615 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 626 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 627 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 632 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Cross-linki | 638 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
Modified residuei | 651 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 652 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 653 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Cross-linki | 670 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
Modified residuei | 675 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Cross-linki | 689 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
Modified residuei | 736 | PhosphoserineCombined sources 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">PTM/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
Manual assertion based on experiment ini
- Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96JM3 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | Q96JM3 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | Q96JM3 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96JM3 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96JM3 |
PeptideAtlas More...PeptideAtlasi | Q96JM3 |
PRoteomics IDEntifications database More...PRIDEi | Q96JM3 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 76984 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96JM3 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96JM3 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q96JM3 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000198824 Expressed in 188 organ(s), highest expression level in amniotic fluid |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96JM3 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96JM3 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA006623 HPA008900 |
<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
Interacts with MAD2L2.
Interacts with POGZ, CBX1, CBX3 and CBX5.
2 PublicationsManual assertion based on experiment ini
- Ref.11"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH POGZ; CBX1; CBX3 AND CBX5. - Ref.14"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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 |
---|---|---|---|---|
Q9UI95 | 6 | EBI-2560420,EBI-77889 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 129584, 54 interactors |
Protein interaction database and analysis system More...IntActi | Q96JM3, 34 interactors |
Molecular INTeraction database More...MINTi | Q96JM3 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000354730 |
<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 <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> 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 | 331 – 338 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96JM3 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<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
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 | 271 – 490 | Mediates interaction with MAD2L21 Publication Manual assertion based on experiment ini
| 220 | |
Regioni | 451 – 590 | Mediates localization to the spindle and the kinetochore and is required for the attachment of spindle microtubules to the kinetochoreAdd BLAST | 140 | |
Regioni | 591 – 812 | Mediates localization to the chromosome and the spindle and negatively regulates chromosome alignmentAdd BLAST | 222 |
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 | 105 – 564 | Pro-richAdd BLAST | 460 |
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 738 – 760 | C2H2-typePROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 23 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IFC8 Eukaryota ENOG410XXII LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00730000111351 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000065731 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96JM3 |
KEGG Orthology (KO) More...KOi | K22593 |
Identification of Orthologs from Complete Genome Data More...OMAi | TSKMYSN |
Database of Orthologous Groups More...OrthoDBi | 277957at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96JM3 |
TreeFam database of animal gene trees More...TreeFami | TF350859 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR039330 CAMP IPR036236 Znf_C2H2_sf IPR013087 Znf_C2H2_type |
The PANTHER Classification System More...PANTHERi | PTHR37354 PTHR37354, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00355 ZnF_C2H2, 5 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57667 SSF57667, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00028 ZINC_FINGER_C2H2_1, 1 hit PS50157 ZINC_FINGER_C2H2_2, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MEAFQELRKP SARLECDHCS FRGTDYENVQ IHMGTIHPEF CDEMDAGGLG
60 70 80 90 100
KMIFYQKSAK LFHCHKCFFT SKMYSNVYYH ITSKHASPDK WNDKPKNQLN
110 120 130 140 150
KETDPVKSPP LPEHQKIPCN SAEPKSIPAL SMETQKLGSV LSPESPKPTP
160 170 180 190 200
LTPLEPQKPG SVVSPELQTP LPSPEPSKPA SVSSPEPPKS VPVCESQKLA
210 220 230 240 250
PVPSPEPQKP APVSPESVKA TLSNPKPQKQ SHFPETLGPP SASSPESPVL
260 270 280 290 300
AASPEPWGPS PAASPESRKS ARTTSPEPRK PSPSESPEPW KPFPAVSPEP
310 320 330 340 350
RRPAPAVSPG SWKPGPPGSP RPWKSNPSAS SGPWKPAKPA PSVSPGPWKP
360 370 380 390 400
IPSVSPGPWK PTPSVSSASW KSSSVSPSSW KSPPASPESW KSGPPELRKT
410 420 430 440 450
APTLSPEHWK AVPPVSPELR KPGPPLSPEI RSPAGSPELR KPSGSPDLWK
460 470 480 490 500
LSPDQRKTSP ASLDFPESQK SSRGGSPDLW KSSFFIEPQK PVFPETRKPG
510 520 530 540 550
PSGPSESPKA ASDIWKPVLS IDTEPRKPAL FPEPAKTAPP ASPEARKRAL
560 570 580 590 600
FPEPRKHALF PELPKSALFS ESQKAVELGD ELQIDAIDDQ KCDILVQEEL
610 620 630 640 650
LASPKKLLED TLFPSSKKLK KDNQESSDAE LSSSEYIKTD LDAMDIKGQE
660 670 680 690 700
SSSDQEQVDV ESIDFSKENK MDMTSPEQSR NVLQFTEEKE AFISEEEIAK
710 720 730 740 750
YMKRGKGKYY CKICCCRAMK KGAVLHHLVN KHNVHSPYKC TICGKAFLLE
760 770 780 790 800
SLLKNHVAAH GQSLLKCPRC NFESNFPRGF KKHLTHCQSR HNEEANKKLM
810
EALEPPLEEQ QI
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketEntry | Entry name | Protein names | Gene names | Length | Annotation | ||
---|---|---|---|---|---|---|---|
S4R3K0 | S4R3K0_HUMAN | Chromosome alignment-maintaining ph... Chromosome alignment-maintaining phosphoprotein 1 | CHAMP1 | 145 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
A0A2R8Y4S6 | A0A2R8Y4S6_HUMAN | Chromosome alignment-maintaining ph... Chromosome alignment-maintaining phosphoprotein 1 | CHAMP1 | 122 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
A0A2R8Y735 | A0A2R8Y735_HUMAN | Chromosome alignment-maintaining ph... Chromosome alignment-maintaining phosphoprotein 1 | CHAMP1 | 194 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> |
<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 | 81 | I → T in BAC11273 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 140 | V → A in BAC11273 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 576 | V → A in BAC11273 (PubMed:14702039).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_027270 | 568 | L → V. Corresponds to variant dbSNP:rs3764522Ensembl. | 1 | |
Natural variantiVAR_052910 | 591 | K → R. Corresponds to variant dbSNP:rs35564629Ensembl. | 1 | |
Natural variantiVAR_027271 | 604 | P → R. Corresponds to variant dbSNP:rs12428067Ensembl. | 1 |
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 | AB058705 mRNA Translation: BAB47431.1 Different initiation. AK074894 mRNA Translation: BAC11273.1 Different initiation. AK096346 mRNA Translation: BAG53268.1 AL845154 Genomic DNA No translation available. CH471085 Genomic DNA Translation: EAX09253.1 BC004820 mRNA Translation: AAH04820.1 BC065237 mRNA Translation: AAH65237.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS9545.1 |
NCBI Reference Sequences More...RefSeqi | NP_001157616.1, NM_001164144.2 NP_001157617.1, NM_001164145.2 NP_115812.1, NM_032436.3 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000361283; ENSP00000354730; ENSG00000198824 ENST00000643483; ENSP00000496699; ENSG00000198824 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 283489 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:283489 |
UCSC genome browser More...UCSCi | uc001vuv.4 human |
Keywords - Coding sequence diversityi
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 | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q96JM3 | Chromosome alignment-maintaining phosphoprotein 1 (Fragment) | 145 | UniRef100_Q96JM3 | |||
Chromosome alignment-maintaining phosphoprotein 1 (Fragment) | 194 | |||||
Chromosome alignment-maintaining phosphoprotein 1 (Fragment) | 122 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q96JM3 | Chromosome alignment-maintaining phosphoprotein 1 (Fragment) | 145 | UniRef90_Q96JM3 | |||
C2H2-type domain-containing protein (Fragment) | 878 | |||||
Chromosome alignment maintaining phosphoprotein 1 | 831 | |||||
chromosome alignment-maintaining phosphoprotein 1 | 826 | |||||
chromosome alignment-maintaining phosphoprotein 1 | 826 | |||||
+54 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q96JM3 | Chromosome alignment-maintaining phosphoprotein 1 (Fragment) | 145 | UniRef50_Q96JM3 | |||
C2H2-type domain-containing protein (Fragment) | 878 | |||||
Chromosome alignment maintaining phosphoprotein 1 | 831 | |||||
chromosome alignment-maintaining phosphoprotein 1 | 826 | |||||
chromosome alignment-maintaining phosphoprotein 1 | 826 | |||||
+227 |
<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: EMBLi GenBanki DDBJi Links Updated | AB058705 mRNA Translation: BAB47431.1 Different initiation. AK074894 mRNA Translation: BAC11273.1 Different initiation. AK096346 mRNA Translation: BAG53268.1 AL845154 Genomic DNA No translation available. CH471085 Genomic DNA Translation: EAX09253.1 BC004820 mRNA Translation: AAH04820.1 BC065237 mRNA Translation: AAH65237.1 |
CCDSi | CCDS9545.1 |
RefSeqi | NP_001157616.1, NM_001164144.2 NP_001157617.1, NM_001164145.2 NP_115812.1, NM_032436.3 |
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 |
5XPT | X-ray | 2.10 | B | 325-344 | [»] | |
5XPU | X-ray | 2.30 | B | 325-344 | [»] | |
6EKJ | X-ray | 1.60 | B | 328-355 | [»] | |
6EKL | X-ray | 1.60 | B | 328-355 | [»] | |
SMRi | Q96JM3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 129584, 54 interactors |
IntActi | Q96JM3, 34 interactors |
MINTi | Q96JM3 |
STRINGi | 9606.ENSP00000354730 |
PTM databases
iPTMneti | Q96JM3 |
PhosphoSitePlusi | Q96JM3 |
SwissPalmi | Q96JM3 |
Polymorphism and mutation databases
BioMutai | CHAMP1 |
DMDMi | 114149935 |
Proteomic databases
EPDi | Q96JM3 |
jPOSTi | Q96JM3 |
MassIVEi | Q96JM3 |
MaxQBi | Q96JM3 |
PaxDbi | Q96JM3 |
PeptideAtlasi | Q96JM3 |
PRIDEi | Q96JM3 |
ProteomicsDBi | 76984 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 283489 |
Genome annotation databases
Ensembli | ENST00000361283; ENSP00000354730; ENSG00000198824 ENST00000643483; ENSP00000496699; ENSG00000198824 |
GeneIDi | 283489 |
KEGGi | hsa:283489 |
UCSCi | uc001vuv.4 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 283489 |
DisGeNETi | 283489 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CHAMP1 |
HGNCi | HGNC:20311 CHAMP1 |
HPAi | HPA006623 HPA008900 |
MalaCardsi | CHAMP1 |
MIMi | 616327 gene 616579 phenotype |
neXtProti | NX_Q96JM3 |
OpenTargetsi | ENSG00000198824 |
Orphaneti | 178469 Autosomal dominant non-syndromic intellectual disability |
PharmGKBi | PA162410749 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG410IFC8 Eukaryota ENOG410XXII LUCA |
GeneTreei | ENSGT00730000111351 |
HOGENOMi | HOG000065731 |
InParanoidi | Q96JM3 |
KOi | K22593 |
OMAi | TSKMYSN |
OrthoDBi | 277957at2759 |
PhylomeDBi | Q96JM3 |
TreeFami | TF350859 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CHAMP1 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | C13orf8 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 283489 |
Pharosi | Q96JM3 |
Protein Ontology More...PROi | PR:Q96JM3 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000198824 Expressed in 188 organ(s), highest expression level in amniotic fluid |
ExpressionAtlasi | Q96JM3 baseline and differential |
Genevisiblei | Q96JM3 HS |
Family and domain databases
InterProi | View protein in InterPro IPR039330 CAMP IPR036236 Znf_C2H2_sf IPR013087 Znf_C2H2_type |
PANTHERi | PTHR37354 PTHR37354, 1 hit |
SMARTi | View protein in SMART SM00355 ZnF_C2H2, 5 hits |
SUPFAMi | SSF57667 SSF57667, 1 hit |
PROSITEi | View protein in PROSITE PS00028 ZINC_FINGER_C2H2_1, 1 hit PS50157 ZINC_FINGER_C2H2_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 | CHAP1_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 | Q96JM3Primary (citable) accession number: Q96JM3 Secondary accession number(s): B3KU06 , Q6P181, Q8NC88, Q9BST0 | |
<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: | September 5, 2006 |
Last sequence update: | September 5, 2006 | |
Last modified: | November 13, 2019 | |
This is version 152 of the entry and version 2 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. |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 13
Human chromosome 13: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references