TRIM9

Protein identityUniProt · HPA

UniProt accession

Q9C026

Gene

TRIM9

Ensembl

ENSG00000100505

Chromosome

14

Canonical length

710 aa

Protein class

Enzymes, Predicted intracellular proteins

OverviewNCBI Gene

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

710 residues, UniProt reviewed canonical sequence.

>Q9C026|TRIM9
     1  MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY
    61  DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV
   121  PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
   181  MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
   241  CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN
   301  MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
   361  RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
   421  PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD
   481  DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF
   541  DPGSAHSDII LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR
   601  MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKNLTF
   661  FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TRIM9 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)

0.38

Highest tissue expression

46 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about TRIM9.

Disease | ImmuneIEDB

Conditions an epitope on TRIM9 was assayed in.

• encephalitis B cell
• lung adenocarcinoma B cell

ReferencesPubMed · IEDB

Publications for TRIM9 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. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). 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)

0.17

gnomAD pLI

1

gnomAD missense Z

3.01

DepMap mean gene effect

-0.23

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• proteasome-mediated ubiquitin-dependent protein catabolic process
• protein ubiquitination

Molecular functions

• protein domain specific binding
• protein homodimerization activity
• ubiquitin protein ligase activity
• zinc ion binding

Cellular components

• cytoplasm
• cytoskeleton
• dendrite
• synaptic vesicle

Protein domainsUniProt · Pfam · InterPro

• B-box-type zinc finger
• Zinc finger, RING-type
• B30.2/SPRY domain
• B-box, C-terminal
• SPRY domain
• Fibronectin type III
• Zinc finger, RING/FYVE/PHD-type
• Concanavalin A-like lectin/glucanase domain superfamily
• Immunoglobulin-like fold
• COS domain
• Zinc finger, RING-type, conserved site
• Zinc finger, C3HC4 RING-type
• Fibronectin type III superfamily
• B30.2/SPRY domain superfamily
• E3 ubiquitin-protein ligases and FN3/SPRY domain-containing proteins
• Fibronectin type III domain
• Zinc finger, C3HC4 type (RING finger)
• SPRY domain
• B-box zinc finger
• ANCHR-like B-box zinc-binding domain
• Tripartite motif-containing protein 9, B-box-type 1 zinc finger

KeywordsUniProt

• Cell projection
• Coiled coil
• Cytoplasm
• Cytoplasmic vesicle
• Cytoskeleton
• Metal-binding
• Phosphoprotein
• Repeat
• Synapse
• Transferase
• Ubl conjugation
• Ubl conjugation pathway
• Zinc
• Zinc-finger

InteractionsUniProt · HPA

Protein binding partners of TRIM9 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• SNAP25
• BTRC
• EXOC1
• VASP