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Protein

E3 ubiquitin-protein ligase TRIM32

Gene

TRIM32

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

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
Zinc fingeri20 – 65RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri103 – 133B box-typePROSITE-ProRule annotationAdd BLAST31

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • myosin binding Source: BHF-UCL
  • protein self-association Source: UniProtKB
  • RNA binding Source: BHF-UCL
  • Tat protein binding Source: BHF-UCL
  • transcription coactivator activity Source: ProtInc
  • translation initiation factor binding Source: BHF-UCL
  • ubiquitin binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13049.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM32 (EC:2.3.2.27)
Alternative name(s):
72 kDa Tat-interacting protein
RING-type E3 ubiquitin transferase TRIM32Curated
Tripartite motif-containing protein 32
Zinc finger protein HT2A
Gene namesi
Name:TRIM32
Synonyms:HT2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000119401.10.
HGNCiHGNC:16380. TRIM32.

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Limb-girdle muscular dystrophy 2H (LGMD2H)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:254110
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042939394R → H in LGMD2H. 1 PublicationCorresponds to variant dbSNP:rs121434447Ensembl.1
Natural variantiVAR_018725487D → N in LGMD2H. 1 PublicationCorresponds to variant dbSNP:rs111033570Ensembl.1
Natural variantiVAR_042940588Missing in LGMD2H. 1 Publication1
Bardet-Biedl syndrome 11 (BBS11)1 Publication
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 (PubMed:22500027).1 Publication
Disease descriptionA 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.
See also OMIM:615988
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038807130P → S in BBS11. 1 PublicationCorresponds to variant dbSNP:rs111033571Ensembl.1

Keywords - Diseasei

Bardet-Biedl syndrome, Ciliopathy, Disease mutation, Limb-girdle muscular dystrophy, Mental retardation, Obesity

Organism-specific databases

DisGeNETi22954.
GeneReviewsiTRIM32.
MalaCardsiTRIM32.
MIMi254110. phenotype.
615988. phenotype.
OpenTargetsiENSG00000119401.
Orphaneti1878. Autosomal recessive limb-girdle muscular dystrophy type 2H.
110. Bardet-Biedl syndrome.
PharmGKBiPA38130.

Polymorphism and mutation databases

BioMutaiTRIM32.
DMDMi20178303.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000562462 – 653E3 ubiquitin-protein ligase TRIM32Add BLAST652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei328PhosphoserineBy similarity1
Modified residuei335PhosphoserineCombined sources1
Modified residuei339PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13049.
MaxQBiQ13049.
PaxDbiQ13049.
PeptideAtlasiQ13049.
PRIDEiQ13049.

PTM databases

iPTMnetiQ13049.
PhosphoSitePlusiQ13049.

Expressioni

Tissue specificityi

Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle.1 Publication

Gene expression databases

BgeeiENSG00000119401.
CleanExiHS_TRIM32.
ExpressionAtlasiQ13049. baseline and differential.
GenevisibleiQ13049. HS.

Organism-specific databases

HPAiHPA050060.

Interactioni

Subunit structurei

Interacts with DTNBP1. It self-associates.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • myosin binding Source: BHF-UCL
  • protein self-association Source: UniProtKB
  • Tat protein binding Source: BHF-UCL
  • translation initiation factor binding Source: BHF-UCL
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116608. 86 interactors.
CORUMiQ13049.
IntActiQ13049. 56 interactors.
MINTiMINT-2854880.
STRINGi9606.ENSP00000363095.

Structurei

Secondary structure

1653
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 16Combined sources6
Turni21 – 23Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi42 – 44Combined sources3
Helixi45 – 51Combined sources7
Beta strandi62 – 64Combined sources3
Turni73 – 75Combined sources3
Beta strandi76 – 78Combined sources3
Helixi80 – 85Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CT2NMR-A10-84[»]
5FEYX-ray2.23A/B7-93[»]
ProteinModelPortaliQ13049.
SMRiQ13049.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13049.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati358 – 401NHL 1Add BLAST44
Repeati415 – 458NHL 2Add BLAST44
Repeati459 – 499NHL 3Add BLAST41
Repeati562 – 605NHL 4Add BLAST44
Repeati606 – 646NHL 5Add BLAST41

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili138 – 197Sequence analysisAdd BLAST60

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 6Poly-Ala5

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri20 – 65RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri103 – 133B box-typePROSITE-ProRule annotationAdd BLAST31

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITFD. Eukaryota.
ENOG410XRCH. LUCA.
GeneTreeiENSGT00890000139359.
HOGENOMiHOG000120114.
HOVERGENiHBG060344.
InParanoidiQ13049.
KOiK10607.
OMAiCITGMCV.
OrthoDBiEOG091G0KUF.
PhylomeDBiQ13049.
TreeFamiTF331018.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR011042. 6-blade_b-propeller_TolB-like.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR033569. TRIM32.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
PANTHERiPTHR24103:SF430. PTHR24103:SF430. 1 hit.
PfamiView protein in Pfam
PF01436. NHL. 3 hits.
PF13445. zf-RING_UBOX. 1 hit.
SMARTiView protein in SMART
SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS51125. NHL. 5 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK
60 70 80 90 100
LLASSINGVR CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC
110 120 130 140 150
RSCGRRLPRQ FCRSCGLVLC EPCREADHQP PGHCTLPVKE AAEERRRDFG
160 170 180 190 200
EKLTRLRELM GELQRRKAAL EGVSKDLQAR YKAVLQEYGH EERRVQDELA
210 220 230 240 250
RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD YFLAKIKQAD
260 270 280 290 300
VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT
310 320 330 340 350
VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS
360 370 380 390 400
NIQQCLFLKK MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR
410 420 430 440 450
KGFLKEIRRS PSGIDSFVLS FLGADLPNLT PLSVAMNCQG LIGVTDSYDN
460 470 480 490 500
SLKVYTLDGH CVACHRSQLS KPWGITALPS GQFVVTDVEG GKLWCFTVDR
510 520 530 540 550
GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR QNEHHLEGGF
560 570 580 590 600
SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL
610 620 630 640 650
HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY

STP
Length:653
Mass (Da):71,989
Last modified:April 16, 2002 - v2
Checksum:iD83B1595CA8378FD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27F → I in AAA86474 (PubMed:7778269).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038807130P → S in BBS11. 1 PublicationCorresponds to variant dbSNP:rs111033571Ensembl.1
Natural variantiVAR_038808257T → R. Corresponds to variant dbSNP:rs3747834Ensembl.1
Natural variantiVAR_066295299R → Q in a patient with Bardet-Biedl syndrome; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766439806Ensembl.1
Natural variantiVAR_042939394R → H in LGMD2H. 1 PublicationCorresponds to variant dbSNP:rs121434447Ensembl.1
Natural variantiVAR_038809408R → C. Corresponds to variant dbSNP:rs3747835Ensembl.1
Natural variantiVAR_018725487D → N in LGMD2H. 1 PublicationCorresponds to variant dbSNP:rs111033570Ensembl.1
Natural variantiVAR_042940588Missing in LGMD2H. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18543 mRNA. Translation: AAA86474.1.
AL133284 Genomic DNA. No translation available.
BC003154 mRNA. Translation: AAH03154.1.
CCDSiCCDS6817.1.
RefSeqiNP_001093149.1. NM_001099679.1.
NP_036342.2. NM_012210.3.
XP_005251870.1. XM_005251813.3.
XP_011516700.1. XM_011518398.2.
XP_016869975.1. XM_017014486.1.
UniGeneiHs.591910.

Genome annotation databases

EnsembliENST00000373983; ENSP00000363095; ENSG00000119401.
ENST00000450136; ENSP00000408292; ENSG00000119401.
GeneIDi22954.
KEGGihsa:22954.
UCSCiuc004bjw.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTRI32_HUMAN
AccessioniPrimary (citable) accession number: Q13049
Secondary accession number(s): Q9NQP8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 16, 2002
Last modified: September 27, 2017
This is version 190 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families