UniProtKB - Q04002 (SCC2_YEAST)
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Protein
Sister chromatid cohesion protein 2
Gene
SCC2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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).5 Publications
Miscellaneous
Present with 3310 molecules/cell in log phase SD medium.1 Publication
GO - Molecular functioni
- chromatin binding Source: InterPro
- sequence-specific DNA binding Source: UniProtKB
GO - Biological processi
- 2-micrometer plasmid partitioning Source: SGD
- double-strand break repair Source: SGD
- establishment of mitotic sister chromatid cohesion Source: SGD
- establishment of protein localization to chromatin Source: SGD
- mitotic chromosome condensation Source: SGD
- mitotic sister chromatid cohesion Source: UniProtKB
- protein localization to chromatin Source: SGD
- rDNA condensation Source: SGD
- regulation of gene expression Source: UniProtKB
- regulation of transcription, DNA-templated Source: UniProtKB-KW
- replication-born double-strand break repair via sister chromatid exchange Source: SGD
- transcription, DNA-templated Source: UniProtKB-KW
- transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
- tRNA gene clustering Source: SGD
Keywordsi
Biological process | Cell cycle, Transcription, Transcription regulation |
Enzyme and pathway databases
BioCyci | YEAST:G3O-29769-MONOMER. |
Names & Taxonomyi
Protein namesi | Recommended name: Sister chromatid cohesion protein 2 |
Gene namesi | Name:SCC2 Ordered Locus Names:YDR180W ORF Names:YD9395.14 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YDR180W. |
SGDi | S000002588. SCC2. |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 67 | T → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated with A-127; A-157; A-163; A-231; A-236; A-305 and A-320. 1 Publication | 1 | |
Mutagenesisi | 67 | T → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-127; E-157; E-163; E-231; E-236; E-305 and E-320. 1 Publication | 1 | |
Mutagenesisi | 127 | S → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated with A-67; A-157; A-163; A-231; A-236; A-305 and A-320. 1 Publication | 1 | |
Mutagenesisi | 127 | S → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-157; E-163; E-231; E-236; E-305 and E-320. 1 Publication | 1 | |
Mutagenesisi | 157 | S → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated with A-67; A-127; A-163; A-231; A-236; A-305 and A-320. 1 Publication | 1 | |
Mutagenesisi | 157 | S → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-127; E-163; E-231; E-236; E-305 and E-320. 1 Publication | 1 | |
Mutagenesisi | 163 | S → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated with A-67; A-127; A-157; A-231; A-236; A-305 and A-320. 1 Publication | 1 | |
Mutagenesisi | 163 | S → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-127; E-157; E-231; E-236; E-305 and E-320. 1 Publication | 1 | |
Mutagenesisi | 231 | T → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated with A-67; A-127; A-157; A-163; A-236; A-305 and A-320. 1 Publication | 1 | |
Mutagenesisi | 231 | T → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-127; E-157; E-163; E-236; E-305 and E-320. In scc2-2NE; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-236; E-305 and E-320. 1 Publication | 1 | |
Mutagenesisi | 236 | T → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated with A-67; A-127; A-157; A-163; A-231; A-305 and A-320. 1 Publication | 1 | |
Mutagenesisi | 236 | T → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-127; E-157; E-163; E-231; E-305 and E-320. In scc2-2NE; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-231; E-305 and E-320. 1 Publication | 1 | |
Mutagenesisi | 305 | S → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43; S-74; S-162; S-360; S-1179 and Ser-1183; when associated with A-67; A-127; A-157; A-163; A-231; A-236 and A-320. 1 Publication | 1 | |
Mutagenesisi | 305 | S → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-127; E-157; E-163; E-231; E-236 and E-320. In scc2-2NE; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-231; E-236 and E-320. 1 Publication | 1 | |
Mutagenesisi | 320 | S → A in scc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at S-43; S-74; S-162; S-360; S-1179 and S-1183; when associated with A-67; A-127; A-157; A-163; A-231; A-236 and A-305. 1 Publication | 1 | |
Mutagenesisi | 320 | S → E in scc2-8E; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-67; E-127; E-157; E-163; E-231; E-236 and E-305. In scc2-2NE; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU), and decreased stability of the MCD1 cohesin subunit in mitotic cells; when associated with E-231; E-236 and E-305. 1 Publication | 1 | |
Mutagenesisi | 753 | S → E: Mimics constitutive phosphorylation and causes inviability through protein instability. 1 Publication | 1 | |
Mutagenesisi | 1182 | S → E in scc2-CE; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU); when associated with E-1185. 1 Publication | 1 | |
Mutagenesisi | 1185 | S → E in scc2-CE; mimics constitutive phosphorylation, retains normal SCC2-SCC4 interactions and chromatin association, but exhibits decreased viability, sensitivity to genotoxic agents methyl methanesulfonate (MMS) and hydroxyurea (HU); when associated with E-1182. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000218603 | 1 – 1493 | Sister chromatid cohesion protein 2Add BLAST | 1493 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 43 | Phosphoserine; in mutant scc2-8A1 Publication | 1 | |
Modified residuei | 67 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 74 | Phosphoserine; in mutant scc2-8A1 Publication | 1 | |
Modified residuei | 127 | Phosphoserine1 Publication | 1 | |
Modified residuei | 157 | Phosphoserine1 Publication | 1 | |
Modified residuei | 162 | Phosphoserine; in mutant scc2-8A1 Publication | 1 | |
Modified residuei | 163 | Phosphoserine1 Publication | 1 | |
Modified residuei | 231 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 236 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 305 | Phosphoserine1 Publication | 1 | |
Modified residuei | 320 | Phosphoserine1 Publication | 1 | |
Modified residuei | 360 | Phosphothreonine; in mutant scc2-8A1 Publication | 1 | |
Modified residuei | 753 | Phosphoserine1 Publication | 1 | |
Modified residuei | 1179 | Phosphoserine; in mutant scc2-8A1 Publication | 1 | |
Modified residuei | 1182 | Phosphoserine1 Publication | 1 | |
Modified residuei | 1183 | Phosphoserine; in mutant scc2-8A1 Publication | 1 | |
Modified residuei | 1185 | Phosphoserine1 Publication | 1 |
Post-translational modificationi
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.1 Publication
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | Q04002. |
PaxDbi | Q04002. |
PRIDEi | Q04002. |
PTM databases
CarbonylDBi | Q04002. |
iPTMneti | Q04002. |
Interactioni
Subunit structurei
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).3 Publications
Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
SCC4 | P40090 | 12 | EBI-16662,EBI-16679 |
Protein-protein interaction databases
BioGridi | 32234. 251 interactors. |
DIPi | DIP-831N. |
IntActi | Q04002. 8 interactors. |
MINTi | Q04002. |
STRINGi | 4932.YDR180W. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Turni | 4 – 7 | Combined sources | 4 | |
Helixi | 14 – 17 | Combined sources | 4 | |
Turni | 18 – 20 | Combined sources | 3 | |
Helixi | 32 – 37 | Combined sources | 6 | |
Beta strandi | 41 – 43 | Combined sources | 3 | |
Beta strandi | 59 – 61 | Combined sources | 3 | |
Helixi | 79 – 81 | Combined sources | 3 | |
Beta strandi | 85 – 87 | Combined sources | 3 | |
Turni | 106 – 109 | Combined sources | 4 | |
Helixi | 112 – 120 | Combined sources | 9 | |
Turni | 121 – 124 | Combined sources | 4 | |
Beta strandi | 128 – 130 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4XDN | X-ray | 2.08 | B | 1-181 | [»] | |
5W94 | X-ray | 3.19 | B/D | 1-181 | [»] | |
ProteinModelPortali | Q04002. | |||||
SMRi | Q04002. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 695 – 732 | HEAT 1Add BLAST | 38 | |
Repeati | 734 – 771 | HEAT 2Add BLAST | 38 | |
Repeati | 806 – 843 | HEAT 3Add BLAST | 38 | |
Repeati | 1132 – 1169 | HEAT 4Add BLAST | 38 | |
Repeati | 1244 – 1281 | HEAT 5Add BLAST | 38 |
Domaini
The N-terminus (residues 1-181) is sufficient for the interaction with SCC4 (PubMed:26038942).1 Publication
Sequence similaritiesi
Belongs to the SCC2/Nipped-B family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
GeneTreei | ENSGT00390000010427. |
HOGENOMi | HOG000154264. |
InParanoidi | Q04002. |
KOi | K06672. |
OMAi | EAMPLIW. |
OrthoDBi | EOG092C04BG. |
Family and domain databases
InterProi | View protein in InterPro IPR016024. ARM-type_fold. IPR026003. Cohesin_HEAT. IPR024986. Nipped-B_C. IPR033031. SCC2/Nipped-B. |
PANTHERi | PTHR21704. PTHR21704. 1 hit. |
Pfami | View protein in Pfam PF12765. Cohesin_HEAT. 1 hit. PF12830. Nipped-B_C. 1 hit. |
SUPFAMi | SSF48371. SSF48371. 3 hits. |
i Sequence
Sequence statusi: Complete.
Q04002-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSYPGKDKNI PGRIIEALED LPLSYLVPKD GLAALVNAPM RVSLPFDKTI
60 70 80 90 100
FTSADDGRDV NINVLGTANS TTSSIKNEAE KERLVFKRPS NFTSSANSVD
110 120 130 140 150
YVPTNFLEGL SPLAQSVLST HKGLNDSINI EKKSEIVSRP EAKHKLESVT
160 170 180 190 200
SNAGNLSFND NSSNKKTKTS TGVTMTQANL AEQYLNDLKN ILDIVGFDQN
210 220 230 240 250
SAEIGNIEYW LQLPNKKFVL TTNCLTKLQM TIKNITDNPQ LSNSIEITWL
260 270 280 290 300
LRLLDVMVCN IKFSKSSLKM GLDDSMLRYI ALLSTIVLFN IFLLGKNDSN
310 320 330 340 350
LHRESYIMEP VNFLSDLIES LKILTIEYGS LKIEFDTFQE ALELLPKYIR
360 370 380 390 400
NGPFLDDNVT AKLVYIFSDL LMNNDIEATT NIQFQSFWDN VKRISSDILV
410 420 430 440 450
SLFGSFDQQR GFIIEELLSH IEKLPTKRIQ KKLRKVGNQN IYITDFTFTL
460 470 480 490 500
MSMLENINCY SFCNQMKDIA PENIDLLKNE YKKQEEFLFN IVEHINDTIL
510 520 530 540 550
ERFFKNPSAL RYVIDNFVQD LLLLISSPQW PVTEKILSSL LKRLLSVYSP
560 570 580 590 600
SMQVSANIET ICLQLIGNIG STIFDIKCST RDHEDNNLIK MINYPETLPH
610 620 630 640 650
FFKSFEECIA YNETIKCRRS ATRFLWNLRL GTILILEEYT KDAKEQIITV
660 670 680 690 700
DNELKKILEQ IKDGGLGPEL ENREADFSTI KLDYFSILHA FELLNLYDPY
710 720 730 740 750
LKLILSLLAK DKIKLRSTAI KCLSMLASKD KVILSNPMVK ETIHRRLNDS
760 770 780 790 800
SASVKDAILD LVSINSSYFE FYQQINNNYN DDSIMVRKHV LRINEKMYDE
810 820 830 840 850
TNDIVTKVYV IARILMKIED EEDNIIDMAR LILLNRWILK VHEVLDQPEK
860 870 880 890 900
LKEISSSVLL VMSRVAIMNE KCSQLFDLFL NFYLLNKEAH SKEAYDKITH
910 920 930 940 950
VLTILTDFLV QKIVELNSDD TNEKNSIVDK QNFLNLLAKF ADSTVSFLTK
960 970 980 990 1000
DHITALYPYM VSDEKSDFHY YILQVFRCTF EKLANFKQKF LYDLETTLLS
1010 1020 1030 1040 1050
RLPKMNVREI DEAMPLIWSV ATHRHDTARV AKACSSCLSH LHPYINKANN
1060 1070 1080 1090 1100
EEAAIVVDGK LQRLIYLSTG FARFCFPKPS NDKIAFLQEG ETLYEHITKC
1110 1120 1130 1140 1150
LLVLSKDKIT HVIRRVAVKN LTKLCGNHPK LFNSRHVLHL LDKEFQSDQL
1160 1170 1180 1190 1200
DIKLVILESL YDLFLLEERK SVRNTGVNST LSSNSILKKK LLKTNRVEFA
1210 1220 1230 1240 1250
NDGVCSALAT RFLDNILQLC LLRDLKNSLV AIRLLKLILK FGYTNPSHSI
1260 1270 1280 1290 1300
PTVIALFAST SQYIRHVAYE LLEDLFEKYE TLVFSSLSRG VTKAIHYSIH
1310 1320 1330 1340 1350
TDEKYYYKHD HFLSLLEKLC GTGKKNGPKF FKVLKRIMQS YLDDITDLTS
1360 1370 1380 1390 1400
TNSSVQKSIF VLCTNISNIT FVSQYDLVSL LKTIDLTTDR LKEVIMDEIG
1410 1420 1430 1440 1450
DNVSSLSVSE EKLSGIILIQ LSLQDLGTYL LHLYGLRDDV LLLDIVEESE
1460 1470 1480 1490
LKNKQLPAKK PDISKFSAQL ENIEQYSSNG KLLTYFRKHV KDT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y14279 Genomic DNA. Translation: CAA74656.1. Z46727 Genomic DNA. Translation: CAA86687.1. BK006938 Genomic DNA. Translation: DAA12023.1. |
PIRi | S49777. |
RefSeqi | NP_010466.3. NM_001180488.3. |
Genome annotation databases
EnsemblFungii | YDR180W; YDR180W; YDR180W. |
GeneIDi | 851761. |
KEGGi | sce:YDR180W. |
Similar proteinsi
Entry informationi
Entry namei | SCC2_YEAST | |
Accessioni | Q04002Primary (citable) accession number: Q04002 Secondary accession number(s): D6VSG3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 10, 2002 |
Last sequence update: | November 1, 1996 | |
Last modified: | March 28, 2018 | |
This is version 151 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |