CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019228
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM11 
Protein Synonyms/Alias
 Protein BIA1; RING finger protein 92; Tripartite motif-containing protein 11 
Gene Name
 TRIM11 
Gene Synonyms/Alias
 RNF92 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
136QDAAEDLKAKLEKSLubiquitination[1, 2]
141DLKAKLEKSLEHLRKubiquitination[2]
248LGLLQDIKDALRRVQubiquitination[2]
258LRRVQDVKLQPPEVVubiquitination[1, 2, 3, 4, 5, 6]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. 
Sequence Annotation
 DOMAIN 268 461 B30.2/SPRY.
 ZN_FING 16 57 RING-type.
 ZN_FING 87 128 B box-type.  
Keyword
 Alternative splicing; Antiviral defense; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 468 AA 
Protein Sequence
MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 60
PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA AFCGDELRLL CAACERSGEH 120
WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM QDALLFQAQA DETCVLWQKM VESQRQNVLG 180
EFERLRRLLA EEEQQLLQRL EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA 240
LGLLQDIKDA LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGDVT LDPDTANPEL 300
ILSEDRRSVQ RGDLRQALPD SPERFDPGPC VLGQERFTSG RHYWEVEVGD RTSWALGVCR 360
ENVNRKEKGE LSAGNGFWIL VFLGSYYNSS ERALAPLRDP PRRVGIFLDY EAGHLSFYSA 420
TDGSLLFIFP EIPFSGTLRP LFSPLSSSPT PMTICRPKGG SGDTLAPQ 468 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0050768; P:negative regulation of neurogenesis; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR006574; PRY.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00622; SPRY
 PF00643; zf-B_box
 PF00097; zf-C3HC4 
SMART
 SM00336; BBOX
 SM00589; PRY
 SM00184; RING
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.