UniProtKB - O60271 (JIP4_HUMAN)
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- BLAST>sp|O60271|JIP4_HUMAN C-Jun-amino-terminal kinase-interacting protein 4 OS=Homo sapiens OX=9606 GN=SPAG9 PE=1 SV=4 MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLEN LDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTR VESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLH QLSGSDQLESTAHSRIRKERPISLGIFPLPAGDGLLTPDAQKGGETPGSEQWKFQELSQP RSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIPTDTPLKEENEG FVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGY KGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEGADLLGMGREVENLILENTQL LETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEA EDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE NPAMQEKKRSSIWQFFSRLFSSSSNTTKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLP GDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKEDGRVQAFGWSLPQKYKQVTNG QGENKMKNLPVPVYLRPLDEKDTSMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVAGLD TEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSLVWICTSTHSATKVLIIDAVQPGN ILDSFTVCNSHVLCIASVPGARETDYPAGEDLSESGQVDKASLCGSMTSNSSAETDSLLG GITVVGCSAEGVTGAATSPSTNGASPVMDKPPEMEAENSEVDENVPTAEEATEATEGNAG SAEDTVDISQTGVYTEHVFTDPLGVQIPEDLSPVYQSSNDSDAYKDQISVLPNEQDLVRE EAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADG TLAIFHRGVDGQWDLSNYHLLDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEK SFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGTGK LGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGVPGNRPGSVIRVYGDENSDK VTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVISPQSSSSGTDLTGDKAGPSAQEP GSQTPLKSMLVISGGEGYIDFRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMYGN E
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Protein
C-Jun-amino-terminal kinase-interacting protein 4
Gene
SPAG9
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
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
The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Isoform 5 may play a role in spermatozoa-egg-interaction.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
- Ref.11"A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway."
Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G., Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S., Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J., Schwab M., Stein M.A. , Bauer A., Casari G., Drewes G., Gavin A.-C., Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B., Superti-Furga G.
Nat. Cell Biol. 6:97-105(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NFKB1. - Ref.12"Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein."
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.
Biochem. J. 389:73-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MAPK9; MAPK10 AND MAPK8, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
<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
- JUN kinase binding Source: GO_Central
- kinesin binding Source: GO_Central
- MAP-kinase scaffold activity Source: GO_Central
- mitogen-activated protein kinase p38 binding Source: Ensembl
- receptor signaling complex scaffold activity Source: GO_Central
<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
- activation of JUN kinase activity Source: GO_Central
- negative regulation of protein homodimerization activity Source: Ensembl
- positive regulation of cell migration 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
- positive regulation of muscle cell differentiation Source: Reactome
- positive regulation of neuron differentiation Source: Ensembl
- protein homooligomerization Source: Ensembl
- retrograde transport, endosome to Golgi 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
- spermatogenesis Source: ProtInc <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
- striated muscle cell differentiation Source: Ensembl
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-375170. CDO in myogenesis. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O60271. |
SIGNOR Signaling Network Open Resource More...SIGNORi | O60271. |
<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: C-Jun-amino-terminal kinase-interacting protein 4Short name: JIP-4 Short name: JNK-interacting protein 4 Alternative name(s): Cancer/testis antigen 89 Short name: CT89 Human lung cancer oncogene 6 protein Short name: HLC-6 JNK-associated leucine-zipper protein Short name: JLP Mitogen-activated protein kinase 8-interacting protein 4 Proliferation-inducing protein 6 Protein highly expressed in testis Short name: PHET Sperm surface protein Sperm-associated antigen 9 Sperm-specific protein Sunday driver 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:SPAG9 Synonyms:HSS, KIAA0516, MAPK8IP4, SYD1 ORF Names:HLC6 |
| <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:ENSG00000008294.20. |
Human Gene Nomenclature Database More...HGNCi | HGNC:14524. SPAG9. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605430. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O60271. |
<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
Other locations
Note: Perinuclear distribution in response to stress signals such as UV radiation.
Cytoskeleton
- microtubule organizing center Source: HPA
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Other locations
- acrosomal vesicle Source: UniProtKB-SubCell
- cytoplasm Source: GO_Central
- integral component of membrane Source: ProtInc <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
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
<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
Cytoplasm, Cytoplasmic vesicle<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
Organism-specific databases
DisGeNET More...DisGeNETi | 9043. |
Open Targets More...OpenTargetsi | ENSG00000008294. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA37890. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SPAG9. |
<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_0000234076 | 1 – 1321 | C-Jun-amino-terminal kinase-interacting protein 4Add BLAST | 1321 |
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 | |
| <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 | 109 | 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 | 183 | 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 | 185 | 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 | 194 | 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 | 203 | 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 | 217 | 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 | 238 | 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 | 251 | 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 | 265 | 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 | 268 | 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 | 272 | 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 | 292 | PhosphothreonineBy 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 | 311 | 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 | 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 | 332 | 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 | 347 | 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 | 348 | 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 | 365 | PhosphothreonineBy 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 | 418 | 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 | 586 | 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 | 588 | 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 | 595 | 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 | 705 | 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 | 728 | 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 | 730 | 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 | 732 | 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 | 733 | 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 | 1188 | 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 | 1264 | 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 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
Phosphorylated by MAPK8 and MAPK14.By similarity
<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, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O60271. |
MaxQB - The MaxQuant DataBase More...MaxQBi | O60271. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O60271. |
PeptideAtlas More...PeptideAtlasi | O60271. |
PRoteomics IDEntifications database More...PRIDEi | O60271. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O60271. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O60271. |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | O60271. |
<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
Isoform 5 is expressed only in testis on the round spermatids of stage I, II and II. Isoform 5 is absent in spermatogonia and spermatocyte. Isoform 3 is expressed in testis. Isoform 4 is expressed in testis and in acute myeloid leukemia (AML) patients.3 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.2"Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia."
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J.
Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY. - Ref.8"Cloning of a novel human testis mRNA specifically expressed in testicular haploid germ cells, having unique palindromic sequences and encoding a leucine zipper dimerization motif."
Shankar S., Mohapatra B., Suri A.
Biochem. Biophys. Res. Commun. 243:561-565(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-1321 (ISOFORM 5), TISSUE SPECIFICITY. - Ref.9"A novel protein highly expressed in testis is overexpressed in systemic sclerosis fibroblasts and targeted by autoantibodies."
Yasuoka H., Ihn H., Medsger T.A. Jr., Hirakata M., Kawakami Y., Ikeda Y., Kuwana M.
J. Immunol. 171:6883-6890(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Isoform 3 is increased in systemic sclerosis fibroblasts.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
- Ref.9"A novel protein highly expressed in testis is overexpressed in systemic sclerosis fibroblasts and targeted by autoantibodies."
Yasuoka H., Ihn H., Medsger T.A. Jr., Hirakata M., Kawakami Y., Ikeda Y., Kuwana M.
J. Immunol. 171:6883-6890(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000008294. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O60271. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O60271. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA040446. HPA061458. |
<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
Homodimer. The homodimer interacts with ARF6, forming a heterotetramer. Homooligomer. Interacts with MAX, MAPK8, MAPK9, MAPK10, MAPK14, MAP3K3, MYC, KNS2 and MAP2K4. Interaction with KNS2 is important in the formation of ternary complex with MAPK8. Interacts with NFKB1.3 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.11"A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway."
Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G., Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S., Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J., Schwab M., Stein M.A. , Bauer A., Casari G., Drewes G., Gavin A.-C., Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B., Superti-Furga G.
Nat. Cell Biol. 6:97-105(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NFKB1. - Ref.12"Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein."
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.
Biochem. J. 389:73-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MAPK9; MAPK10 AND MAPK8, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.25"The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4."
Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F., England P., Franco M., Chavrier P., Houdusse A., Menetrey J.
EMBO J. 28:2835-2845(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 406-476 IN COMPLEX WITH ARF6, COILED COIL, SUBUNIT, INTERACTION WITH ARF6.
<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 |
|---|---|---|---|---|
| ARF1 | P84077 | 3 | EBI-1023301,EBI-447171 | |
| ARF6 | P62330 | 8 | EBI-1023301,EBI-638181 | |
| Arf6 | P62331 | 2 | EBI-1023301,EBI-988682 | From Mus musculus. |
| EXOC4 | Q96A65 | 3 | EBI-1023301,EBI-355383 | |
| NFKB1 | P19838 | 2 | EBI-1023301,EBI-300010 | |
| PLK1 | P53350 | 3 | EBI-1023301,EBI-476768 |
<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
- JUN kinase binding Source: GO_Central
- kinesin binding Source: GO_Central
- MAP-kinase scaffold activity Source: GO_Central
- mitogen-activated protein kinase p38 binding Source: Ensembl
- receptor signaling complex scaffold activity Source: GO_Central
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114505. 93 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O60271. |
Protein interaction database and analysis system More...IntActi | O60271. 37 interactors. |
Molecular INTeraction database More...MINTi | O60271. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000262013. |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| 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 | 406 – 465 | 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 | 60 |
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 |
| 2W83 | X-ray | 1.93 | C/D | 406-476 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O60271. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O60271. | |||||
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 | O60271. |
<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 | 7 – 95 | RH1PROSITE-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 | 89 | |
| <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 | 500 – 571 | RH2PROSITE-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 | 72 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 66 – 166 | Sequence analysisAdd BLAST | 101 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 408 – 534 | 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
| 127 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 724 – 758 | Sequence analysisAdd BLAST | 35 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the JIP scaffold family.Curated
<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
Coiled coilPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2077. Eukaryota. ENOG410XQ19. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00670000097546. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000290716. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG024110. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O60271. |
KEGG Orthology (KO) More...KOi | K20317. |
Identification of Orthologs from Complete Genome Data More...OMAi | RENPAMQ. |
Database of Orthologous Groups More...OrthoDBi | EOG091G016S. |
Database for complete collections of gene phylogenies More...PhylomeDBi | O60271. |
TreeFam database of animal gene trees More...TreeFami | TF313096. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.130.10.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR032486. JIP_LZII. IPR019143. JNK/Rab-associated_protein-1_N. IPR034743. RH1. IPR034744. RH2. IPR015943. WD40/YVTN_repeat-like_dom_sf. IPR036322. WD40_repeat_dom_sf. |
Pfam protein domain database More...Pfami | View protein in Pfam PF16471. JIP_LZII. 1 hit. PF09744. Jnk-SapK_ap_N. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50978. SSF50978. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51776. RH1. 1 hit. PS51777. RH2. 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 (6)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 6 <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
Isoform 1 (identifier: O60271-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL
60 70 80 90 100
MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE
110 120 130 140 150
EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA
160 170 180 190 200
ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLES TAHSRIRKER
210 220 230 240 250
PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKVSN
260 270 280 290 300
SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG
310 320 330 340 350
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE
360 370 380 390 400
LDMDKDLSGY KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG
410 420 430 440 450
ADLLGMGREV ENLILENTQL LETKNALNIV KNDLIAKVDE LTCEKDVLQG
460 470 480 490 500
ELEAVKQAKL KLEEKNRELE EELRKARAEA EDARQKAKDD DDSDIPTAQR
510 520 530 540 550
KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE NPAMQEKKRS
560 570 580 590 600
SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
610 620 630 640 650
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL
660 670 680 690 700
PQKYKQVTNG QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT
710 720 730 740 750
RDGGSVVGAS VFYKDVAGLD TEGSKQRSAS QSSLDKLDQE LKEQQKELKN
760 770 780 790 800
QEELSSLVWI CTSTHSATKV LIIDAVQPGN ILDSFTVCNS HVLCIASVPG
810 820 830 840 850
ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG GITVVGCSAE
860 870 880 890 900
GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG
910 920 930 940 950
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV
960 970 980 990 1000
LPNEQDLVRE EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK
1010 1020 1030 1040 1050
DSILSIVHVK GIVLVALADG TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI
1060 1070 1080 1090 1100
RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK SFDAHPRKES QVRQLAWVGD
1110 1120 1130 1140 1150
GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK LGFSFVRITA
1160 1170 1180 1190 1200
LMVSCNRLWV GTGNGVIISI PLTETNKTSG VPGNRPGSVI RVYGDENSDK
1210 1220 1230 1240 1250
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG
1260 1270 1280 1290 1300
DKAGPSAQEP GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE
1310 1320
PSVTKAERSH LIVWQVMYGN E
Length:1,321
Mass (Da):146,205
Last modified:May 2, 2006 - v4
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i5CAE349FBDF91B40
Isoform 2 (identifier: O60271-2) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
248-261: Missing.
555-555: F → FVPTR
10 20 30 40 50
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL
60 70 80 90 100
MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE
110 120 130 140 150
EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA
160 170 180 190 200
ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLES TAHSRIRKER
210 220 230 240 250
PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKDEL
260 270 280 290 300
SDVSQGGSKA TTPASTANSD VATIPTDTPL KEENEGFVKV TDAPNKSEIS
310 320 330 340 350
KHIEVQVAQE TRNVSTGSAE NEEKSEVQAI IESTPELDMD KDLSGYKGSS
360 370 380 390 400
TPTKGIENKA FDRNTESLFE ELSSAGSGLI GDVDEGADLL GMGREVENLI
410 420 430 440 450
LENTQLLETK NALNIVKNDL IAKVDELTCE KDVLQGELEA VKQAKLKLEE
460 470 480 490 500
KNRELEEELR KARAEAEDAR QKAKDDDDSD IPTAQRKRFT RVEMARVLME
510 520 530 540 550
RNQYKERLME LQEAVRWTEM IRASRENPAM QEKKRSSIWQ FVPTRFSRLF
560 570 580 590 600
SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP GDKSKAFDFL
610 620 630 640 650
SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVTNG
660 670 680 690 700
QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT RDGGSVVGAS
710 720 730 740 750
VFYKDVAGLD TEGSKQRSAS QSSLDKLDQE LKEQQKELKN QEELSSLVWI
760 770 780 790 800
CTSTHSATKV LIIDAVQPGN ILDSFTVCNS HVLCIASVPG ARETDYPAGE
810 820 830 840 850
DLSESGQVDK ASLCGSMTSN SSAETDSLLG GITVVGCSAE GVTGAATSPS
860 870 880 890 900
TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG SAEDTVDISQ
910 920 930 940 950
TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV LPNEQDLVRE
960 970 980 990 1000
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK
1010 1020 1030 1040 1050
GIVLVALADG TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV
1060 1070 1080 1090 1100
WCGYRNKIYV VQPKAMKIEK SFDAHPRKES QVRQLAWVGD GVWVSIRLDS
1110 1120 1130 1140 1150
TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK LGFSFVRITA LMVSCNRLWV
1160 1170 1180 1190 1200
GTGNGVIISI PLTETNKTSG VPGNRPGSVI RVYGDENSDK VTPGTFIPYC
1210 1220 1230 1240 1250
SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG DKAGPSAQEP
1260 1270 1280 1290 1300
GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH
1310
LIVWQVMYGN E
Length:1,311
Mass (Da):145,135
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iD60A544D70BD1F97
Isoform 3 (identifier: O60271-3) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
938-945: SNDSDAYK → RYNNGSST
946-1321: Missing.
10 20 30 40 50
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL
60 70 80 90 100
MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE
110 120 130 140 150
EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA
160 170 180 190 200
ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLES TAHSRIRKER
210 220 230 240 250
PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKVSN
260 270 280 290 300
SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG
310 320 330 340 350
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE
360 370 380 390 400
LDMDKDLSGY KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG
410 420 430 440 450
ADLLGMGREV ENLILENTQL LETKNALNIV KNDLIAKVDE LTCEKDVLQG
460 470 480 490 500
ELEAVKQAKL KLEEKNRELE EELRKARAEA EDARQKAKDD DDSDIPTAQR
510 520 530 540 550
KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE NPAMQEKKRS
560 570 580 590 600
SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
610 620 630 640 650
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL
660 670 680 690 700
PQKYKQVTNG QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT
710 720 730 740 750
RDGGSVVGAS VFYKDVAGLD TEGSKQRSAS QSSLDKLDQE LKEQQKELKN
760 770 780 790 800
QEELSSLVWI CTSTHSATKV LIIDAVQPGN ILDSFTVCNS HVLCIASVPG
810 820 830 840 850
ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG GITVVGCSAE
860 870 880 890 900
GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG
910 920 930 940
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSRYN NGSST
Note: Due to intron retention.
Show »Length:945
Mass (Da):104,736
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iEB17642AA2BF0BB4
Isoform 4 (identifier: O60271-4) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
248-261: Missing.
10 20 30 40 50
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL
60 70 80 90 100
MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE
110 120 130 140 150
EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA
160 170 180 190 200
ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLES TAHSRIRKER
210 220 230 240 250
PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKDEL
260 270 280 290 300
SDVSQGGSKA TTPASTANSD VATIPTDTPL KEENEGFVKV TDAPNKSEIS
310 320 330 340 350
KHIEVQVAQE TRNVSTGSAE NEEKSEVQAI IESTPELDMD KDLSGYKGSS
360 370 380 390 400
TPTKGIENKA FDRNTESLFE ELSSAGSGLI GDVDEGADLL GMGREVENLI
410 420 430 440 450
LENTQLLETK NALNIVKNDL IAKVDELTCE KDVLQGELEA VKQAKLKLEE
460 470 480 490 500
KNRELEEELR KARAEAEDAR QKAKDDDDSD IPTAQRKRFT RVEMARVLME
510 520 530 540 550
RNQYKERLME LQEAVRWTEM IRASRENPAM QEKKRSSIWQ FFSRLFSSSS
560 570 580 590 600
NTTKKPEPPV NLKYNAPTSH VTPSVKKRSS TLSQLPGDKS KAFDFLSEET
610 620 630 640 650
EASLASRREQ KREQYRQVKA HVQKEDGRVQ AFGWSLPQKY KQVTNGQGEN
660 670 680 690 700
KMKNLPVPVY LRPLDEKDTS MKLWCAVGVN LSGGKTRDGG SVVGASVFYK
710 720 730 740 750
DVAGLDTEGS KQRSASQSSL DKLDQELKEQ QKELKNQEEL SSLVWICTST
760 770 780 790 800
HSATKVLIID AVQPGNILDS FTVCNSHVLC IASVPGARET DYPAGEDLSE
810 820 830 840 850
SGQVDKASLC GSMTSNSSAE TDSLLGGITV VGCSAEGVTG AATSPSTNGA
860 870 880 890 900
SPVMDKPPEM EAENSEVDEN VPTAEEATEA TEGNAGSAED TVDISQTGVY
910 920 930 940 950
TEHVFTDPLG VQIPEDLSPV YQSSNDSDAY KDQISVLPNE QDLVREEAQK
960 970 980 990 1000
MSSLLPTMWL GAQNGCLYVH SSVAQWRKCL HSIKLKDSIL SIVHVKGIVL
1010 1020 1030 1040 1050
VALADGTLAI FHRGVDGQWD LSNYHLLDLG RPHHSIRCMT VVHDKVWCGY
1060 1070 1080 1090 1100
RNKIYVVQPK AMKIEKSFDA HPRKESQVRQ LAWVGDGVWV SIRLDSTLRL
1110 1120 1130 1140 1150
YHAHTYQHLQ DVDIEPYVSK MLGTGKLGFS FVRITALMVS CNRLWVGTGN
1160 1170 1180 1190 1200
GVIISIPLTE TNKTSGVPGN RPGSVIRVYG DENSDKVTPG TFIPYCSMAH
1210 1220 1230 1240 1250
AQLCFHGHRD AVKFFVAVPG QVISPQSSSS GTDLTGDKAG PSAQEPGSQT
1260 1270 1280 1290 1300
PLKSMLVISG GEGYIDFRMG DEGGESELLG EDLPLEPSVT KAERSHLIVW
QVMYGNE
Length:1,307
Mass (Da):144,682
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i55B30E422A8ABD0E
Isoform 5 (identifier: O60271-5) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
248-261: Missing.
938-945: SNDSDAYK → RYNNGSST
946-1321: Missing.
10 20 30 40 50
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL
60 70 80 90 100
MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE
110 120 130 140 150
EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA
160 170 180 190 200
ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLES TAHSRIRKER
210 220 230 240 250
PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKDEL
260 270 280 290 300
SDVSQGGSKA TTPASTANSD VATIPTDTPL KEENEGFVKV TDAPNKSEIS
310 320 330 340 350
KHIEVQVAQE TRNVSTGSAE NEEKSEVQAI IESTPELDMD KDLSGYKGSS
360 370 380 390 400
TPTKGIENKA FDRNTESLFE ELSSAGSGLI GDVDEGADLL GMGREVENLI
410 420 430 440 450
LENTQLLETK NALNIVKNDL IAKVDELTCE KDVLQGELEA VKQAKLKLEE
460 470 480 490 500
KNRELEEELR KARAEAEDAR QKAKDDDDSD IPTAQRKRFT RVEMARVLME
510 520 530 540 550
RNQYKERLME LQEAVRWTEM IRASRENPAM QEKKRSSIWQ FFSRLFSSSS
560 570 580 590 600
NTTKKPEPPV NLKYNAPTSH VTPSVKKRSS TLSQLPGDKS KAFDFLSEET
610 620 630 640 650
EASLASRREQ KREQYRQVKA HVQKEDGRVQ AFGWSLPQKY KQVTNGQGEN
660 670 680 690 700
KMKNLPVPVY LRPLDEKDTS MKLWCAVGVN LSGGKTRDGG SVVGASVFYK
710 720 730 740 750
DVAGLDTEGS KQRSASQSSL DKLDQELKEQ QKELKNQEEL SSLVWICTST
760 770 780 790 800
HSATKVLIID AVQPGNILDS FTVCNSHVLC IASVPGARET DYPAGEDLSE
810 820 830 840 850
SGQVDKASLC GSMTSNSSAE TDSLLGGITV VGCSAEGVTG AATSPSTNGA
860 870 880 890 900
SPVMDKPPEM EAENSEVDEN VPTAEEATEA TEGNAGSAED TVDISQTGVY
910 920 930
TEHVFTDPLG VQIPEDLSPV YQSRYNNGSS T
Length:931
Mass (Da):103,212
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1A427D7B60367814
Isoform 6 (identifier: O60271-9) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-196: MELEDGVVYQ...QLESTAHSRI → MSPGCMLLFV...ALTQNLPRIL
248-261: Missing.
1175-1175: T → TVILHQGRLLGLRA
10 20 30 40 50
MSPGCMLLFV FGFVGGAVVI NSAILVSLSV LLLVHFSIST GVPALTQNLP
60 70 80 90 100
RILRKERPIS LGIFPLPAGD GLLTPDAQKG GETPGSEQWK FQELSQPRSH
110 120 130 140 150
TSLKDELSDV SQGGSKATTP ASTANSDVAT IPTDTPLKEE NEGFVKVTDA
160 170 180 190 200
PNKSEISKHI EVQVAQETRN VSTGSAENEE KSEVQAIIES TPELDMDKDL
210 220 230 240 250
SGYKGSSTPT KGIENKAFDR NTESLFEELS SAGSGLIGDV DEGADLLGMG
260 270 280 290 300
REVENLILEN TQLLETKNAL NIVKNDLIAK VDELTCEKDV LQGELEAVKQ
310 320 330 340 350
AKLKLEEKNR ELEEELRKAR AEAEDARQKA KDDDDSDIPT AQRKRFTRVE
360 370 380 390 400
MARVLMERNQ YKERLMELQE AVRWTEMIRA SRENPAMQEK KRSSIWQFFS
410 420 430 440 450
RLFSSSSNTT KKPEPPVNLK YNAPTSHVTP SVKKRSSTLS QLPGDKSKAF
460 470 480 490 500
DFLSEETEAS LASRREQKRE QYRQVKAHVQ KEDGRVQAFG WSLPQKYKQV
510 520 530 540 550
TNGQGENKMK NLPVPVYLRP LDEKDTSMKL WCAVGVNLSG GKTRDGGSVV
560 570 580 590 600
GASVFYKDVA GLDTEGSKQR SASQSSLDKL DQELKEQQKE LKNQEELSSL
610 620 630 640 650
VWICTSTHSA TKVLIIDAVQ PGNILDSFTV CNSHVLCIAS VPGARETDYP
660 670 680 690 700
AGEDLSESGQ VDKASLCGSM TSNSSAETDS LLGGITVVGC SAEGVTGAAT
710 720 730 740 750
SPSTNGASPV MDKPPEMEAE NSEVDENVPT AEEATEATEG NAGSAEDTVD
760 770 780 790 800
ISQTGVYTEH VFTDPLGVQI PEDLSPVYQS SNDSDAYKDQ ISVLPNEQDL
810 820 830 840 850
VREEAQKMSS LLPTMWLGAQ NGCLYVHSSV AQWRKCLHSI KLKDSILSIV
860 870 880 890 900
HVKGIVLVAL ADGTLAIFHR GVDGQWDLSN YHLLDLGRPH HSIRCMTVVH
910 920 930 940 950
DKVWCGYRNK IYVVQPKAMK IEKSFDAHPR KESQVRQLAW VGDGVWVSIR
960 970 980 990 1000
LDSTLRLYHA HTYQHLQDVD IEPYVSKMLG TGKLGFSFVR ITALMVSCNR
1010 1020 1030 1040 1050
LWVGTGNGVI ISIPLTETVI LHQGRLLGLR ANKTSGVPGN RPGSVIRVYG
1060 1070 1080 1090 1100
DENSDKVTPG TFIPYCSMAH AQLCFHGHRD AVKFFVAVPG QVISPQSSSS
1110 1120 1130 1140 1150
GTDLTGDKAG PSAQEPGSQT PLKSMLVISG GEGYIDFRMG DEGGESELLG
1160 1170
EDLPLEPSVT KAERSHLIVW QVMYGNE
Note: No experimental confirmation available.Curated
Show »Length:1,177
Mass (Da):128,607
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i8CD074A547DCC690
<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
The sequence AAI06049 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAO66462 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA25442 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA62987 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
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 | 451 | E → G in AAO66462 (PubMed:14662895).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 | 680 | E → K in CAA62987 (PubMed:9480848).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 | 680 | E → K in AAO66462 (PubMed:14662895).Curated | 1 | ||
| Isoform 6 (identifier: O60271-9) | |||||
| <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 | 9 | F → S in BAG58134 (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_059364 | 1320 | N → S. Corresponds to variant dbSNP:rs9896965Ensembl. | 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_042253 | 1 – 196 | MELED…AHSRI → MSPGCMLLFVFGFVGGAVVI NSAILVSLSVLLLVHFSIST GVPALTQNLPRIL in isoform 6. 2 Publications <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
| 196 | |
| <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_018214 | 248 – 261 | Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 5 Publications <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
| 14 | |
| <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_018220 | 555 | F → FVPTR in isoform 2. 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
| 1 | |
| <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_018221 | 938 – 945 | SNDSDAYK → RYNNGSST in isoform 3 and isoform 5. 2 Publications <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
| 8 | |
| <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_018222 | 946 – 1321 | Missing in isoform 3 and isoform 5. 2 Publications <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
| 376 | |
| <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_042254 | 1175 | T → TVILHQGRLLGLRA in isoform 6. 2 Publications <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
| 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 | AF327452 mRNA. Translation: AAN61565.1. AY850123 mRNA. Translation: AAX47276.1. AB011088 mRNA. Translation: BAA25442.3. Different initiation. AK024068 mRNA. Translation: BAB14812.1. Sequence problems. AK295098 mRNA. Translation: BAG58134.1. AK302789 mRNA. Translation: BAG63993.1. AC005920 Genomic DNA. No translation available. AC005839 Genomic DNA. No translation available. BC007524 mRNA. Translation: AAH07524.1. Sequence problems. BC059946 mRNA. Translation: AAH59946.1. Sequence problems. BC106048 mRNA. Translation: AAI06049.1. Sequence problems. BC146755 mRNA. Translation: AAI46756.1. BC153878 mRNA. Translation: AAI53879.1. X91879 mRNA. Translation: CAA62987.1. Different initiation. AY219897 mRNA. Translation: AAO66462.1. Different initiation. AY219898 mRNA. Translation: AAO66463.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS11577.1. [O60271-4] CCDS45740.1. [O60271-1] CCDS58577.1. [O60271-9] CCDS58578.1. [O60271-2] |
Protein sequence database of the Protein Information Resource More...PIRi | JC5958. |
NCBI Reference Sequences More...RefSeqi | NP_001123999.1. NM_001130527.2. [O60271-2] NP_001124000.1. NM_001130528.2. [O60271-1] NP_001238900.1. NM_001251971.1. [O60271-9] NP_003962.3. NM_003971.5. [O60271-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.463439. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000262013; ENSP00000262013; ENSG00000008294. [O60271-1] ENST00000357122; ENSP00000349636; ENSG00000008294. [O60271-4] ENST00000505279; ENSP00000426900; ENSG00000008294. [O60271-2] ENST00000510283; ENSP00000423165; ENSG00000008294. [O60271-9] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9043. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9043. |
UCSC genome browser More...UCSCi | uc002ita.4. human. [O60271-1] |
<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
<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 | AF327452 mRNA. Translation: AAN61565.1. AY850123 mRNA. Translation: AAX47276.1. AB011088 mRNA. Translation: BAA25442.3. Different initiation. AK024068 mRNA. Translation: BAB14812.1. Sequence problems. AK295098 mRNA. Translation: BAG58134.1. AK302789 mRNA. Translation: BAG63993.1. AC005920 Genomic DNA. No translation available. AC005839 Genomic DNA. No translation available. BC007524 mRNA. Translation: AAH07524.1. Sequence problems. BC059946 mRNA. Translation: AAH59946.1. Sequence problems. BC106048 mRNA. Translation: AAI06049.1. Sequence problems. BC146755 mRNA. Translation: AAI46756.1. BC153878 mRNA. Translation: AAI53879.1. X91879 mRNA. Translation: CAA62987.1. Different initiation. AY219897 mRNA. Translation: AAO66462.1. Different initiation. AY219898 mRNA. Translation: AAO66463.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS11577.1. [O60271-4] CCDS45740.1. [O60271-1] CCDS58577.1. [O60271-9] CCDS58578.1. [O60271-2] |
Protein sequence database of the Protein Information Resource More...PIRi | JC5958. |
NCBI Reference Sequences More...RefSeqi | NP_001123999.1. NM_001130527.2. [O60271-2] NP_001124000.1. NM_001130528.2. [O60271-1] NP_001238900.1. NM_001251971.1. [O60271-9] NP_003962.3. NM_003971.5. [O60271-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.463439. |
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 |
| 2W83 | X-ray | 1.93 | C/D | 406-476 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O60271. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O60271. | |||||
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 | 114505. 93 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O60271. |
Protein interaction database and analysis system More...IntActi | O60271. 37 interactors. |
Molecular INTeraction database More...MINTi | O60271. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000262013. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O60271. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O60271. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SPAG9. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O60271. |
MaxQB - The MaxQuant DataBase More...MaxQBi | O60271. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O60271. |
PeptideAtlas More...PeptideAtlasi | O60271. |
PRoteomics IDEntifications database More...PRIDEi | O60271. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 9043. |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000262013; ENSP00000262013; ENSG00000008294. [O60271-1] ENST00000357122; ENSP00000349636; ENSG00000008294. [O60271-4] ENST00000505279; ENSP00000426900; ENSG00000008294. [O60271-2] ENST00000510283; ENSP00000423165; ENSG00000008294. [O60271-9] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9043. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9043. |
UCSC genome browser More...UCSCi | uc002ita.4. human. [O60271-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9043. |
DisGeNET More...DisGeNETi | 9043. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000008294.20. |
GeneCards: human genes, protein and diseases More...GeneCardsi | SPAG9. |
Human Gene Nomenclature Database More...HGNCi | HGNC:14524. SPAG9. |
Human Protein Atlas More...HPAi | HPA040446. HPA061458. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605430. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O60271. |
Open Targets More...OpenTargetsi | ENSG00000008294. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA37890. |
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 | KOG2077. Eukaryota. ENOG410XQ19. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00670000097546. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000290716. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG024110. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O60271. |
KEGG Orthology (KO) More...KOi | K20317. |
Identification of Orthologs from Complete Genome Data More...OMAi | RENPAMQ. |
Database of Orthologous Groups More...OrthoDBi | EOG091G016S. |
Database for complete collections of gene phylogenies More...PhylomeDBi | O60271. |
TreeFam database of animal gene trees More...TreeFami | TF313096. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-375170. CDO in myogenesis. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O60271. |
SIGNOR Signaling Network Open Resource More...SIGNORi | O60271. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SPAG9. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O60271. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SPAG9. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9043. |
CutDB - Proteolytic event database More...PMAP-CutDBi | O60271. |
Protein Ontology More...PROi | PR:O60271. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000008294. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O60271. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O60271. HS. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.130.10.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR032486. JIP_LZII. IPR019143. JNK/Rab-associated_protein-1_N. IPR034743. RH1. IPR034744. RH2. IPR015943. WD40/YVTN_repeat-like_dom_sf. IPR036322. WD40_repeat_dom_sf. |
Pfam protein domain database More...Pfami | View protein in Pfam PF16471. JIP_LZII. 1 hit. PF09744. Jnk-SapK_ap_N. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50978. SSF50978. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51776. RH1. 1 hit. PS51777. RH2. 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 | JIP4_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 | O60271Primary (citable) accession number: O60271 Secondary accession number(s): A6H8U5 , A8MSX0, B4DHH2, O60905, Q3KQU8, Q3MKM7, Q86WC7, Q86WC8, Q8IZX7, Q96II0, Q9H811 | |
| <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: | May 2, 2006 |
| Last sequence update: | May 2, 2006 | |
| Last modified: | March 28, 2018 | |
| This is version 154 of the entry and version 4 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. | |