Skip Header

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

UniProtKB - Q9UPN9 (TRI33_HUMAN)

Entry version 198 (17 Jun 2020)
Sequence version 3 (30 Nov 2010)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

E3 ubiquitin-protein ligase TRIM33

Gene

TRIM33

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

Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri125 – 154RING-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri212 – 259B box-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri271 – 312B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri887 – 934PHD-typePROSITE-ProRule annotationAdd BLAST48

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Molecular functionDNA-binding, Repressor, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity

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

More...SignaLinki		Q9UPN9

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9UPN9

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

<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:
E3 ubiquitin-protein ligase TRIM33 (EC:2.3.2.27)
Alternative name(s):
Ectodermin homolog
RET-fused gene 7 protein
Short name:
Protein Rfg7
RING-type E3 ubiquitin transferase TRIM33Curated
Transcription intermediary factor 1-gamma
Short name:
TIF1-gamma
Tripartite motif-containing protein 33
<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:TRIM33
Synonyms:KIAA1113, RFG7, TIF1G
<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 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%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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000197323.10

Human Gene Nomenclature Database

More...HGNCi		HGNC:16290 TRIM33

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605769 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UPN9

<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

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

A chromosomal aberration involving TRIM33 is found in papillary thyroid carcinomas (PTCs). Translocation t(1;10)(p13;q11) with RET. The translocation generates the TRIM33/RET (PTC7) oncogene.1 Publication

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>Mutagenesisi125C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128. 1 Publication1
Mutagenesisi128C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125. 1 Publication1

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>Sitei964 – 965Breakpoint for translocation to form TRIM33-RET oncogene2

Organism-specific databases

DisGeNET

More...DisGeNETi		51592

MalaCards human disease database

More...MalaCardsi		TRIM33

Open Targets

More...OpenTargetsi		ENSG00000197323

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

More...Orphaneti		146 Differentiated thyroid carcinoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA38118

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9UPN9 Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2176772

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TRIM33

Domain mapping of disease mutations (DMDM)

More...DMDMi		313104270

<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_00000563951 – 1127E3 ubiquitin-protein ligase TRIM33Add BLAST1127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki504Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<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 residuei515Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei515Omega-N-methylarginine; alternateCombined sources1
Cross-linki527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei535Omega-N-methylarginineCombined sources1
Modified residuei577Asymmetric dimethylarginineCombined sources1
Modified residuei591Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei591Omega-N-methylarginine; alternateCombined sources1
Modified residuei598Asymmetric dimethylarginineCombined sources1
Modified residuei604Asymmetric dimethylarginineCombined sources1
Modified residuei763N6-acetyllysine; alternateCombined sources1
Cross-linki763Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei769N6-acetyllysine; alternateCombined sources1
Cross-linki769Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei793N6-acetyllysine; alternateBy similarity1
Cross-linki793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki793Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki796Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei803PhosphoserineBy similarity1
Modified residuei815PhosphothreonineBy similarity1
Cross-linki861Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei862PhosphoserineCombined sources1
Modified residuei951N6-acetyllysineBy similarity1
Modified residuei953N6-acetyllysine; alternateCombined sources1
Cross-linki953Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1007Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1043Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1051PhosphothreonineCombined sources1
Cross-linki1057Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1102PhosphothreonineCombined sources1
Modified residuei1105PhosphoserineCombined sources1
Cross-linki1118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1119PhosphoserineCombined sources1

<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

Sumoylated with SUMO1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9UPN9

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9UPN9

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9UPN9

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

More...PaxDbi		Q9UPN9

PeptideAtlas

More...PeptideAtlasi		Q9UPN9

PRoteomics IDEntifications database

More...PRIDEi		Q9UPN9

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		85392 [Q9UPN9-1]
85393 [Q9UPN9-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UPN9

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

More...PhosphoSitePlusi		Q9UPN9

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

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

Expressed in stem cells at the bottom of the crypts of the colon (at protein level). Expressed in colon adenomas and adenocarcinomas (at protein level). Expressed in brain, lung, liver, spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, small intestine, ovary, colon, skeletal muscle and hematopoietic progenitors.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000197323 Expressed in endometrium epithelium and 241 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9UPN9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9UPN9 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000197323 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

Homooligomer and heterooligomer with TRIM24 and TRIM28 family members.

Interacts with SMAD4 in unstimulated cells.

Found in a complex with SMAD2 and SMAD3 upon addition of TGF-beta.

Interacts with SMAD2 and SMAD3.

Interacts with SMAD4 under basal and induced conditions and, upon TGF-beta signaling, with activated SMAD2.

Forms a ternary complex with SMAD4 and SMAD2 upon TGF-beta signaling.

5 Publications

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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		119625, 99 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9UPN9

Database of interacting proteins

More...DIPi		DIP-54262N

Protein interaction database and analysis system

More...IntActi		Q9UPN9, 69 interactors

Molecular INTeraction database

More...MINTi		Q9UPN9

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000351250

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9UPN9

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9UPN9 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

11127
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		Q9UPN9

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>Domaini974 – 1046BromoPROSITE-ProRule annotationAdd BLAST73

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>Regioni1 – 147Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repressionAdd BLAST147
Regioni299 – 401Necessary for oligomerizationAdd BLAST103

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 coili299 – 401Sequence analysisAdd BLAST103

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi13 – 18Poly-Gly6
Compositional biasi44 – 49Poly-Glu6
Compositional biasi545 – 550Poly-Thr6

<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 TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri125 – 154RING-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri212 – 259B box-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri271 – 312B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri887 – 934PHD-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410ITFN Eukaryota
ENOG410Z421 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156361

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9UPN9

KEGG Orthology (KO)

More...KOi		K08883

Identification of Orthologs from Complete Genome Data

More...OMAi		CQLHTQE

Database of Orthologous Groups

More...OrthoDBi		756911at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9UPN9

TreeFam database of animal gene trees

More...TreeFami		TF106455

Family and domain databases

Conserved Domains Database

More...CDDi		cd00021 BBOX, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.920.10, 1 hit
3.30.40.10, 2 hits

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00505

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003649 Bbox_C
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR019786 Zinc_finger_PHD-type_CS
IPR027370 Znf-RING_LisH
IPR000315 Znf_B-box
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00439 Bromodomain, 1 hit
PF00628 PHD, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00503 BROMODOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00297 BROMO, 1 hit
SM00249 PHD, 2 hits
SM00184 RING, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50014 BROMODOMAIN_2, 1 hit
PS50119 ZF_BBOX, 2 hits
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_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%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>Sequences (2+)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 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform Alpha (identifier: Q9UPN9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG 
        60         70         80         90        100
GRAGAEGGAA GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA 
       110        120        130        140        150
PASAPAPGPS AGPPPGPPAS LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC 
       160        170        180        190        200
LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR CPVCRQECRQ IDLVDNYFVK 
       210        220        230        240        250
DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT CIEAHQRVKF 
       260        270        280        290        300
TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ 
       310        320        330        340        350
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE 
       360        370        380        390        400
VNETNKRVEQ EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN 
       410        420        430        440        450
DITGLSRQVK HVMNFTNWAI ASGSSTALLY SKRLITFQLR HILKARCDPV 
       460        470        480        490        500
PAANGAIRFH CDPTFWAKNV VNLGNLVIES KPAPGYTPNV VVGQVPPGTN 
       510        520        530        540        550
HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP APVPTTTTTT 
       560        570        580        590        600
QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP 
       610        620        630        640        650
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM 
       660        670        680        690        700
ANANRGPTSP SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL 
       710        720        730        740        750
SRYISGSHLP PQPTSTMNPS PGPSALSPGS SGLSNSHTPV RPPSTSSTGS 
       760        770        780        790        800
RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG TEDEICSFSG GVKQEKTEDG 
       810        820        830        840        850
RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI EPADMNESCK 
       860        870        880        890        900
QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL 
       910        920        930        940        950
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK 
       960        970        980        990       1000
KGKTAQGLSP VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP 
      1010       1020       1030       1040       1050
MDLSTVKKKL QKKHSQHYQI PDDFVADVRL IFKNCERFNE MMKVVQVYAD 
      1060       1070       1080       1090       1100
TQEINLKADS EVAQAGKAVA LYFEDKLTEI YSDRTFAPLP EFEQEEDDGE 
      1110       1120 
VTEDSDEDFI QPRRKRLKSD ERPVHIK
Length:1,127
Mass (Da):122,533
Last modified:November 30, 2010 - v3
<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:i7A36013799E9933C
GO
Isoform Beta (identifier: Q9UPN9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1041-1057: Missing.

Show »
Length:1,110
Mass (Da):120,541
Checksum:i1D415E1C620703A8
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y612H0Y612_HUMAN
E3 ubiquitin-protein ligase TRIM33
TRIM33
888Annotation 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>

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

The sequence AAD17259 differs from that shown. Reason: Frameshift.Curated
The sequence BAA83065 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti89V → E in CAB55313 (PubMed:10439047).Curated1
Sequence conflicti451 – 453PAA → LLH in CAB55313 (PubMed:10439047).Curated3
Sequence conflicti909F → S in CAB55313 (PubMed:10439047).Curated1
Sequence conflicti1037R → T in AAD17259 (PubMed:10022127).Curated1

Natural variant

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_02949467V → A. Corresponds to variant dbSNP:rs6691166Ensembl.1
Natural variantiVAR_042376580M → I in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042377696L → S1 PublicationCorresponds to variant dbSNP:rs56151583Ensembl.1
Natural variantiVAR_042378811E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_024616840I → T4 PublicationsCorresponds to variant dbSNP:rs6537825Ensembl.1
Natural variantiVAR_042379885P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042380961V → M1 PublicationCorresponds to variant dbSNP:rs55688622Ensembl.1
Natural variantiVAR_0423811090P → T1 PublicationCorresponds to variant dbSNP:rs55784699Ensembl.1

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_0057741041 – 1057Missing in isoform Beta. 2 PublicationsAdd BLAST17

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
AF119043 mRNA Translation: AAD17259.1 Frameshift.
AF220136 mRNA Translation: AAG53509.1
AF220137 mRNA Translation: AAG53510.1
AB029036 mRNA Translation: BAA83065.1 Different initiation.
AL035410 Genomic DNA No translation available.
AL390241 Genomic DNA No translation available.
AJ132948 mRNA Translation: CAB55313.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS872.1 [Q9UPN9-1]
CCDS873.1 [Q9UPN9-2]

NCBI Reference Sequences

More...RefSeqi		NP_056990.3, NM_015906.3 [Q9UPN9-1]
NP_148980.2, NM_033020.2 [Q9UPN9-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000358465; ENSP00000351250; ENSG00000197323 [Q9UPN9-1]
ENST00000369543; ENSP00000358556; ENSG00000197323 [Q9UPN9-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		51592

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:51592

UCSC genome browser

More...UCSCi		uc001eew.3 human [Q9UPN9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<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
AF119043 mRNA Translation: AAD17259.1 Frameshift.
AF220136 mRNA Translation: AAG53509.1
AF220137 mRNA Translation: AAG53510.1
AB029036 mRNA Translation: BAA83065.1 Different initiation.
AL035410 Genomic DNA No translation available.
AL390241 Genomic DNA No translation available.
AJ132948 mRNA Translation: CAB55313.1
CCDSiCCDS872.1 [Q9UPN9-1]
CCDS873.1 [Q9UPN9-2]
RefSeqiNP_056990.3, NM_015906.3 [Q9UPN9-1]
NP_148980.2, NM_033020.2 [Q9UPN9-2]

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
3U5MX-ray3.08A/B/C/D/E/F/G/H/I/J/K/L882-1087[»]
3U5NX-ray1.95A/B882-1087[»]
3U5OX-ray2.70A/B/C/D/E/F/G/H882-1087[»]
3U5PX-ray2.80A/B/C/D/E/F/G/H882-1087[»]
5MR8X-ray1.74A882-1090[»]
SMRiQ9UPN9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi119625, 99 interactors
CORUMiQ9UPN9
DIPiDIP-54262N
IntActiQ9UPN9, 69 interactors
MINTiQ9UPN9
STRINGi9606.ENSP00000351250

Chemistry databases

BindingDBiQ9UPN9
ChEMBLiCHEMBL2176772

PTM databases

iPTMnetiQ9UPN9
PhosphoSitePlusiQ9UPN9

Polymorphism and mutation databases

BioMutaiTRIM33
DMDMi313104270

Proteomic databases

EPDiQ9UPN9
jPOSTiQ9UPN9
MassIVEiQ9UPN9
PaxDbiQ9UPN9
PeptideAtlasiQ9UPN9
PRIDEiQ9UPN9
ProteomicsDBi85392 [Q9UPN9-1]
85393 [Q9UPN9-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1303 397 antibodies

Genome annotation databases

EnsembliENST00000358465; ENSP00000351250; ENSG00000197323 [Q9UPN9-1]
ENST00000369543; ENSP00000358556; ENSG00000197323 [Q9UPN9-2]
GeneIDi51592
KEGGihsa:51592
UCSCiuc001eew.3 human [Q9UPN9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		51592
DisGeNETi51592
EuPathDBiHostDB:ENSG00000197323.10

GeneCards: human genes, protein and diseases

More...GeneCardsi		TRIM33
HGNCiHGNC:16290 TRIM33
HPAiENSG00000197323 Low tissue specificity
MalaCardsiTRIM33
MIMi605769 gene
neXtProtiNX_Q9UPN9
OpenTargetsiENSG00000197323
Orphaneti146 Differentiated thyroid carcinoma
PharmGKBiPA38118

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410ITFN Eukaryota
ENOG410Z421 LUCA
GeneTreeiENSGT00940000156361
InParanoidiQ9UPN9
KOiK08883
OMAiCQLHTQE
OrthoDBi756911at2759
PhylomeDBiQ9UPN9
TreeFamiTF106455

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
SignaLinkiQ9UPN9
SIGNORiQ9UPN9

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		51592 15 hits in 791 CRISPR screens

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

More...ChiTaRSi		TRIM33 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TRIM33

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

More...GenomeRNAii		51592
PharosiQ9UPN9 Tbio

Protein Ontology

More...PROi		PR:Q9UPN9
RNActiQ9UPN9 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000197323 Expressed in endometrium epithelium and 241 other tissues
ExpressionAtlasiQ9UPN9 baseline and differential
GenevisibleiQ9UPN9 HS

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di1.20.920.10, 1 hit
3.30.40.10, 2 hits
IDEALiIID00505
InterProiView protein in InterPro
IPR003649 Bbox_C
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR019786 Zinc_finger_PHD-type_CS
IPR027370 Znf-RING_LisH
IPR000315 Znf_B-box
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF00439 Bromodomain, 1 hit
PF00628 PHD, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00297 BROMO, 1 hit
SM00249 PHD, 2 hits
SM00184 RING, 2 hits
SUPFAMiSSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50014 BROMODOMAIN_2, 1 hit
PS50119 ZF_BBOX, 2 hits
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiTRI33_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: Q9UPN9
Secondary accession number(s): O95855
, Q5TG72, Q5TG73, Q5TG74, Q9C017, Q9UJ79
<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: January 24, 2001
Last sequence update: November 30, 2010
Last modified: June 17, 2020
This is version 198 of the entry and version 3 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again