Protein INCA1

<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>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

• cyclin binding 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.6

    "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1 (INCA1) regulates proliferation and is repressed by oncogenic signaling."
    Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S., Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G., Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.
    J. Biol. Chem. 286:28210-28222(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CCNA1; CCNA2; CCNB1 AND CCNE1, INTERACTION WITH THE CCNA1/CDK2 COMPLEX, INDUCTION.
• cyclin-dependent protein serine/threonine kinase inhibitor activity Source: MGIInferred from direct assayⁱ
  • Ref.6

    "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1 (INCA1) regulates proliferation and is repressed by oncogenic signaling."
    Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S., Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G., Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.
    J. Biol. Chem. 286:28210-28222(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CCNA1; CCNA2; CCNB1 AND CCNE1, INTERACTION WITH THE CCNA1/CDK2 COMPLEX, INDUCTION.
• 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
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Identification of interaction partners and substrates of the cyclin A1-CDK2 complex."
    Diederichs S., Baeumer N., Ji P., Metzelder S.K., Idos G.E., Cauvet T., Wang W., Moeller M., Pierschalski S., Gromoll J., Schrader M.G., Koeffler H.P., Berdel W.E., Serve H., Mueller-Tidow C.
    J. Biol. Chem. 279:33727-33741(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CCNA1, IDENTIFICATION IN A COMPLEX WITH CCNA1 AND CDK2, PHOSPHORYLATION AT SER-23; THR-182; SER-191 AND SER-194, MUTAGENESIS OF SER-23; THR-182; SER-191 AND SER-194, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

GO - Biological processⁱ

• negative regulation of cell population proliferation Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: MGIInferred from direct assayⁱ
  • Ref.6

    "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1 (INCA1) regulates proliferation and is repressed by oncogenic signaling."
    Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S., Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G., Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.
    J. Biol. Chem. 286:28210-28222(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CCNA1; CCNA2; CCNB1 AND CCNE1, INTERACTION WITH THE CCNA1/CDK2 COMPLEX, INDUCTION.
• positive regulation of apoptotic signaling pathway 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

• UniProt annotation
• GO - Cellular component

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

Amino acid modifications

<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

<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

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

• cyclin binding Source: MGIInferred from direct assayⁱ
  • Ref.6

    "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1 (INCA1) regulates proliferation and is repressed by oncogenic signaling."
    Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S., Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G., Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.
    J. Biol. Chem. 286:28210-28222(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CCNA1; CCNA2; CCNB1 AND CCNE1, INTERACTION WITH THE CCNA1/CDK2 COMPLEX, INDUCTION.
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous 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

Region

Motif

<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

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>Sequences (2)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.

        10         20         30         40         50
MQVQDDGVNL IPFAKCSRVV SRSPPPRLPS QSLRPMPQRY GDVFWKNLNQ 
        60         70         80         90        100
RPTPTWLEEQ HIPPMLRATG CSQLGLYPPE QLPPPEMLWR RKKRRPCLEG 
       110        120        130        140        150
MQQQGLGGVP ARVRAVTYHL EDLRRRQSII NELKKAQWGS SGAASEPVVL 
       160        170        180        190        200
GEEGCGFPST NEYPDLEEER ATYPQEEDRF LTPGRAQLLW SPWSPLDQEE 
       210        220        230 
ACASRQLHSL ASFSTVTARR NPLHNPWGME LAASEE                

        10         20         30         40         50
MQVQDDGVNL IPFAKCSRVV SRSPPPRLPS QSLRPMPQRY GDVFWKNLNQ 
        60         70         80         90        100
RPTPTWLEEQ HIPPMLLPPP EMLWRRKKRR PCLEGMQQQG LGGVPARVRA 
       110        120        130        140        150
VTYHLEDLRR RQSIINELKK AQWGSSGAAS EPVVLGEEGC GFPSTNEYPD 
       160        170        180        190        200
LEEERATYPQ EEDRFLTPGR AQLLWSPWSP LDQEEACASR QLHSLASFST 
       210        220 
VTARRNPLHN PWGMELAASE E                                

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

• 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 17
   Human chromosome 17: 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. SIMILARITY comments
   Index of protein domains and families