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Identification
HMDB Protein ID HMDBP09271
Secondary Accession Numbers
  • 15099
Name E3 ubiquitin-protein ligase TRIM32
Synonyms
  1. 72 kDa Tat-interacting protein
  2. Tripartite motif-containing protein 32
  3. Zinc finger protein HT2A
Gene Name TRIM32
Protein Type Enzyme
Biological Properties
General Function Involved in zinc ion binding
Specific Function Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
zinc ion binding
protein binding
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location Chromosome:9
Locus 9q33.1
SNPs TRIM32
Gene Sequence
>1962 bp
ATGGCTGCAGCAGCAGCTTCTCACCTGAACCTGGATGCCCTCCGGGAAGTGCTAGAATGC
CCCATCTGCATGGAGTCCTTCACAGAAGAGCAGCTGCGTCCCAAGCTTCTGCACTGTGGC
CATACCATCTGCCGCCAGTGCCTGGAGAAGCTATTGGCCAGTAGCATCAATGGTGTCCGC
TGTCCCTTTTGCAGCAAGATTACCCGCATAACCAGCTTGACCCAGCTGACAGACAATCTG
ACAGTGCTAAAGATCATTGATACAGCTGGGCTCAGCGAGGCTGTGGGGCTGCTCATGTGT
CGGTCCTGTGGGCGGCGTCTGCCCCGGCAATTCTGCCGGAGCTGTGGTTTGGTGTTATGT
GAGCCCTGCCGGGAGGCAGACCATCAGCCTCCTGGCCACTGTACACTCCCTGTCAAAGAA
GCAGCTGAGGAGCGGCGTCGGGACTTTGGAGAGAAGTTAACTCGTCTGCGGGAACTTATG
GGGGAGCTGCAGCGGCGGAAGGCAGCCTTGGAAGGTGTCTCCAAGGACCTTCAGGCAAGG
TATAAAGCAGTTCTCCAGGAGTATGGGCATGAGGAGCGCAGGGTCCAGGATGAGCTGGCT
CGCTCTCGGAAGTTCTTCACAGGCTCTTTGGCTGAAGTTGAGAAGTCCAATAGTCAAGTG
GTAGAGGAGCAGAGTTACCTGCTTAACATTGCAGAGGTGCAGGCTGTGTCTCGCTGTGAC
TACTTCCTGGCCAAGATCAAGCAGGCAGATGTAGCACTACTGGAGGAGACAGCTGATGAG
GAGGAGCCAGAGCTCACTGCCAGCTTGCCTCGGGAGCTCACCCTGCAAGATGTGGAGCTC
CTTAAGGTAGGTCATGTTGGCCCCCTCCAAATTGGACAAGCTGTTAAGAAGCCCCGGACA
GTTAACGTGGAAGATTCCTGGGCCATGGAGGCCACAGCGTCTGCTGCCTCTACCTCTGTT
ACTTTTAGAGAGATGGACATGAGCCCGGAGGAAGTGGTTGCCAGCCCTAGGGCCTCACCT
GCTAAACAGCGGGGTCCTGAGGCAGCCTCCAATATCCAGCAGTGCCTCTTTCTCAAGAAG
ATGGGGGCCAAAGGCAGCACTCCAGGAATGTTCAATCTTCCAGTCAGTCTCTACGTGACC
AGTCAAGGTGAAGTACTAGTCGCTGACCGTGGTAACTATCGTATACAAGTCTTTACCCGC
AAAGGCTTTTTGAAGGAAATCCGCCGCAGCCCCAGTGGCATTGATAGCTTTGTGCTAAGC
TTCCTTGGGGCAGATCTACCCAACCTCACTCCTCTCTCAGTGGCAATGAACTGCCAGGGG
CTGATTGGTGTGACTGACAGCTATGATAACTCCCTCAAGGTATATACCTTGGATGGCCAC
TGCGTGGCCTGTCACAGGAGCCAGCTGAGCAAACCATGGGGTATCACAGCCTTGCCATCT
GGCCAGTTTGTAGTAACCGATGTGGAAGGTGGAAAGCTTTGGTGTTTCACAGTTGATCGA
GGATCAGGGGTGGTCAAATACAGCTGCCTATGTAGTGCTGTGCGGCCCAAATTTGTCACC
TGTGATGCTGAGGGCACCGTCTACTTCACCCAGGGCTTAGGCCTCAATCTGGAGAATCGG
CAGAATGAGCACCACCTGGAGGGTGGCTTTTCCATTGGCTCTGTAGGCCCTGATGGGCAG
CTGGGTCGCCAGATTAGCCACTTCTTCTCGGAGAATGAGGATTTCCGCTGCATTGCTGGC
ATGTGTGTGGATGCTCGTGGTGATCTCATCGTGGCTGACAGTAGTCGCAAGGAAATTCTC
CATTTTCCTAAGGGTGGGGGCTATAGTGTCCTTATTCGAGAGGGACTTACCTGTCCGGTG
GGCATAGCCCTAACTCCTAAGGGGCAGCTGCTGGTCTTGGACTGTTGGGATCATTGCATC
AAGATCTACAGCTACCATCTGAGAAGATATTCCACCCCATAG
Protein Properties
Number of Residues 653
Molecular Weight 71987.9
Theoretical pI 6.98
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>E3 ubiquitin-protein ligase TRIM32
MAAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVR
CPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRSCGRRLPRQFCRSCGLVLC
EPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELMGELQRRKAALEGVSKDLQAR
YKAVLQEYGHEERRVQDELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCD
YFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRT
VNVEDSWAMEATASAASTSVTFREMDMSPEEVVASPRASPAKQRGPEAASNIQQCLFLKK
MGAKGSTPGMFNLPVSLYVTSQGEVLVADRGNYRIQVFTRKGFLKEIRRSPSGIDSFVLS
FLGADLPNLTPLSVAMNCQGLIGVTDSYDNSLKVYTLDGHCVACHRSQLSKPWGITALPS
GQFVVTDVEGGKLWCFTVDRGSGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNLENR
QNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEIL
HFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCIKIYSYHLRRYSTP
GenBank ID Protein 8217434
UniProtKB/Swiss-Prot ID Q13049
UniProtKB/Swiss-Prot Entry Name TRI32_HUMAN
PDB IDs Not Available
GenBank Gene ID AL133284
GeneCard ID TRIM32
GenAtlas ID TRIM32
HGNC ID HGNC:16380
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  6. Fridell RA, Harding LS, Bogerd HP, Cullen BR: Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. Virology. 1995 Jun 1;209(2):347-57. [PubMed:7778269 ]
  7. Locke M, Tinsley CL, Benson MA, Blake DJ: TRIM32 is an E3 ubiquitin ligase for dysbindin. Hum Mol Genet. 2009 Jul 1;18(13):2344-58. doi: 10.1093/hmg/ddp167. Epub 2009 Apr 6. [PubMed:19349376 ]
  8. Frosk P, Weiler T, Nylen E, Sudha T, Greenberg CR, Morgan K, Fujiwara TM, Wrogemann K: Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene. Am J Hum Genet. 2002 Mar;70(3):663-72. Epub 2002 Jan 29. [PubMed:11822024 ]
  9. Chiang AP, Beck JS, Yen HJ, Tayeh MK, Scheetz TE, Swiderski RE, Nishimura DY, Braun TA, Kim KY, Huang J, Elbedour K, Carmi R, Slusarski DC, Casavant TL, Stone EM, Sheffield VC: Homozygosity mapping with SNP arrays identifies TRIM32, an E3 ubiquitin ligase, as a Bardet-Biedl syndrome gene (BBS11). Proc Natl Acad Sci U S A. 2006 Apr 18;103(16):6287-92. Epub 2006 Apr 10. [PubMed:16606853 ]
  10. Saccone V, Palmieri M, Passamano L, Piluso G, Meroni G, Politano L, Nigro V: Mutations that impair interaction properties of TRIM32 associated with limb-girdle muscular dystrophy 2H. Hum Mutat. 2008 Feb;29(2):240-7. [PubMed:17994549 ]