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P40541 (SCC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Cohesin subunit SCC3
Alternative name(s):
Irregular cell behavior protein 1
Gene names
Name:IRR1
Synonyms:SCC3
Ordered Locus Names:YIL026C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1150 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 MCD1/SCC1 subunit of the 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.

Subunit structure

Interacts directly with MCD1 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes. Interacts with LIN1. Ref.4 Ref.5 Ref.6

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes remain. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Ref.4

Post-translational modification

Acetylated by ECO1. Ref.7

Miscellaneous

Present with 4090 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SCC3 family.

Contains 1 SCD (stromalin conservative) domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11501150Cohesin subunit SCC3
PRO_0000120191

Regions

Domain367 – 45791SCD
Coiled coil305 – 34945 Potential
Compositional bias44 – 485Poly-Glu
Compositional bias65 – 706Poly-Asp

Amino acid modifications

Modified residue281Phosphoserine Ref.10
Modified residue6281Phosphoserine Ref.10

Experimental info

Sequence conflict9391V → G in AAC49039. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40541 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 89688EA09485AC28

FASTA1,150133,009
        10         20         30         40         50         60 
MTAVRRSTRI RTKSQVIEED YDDEQNTSAQ HVESDKITAK TQHEEEEEQD TGESEESSSE 

        70         80         90        100        110        120 
DDYEDQDDDD YVDTATAKRK SRKRKPKSAS NTSSKRQKKK PTSAQKSAVS HAPAYHRSKK 

       130        140        150        160        170        180 
DQDQYLEIAK DFQPTELFDI LSTSEDVSIE ELLREWLETY SENRDKFLQE FINLLLNCCG 

       190        200        210        220        230        240 
SVARVEDHDV HSNESSNETI GEIQLLFQRQ KLHEFYLLIS KENKKRKNFK MGPLYQNFAE 

       250        260        270        280        290        300 
FMTKLLEVAN DLQLLYVESD EDDTQIVTGN LVLDLLTWLS SFSVCKIRCF RYISTLTLYL 

       310        320        330        340        350        360 
FQDYLTQQAV NLEKNYLAKL SKQLSLEEKK KRPNNKTLEK LESTIAETQG SKVVIDSIID 

       370        380        390        400        410        420 
NIVKLCFVHR YKDVSDLIRS ESMLHLSIWI KNYPEYFLKV TFLKYFGWLL SDNSVSVRLQ 

       430        440        450        460        470        480 
VTKILPHLII QNHNSKSTDN SAIRQVFERF KTKILEVAIR DVNLDVRIHS IQVLTEASSL 

       490        500        510        520        530        540 
GYLDDSEILI ISSLMFDEEF DPFKTSSFNK RSKFLSTVAK FLARVIKEKF DEFIKTHEDL 

       550        560        570        580        590        600 
PKEVDGLEVG PVVQVGIFIK ILNDSLIYHL KDCAEVDSRT KIRMLTQAAE FLSPYISTHL 

       610        620        630        640        650        660 
KTICNLLISD TESNELIQKL QNSANNNSDD EDVDDEELDI TPLFPIDRNS TILYLNVFHG 

       670        680        690        700        710        720 
LCAGANNPKI QTKDSVKEIV LPLFYDLLNA ASIESADILC PLLESFITFS LDDWISIGYE 

       730        740        750        760        770        780 
TELKKITDKT IKAFMDSTIG NSKVDMKYDI FAKFIHHIHH FEKKELQEKF LNQIATLKIH 

       790        800        810        820        830        840 
LKKFLQEKMD PNNSRDDYKD LTCSLYELYI NKLTILGRDY PIEVDEELLQ LFLNNFVSRI 

       850        860        870        880        890        900 
PIMFQDFDDS TAQEINFKML VLLATWNLEK WREIIEKVRD YENSISKDLR SVWKPIAAII 

       910        920        930        940        950        960 
GRLNTLVISL AATNETFENI NSLFYLKWSA CTSLMDIIVA IKIFELKLPA DATTWRYSMS 

       970        980        990       1000       1010       1020 
EQFPFYLHDN ASKVLLKIFL YLESLFAKQV DVQLERVADE DANLNDLPET GFFENIETEF 

      1030       1040       1050       1060       1070       1080 
LLFTVKLKGL MKLNILDERF ASRVALNKEK LGPLFKKIVD DTIMENPEPN KKNIQKAKSN 

      1090       1100       1110       1120       1130       1140 
QTQREKAPLQ PNSERETDHA NTENNDPDIP MTIDLEPIEE SSQNNSELAP IEEHPTVVDA 

      1150 
IDNSDEITQD 

« Hide

References

« Hide 'large scale' references
[1]"A new essential gene located on Saccharomyces cerevisiae chromosome IX."
Kurlandzka A., Rytka J., Gromadka R., Murawski M.
Yeast 11:885-890(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication."
Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.
Genes Dev. 13:320-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MCD1, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND MCD1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
[5]"Proteins interacting with Lin 1p, a putative link between chromosome segregation, mRNA splicing and DNA replication in Saccharomyces cerevisiae."
Bialkowska A., Kurlandzka A.
Yeast 19:1323-1333(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIN1.
[6]"Molecular architecture of SMC proteins and the yeast cohesin complex."
Haering C.H., Loewe J., Hochwagen A., Nasmyth K.
Mol. Cell 9:773-788(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND MCD1, STRUCTURE.
[7]"Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion."
Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H., Nasmyth K.
Curr. Biol. 12:323-328(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17918 Genomic DNA. Translation: AAC49039.1.
Z46881 Genomic DNA. Translation: CAA86966.1.
BK006942 Genomic DNA. Translation: DAA08520.1.
PIRS49956.
RefSeqNP_012238.1. NM_001179376.1.

3D structure databases

ProteinModelPortalP40541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34963. 28 interactions.
DIPDIP-5640N.
IntActP40541. 20 interactions.
MINTMINT-567741.
STRING4932.YIL026C.

Proteomic databases

MaxQBP40541.
PaxDbP40541.
PeptideAtlasP40541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL026C; YIL026C; YIL026C.
GeneID854786.
KEGGsce:YIL026C.

Organism-specific databases

CYGDYIL026c.
SGDS000001288. IRR1.

Phylogenomic databases

eggNOGCOG5537.
GeneTreeENSGT00390000014094.
HOGENOMHOG000141696.
KOK06671.
OMAKYFGWLL.
OrthoDBEOG7QRR35.

Enzyme and pathway databases

BioCycYEAST:G3O-31300-MONOMER.

Gene expression databases

GenevestigatorP40541.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR020839. SCD.
IPR013721. STAG.
[Graphical view]
PfamPF08514. STAG. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS51425. SCD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977573.

Entry information

Entry nameSCC3_YEAST
AccessionPrimary (citable) accession number: P40541
Secondary accession number(s): D6VVQ4, Q02511
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families