CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012301
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin/ISG15 ligase TRIM25 
Protein Synonyms/Alias
 Estrogen-responsive finger protein; RING finger protein 147; Tripartite motif-containing protein 25; Ubiquitin/ISG15-conjugating enzyme TRIM25; Zinc finger protein 147 
Gene Name
 TRIM25 
Gene Synonyms/Alias
 EFP; RNF147; ZNF147 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
112VACDHCLKEAAVKTCubiquitination[1, 2]
117CLKEAAVKTCLVCMAubiquitination[1, 3]
205LEATLRHKLTVMYSQubiquitination[4]
237VRMTANRKVEQLQQEacetylation[5]
237VRMTANRKVEQLQQEubiquitination[1, 2, 4]
249QQEYTEMKALLDASEubiquitination[4]
273EEKRVNSKFDTIYQIacetylation[5, 6]
273EEKRVNSKFDTIYQIubiquitination[1, 4, 7, 8]
283TIYQILLKKKSEIQTubiquitination[3, 4, 7, 8]
284IYQILLKKKSEIQTLubiquitination[1]
292KSEIQTLKEEIEQSLubiquitination[4]
301EIEQSLTKRDEFEFLubiquitination[4]
310DEFEFLEKASKLRGIubiquitination[1, 4]
320KLRGISTKPVYIPEVacetylation[6]
320KLRGISTKPVYIPEVubiquitination[1, 2, 7, 8]
332PEVELNHKLIKGIHQubiquitination[1]
335ELNHKLIKGIHQSTIacetylation[5]
335ELNHKLIKGIHQSTIubiquitination[2, 7]
345HQSTIDLKNELKQCIubiquitination[1, 4]
349IDLKNELKQCIGRLQubiquitination[1]
392KEEKKSKKPPPVPALubiquitination[1, 4, 8]
402PVPALPSKLPTFGAPubiquitination[1, 2, 4, 8]
416PEQLVDLKQAGLEAAubiquitination[1, 3, 4, 8]
425AGLEAAAKATSSHPNubiquitination[1, 2, 4]
437HPNSTSLKAKVLETFubiquitination[1]
439NSTSLKAKVLETFLAubiquitination[1, 2, 4]
447VLETFLAKSRPELLEubiquitination[1, 2]
508VLGLHCYKKGIHYWEubiquitination[1]
509LGLHCYKKGIHYWEVubiquitination[1, 2, 4]
567AWHNNVEKTLPSTKAacetylation[6, 9]
567AWHNNVEKTLPSTKAubiquitination[1, 2, 7]
573EKTLPSTKATRVGVLubiquitination[1, 2]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] 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]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
Functional Description
 Functions as an ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. 
Sequence Annotation
 DOMAIN 439 630 B30.2/SPRY.
 ZN_FING 13 54 RING-type.
 REGION 180 450 Interaction with influenza A virus NS1.
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 273 273 N6-acetyllysine.
 MOD_RES 567 567 N6-acetyllysine.
 CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Antiviral defense; Coiled coil; Complete proteome; Cytoplasm; Host-virus interaction; Immunity; Innate immunity; Isopeptide bond; Ligase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 630 AA 
Protein Sequence
MAELCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGSPYLC PQCRAVYQAR 60
PQLHKNTVLC NVVEQFLQAD LAREPPADVW TPPARASAPS PNAQVACDHC LKEAAVKTCL 120
VCMASFCQEH LQPHFDSPAF QDHPLQPPVR DLLRRKCSQH NRLREFFCPE HSECICHICL 180
VEHKTCSPAS LSQASADLEA TLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ 240
LQQEYTEMKA LLDASETTST RKIKEEEKRV NSKFDTIYQI LLKKKSEIQT LKEEIEQSLT 300
KRDEFEFLEK ASKLRGISTK PVYIPEVELN HKLIKGIHQS TIDLKNELKQ CIGRLQEPTP 360
SSGDPGEHDP ASTHKSTRPV KKVSKEEKKS KKPPPVPALP SKLPTFGAPE QLVDLKQAGL 420
EAAAKATSSH PNSTSLKAKV LETFLAKSRP ELLEYYIKVI LDYNTAHNKV ALSECYTVAS 480
VAEMPQNYRP HPQRFTYCSQ VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES 540
RLGRNSASWC VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADKVHLM 600
YKFRVDFTEA LYPAFWVFSA GATLSICSPK 630 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR006574; PRY.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00622; SPRY 
SMART
 SM00589; PRY
 SM00184; RING
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.