CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020425
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM9 
Protein Synonyms/Alias
 RING finger protein 91; Tripartite motif-containing protein 9 
Gene Name
 TRIM9 
Gene Synonyms/Alias
 KIAA0282; RNF91 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
347KEHEHKLKVVRDQISphosphoglycerylation[1]
Reference
 [1] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
Functional Description
 E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation. 
Sequence Annotation
 DOMAIN 374 432 COS.
 DOMAIN 439 532 Fibronectin type-III.
 DOMAIN 533 702 B30.2/SPRY.
 ZN_FING 10 50 RING-type.
 ZN_FING 163 212 B box-type 1.
 ZN_FING 224 266 B box-type 2.  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Ligase; Metal-binding; Polymorphism; Reference proteome; Repeat; Synapse; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 710 AA 
Protein Sequence
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY 60
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV 120
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV 180
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY 240
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN 300
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL 360
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS 420
PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD 480
DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF 540
DPGSAHSDII LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR 600
MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKNLTF 660
FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA 710 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0030425; C:dendrite; IDA:UniProtKB.
 GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Compara.
 GO:0035544; P:negative regulation of SNARE complex assembly; IEA:Compara.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0016079; P:synaptic vesicle exocytosis; IEA:Compara. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003649; Bbox_C.
 IPR008985; ConA-like_lec_gl_sf.
 IPR017903; COS_domain.
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00041; fn3
 PF00622; SPRY
 PF00643; zf-B_box 
SMART
 SM00502; BBC
 SM00336; BBOX
 SM00060; FN3
 SM00184; RING 
PROSITE
 PS50188; B302_SPRY
 PS51262; COS
 PS50853; FN3
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS