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Entry version 168 (13 Feb 2019)
Sequence version 2 (25 Mar 2003)
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Protein

Structural maintenance of chromosomes protein 3

Gene

Smc3

Organism
Mus musculus (Mouse)
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

Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form 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. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement.1 Publication

Caution

Was originally isolated as a proteoglycan protein (explaining its name). Although not excluded, such secreted function is not clear.Curated

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

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, Cell division, DNA damage, DNA repair, Meiosis, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2468052 Establishment of Sister Chromatid Cohesion
R-MMU-2470946 Cohesin Loading onto Chromatin
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
Q9CW03

<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
Short name:
SMC protein 3
Short name:
SMC-3
Alternative name(s):
Basement membrane-associated chondroitin proteoglycan
Short name:
Bamacan
Chondroitin sulfate proteoglycan 6
Chromosome segregation protein SmcD
Mad member-interacting protein 1
<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
Synonyms:Bam, Bmh, Cspg6, Mmip1, Smc3l1, Smcd
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 19

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1339795 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 Cytoskeleton Lysosome 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>Mutagenesisi807L → P: Abolishes interaction with MXI1. 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_00001190021 – 1217Structural maintenance of chromosomes protein 3Add BLAST1217

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 residuei105N6-acetyllysineCombined sources1
Modified residuei106N6-acetyllysineCombined sources1
Modified residuei140N6-acetyllysineBy similarity1
Modified residuei783PhosphothreonineBy similarity1
Modified residuei787PhosphoserineCombined sources1
Modified residuei886PhosphoserineBy similarity1
Modified residuei1013Phosphoserine1 Publication1
Modified residuei1065PhosphoserineBy similarity1
Modified residuei1067PhosphoserineCombined sources1
Modified residuei1074PhosphoserineBy similarity1
Modified residuei1083Phosphoserine1 Publication1
Modified residuei1190N6-acetyllysineBy similarity1

<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 Ser-1083 in a SPO11-dependent manner.2 Publications
Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. Regulated by DSCC1, it is required for processive DNA synthesis, coupling sister chromatid cohesion establishment during S phase to DNA replication (By similarity). Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9CW03

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9CW03

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9CW03

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

More...
PaxDbi
Q9CW03

PRoteomics IDEntifications database

More...
PRIDEi
Q9CW03

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9CW03

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9CW03

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Spermatocytes (at protein level). Widely expressed, with higher expression in testis and brain.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000024974 Expressed in 280 organ(s), highest expression level in placenta

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9CW03 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9CW03 MM

<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

Forms a heterodimer with SMC1A or SMC1B in cohesin complexes (PubMed:11564881). Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their SMC hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Also found in meiosis-specific cohesin complexes. Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with PDS5A and WAPL; regulated by SMC3 acetylation. Interacts with NUMA1, and forms a ternary complex with KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to the spindle pole and a function in chromosome movement. Interacts with SYCP2 and RPGR. Interacts (via SMC hinge domain) with KIAA1328 (via N- and C-terminal domains). Interacts with DDX11. Found in a cohesin complex with SMC1A, STAG1 and RAD21. The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By similarity). Interacts with MXI1, MXD3 and MXD4 (PubMed:9528857). Interacts with STAG3 (PubMed:11483963).By similarity3 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
Mecp2Q9Z2D63EBI-2550068,EBI-1188816

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
198951, 48 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9CW03

Database of interacting proteins

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DIPi
DIP-57028N

Protein interaction database and analysis system

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IntActi
Q9CW03, 51 interactors

Molecular INTeraction database

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MINTi
Q9CW03

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000025930

<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

11217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

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
2WD5X-ray2.70B484-696[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9CW03

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

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SMRi
Q9CW03

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9CW03

<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>Domaini530 – 642SMC hingeAdd BLAST113

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 coili179 – 350Sequence analysisAdd BLAST172
Coiled coili393 – 503Sequence analysisAdd BLAST111
Coiled coili669 – 916Sequence analysisAdd BLAST248
Coiled coili958 – 989Sequence analysisAdd BLAST32

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 biasi1115 – 1150Ala/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 SMC1A or SMC1B, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0964 Eukaryota
COG1196 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00580000081628

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000166512

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG039849

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9CW03

KEGG Orthology (KO)

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KOi
K06669

Identification of Orthologs from Complete Genome Data

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OMAi
QGEIRLM

Database of Orthologous Groups

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OrthoDBi
119789at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9CW03

TreeFam database of animal gene trees

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TreeFami
TF105602

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

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PIRSFi
PIRSF005719 SMC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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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.

Q9CW03-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS
60 70 80 90 100
DEFSHLRPEQ RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR
110 120 130 140 150
VIGAKKDQYF LDKKMVTKND VMNLLESAGF SRSNPYYIVK QGKINQMATA
160 170 180 190 200
PDSQRLKLLR EVAGTRVYDE RKEESISLMK ETEGKREKIN ELLKYIEERL
210 220 230 240 250
HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD ELSAKRETSG
260 270 280 290 300
EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK
310 320 330 340 350
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK
360 370 380 390 400
FNSVKEKEER GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK
410 420 430 440 450
SLDQAINDKK RQIAAIHKDL EDTEANKEKN LEQYNKLDQD LNEVKARVEE
460 470 480 490 500
LDRKYYEVKN KKDELQSERN YLWREENAEQ QALAAKREDL EKKQQLLRAA
510 520 530 540 550
TGKAILNGID SINKVLEHFR RKGINQHVQN GYHGIVMNNF ECEPAFYTCV
560 570 580 590 600
EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
610 620 630 640 650
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC
660 670 680 690 700
ITLEGDQVSH RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL
710 720 730 740 750
RRNIERINNE IDQLMNQMQQ IETQQRKFKA SRDSILSEMK MLKEKRQQSE
760 770 780 790 800
KTFMPKQRSL QSLEASLHAM ESTRESLKAE LGTDLLSQLS LEDQKRVDAL
810 820 830 840 850
NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL DQVEQELNEL
860 870 880 890 900
RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
910 920 930 940 950
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP
960 970 980 990 1000
QEAFEKYQTL SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL
1010 1020 1030 1040 1050
IKRQEELDRG YKSIMELMNV LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG
1060 1070 1080 1090 1100
GKATLVMKKG DVEGSQSQDE GEGSGESERG SGSQSSVPSV DQFTGVGIRV
1110 1120 1130 1140 1150
SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY LFDEIDQALD
1160 1170 1180 1190 1200
AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV
1210
ITAEMAKDFV EDDTTHG
Length:1,217
Mass (Da):141,556
Last modified:March 25, 2003 - v2
<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:i11FF55165BE6A88E
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA75400 differs from that shown. Reason: Frameshift at positions 522, 1018 and 1144.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti999K → R in CAA75400 (PubMed:9528857).Curated1
Sequence conflicti1175F → L (PubMed:9528857).Curated1

Sequence databases

Select the link destinations:

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
AF141294 mRNA Translation: AAD42073.1
AF047601 mRNA Translation: AAD27754.1
Y15128 mRNA Translation: CAA75400.1 Frameshift.
AK005647 mRNA Translation: BAB24167.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS38025.1

NCBI Reference Sequences

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RefSeqi
NP_031816.2, NM_007790.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.14910

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974

Database of genes from NCBI RefSeq genomes

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GeneIDi
13006

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13006

UCSC genome browser

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UCSCi
uc008hwy.2 mouse

<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
AF141294 mRNA Translation: AAD42073.1
AF047601 mRNA Translation: AAD27754.1
Y15128 mRNA Translation: CAA75400.1 Frameshift.
AK005647 mRNA Translation: BAB24167.1
CCDSiCCDS38025.1
RefSeqiNP_031816.2, NM_007790.3
UniGeneiMm.14910

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70B484-696[»]
ProteinModelPortaliQ9CW03
SMRiQ9CW03
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198951, 48 interactors
CORUMiQ9CW03
DIPiDIP-57028N
IntActiQ9CW03, 51 interactors
MINTiQ9CW03
STRINGi10090.ENSMUSP00000025930

Protein family/group databases

MoonProtiQ9CW03

PTM databases

iPTMnetiQ9CW03
PhosphoSitePlusiQ9CW03

Proteomic databases

EPDiQ9CW03
jPOSTiQ9CW03
MaxQBiQ9CW03
PaxDbiQ9CW03
PRIDEiQ9CW03

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974
GeneIDi13006
KEGGimmu:13006
UCSCiuc008hwy.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9126
MGIiMGI:1339795 Smc3

Phylogenomic databases

eggNOGiKOG0964 Eukaryota
COG1196 LUCA
GeneTreeiENSGT00580000081628
HOGENOMiHOG000166512
HOVERGENiHBG039849
InParanoidiQ9CW03
KOiK06669
OMAiQGEIRLM
OrthoDBi119789at2759
PhylomeDBiQ9CW03
TreeFamiTF105602

Enzyme and pathway databases

ReactomeiR-MMU-2467813 Separation of Sister Chromatids
R-MMU-2468052 Establishment of Sister Chromatid Cohesion
R-MMU-2470946 Cohesin Loading onto Chromatin
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Smc3 mouse
EvolutionaryTraceiQ9CW03

Protein Ontology

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PROi
PR:Q9CW03

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000024974 Expressed in 280 organ(s), highest expression level in placenta
ExpressionAtlasiQ9CW03 baseline and differential
GenevisibleiQ9CW03 MM

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

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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_MOUSE
<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: Q9CW03
Secondary accession number(s): O35667, Q9QUS3
<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: March 25, 2003
Last sequence update: March 25, 2003
Last modified: February 13, 2019
This is version 168 of the entry and version 2 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 programChordata 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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