| Tag | Content |
|---|
| CPLM ID | CPLM-021864 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Short transient receptor potential channel 4-associated protein |
Protein Synonyms/Alias | Trp4-associated protein; Trpc4-associated protein; Protein TAP1; Rabex-5/Rin2-interacting protein; TNF-receptor ubiquitous scaffolding/signaling protein; Protein TRUSS |
Gene Name | Trpc4ap |
Gene Synonyms/Alias | Trrp4ap |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 263 | MDTGNDDKHTLLAKN | ubiquitination | [1] | | 269 | DKHTLLAKNAQQKKS | ubiquitination | [1] | | 275 | AKNAQQKKSLSLGPS | ubiquitination | [1] | | 303 | GFVERLCKLATRKVS | ubiquitination | [1] | | 557 | ADQMFLLKRGLLEHI | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRUSS) complex specifically mediates the polyubiquitination and subsequent degradation of MYC (By similarity). Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1. |
Sequence Annotation | REGION 1 400 Interaction with TNFRSF1A. |
Keyword | Alternative splicing; Complete proteome; Reference proteome; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 797 AA |
Protein Sequence | MAAAPAAAGA GASRGRRLAA TAAAWGGWGG RPRPGNILLQ LRQGQLTGRG LVRAVQFTET 60
FLTERDKLSK WSGIPQLLLK LYATSHLHSD FVECQSILKE ISPLLSMEAM AFVTEDRKFT 120
QEATYPNTYI FDLFGGVDLL VEILMRPTIS IRGQKLKISD EMSKDCLSIL YNTCVCTEGV 180
TKRLAEKNDF VIFLFTLMTS KKTFLQTATL IEDILGVKKE MIRLDEVPNL SSLVSNFDQQ 240
QLANFCRILA VTISEMDTGN DDKHTLLAKN AQQKKSLSLG PSAAEINQAA LLSIPGFVER 300
LCKLATRKVS ESTGTASFLQ ELEEWYTWLD NALVLDALMR VANEESEHNQ APTVFPSLGT 360
SEEGGLPHTS ARAQLPQSMK IMHEIMYKLE VLYVLCVLLM GRQRNQVHRM IAEFKLIPGL 420
NNLFDKLIWR KHSASALVLH GHNQNCDCSP DITLKIQFLR LLQSFSDHHE NKYLLLNNQE 480
LNELSAISLK ANIPEVEAVL NTDRSLVCDG KRGLLTRLLQ VMKKEPAESS FRFWQARAVE 540
SFLRGTTSYA DQMFLLKRGL LEHILYCIVD SECKSRDVLQ SYFDLLGELM KFNVDAFKRF 600
NKYINTDAKF QVFLKQINSS LVDSNMLVRC VTLSLDRFEN QVDMKVAEVL SECRLLAYIS 660
QVPTQMSFLF RLINIIHVQT LTQENVSCLN TSLVILMLAR RKERLPLYLR LLQRMEHSKK 720
YPGFLLNNFH NLLRFWQQHY LHKDKDSTCL ENSSCISFSY WKETVSILLN PDRQSPSALV 780
SYIEEPYMDI DRDFTEE 797 |
Gene Ontology | GO:0031464; C:Cul4A-RING ubiquitin ligase complex; ISS:UniProtKB. GO:0019902; F:phosphatase binding; ISS:UniProtKB. GO:0016567; P:protein ubiquitination; ISS:UniProtKB. GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |