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
Homo sapiens (Human)
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.2 Publications

Miscellaneous

Mutated Cornelia de Lange cell lines display genomic instability and sensitivity to ionizing radiation and interstrand cross-linking agents.

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

  • ATP binding Source: UniProtKB-KW
  • beta-tubulin binding Source: UniProtKB
  • chromatin binding Source: Ensembl
  • dynein complex binding Source: UniProtKB
  • mediator complex binding Source: Ensembl
  • microtubule motor activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

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-HSA-1221632 Meiotic synapsis
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2468052 Establishment of Sister Chromatid Cohesion
R-HSA-2470946 Cohesin Loading onto Chromatin
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-9018519 Estrogen-dependent gene expression

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9UQE7

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
Q9UQE7 Curated

<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-associated polypeptide
Short name:
hCAP
<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, SMC3L1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000108055.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2468 SMC3

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606062 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UQE7

<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; 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cornelia de Lange syndrome 3 (CDLS3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. Cornelia de Lange syndrome type 3 is a mild form with absence of major structural anomalies. The phenotype in some instances approaches that of apparently non-syndromic mental retardation.
See also OMIM:610759
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_032845491Missing in CDLS3; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 Publications1

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>Mutagenesisi105K → A: 20% loss of sister chromatid cohesion; when associated with A-106. 2 Publications1
Mutagenesisi105K → R: Stabilizes interaction with PDS5A and WAPL; when associated with R-106. 2 Publications1
Mutagenesisi106K → A: 20% loss of sister chromatid cohesion; when associated with A-105. 2 Publications1
Mutagenesisi106K → R: Stabilizes interaction with PDS5A and WAPL; when associated with R-105. 2 Publications1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
9126

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
SMC3

MalaCards human disease database

More...
MalaCardsi
SMC3
MIMi610759 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000108055

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
199 Cornelia de Lange syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA26966

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SMC3

Domain mapping of disease mutations (DMDM)

More...
DMDMi
29337005

<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_00001190011 – 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 sources2 Publications1
Modified residuei106N6-acetyllysineCombined sources2 Publications1
Modified residuei140N6-acetyllysineCombined sources1
Modified residuei783PhosphothreonineCombined sources1
Modified residuei787PhosphoserineCombined sources1
Modified residuei886PhosphoserineCombined sources1
Modified residuei1013PhosphoserineBy similarity1
Modified residuei1065PhosphoserineCombined sources1
Modified residuei1067PhosphoserineCombined sources1
Modified residuei1074PhosphoserineBy similarity1
Modified residuei1083PhosphoserineCombined sources1
Modified residuei1190N6-acetyllysineCombined sources1

<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.By similarity
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. Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9UQE7

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9UQE7

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

More...
PaxDbi
Q9UQE7

PeptideAtlas

More...
PeptideAtlasi
Q9UQE7

PRoteomics IDEntifications database

More...
PRIDEi
Q9UQE7

ProteomicsDB human proteome resource

More...
ProteomicsDBi
85549

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9UQE7

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

More...
PhosphoSitePlusi
Q9UQE7

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9UQE7

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000108055 Expressed in 225 organ(s), highest expression level in tendon of biceps brachii

CleanEx database of gene expression profiles

More...
CleanExi
HS_SMC3

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9UQE7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA037411
HPA043206

<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:22628566). 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 (PubMed:11076961). Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN (PubMed:15837422). Interacts with NUMA1, and forms a ternary complex with KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to the spindle pole and in chromosome movement (PubMed:9506951, PubMed:11590136). Interacts with PDS5A and WAPL; regulated by SMC3 acetylation (PubMed:19907496). Interacts (via SMC hinge domain) with KIAA1328 (via N- and C-terminal domains) (PubMed:15656913). Interacts with DDX11 (PubMed:17105772). Found in a cohesin complex with SMC1A, STAG1 and RAD21 (PubMed:22628566). The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (PubMed:22628566). Interacts with MXI1, MXD3, MXD4, SYCP2, RPGR and STAG3 (By similarity).By similarity8 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
114574, 148 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9UQE7

Database of interacting proteins

More...
DIPi
DIP-29200N

Protein interaction database and analysis system

More...
IntActi
Q9UQE7, 86 interactors

Molecular INTeraction database

More...
MINTi
Q9UQE7

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000354720

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9UQE7

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

More...
SMRi
Q9UQE7

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>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

More...
GeneTreei
ENSGT00580000081628

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000166512

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG039849

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9UQE7

KEGG Orthology (KO)

More...
KOi
K06669

Identification of Orthologs from Complete Genome Data

More...
OMAi
QGEIRLM

Database of Orthologous Groups

More...
OrthoDBi
EOG091G011B

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9UQE7

TreeFam database of animal gene trees

More...
TreeFami
TF105602

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.

Q9UQE7-1 [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 SINKVLDHFR 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):141,542
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:i21EF9A08A5D8096A
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 AAD32447 differs from that shown. Reason: Frameshift at positions 457, 488 and 523.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 conflicti462K → T in AAD32447 (PubMed:11042152).Curated1
Sequence conflicti509I → V in AAD32447 (PubMed:11042152).Curated1
Sequence conflicti526Q → P in AAD32447 (PubMed:11042152).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032845491Missing in CDLS3; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 Publications1

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
AF020043 mRNA Translation: AAC14893.1
AK289771 mRNA Translation: BAF82460.1
AL359260 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49557.1
AF067163 mRNA Translation: AAD32447.1 Frameshift.
AJ005015 mRNA Translation: CAA06289.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31285.1

NCBI Reference Sequences

More...
RefSeqi
NP_005436.1, NM_005445.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.24485

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000361804; ENSP00000354720; ENSG00000108055

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9126

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9126

UCSC genome browser

More...
UCSCi
uc001kze.4 human

<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
AF020043 mRNA Translation: AAC14893.1
AK289771 mRNA Translation: BAF82460.1
AL359260 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49557.1
AF067163 mRNA Translation: AAD32447.1 Frameshift.
AJ005015 mRNA Translation: CAA06289.1
CCDSiCCDS31285.1
RefSeqiNP_005436.1, NM_005445.3
UniGeneiHs.24485

3D structure databases

ProteinModelPortaliQ9UQE7
SMRiQ9UQE7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114574, 148 interactors
CORUMiQ9UQE7
DIPiDIP-29200N
IntActiQ9UQE7, 86 interactors
MINTiQ9UQE7
STRINGi9606.ENSP00000354720

Protein family/group databases

MoonDBiQ9UQE7 Curated

PTM databases

iPTMnetiQ9UQE7
PhosphoSitePlusiQ9UQE7
SwissPalmiQ9UQE7

Polymorphism and mutation databases

BioMutaiSMC3
DMDMi29337005

Proteomic databases

EPDiQ9UQE7
MaxQBiQ9UQE7
PaxDbiQ9UQE7
PeptideAtlasiQ9UQE7
PRIDEiQ9UQE7
ProteomicsDBi85549

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361804; ENSP00000354720; ENSG00000108055
GeneIDi9126
KEGGihsa:9126
UCSCiuc001kze.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9126
DisGeNETi9126
EuPathDBiHostDB:ENSG00000108055.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SMC3
GeneReviewsiSMC3
HGNCiHGNC:2468 SMC3
HPAiHPA037411
HPA043206
MalaCardsiSMC3
MIMi606062 gene
610759 phenotype
neXtProtiNX_Q9UQE7
OpenTargetsiENSG00000108055
Orphaneti199 Cornelia de Lange syndrome
PharmGKBiPA26966

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0964 Eukaryota
COG1196 LUCA
GeneTreeiENSGT00580000081628
HOGENOMiHOG000166512
HOVERGENiHBG039849
InParanoidiQ9UQE7
KOiK06669
OMAiQGEIRLM
OrthoDBiEOG091G011B
PhylomeDBiQ9UQE7
TreeFamiTF105602

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2468052 Establishment of Sister Chromatid Cohesion
R-HSA-2470946 Cohesin Loading onto Chromatin
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-9018519 Estrogen-dependent gene expression
SIGNORiQ9UQE7

Miscellaneous databases

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

More...
ChiTaRSi
SMC3 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SMC3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
9126

Protein Ontology

More...
PROi
PR:Q9UQE7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000108055 Expressed in 225 organ(s), highest expression level in tendon of biceps brachii
CleanExiHS_SMC3
GenevisibleiQ9UQE7 HS

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_HUMAN
<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: Q9UQE7
Secondary accession number(s): A8K156, O60464, Q5T482
<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: December 5, 2018
This is version 186 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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