TRIM33

Protein identityUniProt · HPA

UniProt accession

Q9UPN9

Gene

TRIM33

Ensembl

ENSG00000197323

Chromosome

1

Canonical length

1127 aa

Protein class

Cancer-related genes, Disease related genes, Enzymes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Nucleoplasm,Vesicles

Quaternary structure

Homooligomer

OverviewNCBI Gene

The protein encoded by this gene is thought to be a transcriptional corepressor. However, molecules that interact with this protein have not yet been identified. The protein is a member of the tripartite motif family. This motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. Three alternatively spliced transcript variants for this gene have been described, however, the full-length nature of one variant has not been determined. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1127 residues, UniProt reviewed canonical sequence.

>Q9UPN9|TRIM33
     1  MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG GRAGAEGGAA
    61  GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA PASAPAPGPS AGPPPGPPAS
   121  LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR
   181  CPVCRQECRQ IDLVDNYFVK DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT
   241  CIEAHQRVKF TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ
   301  LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE VNETNKRVEQ
   361  EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN DITGLSRQVK HVMNFTNWAI
   421  ASGSSTALLY SKRLITFQLR HILKARCDPV PAANGAIRFH CDPTFWAKNV VNLGNLVIES
   481  KPAPGYTPNV VVGQVPPGTN HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP
   541  APVPTTTTTT QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP
   601  GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM ANANRGPTSP
   661  SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL SRYISGSHLP PQPTSTMNPS
   721  PGPSALSPGS SGLSNSHTPV RPPSTSSTGS RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG
   781  TEDEICSFSG GVKQEKTEDG RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI
   841  EPADMNESCK QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL
   901  CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK KGKTAQGLSP
   961  VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP MDLSTVKKKL QKKHSQHYQI
  1021  PDDFVADVRL IFKNCERFNE MMKVVQVYAD TQEINLKADS EVAQAGKAVA LYFEDKLTEI
  1081  YSDRTFAPLP EFEQEEDDGE VTEDSDEDFI QPRRKRLKSD ERPVHIK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TRIM33 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.55

Highest tissue expression

28 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about TRIM33.

Disease | AllUniProt

Conditions TRIM33 is implicated in, by any mechanism.

• Developmental dysplasia of the hip 4 (DDH4) MIM:621311

Disease | GeneticClinVar

2 pathogenic / likely-pathogenic of 109 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Developmental dysplasia of the hip
• Developmental dysplasia of the hip 4

Disease | AutoantibodyPubMed

Conditions in which antibodies against TRIM33 are reported. Each links to that disease's full target list.

• Dermatomyositis 103
• Myositis 42
• Lung Diseases, Interstitial 12
• Lung Neoplasms 8
• Polymyositis 5
• Adenocarcinoma 3
• Breast Neoplasms 3

Showing 7 of 9 — disease pages carrying at least 10 antigens.

ReferencesPubMed · IEDB

Publications for TRIM33 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.09

gnomAD pLI

1

gnomAD missense Z

4.49

DepMap mean gene effect

-0.06

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• negative regulation of BMP signaling pathway
• negative regulation of DNA-templated transcription
• negative regulation of transcription by RNA polymerase II
• protein ubiquitination
• regulation of transforming growth factor beta receptor signaling pathway

Molecular functions

• co-SMAD binding
• DNA binding
• R-SMAD binding
• ubiquitin protein ligase activity
• ubiquitin-protein transferase activity
• zinc ion binding

Cellular components

• chromatin
• nucleoplasm
• nucleus

Protein domainsUniProt · Pfam · InterPro

• B-box-type zinc finger
• Bromodomain
• Zinc finger, RING-type
• Zinc finger, PHD-type
• B-box, C-terminal
• Zinc finger, FYVE/PHD-type
• Zinc finger, RING/FYVE/PHD-type
• Zinc finger, RING-type, conserved site
• Zinc finger, PHD-type, conserved site
• Zinc finger, PHD-finger
• Bromodomain-like superfamily
• Bromodomain
• PHD-finger
• B-box zinc finger

KeywordsUniProt

• Acetylation
• Bromodomain
• Chromosomal rearrangement
• Coiled coil
• DNA-binding
• Isopeptide bond
• Metal-binding
• Methylation
• Nucleus
• Phosphoprotein
• Repeat
• Repressor
• Transcription
• Transcription regulation
• Transferase
• Ubl conjugation
• Ubl conjugation pathway
• Zinc
• Zinc-finger

InteractionsUniProt · HPA

Protein binding partners of TRIM33 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• SMAD2
• SMAD3
• SMAD4
• JUN
• SSRP1
• TRIM24
• TRIM28