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Protein

Sister chromatid cohesion protein 2

Gene

SCC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a structural role in chromatin and is involved in sister chromatid cohesion (PubMed:9990856, PubMed:14614819, 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).4 Publications

Miscellaneous

Present with 3310 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

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
  • protein localization to chromatin Source: SGD
  • rDNA condensation Source: SGD
  • regulation of gene expression Source: InterPro
  • replication-born double-strand break repair via sister chromatid exchange Source: SGD
  • transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  • tRNA gene clustering Source: SGD

Keywordsi

Biological processCell cycle

Enzyme and pathway databases

BioCyciYEAST: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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR180W.
SGDiS000002588. SCC2.

Subcellular locationi

GO - Cellular componenti

  • 2-micrometer circle DNA Source: SGD
  • chromosome, centromeric region Source: UniProtKB-SubCell
  • cytosol Source: SGD
  • nuclear chromatin Source: SGD
  • nucleus Source: SGD
  • SMC loading complex Source: SGD

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67T → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-127; A-157; A-163; A-231; A-236; A-305 and A-320. 1 Publication1
Mutagenesisi67T → E in ssc2-8E; 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 Publication1
Mutagenesisi127S → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-157; A-163; A-231; A-236; A-305 and A-320. 1 Publication1
Mutagenesisi127S → E in ssc2-8E; 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 Publication1
Mutagenesisi157S → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-127; A-163; A-231; A-236; A-305 and A-320. 1 Publication1
Mutagenesisi157S → E in ssc2-8E; 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 Publication1
Mutagenesisi163S → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-127; A-157; A-231; A-236; A-305 and A-320. 1 Publication1
Mutagenesisi163S → E in ssc2-8E; 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 Publication1
Mutagenesisi231T → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-127; A-157; A-163; A-236; A-305 and A-320. 1 Publication1
Mutagenesisi231T → E in ssc2-8E; 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 ssc2-2NE; 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 Publication1
Mutagenesisi236T → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-127; A-157; A-163; A-231; A-305 and A-320. 1 Publication1
Mutagenesisi236T → E in ssc2-8E; 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 ssc2-2NE; 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 Publication1
Mutagenesisi305S → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-127; A-157; A-163; A-231; A-236 and A-320. 1 Publication1
Mutagenesisi305S → E in ssc2-8E; 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 ssc2-2NE; 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 Publication1
Mutagenesisi320S → A in ssc2-8A; mimics unphosphorylated form and leads to novel phosphorylation sites at Ser-43, Ser-74, Ser-162, Ser-360, Ser-1179 and Ser-1183; when assocated with A-67; A-127; A-157; A-163; A-231; A-236 and A-305. 1 Publication1
Mutagenesisi320S → E in ssc2-8E; 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 ssc2-2NE; 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 Publication1
Mutagenesisi753S → E: Mimics constitutive phosphorylation and causes inviability through protein instability. 1 Publication1
Mutagenesisi1182S → E in ssc2-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 Publication1
Mutagenesisi1185S → E in ssc2-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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002186031 – 1493Sister chromatid cohesion protein 2Add BLAST1493

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43Phosphoserine; in mutant scc2-8A1 Publication1
Modified residuei67Phosphothreonine1 Publication1
Modified residuei74Phosphoserine; in mutant scc2-8A1 Publication1
Modified residuei127Phosphoserine1 Publication1
Modified residuei157Phosphoserine1 Publication1
Modified residuei162Phosphoserine; in mutant scc2-8A1 Publication1
Modified residuei163Phosphoserine1 Publication1
Modified residuei231Phosphothreonine1 Publication1
Modified residuei236Phosphothreonine1 Publication1
Modified residuei305Phosphoserine1 Publication1
Modified residuei320Phosphoserine1 Publication1
Modified residuei360Phosphothreonine; in mutant scc2-8A1 Publication1
Modified residuei753Phosphoserine1 Publication1
Modified residuei1179Phosphoserine; in mutant scc2-8A1 Publication1
Modified residuei1182Phosphoserine1 Publication1
Modified residuei1183Phosphoserine; in mutant scc2-8A1 Publication1
Modified residuei1185Phosphoserine1 Publication1

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

Phosphoprotein

Proteomic databases

MaxQBiQ04002.
PRIDEiQ04002.

PTM databases

iPTMnetiQ04002.

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

WithEntry#Exp.IntActNotes
SCC4P400905EBI-16662,EBI-16679

Protein-protein interaction databases

BioGridi32234. 248 interactors.
DIPiDIP-831N.
IntActiQ04002. 2 interactors.
MINTiMINT-2783708.

Structurei

Secondary structure

11493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Helixi14 – 17Combined sources4
Turni18 – 20Combined sources3
Helixi32 – 37Combined sources6
Beta strandi41 – 43Combined sources3
Beta strandi59 – 61Combined sources3
Helixi79 – 81Combined sources3
Beta strandi85 – 87Combined sources3
Turni106 – 109Combined sources4
Helixi112 – 120Combined sources9
Beta strandi128 – 130Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XDNX-ray2.08B1-181[»]
ProteinModelPortaliQ04002.
SMRiQ04002.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati695 – 732HEAT 1Add BLAST38
Repeati734 – 771HEAT 2Add BLAST38
Repeati806 – 843HEAT 3Add BLAST38
Repeati1132 – 1169HEAT 4Add BLAST38
Repeati1244 – 1281HEAT 5Add BLAST38

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

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000010427.
HOGENOMiHOG000154264.
InParanoidiQ04002.
KOiK06672.
OMAiEAMPLIW.
OrthoDBiEOG092C04BG.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiView protein in InterPro
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026003. Cohesin_HEAT.
IPR024986. Nipped-B_C.
IPR033031. SCC2/Nipped-B.
PANTHERiPTHR21704. PTHR21704. 1 hit.
PfamiView protein in Pfam
PF12765. Cohesin_HEAT. 1 hit.
PF12830. Nipped-B_C. 1 hit.
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Q04002-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:1,493
Mass (Da):171,102
Last modified:November 1, 1996 - v1
Checksum:i94CC2E8D2F4208D0
GO

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.
PIRiS49777.
RefSeqiNP_010466.3. NM_001180488.3.

Genome annotation databases

EnsemblFungiiYDR180W; YDR180W; YDR180W.
GeneIDi851761.
KEGGisce:YDR180W.

Cross-referencesi

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.
PIRiS49777.
RefSeqiNP_010466.3. NM_001180488.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XDNX-ray2.08B1-181[»]
ProteinModelPortaliQ04002.
SMRiQ04002.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32234. 248 interactors.
DIPiDIP-831N.
IntActiQ04002. 2 interactors.
MINTiMINT-2783708.

PTM databases

iPTMnetiQ04002.

Proteomic databases

MaxQBiQ04002.
PRIDEiQ04002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR180W; YDR180W; YDR180W.
GeneIDi851761.
KEGGisce:YDR180W.

Organism-specific databases

EuPathDBiFungiDB:YDR180W.
SGDiS000002588. SCC2.

Phylogenomic databases

GeneTreeiENSGT00390000010427.
HOGENOMiHOG000154264.
InParanoidiQ04002.
KOiK06672.
OMAiEAMPLIW.
OrthoDBiEOG092C04BG.

Enzyme and pathway databases

BioCyciYEAST:G3O-29769-MONOMER.

Miscellaneous databases

PROiPR:Q04002.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiView protein in InterPro
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026003. Cohesin_HEAT.
IPR024986. Nipped-B_C.
IPR033031. SCC2/Nipped-B.
PANTHERiPTHR21704. PTHR21704. 1 hit.
PfamiView protein in Pfam
PF12765. Cohesin_HEAT. 1 hit.
PF12830. Nipped-B_C. 1 hit.
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiSCC2_YEAST
AccessioniPrimary (citable) accession number: Q04002
Secondary accession number(s): D6VSG3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: April 12, 2017
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.