SCC2

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
Inferred from direct assayⁱ
- 25173104

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Cell cycle, Transcription, Transcription regulation

Biological process

Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29769-MONOMER.

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	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome IV

Organism-specific databases

EuPathDBⁱ	FungiDB:YDR180W.
Saccharomyces Genome Database More...SGDⁱ	S000002588. SCC2.

Keywords - Cellular componentⁱ

Centromere, Chromosome, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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	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

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...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

With

Entry

#Exp.

IntAct

Notes

SCC4

P40090

12

EBI-16662,EBI-16679

Protein-protein interaction databases

BioGridⁱ	32234. 251 interactors.
Database of interacting proteins More...DIPⁱ	DIP-831N.
IntActⁱ	Q04002. 8 interactors.
Molecular INTeraction database More...MINTⁱ	Q04002.
STRINGⁱ	4932.YDR180W.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	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

Repeat

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000010427.
HOGENOMⁱ	HOG000154264.
InParanoidⁱ	Q04002.
KEGG Orthology (KO) More...KOⁱ	K06672.
OMAⁱ	EAMPLIW.
Database of Orthologous Groups More...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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF12765. Cohesin_HEAT. 1 hit. PF12830. Nipped-B_C. 1 hit.
SUPFAMⁱ	SSF48371. SSF48371. 3 hits.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q04002-1 [UniParc]FASTA Add 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.
PIRⁱ	S49777.
NCBI Reference Sequences More...RefSeqⁱ	NP_010466.3. NM_001180488.3.

Genome annotation databases

EnsemblFungiⁱ	YDR180W; YDR180W; YDR180W.
GeneIDⁱ	851761.
KEGGⁱ	sce:YDR180W.

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q04002	C7GN16 G2WAS9 A6ZYD9 C8Z594 A0A0L8VTW3 B3LGA2 N1P8C5 A0A250W8N2 E7KLQ6	Saccharomyces cerevisiae (strain JAY291) (Baker's yeast) Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's yeast) Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) Saccharomyces sp. 'boulardii' Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast) Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast) Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast)	1,493	UniRef90_Q04002	Cluster: Sister chromatid cohesion protein 2	10

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q04002	C8Z594 A0A250W8N2 N1P8C5 A0A0L8VTW3 B3LGA2 C7GN16 A6ZYD9 G2WAS9 E7KLQ6 A0A0L8RN87 +2	Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast) Saccharomyces sp. 'boulardii' Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast) Saccharomyces cerevisiae (strain JAY291) (Baker's yeast) Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's yeast) Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast) Saccharomyces eubayanus (Yeast) And more	1,493	UniRef50_Q04002	Cluster: Sister chromatid cohesion protein 2	13

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.
PIRⁱ	S49777.
NCBI Reference Sequences More...RefSeqⁱ	NP_010466.3. NM_001180488.3.

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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...

Protein-protein interaction databases

BioGridⁱ	32234. 251 interactors.
Database of interacting proteins More...DIPⁱ	DIP-831N.
IntActⁱ	Q04002. 8 interactors.
Molecular INTeraction database More...MINTⁱ	Q04002.
STRINGⁱ	4932.YDR180W.

PTM databases

CarbonylDBⁱ	Q04002.
iPTMnetⁱ	Q04002.

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q04002.
PaxDbⁱ	Q04002.
PRIDEⁱ	Q04002.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YDR180W; YDR180W; YDR180W.
GeneIDⁱ	851761.
KEGGⁱ	sce:YDR180W.

Organism-specific databases

EuPathDBⁱ	FungiDB:YDR180W.
Saccharomyces Genome Database More...SGDⁱ	S000002588. SCC2.

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000010427.
HOGENOMⁱ	HOG000154264.
InParanoidⁱ	Q04002.
KEGG Orthology (KO) More...KOⁱ	K06672.
OMAⁱ	EAMPLIW.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C04BG.

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29769-MONOMER.

BioCycⁱ

YEAST:G3O-29769-MONOMER.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q04002.

PROⁱ

PR:Q04002.

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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF12765. Cohesin_HEAT. 1 hit. PF12830. Nipped-B_C. 1 hit.
SUPFAMⁱ	SSF48371. SSF48371. 3 hits.
ProtoNetⁱ	Search...

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

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

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Supporting data

UniProtKB - Q04002 (SCC2_YEAST)

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Sister chromatid cohesion protein 2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Nucleus

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ