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UniProtKB - P63165 (SUMO1_HUMAN)

Entry version 176 (13 Feb 2019)
Sequence version 1 (27 Sep 2004)
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Protein

Small ubiquitin-related modifier 1

Gene

SUMO1

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

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376).7 Publications

<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

  • enzyme binding Source: CAFA
  • glucocorticoid receptor binding Source: CAFA
  • potassium channel regulator activity Source: UniProtKB
  • protein binding, bridging Source: CAFA
  • protein C-terminus binding Source: CAFA
  • protein tag Source: GO_Central
  • RNA binding Source: UniProtKB
  • small protein activating enzyme binding Source: CAFA
  • SUMO transferase activity Source: Reactome
  • transcription corepressor binding Source: CAFA
  • transcription factor binding Source: AgBase
  • ubiquitin-like protein ligase binding Source: GO_Central
  • ubiquitin protein ligase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 processHost-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:ENSG00000116030-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-HSA-3065679 SUMO is proteolytically processed
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4085377 SUMOylation of SUMOylation proteins
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-4655427 SUMOylation of DNA methylation proteins
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-877312 Regulation of IFNG signaling
R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors

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

More...SignaLinki		P63165

SIGNOR Signaling Network Open Resource

More...SIGNORi		P63165

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P63165 Predicted

<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:
Small ubiquitin-related modifier 1
Short name:
SUMO-1
Alternative name(s):
GAP-modifying protein 1
Short name:
GMP1
SMT3 homolog 3
Sentrin
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein SMT3C
Short name:
Smt3C
Ubiquitin-like protein UBL1
<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:SUMO1
Synonyms:SMT3C, SMT3H3, UBL1
ORF Names:OK/SW-cl.43
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000116030.16

Human Gene Nomenclature Database

More...HGNCi		HGNC:12502 SUMO1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601912 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P63165

<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

Cell membrane, Cytoplasm, Membrane, 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

Non-syndromic orofacial cleft 10 (OFC10)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.
Disease descriptionA birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
See also OMIM:613705

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>Mutagenesisi36F → A: Abolishes binding to PIAS2. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7341

MalaCards human disease database

More...MalaCardsi		SUMO1
MIMi613705 phenotype

Open Targets

More...OpenTargetsi		ENSG00000116030

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

More...Orphaneti		99798 Oligodontia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37149

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2146296

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		SUMO1

Domain mapping of disease mutations (DMDM)

More...DMDMi		52783799

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00000359392 – 97Small ubiquitin-related modifier 1Add BLAST96
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000003594098 – 1011 Publication4

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 residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei9PhosphoserineCombined sources1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residuei32PhosphoserineCombined sources1
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

<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

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.1 Publication
Polymeric SUMO1 chains undergo polyubiquitination by RNF4.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P63165

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P63165

MaxQB - The MaxQuant DataBase

More...MaxQBi		P63165

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

More...PaxDbi		P63165

PeptideAtlas

More...PeptideAtlasi		P63165

PRoteomics IDEntifications database

More...PRIDEi		P63165

ProteomicsDB human proteome resource

More...ProteomicsDBi		12703
57500

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P63165-1 [P63165-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P63165

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

More...PhosphoSitePlusi		P63165

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P63165

<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		ENSG00000116030 Expressed in 202 organ(s), highest expression level in caudate nucleus

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P63165 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P63165 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004269
HPA056956

<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

Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (PubMed:19223394). Interacts with SAE2, RANBP2, PIAS1 and PIAS2. Interacts with PRKN. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1.17 Publications
(Microbial infection) Interacts with Epstein-barr virus BGLF4.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei36Interaction with PIAS21

<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
Q59GP63EBI-80140,EBI-10243413
ARP102757EBI-80140,EBI-608057
ATF2P153365EBI-80140,EBI-1170906
AXIN1A0A0S2Z4M16EBI-80140,EBI-16429430
AXIN1O151693EBI-80140,EBI-710484
BRCA1P383983EBI-80140,EBI-349905
C18orf25Q96B235EBI-80140,EBI-742108
CARD9Q9H2573EBI-80140,EBI-751319
DAXXQ9UER77EBI-80140,EBI-77321
DEUP1Q05D603EBI-80140,EBI-748597
DNMT3BQ9UBC34EBI-80140,EBI-80125
DTX2Q86UW93EBI-80140,EBI-740376
EDARADDQ8WWZ35EBI-80140,EBI-2949647
EIF4EP067305EBI-80140,EBI-73440
ELK1P194195EBI-80140,EBI-726632
ELK1P19419-12EBI-80140,EBI-15799641
ETV6A0A0S2Z3N63EBI-80140,EBI-16434659
FAM118BQ9BPY33EBI-80140,EBI-726822
FBF1Q8TES7-63EBI-80140,EBI-10244131
FLJ13057Q53SE73EBI-80140,EBI-10172181
FSBPO950733EBI-80140,EBI-1059030
HGSO149643EBI-80140,EBI-740220
HIF1AQ166654EBI-80140,EBI-447269
HNRNPCP079105EBI-80140,EBI-357966
HSF1Q006132EBI-80140,EBI-719620
IKBKGQ9Y6K93EBI-80140,EBI-81279
IRF1P109142EBI-80140,EBI-1055781
KCNK1O001803EBI-80140,EBI-3914675
MAPK1IP1LQ8NDC03EBI-80140,EBI-741424
MBD1Q9UIS93EBI-80140,EBI-867196
MEF2AQ02078-13EBI-80140,EBI-15799584
MYBP102423EBI-80140,EBI-298355
NFKB2Q006532EBI-80140,EBI-307326
NPM1P06748-13EBI-80140,EBI-354150
PARP1P098742EBI-80140,EBI-355676
PIAS2O759286EBI-80140,EBI-348555
PMLP295906EBI-80140,EBI-295890
PMLP29590-92EBI-80140,EBI-6861318
PRDM1O75626-22EBI-80140,EBI-7839538
Prdm1Q606363EBI-80140,EBI-7000804From Mus musculus.
PSIP1O754754EBI-80140,EBI-1801773
RAD54L2Q9Y4B45EBI-80140,EBI-948156
RANGAP1P4606013EBI-80140,EBI-396091
RARAP102765EBI-80140,EBI-413374
RHOXF2Q9BQY43EBI-80140,EBI-372094
RWDD3Q9Y3V22EBI-80140,EBI-1549885
SART1O432902EBI-80140,EBI-607761
SATB1Q018262EBI-80140,EBI-743747
SENP1Q9P0U38EBI-80140,EBI-2822935
SENP2Q9HC622EBI-80140,EBI-714881
SOX10P566932EBI-80140,EBI-1167533
SOX2P484313EBI-80140,EBI-6124081
SP100P234976EBI-80140,EBI-751145
SUMO1P1G2XKQ03EBI-80140,EBI-10175576
TANKQ928448EBI-80140,EBI-356349
TFCP2Q128003EBI-80140,EBI-717422
TP53P046373EBI-80140,EBI-366083
TP53BP1Q128882EBI-80140,EBI-396540
TP53BP1Q12888-12EBI-80140,EBI-8022649
TRAF4Q9BUZ43EBI-80140,EBI-3650647
UBA2Q9UBT27EBI-80140,EBI-718569
UBE2IP632799EBI-80140,EBI-80168
UBE2IQ7KZS05EBI-80140,EBI-10180829
USPL1Q5W0Q75EBI-80140,EBI-2513899
ZBTB26Q9HCK05EBI-80140,EBI-3918996
ZBTB6Q159163EBI-80140,EBI-7227791
ZCCHC12Q6PEW16EBI-80140,EBI-748373
ZMYM5Q9UJ783EBI-80140,EBI-7228860

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113188, 178 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3042 activated SUMO1-E1 ligase complex
CPX-3043 sumoylated E2 ligase complex (SUMO1)

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P63165

Database of interacting proteins

More...DIPi		DIP-29080N

Protein interaction database and analysis system

More...IntActi		P63165, 164 interactors

Molecular INTeraction database

More...MINTi		P63165

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000376076

<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

1101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1A5RNMR-A1-101[»]
1TGZX-ray2.80B18-97[»]
1WYWX-ray2.10B1-97[»]
1Y8RX-ray2.75C/F1-97[»]
1Z5SX-ray3.01B18-97[»]
2ASQNMR-A1-97[»]
2BF8X-ray2.30B21-97[»]
2G4DX-ray2.80B/D20-97[»]
2IO2X-ray2.90B18-97[»]
2IY0X-ray2.77B20-101[»]
2IY1X-ray2.46B/D20-101[»]
2KQSNMR-A1-97[»]
2LASNMR-A1-101[»]
2MW5NMR-A1-97[»]
2N1ANMR-A1-101[»]
2N1VNMR-A1-97[»]
2PE6X-ray2.40B1-97[»]
2UYZX-ray1.40B20-97[»]
2VRRX-ray2.22B20-97[»]
3KYCX-ray2.45D1-97[»]
3KYDX-ray2.61D1-94[»]
3RZWX-ray2.15C/D1-97[»]
3UIPX-ray2.29B18-97[»]
4WJNX-ray1.50A17-97[»]
4WJOX-ray1.46A17-97[»]
4WJPX-ray1.70A/C17-97[»]
4WJQX-ray1.35A/C17-97[»]
5AEKX-ray3.00B/D/F/H/J/L/N/P/R/T/V/X20-97[»]
5B7ANMR-A1-97[»]
5ELJX-ray1.98B18-97[»]
5GHDNMR-A1-97[»]
6EOPX-ray2.40D/E/F61-68[»]
6EOTX-ray3.50C/E/F/H/J/L61-68[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P63165

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

More...SMRi		P63165

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P63165

<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>Domaini20 – 97Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78

<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 ubiquitin family. SUMO subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1769 Eukaryota
COG5227 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154319

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000207495

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG053025

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P63165

KEGG Orthology (KO)

More...KOi		K12160

Database of Orthologous Groups

More...OrthoDBi		1583700at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P63165

TreeFam database of animal gene trees

More...TreeFami		TF315116

Family and domain databases

Conserved Domains Database

More...CDDi		cd01763 Sumo, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11976 Rad60-SLD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54236 SSF54236, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50053 UBIQUITIN_2, 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>Sequences (2+)i

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P63165-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES 
        60         70         80         90        100
YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST 

V
Length:101
Mass (Da):11,557
Last modified:September 27, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i89BE97D2D054FB33
GO
Isoform 2 (identifier: P63165-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     4-28: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:76
Mass (Da):8,799
Checksum:i709FCA25A95F9020
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B8ZZN6B8ZZN6_HUMAN
Small ubiquitin-related modifier 1
SUMO1
146Annotation 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>
B8ZZJ0B8ZZJ0_HUMAN
Small ubiquitin-related modifier 1
SUMO1
58Annotation 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>
B9A032B9A032_HUMAN
Small ubiquitin-related modifier 1
SUMO1
77Annotation 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>
B8ZZ67B8ZZ67_HUMAN
SMT3 suppressor of mif two 3 homolo...
SUMO1 hCG_1776791
62Annotation 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>
F8WBI1F8WBI1_HUMAN
Small ubiquitin-related modifier 1
SUMO1
73Annotation 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 conflicti75H → N in AAH66306 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0467564 – 28Missing in isoform 2. CuratedAdd BLAST25

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
X99586 mRNA Translation: CAA67898.1
U61397 mRNA Translation: AAB40388.1
U38784 mRNA Translation: AAC50733.1
U67122 mRNA Translation: AAC50996.1
U72722 mRNA Translation: AAB40390.1
U83117 mRNA Translation: AAB39999.1
AB062294 mRNA Translation: BAB93477.1
BT006632 mRNA Translation: AAP35278.1
CR542147 mRNA Translation: CAG46944.1
CR542156 mRNA Translation: CAG46953.1
AK311840 mRNA Translation: BAG34782.1
AC079354 Genomic DNA Translation: AAY24035.1
CH471063 Genomic DNA Translation: EAW70304.1
CH471063 Genomic DNA Translation: EAW70307.1
BC006462 mRNA Translation: AAH06462.1
BC053528 mRNA Translation: AAH53528.1
BC066306 mRNA Translation: AAH66306.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2352.1 [P63165-1]
CCDS46493.1 [P63165-2]

NCBI Reference Sequences

More...RefSeqi		NP_001005781.1, NM_001005781.1 [P63165-1]
NP_001005782.1, NM_001005782.1 [P63165-2]
NP_003343.1, NM_003352.4 [P63165-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.81424

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000392244; ENSP00000376075; ENSG00000116030 [P63165-2]
ENST00000392245; ENSP00000376076; ENSG00000116030 [P63165-1]
ENST00000392246; ENSP00000376077; ENSG00000116030 [P63165-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7341

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7341

UCSC genome browser

More...UCSCi		uc002uyz.2 human [P63165-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

SUMO protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99586 mRNA Translation: CAA67898.1
U61397 mRNA Translation: AAB40388.1
U38784 mRNA Translation: AAC50733.1
U67122 mRNA Translation: AAC50996.1
U72722 mRNA Translation: AAB40390.1
U83117 mRNA Translation: AAB39999.1
AB062294 mRNA Translation: BAB93477.1
BT006632 mRNA Translation: AAP35278.1
CR542147 mRNA Translation: CAG46944.1
CR542156 mRNA Translation: CAG46953.1
AK311840 mRNA Translation: BAG34782.1
AC079354 Genomic DNA Translation: AAY24035.1
CH471063 Genomic DNA Translation: EAW70304.1
CH471063 Genomic DNA Translation: EAW70307.1
BC006462 mRNA Translation: AAH06462.1
BC053528 mRNA Translation: AAH53528.1
BC066306 mRNA Translation: AAH66306.1
CCDSiCCDS2352.1 [P63165-1]
CCDS46493.1 [P63165-2]
RefSeqiNP_001005781.1, NM_001005781.1 [P63165-1]
NP_001005782.1, NM_001005782.1 [P63165-2]
NP_003343.1, NM_003352.4 [P63165-1]
UniGeneiHs.81424

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5RNMR-A1-101[»]
1TGZX-ray2.80B18-97[»]
1WYWX-ray2.10B1-97[»]
1Y8RX-ray2.75C/F1-97[»]
1Z5SX-ray3.01B18-97[»]
2ASQNMR-A1-97[»]
2BF8X-ray2.30B21-97[»]
2G4DX-ray2.80B/D20-97[»]
2IO2X-ray2.90B18-97[»]
2IY0X-ray2.77B20-101[»]
2IY1X-ray2.46B/D20-101[»]
2KQSNMR-A1-97[»]
2LASNMR-A1-101[»]
2MW5NMR-A1-97[»]
2N1ANMR-A1-101[»]
2N1VNMR-A1-97[»]
2PE6X-ray2.40B1-97[»]
2UYZX-ray1.40B20-97[»]
2VRRX-ray2.22B20-97[»]
3KYCX-ray2.45D1-97[»]
3KYDX-ray2.61D1-94[»]
3RZWX-ray2.15C/D1-97[»]
3UIPX-ray2.29B18-97[»]
4WJNX-ray1.50A17-97[»]
4WJOX-ray1.46A17-97[»]
4WJPX-ray1.70A/C17-97[»]
4WJQX-ray1.35A/C17-97[»]
5AEKX-ray3.00B/D/F/H/J/L/N/P/R/T/V/X20-97[»]
5B7ANMR-A1-97[»]
5ELJX-ray1.98B18-97[»]
5GHDNMR-A1-97[»]
6EOPX-ray2.40D/E/F61-68[»]
6EOTX-ray3.50C/E/F/H/J/L61-68[»]
ProteinModelPortaliP63165
SMRiP63165
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113188, 178 interactors
ComplexPortaliCPX-3042 activated SUMO1-E1 ligase complex
CPX-3043 sumoylated E2 ligase complex (SUMO1)
CORUMiP63165
DIPiDIP-29080N
IntActiP63165, 164 interactors
MINTiP63165
STRINGi9606.ENSP00000376076

Chemistry databases

ChEMBLiCHEMBL2146296

Protein family/group databases

MoonDBiP63165 Predicted

PTM databases

iPTMnetiP63165
PhosphoSitePlusiP63165

Polymorphism and mutation databases

BioMutaiSUMO1
DMDMi52783799

Proteomic databases

EPDiP63165
jPOSTiP63165
MaxQBiP63165
PaxDbiP63165
PeptideAtlasiP63165
PRIDEiP63165
ProteomicsDBi12703
57500
TopDownProteomicsiP63165-1 [P63165-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7341
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392244; ENSP00000376075; ENSG00000116030 [P63165-2]
ENST00000392245; ENSP00000376076; ENSG00000116030 [P63165-1]
ENST00000392246; ENSP00000376077; ENSG00000116030 [P63165-1]
GeneIDi7341
KEGGihsa:7341
UCSCiuc002uyz.2 human [P63165-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7341
DisGeNETi7341
EuPathDBiHostDB:ENSG00000116030.16

GeneCards: human genes, protein and diseases

More...GeneCardsi		SUMO1
HGNCiHGNC:12502 SUMO1
HPAiCAB004269
HPA056956
MalaCardsiSUMO1
MIMi601912 gene
613705 phenotype
neXtProtiNX_P63165
OpenTargetsiENSG00000116030
Orphaneti99798 Oligodontia
PharmGKBiPA37149

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1769 Eukaryota
COG5227 LUCA
GeneTreeiENSGT00940000154319
HOGENOMiHOG000207495
HOVERGENiHBG053025
InParanoidiP63165
KOiK12160
OrthoDBi1583700at2759
PhylomeDBiP63165
TreeFamiTF315116

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000116030-MONOMER
ReactomeiR-HSA-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-HSA-3065679 SUMO is proteolytically processed
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4085377 SUMOylation of SUMOylation proteins
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-4655427 SUMOylation of DNA methylation proteins
R-HSA-4755510 SUMOylation of immune response proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-877312 Regulation of IFNG signaling
R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors
SignaLinkiP63165
SIGNORiP63165

Miscellaneous databases

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

More...ChiTaRSi		SUMO1 human
EvolutionaryTraceiP63165

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Small_ubiquitin-related_modifier_1

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

More...GenomeRNAii		7341
PMAP-CutDBiP63165

Protein Ontology

More...PROi		PR:P63165

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000116030 Expressed in 202 organ(s), highest expression level in caudate nucleus
ExpressionAtlasiP63165 baseline and differential
GenevisibleiP63165 HS

Family and domain databases

CDDicd01763 Sumo, 1 hit
InterProiView protein in InterPro
IPR022617 Rad60/SUMO-like_dom
IPR033950 Sumo
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF11976 Rad60-SLD, 1 hit
SMARTiView protein in SMART
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_2, 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 nameiSUMO1_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: P63165
Secondary accession number(s): A8MUS8
, B2R4I5, P55856, Q6FGG0, Q6NZ62, Q93068
<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: September 27, 2004
Last sequence update: September 27, 2004
Last modified: February 13, 2019
This is version 176 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation 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, 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. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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