CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017108
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM22 
Protein Synonyms/Alias
 50 kDa-stimulated trans-acting factor; RING finger protein 94; Staf-50; Tripartite motif-containing protein 22 
Gene Name
 TRIM22 
Gene Synonyms/Alias
 RNF94; STAF50 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
173RQERTAWKNYIQIERubiquitination[1]
396DPSVNYSKVYSRYRPubiquitination[1]
Reference
 [1] 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] 
Functional Description
 Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitination of viral proteins. Plays a role in restricting the replication of HIV-1, encephalomyocarditis virus (EMCV) and hepatitis B virus (HBV). Acts as a transcriptional repressor of HBV core promoter. May have E3 ubiquitin-protein ligase activity. 
Sequence Annotation
 DOMAIN 283 498 B30.2/SPRY.
 ZN_FING 15 60 RING-type.
 ZN_FING 92 133 B box-type.
 MOTIF 257 275 Nuclear localization signal (Potential).  
Keyword
 Alternative splicing; Antiviral defense; Coiled coil; Complete proteome; Cytoplasm; Host-virus interaction; Ligase; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 498 AA 
Protein Sequence
MDFSVKVDIE KEVTCPICLE LLTEPLSLDC GHSFCQACIT AKIKESVIIS RGESSCPVCQ 60
TRFQPGNLRP NRHLANIVER VKEVKMSPQE GQKRDVCEHH GKKLQIFCKE DGKVICWVCE 120
LSQEHQGHQT FRINEVVKEC QEKLQVALQR LIKEDQEAEK LEDDIRQERT AWKNYIQIER 180
QKILKGFNEM RVILDNEEQR ELQKLEEGEV NVLDNLAAAT DQLVQQRQDA STLISDLQRR 240
LRGSSVEMLQ DVIDVMKRSE SWTLKKPKSV SKKLKSVFRV PDLSGMLQVL KELTDVQYYW 300
VDVMLNPGSA TSNVAISVDQ RQVKTVRTCT FKNSNPCDFS AFGVFGCQYF SSGKYYWEVD 360
VSGKIAWILG VHSKISSLNK RKSSGFAFDP SVNYSKVYSR YRPQYGYWVI GLQNTCEYNA 420
FEDSSSSDPK VLTLFMAVPP CRIGVFLDYE AGIVSFFNVT NHGALIYKFS GCRFSRPAYP 480
YFNPWNCLVP MTVCPPSS 498 
Gene Ontology
 GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0006955; P:immune response; TAS:ProtInc.
 GO:0070206; P:protein trimerization; IDA:UniProtKB.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0009615; P:response to virus; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00622; SPRY
 PF00643; zf-B_box 
SMART
 SM00336; BBOX
 SM00184; RING 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.