Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 218 (02 Jun 2021)
Sequence version 2 (01 Oct 2002)
Previous versions | rss
Add a publicationFeedback
Protein

Structural maintenance of chromosomes protein 1A

Gene

SMC1A

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

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. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.

1 Publication

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q14683

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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q14683

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q14683

<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%5Fand%5Ftaxonomy%5Fsection">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 1A
Short name:
SMC protein 1A
Short name:
SMC-1-alpha
Short name:
SMC-1A
Alternative name(s):
Sb1.8
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:SMC1A
Synonyms:DXS423E, KIAA0178, SB1.8, SMC1, SMC1L1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Human Gene Nomenclature Database

More...
HGNCi
HGNC:11111, SMC1A

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
300040, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q14683

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000072501.17

<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

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, 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 2 (CDLS2)8 Publications
The disease is caused by variants 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.
Related information in OMIM
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_06278558 – 62Missing in CDLS2. 3 Publications5
Natural variantiVAR_062786133F → V in CDLS2. 2 Publications1
Natural variantiVAR_062787141E → K in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784420Ensembl.1
Natural variantiVAR_062788196R → H in CDLS2. 4 PublicationsCorresponds to variant dbSNP:rs1556890815Ensembl.1
Natural variantiVAR_062789268Missing in CDLS2. 2 PublicationsCorresponds to variant dbSNP:rs727503773Ensembl.1
Natural variantiVAR_062790306Missing in CDLS2. 1 Publication1
Natural variantiVAR_078274398R → G in CDLS2. 1 Publication1
Natural variantiVAR_062791398R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784403Ensembl.1
Natural variantiVAR_026529493E → A in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 PublicationsCorresponds to variant dbSNP:rs122454122Ensembl.1
Natural variantiVAR_062792496R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 Publications1
Natural variantiVAR_062793496R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 PublicationsCorresponds to variant dbSNP:rs122454123Ensembl.1
Natural variantiVAR_078275651V → M in CDLS2; unknown pathological significance. 1 Publication1
Natural variantiVAR_062794683Missing in CDLS2. 1 Publication1
Natural variantiVAR_062795693R → G in CDLS2. 1 Publication1
Natural variantiVAR_078276693R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784408Ensembl.1
Natural variantiVAR_064542711R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs782176647Ensembl.1
Natural variantiVAR_062796711R → W in CDLS2. 2 PublicationsCorresponds to variant dbSNP:rs587784409Ensembl.1
Natural variantiVAR_062797781C → F in CDLS2. 1 Publication1
Natural variantiVAR_064543784I → T in CDLS2. 2 PublicationsCorresponds to variant dbSNP:rs387906702Ensembl.1
Natural variantiVAR_062798790R → Q in CDLS2. 3 PublicationsCorresponds to variant dbSNP:rs797045993Ensembl.1
Natural variantiVAR_062799816R → G in CDLS2. 1 Publication1
Natural variantiVAR_026530832Missing in CDLS2. 1 Publication1
Natural variantiVAR_0628001049R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784416Ensembl.1
Natural variantiVAR_0628011085Y → C in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784418Ensembl.1
Natural variantiVAR_0628021122F → L in CDLS2. 2 Publications1
Natural variantiVAR_0628031123R → W in CDLS2. 1 Publication1
Natural variantiVAR_0782771166N → T in CDLS2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1556885810EnsemblClinVar.1
Natural variantiVAR_0782781189L → F in CDLS2; unknown pathological significance. 1 Publication1
Developmental and epileptic encephalopathy 85 with or without midline brain defects (DEE85)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn X-linked form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE85 is characterized by onset of severe refractory seizures in the first year of life, global developmental delay with impaired intellectual development and poor or absent speech, and dysmorphic facial features. Many patients have midline brain defects on brain imaging.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_083971171 – 1233Missing in DEE85. 1 PublicationAdd BLAST1063
Natural variantiVAR_083972499 – 1233Missing in DEE85. 1 PublicationAdd BLAST735
Natural variantiVAR_083973531 – 1233Missing in DEE85. 1 PublicationAdd BLAST703
Natural variantiVAR_083974733 – 1233Missing in DEE85. 1 PublicationAdd BLAST501
Natural variantiVAR_083975895R → G in DEE85. 1 Publication1
Natural variantiVAR_083976975 – 1233Missing in DEE85. 1 PublicationAdd BLAST259
Natural variantiVAR_0839771039 – 1233Missing in DEE85. 1 PublicationAdd BLAST195
Natural variantiVAR_0839781049 – 1233Missing in DEE85. 1 PublicationAdd BLAST185

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi957S → A: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966. 1 Publication1
Mutagenesisi966S → A: Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957. 2 Publications1

Keywords - Diseasei

Disease variant, Epilepsy, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8243

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

More...
GeneReviewsi
SMC1A

MalaCards human disease database

More...
MalaCardsi
SMC1A
MIMi300590, phenotype
301044, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000072501

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

More...
Orphaneti
199, Cornelia de Lange syndrome
220386, Semilobar holoprosencephaly
319182, Wiedemann-Steiner syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA35961

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q14683, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4105747

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SMC1A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
29336622

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001189891 – 1233Structural maintenance of chromosomes protein 1AAdd BLAST1233

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 residuei358PhosphoserineCombined sources1
Modified residuei360PhosphoserineCombined sources1
Modified residuei648N6-acetyllysineCombined sources1
Modified residuei713N6-acetyllysineCombined sources1
Modified residuei957Phosphoserine; by ATMCombined sources1 Publication1
Modified residuei962PhosphoserineCombined sources1
Modified residuei966Phosphoserine; by ATM and ATRCombined sources3 Publications1
Modified residuei970PhosphoserineCombined sources1
Modified residuei1037N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ubiquitinated by the DCX(DCAF15) complex, leading to its degradation.1 Publication
Phosphorylated by ATM upon ionizing radiation in a NBS1-dependent manner. Phosphorylated by ATR upon DNA methylation in a MSH2/MSH6-dependent manner. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q14683

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q14683

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q14683

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q14683

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

More...
PaxDbi
Q14683

PeptideAtlas

More...
PeptideAtlasi
Q14683

PRoteomics IDEntifications database

More...
PRIDEi
Q14683

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
60117

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q14683

MetOSite database of methionine sulfoxide sites

More...
MetOSitei
Q14683

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

More...
PhosphoSitePlusi
Q14683

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q14683

<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
ENSG00000072501, Expressed in tendon of biceps brachii and 246 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q14683, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q14683, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000072501, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms a heterodimer with SMC3 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 (PubMed:11076961). In germ cell cohesin complexes, SMC1A is mutually exclusive with SMC1B (By similarity).

Interacts with BRCA1 (PubMed:11877377).

Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN (PubMed:15837422).

Interacts with NDC80 (PubMed:9295362, PubMed:10409732,).

Interacts with BRAT1 (PubMed:22977523).

Found in a complex containing POLE and SMC3.

Interacts with RPGR, STAG3 and SYCP2 (By similarity).

Found in a cohesin complex with SMC3, STAG1 and RAD21 (PubMed:22628566). The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (PubMed:22628566).

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
113871, 276 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-5989, Nuclear meiotic cohesin complex, STAG1 variant
CPX-5991, Nuclear meiotic cohesin complex, STAG2 variant
CPX-6082, Nuclear meiotic cohesin complex, STAG3 variant

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q14683

Database of interacting proteins

More...
DIPi
DIP-30911N

Protein interaction database and analysis system

More...
IntActi
Q14683, 119 interactors

Molecular INTeraction database

More...
MINTi
Q14683

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000323421

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q14683, protein

<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

11233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q14683

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini515 – 629SMC hingeAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni284 – 308DisorderedSequence analysisAdd BLAST25
Regioni348 – 369DisorderedSequence analysisAdd BLAST22
Regioni947 – 966DisorderedSequence analysisAdd BLAST20

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 coili104 – 124Sequence analysisAdd BLAST21
Coiled coili163 – 503Sequence analysisAdd BLAST341
Coiled coili660 – 935Sequence analysisAdd BLAST276
Coiled coili991 – 1068Sequence analysisAdd BLAST78

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi949 – 966Polar residuesSequence analysisAdd BLAST18

<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 SMC3, 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. SMC1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0018, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155614

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001042_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q14683

Identification of Orthologs from Complete Genome Data

More...
OMAi
YMEAIVV

Database of Orthologous Groups

More...
OrthoDBi
326079at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q14683

TreeFam database of animal gene trees

More...
TreeFami
TF101156

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03275, ABC_SMC1_euk, 2 hits

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
IPR028468, Smc1_ABC
IPR029683, SMC1A_metazoan
IPR010935, SMC_hinge
IPR036277, SMC_hinge_sf

The PANTHER Classification System

More...
PANTHERi
PTHR18937:SF170, PTHR18937:SF170, 1 hit

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q14683-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG
60 70 80 90 100
EKTSNLRVKT LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG
110 120 130 140 150
GSSEYKINNK VVQLHEYSEE LEKLGILIKA RNFLVFQGAV ESIAMKNPKE
160 170 180 190 200
RTALFEEISR SGELAQEYDK RKKEMVKAEE DTQFNYHRKK NIAAERKEAK
210 220 230 240 250
QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK ELASKNKEIE
260 270 280 290 300
KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
310 320 330 340 350
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF
360 370 380 390 400
EERMEEESQS QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ
410 420 430 440 450
KADQDRLDLE ERKKVETEAK IKQKLREIEE NQKRIEKLEE YITTSKQSLE
460 470 480 490 500
EQKKLEGELT EEVEMAKRRI DEINKELNQV MEQLGDARID RQESSRQQRK
510 520 530 540 550
AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK NMDAIIVDSE
560 570 580 590 600
KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
610 620 630 640 650
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG
660 670 680 690 700
VISGGASDLK AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ
710 720 730 740 750
VQSQAHGLQM RLKYSQSDLE QTKTRHLALN LQEKSKLESE LANFGPRIND
760 770 780 790 800
IKRIIQSRER EMKDLKEKMN QVEDEVFEEF CREIGVRNIR EFEEEKVKRQ
810 820 830 840 850
NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ TVKKDENEIE
860 870 880 890 900
KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
910 920 930 940 950
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI
960 970 980 990 1000
SQEEGSSQGE DSVSGSQRIS SIYAREALIE IDYGDLCEDL KDAQAEEEIK
1010 1020 1030 1040 1050
QEMNTLQQKL NEQQSVLQRI AAPNMKAMEK LESVRDKFQE TSDEFEAARK
1060 1070 1080 1090 1100
RAKKAKQAFE QIKKERFDRF NACFESVATN IDEIYKALSR NSSAQAFLGP
1110 1120 1130 1140 1150
ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL LFAIHSYKPA
1160 1170 1180 1190 1200
PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
1210 1220 1230
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ
Length:1,233
Mass (Da):143,233
Last modified:October 1, 2002 - 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:iE0A44CA7476C88A6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G8JLG1G8JLG1_HUMAN
Structural maintenance of chromosom...
SMC1A
1,211Annotation score:

Annotation score:3 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>
A0A6Q8PHC3A0A6Q8PHC3_HUMAN
Structural maintenance of chromosom...
SMC1A
977Annotation score:

Annotation score:2 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>
V9GY57V9GY57_HUMAN
Structural maintenance of chromosom...
SMC1A
279Annotation score:

Annotation score:2 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>
V9GYN9V9GYN9_HUMAN
Structural maintenance of chromosom...
SMC1A
54Annotation score:

Annotation score:1 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 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 conflicti163 – 164EL → DV in AAB34405 (PubMed:7757074).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05243828T → P. Corresponds to variant dbSNP:rs34530151Ensembl.1
Natural variantiVAR_06278558 – 62Missing in CDLS2. 3 Publications5
Natural variantiVAR_062786133F → V in CDLS2. 2 Publications1
Natural variantiVAR_062787141E → K in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784420Ensembl.1
Natural variantiVAR_083971171 – 1233Missing in DEE85. 1 PublicationAdd BLAST1063
Natural variantiVAR_062788196R → H in CDLS2. 4 PublicationsCorresponds to variant dbSNP:rs1556890815Ensembl.1
Natural variantiVAR_062789268Missing in CDLS2. 2 PublicationsCorresponds to variant dbSNP:rs727503773Ensembl.1
Natural variantiVAR_062790306Missing in CDLS2. 1 Publication1
Natural variantiVAR_078274398R → G in CDLS2. 1 Publication1
Natural variantiVAR_062791398R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784403Ensembl.1
Natural variantiVAR_026529493E → A in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 PublicationsCorresponds to variant dbSNP:rs122454122Ensembl.1
Natural variantiVAR_062792496R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 Publications1
Natural variantiVAR_062793496R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 PublicationsCorresponds to variant dbSNP:rs122454123Ensembl.1
Natural variantiVAR_083972499 – 1233Missing in DEE85. 1 PublicationAdd BLAST735
Natural variantiVAR_083973531 – 1233Missing in DEE85. 1 PublicationAdd BLAST703
Natural variantiVAR_078275651V → M in CDLS2; unknown pathological significance. 1 Publication1
Natural variantiVAR_062794683Missing in CDLS2. 1 Publication1
Natural variantiVAR_062795693R → G in CDLS2. 1 Publication1
Natural variantiVAR_078276693R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784408Ensembl.1
Natural variantiVAR_064542711R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs782176647Ensembl.1
Natural variantiVAR_062796711R → W in CDLS2. 2 PublicationsCorresponds to variant dbSNP:rs587784409Ensembl.1
Natural variantiVAR_083974733 – 1233Missing in DEE85. 1 PublicationAdd BLAST501
Natural variantiVAR_062797781C → F in CDLS2. 1 Publication1
Natural variantiVAR_064543784I → T in CDLS2. 2 PublicationsCorresponds to variant dbSNP:rs387906702Ensembl.1
Natural variantiVAR_062798790R → Q in CDLS2. 3 PublicationsCorresponds to variant dbSNP:rs797045993Ensembl.1
Natural variantiVAR_062799816R → G in CDLS2. 1 Publication1
Natural variantiVAR_026530832Missing in CDLS2. 1 Publication1
Natural variantiVAR_083975895R → G in DEE85. 1 Publication1
Natural variantiVAR_083976975 – 1233Missing in DEE85. 1 PublicationAdd BLAST259
Natural variantiVAR_0839771039 – 1233Missing in DEE85. 1 PublicationAdd BLAST195
Natural variantiVAR_0839781049 – 1233Missing in DEE85. 1 PublicationAdd BLAST185
Natural variantiVAR_0628001049R → Q in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784416Ensembl.1
Natural variantiVAR_0628011085Y → C in CDLS2. 1 PublicationCorresponds to variant dbSNP:rs587784418Ensembl.1
Natural variantiVAR_0628021122F → L in CDLS2. 2 Publications1
Natural variantiVAR_0628031123R → W in CDLS2. 1 Publication1
Natural variantiVAR_0782771166N → T in CDLS2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1556885810EnsemblClinVar.1
Natural variantiVAR_0782781189L → F in CDLS2; unknown pathological significance. 1 Publication1

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
S78271 mRNA Translation: AAB34405.1
D80000 mRNA Translation: BAA11495.2
AL161779, Z97054 Genomic DNA Translation: CAI42089.1
Z97054, AL161779 Genomic DNA Translation: CAI42646.1
BC112127 mRNA Translation: AAI12128.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS14352.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I54383

NCBI Reference Sequences

More...
RefSeqi
NP_006297.2, NM_006306.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000322213; ENSP00000323421; ENSG00000072501

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8243

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8243

UCSC genome browser

More...
UCSCi
uc004dsg.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
S78271 mRNA Translation: AAB34405.1
D80000 mRNA Translation: BAA11495.2
AL161779, Z97054 Genomic DNA Translation: CAI42089.1
Z97054, AL161779 Genomic DNA Translation: CAI42646.1
BC112127 mRNA Translation: AAI12128.1
CCDSiCCDS14352.1
PIRiI54383
RefSeqiNP_006297.2, NM_006306.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6WG3electron microscopy5.30A1-1233[»]
6WG4X-ray2.31A499-675[»]
6WG6X-ray3.54A/C/E/G/I/K472-702[»]
6WGEelectron microscopy3.90A1-1233[»]
SMRiQ14683
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi113871, 276 interactors
ComplexPortaliCPX-5989, Nuclear meiotic cohesin complex, STAG1 variant
CPX-5991, Nuclear meiotic cohesin complex, STAG2 variant
CPX-6082, Nuclear meiotic cohesin complex, STAG3 variant
CORUMiQ14683
DIPiDIP-30911N
IntActiQ14683, 119 interactors
MINTiQ14683
STRINGi9606.ENSP00000323421

Chemistry databases

ChEMBLiCHEMBL4105747

PTM databases

iPTMnetiQ14683
MetOSiteiQ14683
PhosphoSitePlusiQ14683
SwissPalmiQ14683

Genetic variation databases

BioMutaiSMC1A
DMDMi29336622

Proteomic databases

EPDiQ14683
jPOSTiQ14683
MassIVEiQ14683
MaxQBiQ14683
PaxDbiQ14683
PeptideAtlasiQ14683
PRIDEiQ14683
ProteomicsDBi60117

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
491, 962 antibodies

The DNASU plasmid repository

More...
DNASUi
8243

Genome annotation databases

EnsembliENST00000322213; ENSP00000323421; ENSG00000072501
GeneIDi8243
KEGGihsa:8243
UCSCiuc004dsg.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8243
DisGeNETi8243

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SMC1A
GeneReviewsiSMC1A
HGNCiHGNC:11111, SMC1A
HPAiENSG00000072501, Low tissue specificity
MalaCardsiSMC1A
MIMi300040, gene
300590, phenotype
301044, phenotype
neXtProtiNX_Q14683
OpenTargetsiENSG00000072501
Orphaneti199, Cornelia de Lange syndrome
220386, Semilobar holoprosencephaly
319182, Wiedemann-Steiner syndrome
PharmGKBiPA35961
VEuPathDBiHostDB:ENSG00000072501.17

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0018, Eukaryota
GeneTreeiENSGT00940000155614
HOGENOMiCLU_001042_0_2_1
InParanoidiQ14683
OMAiYMEAIVV
OrthoDBi326079at2759
PhylomeDBiQ14683
TreeFamiTF101156

Enzyme and pathway databases

PathwayCommonsiQ14683
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
SignaLinkiQ14683
SIGNORiQ14683

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
8243, 389 hits in 633 CRISPR screens

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

More...
ChiTaRSi
SMC1A, human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SMC1A

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

More...
GenomeRNAii
8243
PharosiQ14683, Tbio

Protein Ontology

More...
PROi
PR:Q14683
RNActiQ14683, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000072501, Expressed in tendon of biceps brachii and 246 other tissues
ExpressionAtlasiQ14683, baseline and differential
GenevisibleiQ14683, HS

Family and domain databases

CDDicd03275, ABC_SMC1_euk, 2 hits
InterProiView protein in InterPro
IPR027417, P-loop_NTPase
IPR003395, RecF/RecN/SMC_N
IPR024704, SMC
IPR028468, Smc1_ABC
IPR029683, SMC1A_metazoan
IPR010935, SMC_hinge
IPR036277, SMC_hinge_sf
PANTHERiPTHR18937:SF170, PTHR18937:SF170, 1 hit
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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSMC1A_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: Q14683
Secondary accession number(s): O14995, Q16351, Q2M228
<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%5Fand%5Fisoforms">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: October 1, 2002
Last modified: June 2, 2021
This is version 218 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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