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Entry version 165 (16 Oct 2019)
Sequence version 1 (01 Nov 1996)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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

<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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-29769-MONOMER

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sister chromatid cohesion protein 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SCC2
Ordered Locus Names:YDR180W
ORF Names:YD9395.14
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YDR180W

Saccharomyces Genome Database

More...
SGDi
S000002588 SCC2

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi67T → 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 Publication1
Mutagenesisi67T → 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 Publication1
Mutagenesisi127S → 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 Publication1
Mutagenesisi127S → 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 Publication1
Mutagenesisi157S → 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 Publication1
Mutagenesisi157S → 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 Publication1
Mutagenesisi163S → 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 Publication1
Mutagenesisi163S → 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 Publication1
Mutagenesisi231T → 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 Publication1
Mutagenesisi231T → 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 Publication1
Mutagenesisi236T → 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 Publication1
Mutagenesisi236T → 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 Publication1
Mutagenesisi305S → 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 Publication1
Mutagenesisi305S → 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 Publication1
Mutagenesisi320S → 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 Publication1
Mutagenesisi320S → 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 Publication1
Mutagenesisi753S → E: Mimics constitutive phosphorylation and causes inviability through protein instability. 1 Publication1
Mutagenesisi1182S → 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 Publication1
Mutagenesisi1185S → 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 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002186031 – 1493Sister chromatid cohesion protein 2Add BLAST1493

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q04002

PRoteomics IDEntifications database

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PRIDEi
Q04002

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
Q04002

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q04002

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
32234, 273 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1868 SCC2-SCC4 cohesin loader complex

Database of interacting proteins

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DIPi
DIP-831N

Protein interaction database and analysis system

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IntActi
Q04002, 2 interactors

Molecular INTeraction database

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MINTi
Q04002

STRING: functional protein association networks

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STRINGi
4932.YDR180W

<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

11493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q04002

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati695 – 732HEAT 1Add BLAST38
Repeati734 – 771HEAT 2Add BLAST38
Repeati806 – 843HEAT 3Add BLAST38
Repeati1132 – 1169HEAT 4Add BLAST38
Repeati1244 – 1281HEAT 5Add BLAST38

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminus (residues 1-181) is sufficient for the interaction with SCC4 (PubMed:26038942).1 Publication

<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

Belongs to the SCC2/Nipped-B family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000154264

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q04002

KEGG Orthology (KO)

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KOi
K06672

Identification of Orthologs from Complete Genome Data

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OMAi
AIKCLSM

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016024 ARM-type_fold
IPR026003 Cohesin_HEAT
IPR024986 Nipped-B_C
IPR033031 SCC2/Nipped-B

The PANTHER Classification System

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PANTHERi
PTHR21704 PTHR21704, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF12765 Cohesin_HEAT, 1 hit
PF12830 Nipped-B_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i94CC2E8D2F4208D0
GO

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Y14279 Genomic DNA Translation: CAA74656.1
Z46727 Genomic DNA Translation: CAA86687.1
BK006938 Genomic DNA Translation: DAA12023.1

Protein sequence database of the Protein Information Resource

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PIRi
S49777

NCBI Reference Sequences

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RefSeqi
NP_010466.3, NM_001180488.3

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YDR180W_mRNA; YDR180W; YDR180W

Database of genes from NCBI RefSeq genomes

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GeneIDi
851761

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YDR180W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XDNX-ray2.08B1-181[»]
5W94X-ray3.19B/D1-181[»]
SMRiQ04002
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi32234, 273 interactors
ComplexPortaliCPX-1868 SCC2-SCC4 cohesin loader complex
DIPiDIP-831N
IntActiQ04002, 2 interactors
MINTiQ04002
STRINGi4932.YDR180W

PTM databases

CarbonylDBiQ04002
iPTMnetiQ04002

Proteomic databases

MaxQBiQ04002
PaxDbiQ04002
PRIDEiQ04002

Genome annotation databases

EnsemblFungiiYDR180W_mRNA; YDR180W; YDR180W
GeneIDi851761
KEGGisce:YDR180W

Organism-specific databases

EuPathDBiFungiDB:YDR180W
SGDiS000002588 SCC2

Phylogenomic databases

HOGENOMiHOG000154264
InParanoidiQ04002
KOiK06672
OMAiAIKCLSM

Enzyme and pathway databases

BioCyciYEAST:G3O-29769-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:Q04002

Family and domain databases

InterProiView protein in InterPro
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, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSCC2_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q04002
Secondary accession number(s): D6VSG3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: October 16, 2019
This is version 165 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<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

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
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