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Q96FF9 (CDCA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sororin
Alternative name(s):
Cell division cycle-associated protein 5
p35
Gene names
Name:CDCA5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.9 Ref.14

Subunit structure

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. Ref.5 Ref.9 Ref.14

Subcellular location

Nucleus. Chromosome. Cytoplasm. Note: Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown. Ref.5

Domain

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

Post-translational modification

Phosphorylated. Phosphorylation, as cells enter mitosis, disrupts the interaction with PDS5A and relieves the inhibition of WAPAL by CDCA5. Ref.5

Ubiquitinated by the APC/C complex in G1, leading to its degradation Probable. Ref.5

Miscellaneous

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

Sequence similarities

Belongs to the sororin family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from direct assay Ref.5. Source: UniProtKB

double-strand break repair

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mitosis

Inferred from direct assay Ref.5. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic chromosome condensation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mitotic interphase

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic metaphase plate congression

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mitotic sister chromatid cohesion

Inferred from mutant phenotype Ref.9Ref.14. Source: UniProtKB

regulation of cohesin localization to chromatin

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentchromosome

Traceable author statement. Source: Reactome

chromosome, centromeric region

Traceable author statement. Source: Reactome

cohesin complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nuclear chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionchromatin binding

Traceable author statement Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDS5AQ29RF72EBI-718805,EBI-1175454

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Sororin
PRO_0000089449

Regions

Motif88 – 903KEN box
Motif166 – 1683FGF motif

Amino acid modifications

Modified residue211Phosphoserine Ref.15
Modified residue331Phosphoserine Ref.11
Modified residue351Phosphoserine Ref.11
Modified residue751Phosphoserine Ref.7 Ref.10 Ref.15
Modified residue791Phosphoserine Ref.15
Modified residue1071Phosphoserine Ref.13
Modified residue1151Phosphothreonine Ref.11
Modified residue2091Phosphoserine Ref.11 Ref.15 Ref.16

Natural variations

Natural variant1561S → Y.
Corresponds to variant rs34020666 [ dbSNP | Ensembl ].
VAR_050777

Experimental info

Mutagenesis166 – 1683FGF → AGA: Alters interaction with PDS5A and PDS5B and the cohesin complex. Ref.14

Sequences

Sequence LengthMass (Da)Tools
Q96FF9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A4CD6768D3464040

FASTA25227,601
        10         20         30         40         50         60 
MSGRRTRSGG AAQRSGPRAP SPTKPLRRSQ RKSGSELPSI LPEIWPKTPS AAAVRKPIVL 

        70         80         90        100        110        120 
KRIVAHAVEV PAVQSPRRSP RISFFLEKEN EPPGRELTKE DLFKTHSVPA TPTSTPVPNP 

       130        140        150        160        170        180 
EAESSSKEGE LDARDLEMSK KVRRSYSRLE TLGSASTSTP GRRSCFGFEG LLGAEDLSGV 

       190        200        210        220        230        240 
SPVVCSKLTE VPRVCAKPWA PDMTLPGISP PPEKQKRKKK KMPEILKTEL DEWAAAMNAE 

       250 
FEAAEQFDLL VE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Sororin mediates sister chromatid cohesion by antagonizing wapl."
Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A., Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.
Cell 143:737-749(2010) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BG354578 mRNA. No translation available.
AK291490 mRNA. Translation: BAF84179.1.
CH471076 Genomic DNA. Translation: EAW74342.1.
BC011000 mRNA. Translation: AAH11000.1.
RefSeqNP_542399.1. NM_080668.3.
UniGeneHs.434886.

3D structure databases

ProteinModelPortalQ96FF9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125225. 19 interactions.
DIPDIP-47377N.
IntActQ96FF9. 10 interactions.
MINTMINT-1416799.
STRING9606.ENSP00000275517.

PTM databases

PhosphoSiteQ96FF9.

Polymorphism databases

DMDM68565257.

Proteomic databases

PaxDbQ96FF9.
PeptideAtlasQ96FF9.
PRIDEQ96FF9.

Protocols and materials databases

DNASU113130.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275517; ENSP00000275517; ENSG00000146670.
GeneID113130.
KEGGhsa:113130.
UCSCuc001ocp.2. human.

Organism-specific databases

CTD113130.
GeneCardsGC11M064833.
H-InvDBHIX0009780.
HGNCHGNC:14626. CDCA5.
HPAHPA023691.
MIM609374. gene.
neXtProtNX_Q96FF9.
PharmGKBPA26278.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43755.
HOGENOMHOG000232187.
HOVERGENHBG080614.
KOK17390.
PhylomeDBQ96FF9.
TreeFamTF101070.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ96FF9.
BgeeQ96FF9.
CleanExHS_CDCA5.
GenevestigatorQ96FF9.

Family and domain databases

InterProIPR018605. Sororin.
[Graphical view]
PfamPF09666. Sororin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDCA5. human.
GeneWikiCDCA5.
GenomeRNAi113130.
NextBio78748.
PROQ96FF9.
SOURCESearch...

Entry information

Entry nameCDCA5_HUMAN
AccessionPrimary (citable) accession number: Q96FF9
Secondary accession number(s): A8K625
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM