Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Structural maintenance of chromosomes protein 3

Gene

SMC3

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

Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.

Miscellaneous

Present with 2660 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 39ATPSequence analysis8

<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

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein kinase binding Source: SGD

GO - Biological processi

  • ascospore formation Source: SGD
  • cell division Source: UniProtKB-KW
  • meiotic sister chromatid cohesion Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
  • reciprocal meiotic recombination Source: SGD
  • replication-born double-strand break repair via sister chromatid exchange Source: SGD
  • synaptonemal complex assembly Source: SGD

<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, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31532-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:
Structural maintenance of chromosomes protein 3
Alternative name(s):
DA-box protein SMC3
<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:SMC3
Ordered Locus Names:YJL074C
ORF Names:J1049
<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 X

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003610 SMC3

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

<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_00001190151 – 1230Structural maintenance of chromosomes protein 3Add BLAST1230

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 residuei112N6-acetyllysine1 Publication1
Modified residuei113N6-acetyllysine1 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

Acetylation at Lys-112 and Lys-113 by ECO1 is important for genome stability and S phase sister chromatid cohesion.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P47037

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

More...
PaxDbi
P47037

PRoteomics IDEntifications database

More...
PRIDEi
P47037

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P47037

<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

Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their SMC hinge domain, MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.2 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33681, 489 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1408 Nuclear meiotic cohesin complex
CPX-1867 Nuclear mitotic cohesin complex

Database of interacting proteins

More...
DIPi
DIP-2991N

Protein interaction database and analysis system

More...
IntActi
P47037, 57 interactors

Molecular INTeraction database

More...
MINTi
P47037

STRING: functional protein association networks

More...
STRINGi
4932.YJL074C

<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

11230
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P47037

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

More...
SMRi
P47037

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini535 – 651SMC hingeAdd BLAST117

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili172 – 482Sequence analysisAdd BLAST311
Coiled coili685 – 1041Sequence analysisAdd BLAST357

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1126 – 1161Ala/Asp-rich (DA-box)Add BLAST36

<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 flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable MCD1 protein, forming a ring structure (By similarity).By similarity

<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 SMC family. SMC3 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000169262

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000166512

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P47037

KEGG Orthology (KO)

More...
KOi
K06669

Identification of Orthologs from Complete Genome Data

More...
OMAi
QGEIRLM

Database of Orthologous Groups

More...
OrthoDBi
EOG092C0XGI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005719 SMC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00968 SMC_hinge, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF75553 SSF75553, 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>.<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.

P47037-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS
60 70 80 90 100
DDYSNLKREE RQGLIHQGSG GSVMSASVEI VFHDPDHSMI LPSGVLSRGD
110 120 130 140 150
DEVTIRRTVG LKKDDYQLND RNVTKGDIVR MLETAGFSMN NPYNIVPQGK
160 170 180 190 200
IVALTNAKDK ERLQLLEDVV GAKSFEVKLK ASLKKMEETE QKKIQINKEM
210 220 230 240 250
GELNSKLSEM EQERKELEKY NELERNRKIY QFTLYDRELN EVINQMERLD
260 270 280 290 300
GDYNNTVYSS EQYIQELDKR EDMIDQVSKK LSSIEASLKI KNATDLQQAK
310 320 330 340 350
LRESEISQKL TNVNVKIKDV QQQIESNEEQ RNLDSATLKE IKSIIEQRKQ
360 370 380 390 400
KLSKILPRYQ ELTKEEAMYK LQLASLQQKQ RDLILKKGEY ARFKSKDERD
410 420 430 440 450
TWIHSEIEEL KSSIQNLNEL ESQLQMDRTS LRKQYSAIDE EIEELIDSIN
460 470 480 490 500
GPDTKGQLED FDSELIHLKQ KLSESLDTRK ELWRKEQKLQ TVLETLLSDV
510 520 530 540 550
NQNQRNVNET MSRSLANGII NVKEITEKLK ISPESVFGTL GELIKVNDKY
560 570 580 590 600
KTCAEVIGGN SLFHIVVDTE ETATLIMNEL YRMKGGRVTF IPLNRLSLDS
610 620 630 640 650
DVKFPSNTTT QIQFTPLIKK IKYEPRFEKA VKHVFGKTIV VKDLGQGLKL
660 670 680 690 700
AKKHKLNAIT LDGDRADKRG VLTGGYLDQH KRTRLESLKN LNESRSQHKK
710 720 730 740 750
ILEELDFVRN ELNDIDTKID QVNGNIRKVS NDRESVLTNI EVYRTSLNTK
760 770 780 790 800
KNEKLILEES LNAIILKLEK LNTNRTFAQE KLNTFENDLL QEFDSELSKE
810 820 830 840 850
EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL ESKLIPQEND
860 870 880 890 900
LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVLE LGTVQREIES
910 920 930 940 950
LIAEETNNKK LLEKANNQQR LLLKKLDNFQ KSVEKTMIKK TTLVTRREEL
960 970 980 990 1000
QQRIREIGLL PEDALVNDFS DITSDQLLQR LNDMNTEISG LKNVNKRAFE
1010 1020 1030 1040 1050
NFKKFNERRK DLAERASELD ESKDSIQDLI VKLKQQKVNA VDSTFQKVSE
1060 1070 1080 1090 1100
NFEAVFERLV PRGTAKLIIH RKNDNANDHD ESIDVDMDAE SNESQNGKDS
1110 1120 1130 1140 1150
EIMYTGVSIS VSFNSKQNEQ LHVEQLSGGQ KTVCAIALIL AIQMVDPASF
1160 1170 1180 1190 1200
YLFDEIDAAL DKQYRTAVAT LLKELSKNAQ FICTTFRTDM LQVADKFFRV
1210 1220 1230
KYENKISTVI EVNREEAIGF IRGSNKFAEV
Length:1,230
Mass (Da):141,336
Last modified:February 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:iB152D88F7780341F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y14278 Genomic DNA Translation: CAA74655.1
Z49349 Genomic DNA Translation: CAA89366.1
X88851 Genomic DNA Translation: CAA61313.1
BK006943 Genomic DNA Translation: DAA08725.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S56850

NCBI Reference Sequences

More...
RefSeqi
NP_012461.1, NM_001181507.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL074C_mRNA; YJL074C_mRNA; YJL074C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853371

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL074C

<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
Y14278 Genomic DNA Translation: CAA74655.1
Z49349 Genomic DNA Translation: CAA89366.1
X88851 Genomic DNA Translation: CAA61313.1
BK006943 Genomic DNA Translation: DAA08725.1
PIRiS56850
RefSeqiNP_012461.1, NM_001181507.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
4UX3X-ray3.30A2-261[»]
A970-1230[»]
ProteinModelPortaliP47037
SMRiP47037
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33681, 489 interactors
ComplexPortaliCPX-1408 Nuclear meiotic cohesin complex
CPX-1867 Nuclear mitotic cohesin complex
DIPiDIP-2991N
IntActiP47037, 57 interactors
MINTiP47037
STRINGi4932.YJL074C

PTM databases

iPTMnetiP47037

Proteomic databases

MaxQBiP47037
PaxDbiP47037
PRIDEiP47037

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL074C_mRNA; YJL074C_mRNA; YJL074C
GeneIDi853371
KEGGisce:YJL074C

Organism-specific databases

SGDiS000003610 SMC3

Phylogenomic databases

GeneTreeiENSGT00940000169262
HOGENOMiHOG000166512
InParanoidiP47037
KOiK06669
OMAiQGEIRLM
OrthoDBiEOG092C0XGI

Enzyme and pathway databases

BioCyciYEAST:G3O-31532-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P47037

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR003395 RecF/RecN/SMC_N
IPR024704 SMC
IPR010935 SMC_hinge
IPR036277 SMC_hinge_sf
PfamiView protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit
PIRSFiPIRSF005719 SMC, 1 hit
SMARTiView protein in SMART
SM00968 SMC_hinge, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF75553 SSF75553, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiSMC3_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: P47037
Secondary accession number(s): D6VWA9
<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: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 174 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again