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Q96FF9

- CDCA5_HUMAN

UniProt

Q96FF9 - CDCA5_HUMAN

Protein

Sororin

Gene

CDCA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPAL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. double-strand break repair Source: UniProtKB
    2. G1/S transition of mitotic cell cycle Source: UniProtKB
    3. mitotic cell cycle Source: Reactome
    4. mitotic chromosome condensation Source: UniProtKB
    5. mitotic interphase Source: UniProtKB
    6. mitotic metaphase plate congression Source: UniProtKB
    7. mitotic nuclear division Source: UniProtKB
    8. mitotic sister chromatid cohesion Source: UniProtKB
    9. regulation of cohesin localization to chromatin Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sororin
    Alternative name(s):
    Cell division cycle-associated protein 5
    p35
    Gene namesi
    Name:CDCA5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14626. CDCA5.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication. Cytoplasm 1 Publication
    Note: Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown.

    GO - Cellular componenti

    1. chromosome Source: Reactome
    2. chromosome, centromeric region Source: Reactome
    3. cohesin complex Source: Ensembl
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: Reactome
    6. nuclear chromatin Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi166 – 1683FGF → AGA: Alters interaction with PDS5A and PDS5B and the cohesin complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA26278.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252SororinPRO_0000089449Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine2 Publications
    Modified residuei33 – 331Phosphoserine2 Publications
    Modified residuei35 – 351Phosphoserine2 Publications
    Modified residuei75 – 751Phosphoserine4 Publications
    Modified residuei79 – 791Phosphoserine2 Publications
    Modified residuei107 – 1071Phosphoserine2 Publications
    Modified residuei115 – 1151Phosphothreonine2 Publications
    Modified residuei209 – 2091Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation, as cells enter mitosis, disrupts the interaction with PDS5A and relieves the inhibition of WAPAL by CDCA5.7 Publications
    Ubiquitinated by the APC/C complex in G1, leading to its degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96FF9.
    PaxDbiQ96FF9.
    PeptideAtlasiQ96FF9.
    PRIDEiQ96FF9.

    PTM databases

    PhosphoSiteiQ96FF9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96FF9.
    BgeeiQ96FF9.
    CleanExiHS_CDCA5.
    GenevestigatoriQ96FF9.

    Organism-specific databases

    HPAiHPA023691.

    Interactioni

    Subunit structurei

    Interacts with the APC/C complex By similarity. Interacts with the chromatin-bound cohesin complex; the interaction is indirect, occurs after DNA replication and requires acetylation of the cohesin component SMC3. Interacts (via the FGF motif) with PDS5A and PDS5B; the interaction is direct and prevents the interaction of PDS5A with WAPAL.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDS5AQ29RF72EBI-718805,EBI-1175454

    Protein-protein interaction databases

    BioGridi125225. 19 interactions.
    DIPiDIP-47377N.
    IntActiQ96FF9. 10 interactions.
    MINTiMINT-1416799.
    STRINGi9606.ENSP00000275517.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96FF9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi88 – 903KEN box
    Motifi166 – 1683FGF motif

    Domaini

    The KEN box is required for the association with the APC/C complex.By similarity

    Sequence similaritiesi

    Belongs to the sororin family.Curated

    Phylogenomic databases

    eggNOGiNOG43755.
    HOGENOMiHOG000232187.
    HOVERGENiHBG080614.
    KOiK17390.
    PhylomeDBiQ96FF9.
    TreeFamiTF101070.

    Family and domain databases

    InterProiIPR018605. Sororin.
    [Graphical view]
    PfamiPF09666. Sororin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96FF9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRRTRSGG AAQRSGPRAP SPTKPLRRSQ RKSGSELPSI LPEIWPKTPS    50
    AAAVRKPIVL KRIVAHAVEV PAVQSPRRSP RISFFLEKEN EPPGRELTKE 100
    DLFKTHSVPA TPTSTPVPNP EAESSSKEGE LDARDLEMSK KVRRSYSRLE 150
    TLGSASTSTP GRRSCFGFEG LLGAEDLSGV SPVVCSKLTE VPRVCAKPWA 200
    PDMTLPGISP PPEKQKRKKK KMPEILKTEL DEWAAAMNAE FEAAEQFDLL 250
    VE 252
    Length:252
    Mass (Da):27,601
    Last modified:December 1, 2001 - v1
    Checksum:iA4CD6768D3464040
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti156 – 1561S → Y.
    Corresponds to variant rs34020666 [ dbSNP | Ensembl ].
    VAR_050777

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BG354578 mRNA. No translation available.
    AK291490 mRNA. Translation: BAF84179.1.
    CH471076 Genomic DNA. Translation: EAW74342.1.
    BC011000 mRNA. Translation: AAH11000.1.
    CCDSiCCDS8091.1.
    RefSeqiNP_542399.1. NM_080668.3.
    UniGeneiHs.434886.

    Genome annotation databases

    EnsembliENST00000275517; ENSP00000275517; ENSG00000146670.
    GeneIDi113130.
    KEGGihsa:113130.
    UCSCiuc001ocp.2. human.

    Polymorphism databases

    DMDMi68565257.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BG354578 mRNA. No translation available.
    AK291490 mRNA. Translation: BAF84179.1 .
    CH471076 Genomic DNA. Translation: EAW74342.1 .
    BC011000 mRNA. Translation: AAH11000.1 .
    CCDSi CCDS8091.1.
    RefSeqi NP_542399.1. NM_080668.3.
    UniGenei Hs.434886.

    3D structure databases

    ProteinModelPortali Q96FF9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125225. 19 interactions.
    DIPi DIP-47377N.
    IntActi Q96FF9. 10 interactions.
    MINTi MINT-1416799.
    STRINGi 9606.ENSP00000275517.

    PTM databases

    PhosphoSitei Q96FF9.

    Polymorphism databases

    DMDMi 68565257.

    Proteomic databases

    MaxQBi Q96FF9.
    PaxDbi Q96FF9.
    PeptideAtlasi Q96FF9.
    PRIDEi Q96FF9.

    Protocols and materials databases

    DNASUi 113130.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000275517 ; ENSP00000275517 ; ENSG00000146670 .
    GeneIDi 113130.
    KEGGi hsa:113130.
    UCSCi uc001ocp.2. human.

    Organism-specific databases

    CTDi 113130.
    GeneCardsi GC11M064833.
    H-InvDB HIX0009780.
    HGNCi HGNC:14626. CDCA5.
    HPAi HPA023691.
    MIMi 609374. gene.
    neXtProti NX_Q96FF9.
    PharmGKBi PA26278.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43755.
    HOGENOMi HOG000232187.
    HOVERGENi HBG080614.
    KOi K17390.
    PhylomeDBi Q96FF9.
    TreeFami TF101070.

    Enzyme and pathway databases

    Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.

    Miscellaneous databases

    ChiTaRSi CDCA5. human.
    GeneWikii CDCA5.
    GenomeRNAii 113130.
    NextBioi 78748.
    PROi Q96FF9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96FF9.
    Bgeei Q96FF9.
    CleanExi HS_CDCA5.
    Genevestigatori Q96FF9.

    Family and domain databases

    InterProi IPR018605. Sororin.
    [Graphical view ]
    Pfami PF09666. Sororin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Drug target discovery by gene expression analysis: cell cycle genes."
      Walker M.G.
      Curr. Cancer Drug Targets 1:73-83(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ovary.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    5. "Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates."
      Rankin S., Ayad N.G., Kirschner M.W.
      Mol. Cell 18:185-200(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, IDENTIFICATION IN A COMPLEX WITH SMC1A; SMC3; RAD21; PDS5A AND PDS5B.
    6. Erratum
      Rankin S., Ayad N.G., Kirschner M.W.
      Mol. Cell 18:609-609(2005)
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Sororin is required for stable binding of cohesin to chromatin and for sister chromatid cohesion in interphase."
      Schmitz J., Watrin E., Lenart P., Mechtler K., Peters J.M.
      Curr. Biol. 17:630-636(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE COHESIN COMPLEX.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-35; THR-115 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: FUNCTION, INTERACTION WITH PDS5A AND PDS5B, MUTAGENESIS OF 166-PHE--PHE-168, FGF MOTIF.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-75; SER-79 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCDCA5_HUMAN
    AccessioniPrimary (citable) accession number: Q96FF9
    Secondary accession number(s): A8K625
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Miscellaneous

    Named sororin after the Latin word 'soror', which means 'sister', because of its critical role in sister chromatid cohesion.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3