E3 ubiquitin-protein ligase CCNB1IP1

<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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.1

    "A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
    Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
    Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-28; HIS-30 AND CYS-33, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND CCNB1, UBIQUITINATION, PHOSPHORYLATION, TISSUE SPECIFICITY.

  EC:2.3.2.27

Regions

<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

• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Towards a proteome-scale map of the human protein-protein interaction network."
    Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N., Berriz G.F., Gibbons F.D., Dreze M., Ayivi-Guedehoussou N., Klitgord N., Simon C., Boxem M., Milstein S., Rosenberg J., Goldberg D.S., Zhang L.V., Wong S.L.

    , Franklin G., Li S., Albala J.S., Lim J., Fraughton C., Llamosas E., Cevik S., Bex C., Lamesch P., Sikorski R.S., Vandenhaute J., Zoghbi H.Y., Smolyar A., Bosak S., Sequerra R., Doucette-Stamm L., Cusick M.E., Hill D.E., Roth F.P., Vidal M.
    Nature 437:1173-1178(2005) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
  • "Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations."
    Fragoza R., Das J., Wierbowski S.D., Liang J., Tran T.N., Liang S., Beltran J.F., Rivera-Erick C.A., Ye K., Wang T.Y., Yao L., Mort M., Stenson P.D., Cooper D.N., Wei X., Keinan A., Schimenti J.C., Clark A.G., Yu H.
    Nat Commun 10:4141-4141(2019) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• ubiquitin protein ligase activity Source: InterPro

GO - Biological processⁱ

• blastocyst formation Source: Ensembl
• chiasma assembly Source: UniProtKB
• reciprocal meiotic recombination Source: UniProtKB
• spermatid development Source: Ensembl

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Towards a proteome-scale map of the human protein-protein interaction network."
    Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N., Berriz G.F., Gibbons F.D., Dreze M., Ayivi-Guedehoussou N., Klitgord N., Simon C., Boxem M., Milstein S., Rosenberg J., Goldberg D.S., Zhang L.V., Wong S.L.

    , Franklin G., Li S., Albala J.S., Lim J., Fraughton C., Llamosas E., Cevik S., Bex C., Lamesch P., Sikorski R.S., Vandenhaute J., Zoghbi H.Y., Smolyar A., Bosak S., Sequerra R., Doucette-Stamm L., Cusick M.E., Hill D.E., Roth F.P., Vidal M.
    Nature 437:1173-1178(2005) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
  • "Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations."
    Fragoza R., Das J., Wierbowski S.D., Liang J., Tran T.N., Liang S., Beltran J.F., Rivera-Erick C.A., Ye K., Wang T.Y., Yao L., Mort M., Stenson P.D., Cooper D.N., Wei X., Keinan A., Schimenti J.C., Clark A.G., Yu H.
    Nat Commun 10:4141-4141(2019) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

<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

Coiled coil

Zinc finger

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSLCEDMLLC NYRKCRIKLS GYAWVTACSH IFCDQHGSGE FSRSPAICPA 
        60         70         80         90        100
CNSTLSGKLD IVRTELSPSE EYKAMVLAGL RPEIVLDISS RALAFWTYQV 
       110        120        130        140        150
HQERLYQEYN FSKAEGHLKQ MEKIYTQQIQ SKDVELTSMK GEVTSMKKVL 
       160        170        180        190        200
EEYKKKFSDI SEKLMERNRQ YQKLQGLYDS LRLRNITIAN HEGTLEPSMI 
       210        220        230        240        250
AQSGVLGFPL GNNSKFPLDN TPVRNRGDGD GDFQFRPFFA GSPTAPEPSN 
       260        270 
SFFSFVSPSR ELEQQQVSSR AFKVKRI                          

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

1. Human chromosome 14
   Human chromosome 14: entries, gene names and cross-references to MIM
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PATHWAY comments
   Index of metabolic and biosynthesis pathways