Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cohesin subunit psc3

Gene

psc3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the rad21 subunit of the cohesin complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.1 Publication

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic sister chromatid cohesion Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis

Enzyme and pathway databases

ReactomeiR-SPO-2500257. Resolution of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
Recommended name:
Cohesin subunit psc3
Alternative name(s):
SCC3 homolog
Gene namesi
Name:psc3
ORF Names:SPAC17H9.20, SPAC607.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17H9.20.
PomBaseiSPAC17H9.20. psc3.

Subcellular locationi

GO - Cellular componenti

  • condensed nuclear chromosome Source: PomBase
  • mating-type region heterochromatin Source: PomBase
  • nuclear mitotic cohesin complex Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
  • nuclear subtelomeric heterochromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 962962Cohesin subunit psc3PRO_0000120192Add
BLAST

Proteomic databases

MaxQBiO13816.

Interactioni

Subunit structurei

Cohesin complexes are composed of the psm1/smc1 and psm3/smc3 heterodimer attached via their hinge domain, rad21/scc1 which link them, and psc3/scc3, which interacts with rad21. Interacts with swi6 (By similarity). The interaction with swi6 may contribute to recruit cohesin complex to heterochromatin.By similarity1 Publication

Protein-protein interaction databases

BioGridi278851. 5 interactions.
DIPiDIP-37866N.
IntActiO13816. 2 interactions.
MINTiMINT-4668174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini297 – 38286SCDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili236 – 27540Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 388Poly-Ser

Sequence similaritiesi

Belongs to the SCC3 family.Curated
Contains 1 SCD (stromalin conservative) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiO13816.
KOiK06671.
OMAiARIRSEC.
OrthoDBiEOG7QRR35.
PhylomeDBiO13816.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR020839. SCD.
IPR013721. STAG.
[Graphical view]
PfamiPF08514. STAG. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
PROSITEiPS51425. SCD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESVTTGSD DDGGDRESSP VMLSQSFDPM SSSSNSSSEE NSDDDYEKTI
60 70 80 90 100
SSKKRHPRPN SKGVNVKRSR RNAIVEEDPQ EEIFNNLFAF LLDQKVDTMD
110 120 130 140 150
IAVSWFADYA KDNQSALANL INFILKCCGC NRAINVFDVQ DQDSASATLS
160 170 180 190 200
QIQLSVERTS TRDYPLNSKN LKFRNFRKRL TGLLSNFVSQ LSIRNYLYNS
210 220 230 240 250
TVFEDIMSWV VAMSSSTMRP IRHTATVFCL NIMTFLCEKS KELLNEHAIA
260 270 280 290 300
TKQLEKEEKR SRVNRNRINE LNNSLGEIVK QQDTLTTYLN DYFDSVFVHR
310 320 330 340 350
YRDVEPKIRV DCLQELGVWI NTVPSIFFSG SYLRYLGWML SDINTTVRLT
360 370 380 390 400
VVKVLRKFFE TDSFIGGLRH FSSRFKERIL EMSCVDADIG VRVASIRLCN
410 420 430 440 450
AMRTCGFLEN SEILKVLKLI LDINPRVQRE AVLFLCKVVD ESVNEKIDLW
460 470 480 490 500
GEEDYILKAF SQTSLTTFSV HWIKFSQMCK LLEEVRLSYQ SSFDYDTLLR
510 520 530 540 550
IFQKNGNFIT PITQALLNAC EIDSIYQSWE DISNFVLFDN YTSTLKDPID
560 570 580 590 600
SILSFCKLND FQESILLQLL SASIQTVCNN NFITPKTVHN KQAAETTNDQ
610 620 630 640 650
NKDKDLLYLN LLPYINSITE RNSASPTLLH DSLRLLFSMD LTEMTDPQLS
660 670 680 690 700
RHFELLINNL KKFFLTNNDL QIIQGCTILF LRLDSIPALK EDLKLLVTDI
710 720 730 740 750
CDQTVTEFLK NFGSFNIQDA VITKDEFVIF EACLTRIEGC TSLKDFSDYP
760 770 780 790 800
EFDIIYERLV SLLSRVPNSY EDTLKFSAIN TLQSLLFWFF LRKDNPADEE
810 820 830 840 850
KKKDDETKVF NCLINIMNND SSKILQLQAA RTFLETVIMK EGVKASHYND
860 870 880 890 900
DNRVSEEHNF LKPQFLDALL KILEGWLYTY AKVGQFPFKR LTQASSPHTQ
910 920 930 940 950
ISLDKNPLNR RLLEHVCCDL TSKLLIVVSL SNTITPEFSQ QFCELRGHYG
960
PKLSAIVDEF LN
Length:962
Mass (Da):110,652
Last modified:May 16, 2006 - v3
Checksum:iF45C2C2A2E0443CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAJ41421.1.
PIRiT37885. T50221.
RefSeqiXP_001713063.1. XM_001713011.2.

Genome annotation databases

EnsemblFungiiSPAC17H9.20.1; SPAC17H9.20.1:pep; SPAC17H9.20.
GeneIDi2542387.
KEGGispo:SPAC17H9.20.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAJ41421.1.
PIRiT37885. T50221.
RefSeqiXP_001713063.1. XM_001713011.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278851. 5 interactions.
DIPiDIP-37866N.
IntActiO13816. 2 interactions.
MINTiMINT-4668174.

Proteomic databases

MaxQBiO13816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17H9.20.1; SPAC17H9.20.1:pep; SPAC17H9.20.
GeneIDi2542387.
KEGGispo:SPAC17H9.20.

Organism-specific databases

EuPathDBiFungiDB:SPAC17H9.20.
PomBaseiSPAC17H9.20. psc3.

Phylogenomic databases

InParanoidiO13816.
KOiK06671.
OMAiARIRSEC.
OrthoDBiEOG7QRR35.
PhylomeDBiO13816.

Enzyme and pathway databases

ReactomeiR-SPO-2500257. Resolution of Sister Chromatid Cohesion.

Miscellaneous databases

NextBioi20803446.
PROiO13816.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR020839. SCD.
IPR013721. STAG.
[Graphical view]
PfamiPF08514. STAG. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
PROSITEiPS51425. SCD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of fission yeast cohesin: essential anaphase proteolysis of Rad21 phosphorylated in the S phase."
    Tomonaga T., Nagao K., Kawasaki Y., Furuya K., Murakami A., Morishita J., Yuasa T., Sutani T., Kearsey S.E., Uhlmann F., Nasmyth K., Yanagida M.
    Genes Dev. 14:2757-2770(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Skelton J., Churcher C.M., Barrell B.G., Rajandream M.A., Wood V.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast."
    Nonaka N., Kitajima T., Yokobayashi S., Xiao G., Yamamoto M., Grewal S.I.S., Watanabe Y.
    Nat. Cell Biol. 4:89-93(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SWI6.
  5. "Psc3 cohesin of Schizosaccharomyces pombe: cell cycle analysis and identification of three distinct isoforms."
    Ilyushik E., Pryce D.W., Walerych D., Riddell T., Wakeman J.A., McInerny C.J., McFarlane R.J.
    Biol. Chem. 386:613-621(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF INTRON.

Entry informationi

Entry nameiSCC3_SCHPO
AccessioniPrimary (citable) accession number: O13816
Secondary accession number(s): Q38G50, Q9US16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 16, 2006
Last modified: November 11, 2015
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.