| Tag | Content |
|---|
| CPLM ID | CPLM-018617 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase TRIM9 |
Protein Synonyms/Alias | SNAP-25-interacting RING finger protein; Tripartite motif-containing protein 9 |
Gene Name | Trim9 |
Gene Synonyms/Alias | Spring |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 271 | KALGAMWKLHKSQLS | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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 (By similarity). 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 | Cell junction; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Ligase; Metal-binding; 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 TPESESPQSR RASGSGVSDY 60
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPP THLSPALAPV 120
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV 180
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY 240
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRT 300
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL 360
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS 420
PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV AADGYILELD 480
DGSGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF 540
DPGSAHSDII FSNDNLTVTC SSYDDRVVLG KTGFSKGVHY WELTIDRYDN HPDPAFGVAR 600
IDVMKDMMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKTLTF 660
FVNNEQQGPI AFENVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA 710 |
Gene Ontology | GO:0030054; C:cell junction; IEA:UniProtKB-KW. GO:0005856; C:cytoskeleton; IDA:RGD. GO:0030425; C:dendrite; ISS:UniProtKB. GO:0008021; C:synaptic vesicle; IDA:RGD. GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:RGD. GO:0035544; P:negative regulation of SNARE complex assembly; IDA:RGD. GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. GO:0016079; P:synaptic vesicle exocytosis; IEP:RGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |