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Q13049 (TRI32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM32

EC=6.3.2.-
Alternative name(s):
72 kDa Tat-interacting protein
Tripartite motif-containing protein 32
Zinc finger protein HT2A
Gene names
Name:TRIM32
Synonyms:HT2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Ref.6 Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with DTNBP1. It self-associates. Ref.6

Subcellular location

Cytoplasm. Note: Localized in cytoplasmic bodies, often located around the nucleus.

Tissue specificity

Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle. Ref.9

Post-translational modification

Ubiquitinated. Ref.6

Involvement in disease

Limb-girdle muscular dystrophy 2H (LGMD2H) [MIM:254110]: An autosomal recessive degenerative myopathy characterized by pelvic girdle, shoulder girdle and quadriceps muscle weakness. Clinical phenotype and severity are highly variable. Disease progression is slow and most patients remain ambulatory into the sixth decade of life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11

Bardet-Biedl syndrome 11 (BBS11) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. It has been suggested that TRIM32 might be the E3 ubiquitin ligase for BBS2, a component of the BBSome complex involved in ciliogenesis, that is ubiquitinated and degraded by the proteasome (Ref.7). Ref.10

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 5 NHL repeats.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseBardet-Biedl syndrome
Ciliopathy
Disease mutation
Limb-girdle muscular dystrophy
Mental retardation
Obesity
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfat cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

innate immune response

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

negative regulation of viral release from host cell

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of viral transcription

Inferred from direct assay PubMed 18248090. Source: UniProt

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay PubMed 23077300. Source: UniProt

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 23077300. Source: UniProt

positive regulation of cell cycle

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

positive regulation of cell growth

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

positive regulation of cell migration

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

positive regulation of cell motility

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of proteolysis

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 23077300. Source: UniProt

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

protein polyubiquitination

Inferred from direct assay PubMed 18632609. Source: BHF-UCL

protein ubiquitination

Inferred from direct assay PubMed 16816390. Source: BHF-UCL

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of type I interferon production

Traceable author statement. Source: Reactome

response to UV

Inferred from sequence or structural similarity. Source: BHF-UCL

response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

striated muscle myosin thick filament

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Tat protein binding

Traceable author statement PubMed 16175175. Source: BHF-UCL

myosin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein self-association

Inferred from direct assay Ref.6. Source: UniProtKB

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

translation initiation factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

ubiquitin binding

Inferred from direct assay Ref.6. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.6. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 653652E3 ubiquitin-protein ligase TRIM32
PRO_0000056246

Regions

Repeat358 – 40144NHL 1
Repeat415 – 45844NHL 2
Repeat459 – 49941NHL 3
Repeat562 – 60544NHL 4
Repeat606 – 64641NHL 5
Zinc finger20 – 6546RING-type
Zinc finger103 – 13331B box-type
Coiled coil138 – 19760 Potential
Compositional bias2 – 65Poly-Ala

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Natural variations

Natural variant1301P → S in BBS11. Ref.10
VAR_038807
Natural variant2571T → R.
Corresponds to variant rs3747834 [ dbSNP | Ensembl ].
VAR_038808
Natural variant2991R → Q in a patient with Bardet-Biedl syndrome; unknown pathological significance. Ref.12
VAR_066295
Natural variant3941R → H in LGMD2H. Ref.11
VAR_042939
Natural variant4081R → C.
Corresponds to variant rs3747835 [ dbSNP | Ensembl ].
VAR_038809
Natural variant4871D → N in LGMD2H. Ref.9
VAR_018725
Natural variant5881Missing in LGMD2H. Ref.11
VAR_042940

Experimental info

Sequence conflict271F → I in AAA86474. Ref.1

Secondary structure

................. 653
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13049 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: D83B1595CA8378FD

FASTA65371,989
        10         20         30         40         50         60 
MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR 

        70         80         90        100        110        120 
CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC 

       130        140        150        160        170        180 
EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR 

       190        200        210        220        230        240 
YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD 

       250        260        270        280        290        300 
YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT 

       310        320        330        340        350        360 
VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK 

       370        380        390        400        410        420 
MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS 

       430        440        450        460        470        480 
FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS 

       490        500        510        520        530        540 
GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR 

       550        560        570        580        590        600 
QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL 

       610        620        630        640        650 
HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins."
Fridell R.A., Harding L.S., Bogerd H.P., Cullen B.R.
Virology 209:347-357(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[4]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-15; 51-60; 70-101; 205-238; 248-282; 345-359; 467-500; 587-596 AND 605-613, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"TRIM32 is an E3 ubiquitin ligase for dysbindin."
Locke M., Tinsley C.L., Benson M.A., Blake D.J.
Hum. Mol. Genet. 18:2344-2358(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION, SELF-ASSOCIATION, INTERACTION WITH DTNBP1.
[7]"Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable Bardet-Biedl syndrome protein complex, the BBSome."
Zhang Q., Yu D., Seo S., Stone E.M., Sheffield V.C.
J. Biol. Chem. 287:20625-20635(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Solution structure of the RING domain of the tripartite motif protein 32."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 10-84.
[9]"Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene."
Frosk P., Weiler T., Nylen E., Sudha T., Greenberg C.R., Morgan K., Fujiwara T.M., Wrogemann K.
Am. J. Hum. Genet. 70:663-672(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD2H ASN-487, TISSUE SPECIFICITY.
[10]"Homozygosity mapping with SNP arrays identifies TRIM32, an E3 ubiquitin ligase, as a Bardet-Biedl syndrome gene (BBS11)."
Chiang A.P., Beck J.S., Yen H.-J., Tayeh M.K., Scheetz T.E., Swiderski R.E., Nishimura D.Y., Braun T.A., Kim K.-Y.A., Huang J., Elbedour K., Carmi R., Slusarski D.C., Casavant T.L., Stone E.M., Sheffield V.C.
Proc. Natl. Acad. Sci. U.S.A. 103:6287-6292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS11 SER-130.
[11]"Mutations that impair interaction properties of TRIM32 associated with limb-girdle muscular dystrophy 2H."
Saccone V., Palmieri M., Passamano L., Piluso G., Meroni G., Politano L., Nigro V.
Hum. Mutat. 29:240-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD2H HIS-394 AND ASP-588 DEL.
[12]"BBS genotype-phenotype assessment of a multiethnic patient cohort calls for a revision of the disease definition."
Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., Jacobson S.G., Innes A.M. expand/collapse author list , Mitchell G.A., Boycott K., Heon E.
Hum. Mutat. 32:610-619(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-299.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18543 mRNA. Translation: AAA86474.1.
AL133284 Genomic DNA. Translation: CAB92723.1.
BC003154 mRNA. Translation: AAH03154.1.
CCDSCCDS6817.1.
RefSeqNP_001093149.1. NM_001099679.1.
NP_036342.2. NM_012210.3.
XP_005251870.1. XM_005251813.1.
UniGeneHs.591910.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT2NMR-A10-84[»]
ProteinModelPortalQ13049.
SMRQ13049. Positions 3-90, 353-594, 614-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116608. 51 interactions.
IntActQ13049. 18 interactions.
MINTMINT-2854880.
STRING9606.ENSP00000363095.

PTM databases

PhosphoSiteQ13049.

Polymorphism databases

DMDM20178303.

Proteomic databases

MaxQBQ13049.
PaxDbQ13049.
PRIDEQ13049.

Protocols and materials databases

DNASU22954.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373983; ENSP00000363095; ENSG00000119401.
ENST00000450136; ENSP00000408292; ENSG00000119401.
GeneID22954.
KEGGhsa:22954.
UCSCuc004bjw.2. human.

Organism-specific databases

CTD22954.
GeneCardsGC09P119449.
GeneReviewsTRIM32.
HGNCHGNC:16380. TRIM32.
HPAHPA050060.
MIM209900. phenotype.
254110. phenotype.
602290. gene.
neXtProtNX_Q13049.
Orphanet1878. Autosomal recessive limb-girdle muscular dystrophy type 2H.
110. Bardet-Biedl syndrome.
PharmGKBPA38130.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269289.
HOGENOMHOG000120114.
HOVERGENHBG060344.
InParanoidQ13049.
KOK10607.
OMAGHTICRQ.
OrthoDBEOG7BCNB8.
PhylomeDBQ13049.
TreeFamTF331018.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ13049.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13049.
BgeeQ13049.
CleanExHS_TRIM32.
GenevestigatorQ13049.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
3.30.40.10. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF01436. NHL. 3 hits.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS51125. NHL. 5 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13049.
GeneWikiTRIM32.
GenomeRNAi22954.
NextBio43741.
PROQ13049.
SOURCESearch...

Entry information

Entry nameTRI32_HUMAN
AccessionPrimary (citable) accession number: Q13049
Secondary accession number(s): Q9NQP8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM