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Q9CPY3 (CDCA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Gene names
Name:Cdca5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length264 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.3

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.3

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.3

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 By similarity.

Ubiquitinated by the APC/C complex in G1, leading to its degradation By similarity.

Sequence similarities

Belongs to the sororin family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CPY3-1)

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.
Isoform 2 (identifier: Q9CPY3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Sororin
PRO_0000089450

Regions

Motif87 – 893KEN box
Motif166 – 1683FGF motif

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue321Phosphoserine By similarity
Modified residue341Phosphoserine By similarity
Modified residue781Phosphoserine By similarity
Modified residue1061Phosphoserine By similarity
Modified residue1141Phosphothreonine By similarity
Modified residue2221Phosphoserine By similarity

Natural variations

Alternative sequence1 – 137137Missing in isoform 2.
VSP_014402

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E8543BBE3593B212

FASTA26428,991
        10         20         30         40         50         60 
MAERRTRSGG AAQRSGPRTS LTKPSKSSKR KSGSDLPNSF SEIWPRTTPA VPVRKAIVLK 

        70         80         90        100        110        120 
KIVAHAVEVP DVHTVRRSPR ISFILEKENN PPLKVPTKED LFKTCSVPGT PSSTPVLYTQ 

       130        140        150        160        170        180 
NVEPDSGEAE LDSRDLEMSQ KVRRSYSRLQ SLGCASTSTP GRRSFFGFEG PDDLPGVSPV 

       190        200        210        220        230        240 
VCSKLIETPK VPAKDLVPAR TKDLVPDSTK DLVPARTLPG ISPPVVKEKR KKKVPEILKS 

       250        260 
ELDKWAVAMN AEFEAAEQFE LLIE 

« Hide

Isoform 2 [UniParc].

Checksum: E3BF12AAE025C1C8
Show »

FASTA12713,979

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
[2]"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] (ISOFORMS 1 AND 2).
Strain: C57BL/6NCr.
Tissue: Hematopoietic stem cell.
[3]"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, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010540 mRNA. Translation: BAB27016.1.
AK011701 mRNA. Translation: BAB27788.1.
BC029626 mRNA. Translation: AAH29626.1.
BC052904 mRNA. Translation: AAH52904.1.
RefSeqNP_080686.1. NM_026410.3.
UniGeneMm.23526.

3D structure databases

ProteinModelPortalQ9CPY3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212479. 9 interactions.
IntActQ9CPY3. 8 interactions.

PTM databases

PhosphoSiteQ9CPY3.

Proteomic databases

PRIDEQ9CPY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025704; ENSMUSP00000025704; ENSMUSG00000024791. [Q9CPY3-1]
GeneID67849.
KEGGmmu:67849.
UCSCuc008ghh.1. mouse. [Q9CPY3-1]
uc008ghi.1. mouse. [Q9CPY3-2]

Organism-specific databases

CTD113130.
MGIMGI:1915099. Cdca5.

Phylogenomic databases

eggNOGNOG43755.
GeneTreeENSGT00390000010028.
HOGENOMHOG000232187.
HOVERGENHBG080614.
InParanoidQ9CPY3.
KOK17390.
OMALEMSQKV.
OrthoDBEOG7N8ZVV.
PhylomeDBQ9CPY3.
TreeFamTF101070.

Gene expression databases

BgeeQ9CPY3.
CleanExMM_CDCA5.
GenevestigatorQ9CPY3.

Family and domain databases

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

Other

NextBio325711.
PROQ9CPY3.
SOURCESearch...

Entry information

Entry nameCDCA5_MOUSE
AccessionPrimary (citable) accession number: Q9CPY3
Secondary accession number(s): Q78HI6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot