UniProt functional annotation for Q04002



	UniProt functional annotation for Q04002

UniProt code: Q04002.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Plays a structural role in chromatin and is involved in sister chromatid cohesion (PubMed:9990856, PubMed:14614819, PubMed:25173104, PubMed:26354421). Forms a complex with SCC4 required for the stable association of the cohesin complex with chromatin, which may act by hydrolyzing ATP from SMC1 and SMC3 heads (PubMed:10882066, PubMed:14614819). Binds to the nucleosome-free promoter regions of ribosomal protein genes and tRNA genes. Involved in transcriptional regulation by cooperating with the RSC complex to maintain nucleosome exhaustion at its binding sites (PubMed:25173104). {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:14614819, ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26354421, ECO:0000269|PubMed:9990856}.

Subunit: Interacts with SCC4 (PubMed:9990856, PubMed:10882066, PubMed:26038942). Interacts with the cohesin complex, which is composed of: the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1 (PubMed:9990856). {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:26038942, ECO:0000269|PubMed:9990856}.

Subcellular location: Nucleus {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26038942}. Chromosome, centromere {ECO:0000269|PubMed:26038942}. Note=Associates with chromatin. {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26038942}.

Domain: The N-terminus (residues 1-181) is sufficient for the interaction with SCC4 (PubMed:26038942). {ECO:0000269|PubMed:26038942}.

Ptm: Phosphorylated at alternative sites Ser-43, Ser-74, Ser-162, Thr- 360, Ser-1179 and Ser-1183 when the principal phosphorylation sites Thr-67, Ser-127, Ser-157, Ser-163, Thr-231, Thr-236, Ser-305 and Ser- 320 are mutated to alanines. {ECO:0000269|PubMed:26354421}.

Miscellaneous: Present with 3310 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Plays a structural role in chromatin and is involved in sister chromatid cohesion (PubMed:9990856, PubMed:14614819, PubMed:25173104, PubMed:26354421). Forms a complex with SCC4 required for the stable association of the cohesin complex with chromatin, which may act by hydrolyzing ATP from SMC1 and SMC3 heads (PubMed:10882066, PubMed:14614819). Binds to the nucleosome-free promoter regions of ribosomal protein genes and tRNA genes. Involved in transcriptional regulation by cooperating with the RSC complex to maintain nucleosome exhaustion at its binding sites (PubMed:25173104). {ECO:0000269\|PubMed:10882066, ECO:0000269\|PubMed:14614819, ECO:0000269\|PubMed:25173104, ECO:0000269\|PubMed:26354421, ECO:0000269\|PubMed:9990856}.


Subunit:		Interacts with SCC4 (PubMed:9990856, PubMed:10882066, PubMed:26038942). Interacts with the cohesin complex, which is composed of: the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1 (PubMed:9990856). {ECO:0000269\|PubMed:10882066, ECO:0000269\|PubMed:26038942, ECO:0000269\|PubMed:9990856}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:10882066, ECO:0000269\|PubMed:25173104, ECO:0000269\|PubMed:26038942}. Chromosome, centromere {ECO:0000269\|PubMed:26038942}. Note=Associates with chromatin. {ECO:0000269\|PubMed:10882066, ECO:0000269\|PubMed:25173104, ECO:0000269\|PubMed:26038942}.
Domain:		The N-terminus (residues 1-181) is sufficient for the interaction with SCC4 (PubMed:26038942). {ECO:0000269\|PubMed:26038942}.
Ptm:		Phosphorylated at alternative sites Ser-43, Ser-74, Ser-162, Thr- 360, Ser-1179 and Ser-1183 when the principal phosphorylation sites Thr-67, Ser-127, Ser-157, Ser-163, Thr-231, Thr-236, Ser-305 and Ser- 320 are mutated to alanines. {ECO:0000269\|PubMed:26354421}.
Miscellaneous:		Present with 3310 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the SCC2/Nipped-B family. {ECO:0000305}.