| Tag | Content |
|---|
| CPLM ID | CPLM-019966 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | BRCA1-associated protein |
Protein Synonyms/Alias | BRAP2; Impedes mitogenic signal propagation; IMP |
Gene Name | Brap |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 78 | DVIIETMKARADEVR | ubiquitination | [1] | | 380 | VHRLVASKTDGKIVQ | ubiquitination | [1] | | 384 | VASKTDGKIVQYECE | ubiquitination | [1] | | 441 | AEEINNMKTKFKETI | ubiquitination | [1] | | 494 | QEEQELNKCLRANQL | ubiquitination | [1] | | 508 | LVLQNQLKEEEKLLK | ubiquitination | [1] | | 579 | PSSGAGGKLQSRKGR | 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 | Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto- polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport (By similarity). |
Sequence Annotation | ZN_FING 263 303 RING-type.
ZN_FING 314 375 UBP-type.
MOD_RES 52 52 Phosphoserine (By similarity).
MOD_RES 116 116 Phosphoserine.
MOD_RES 118 118 Phosphoserine (By similarity). |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 591 AA |
Protein Sequence | MSVSLVVIRL ELAGHSPVPT DFGFSAAAGE MSDEEIKKKT LASAVACLEG KSAGEKAAII 60
HQHLGRREMT DVIIETMKAR ADEVRDTVEE KKPSAAPVSA QRSREQSESV NTAPESPSKQ 120
LPDQISFFSG NPSVEIVHGI MHLYKTNKMT SLKEDVRRSA MLCVLTVPAT MTSHDLMKFV 180
APFNDVIEQM KIIRDSTPNQ YMVLIKFSAQ ADADSFYMAC NGRQFNSIED DVCQLVYVER 240
AEVLKSEDGA SLPVMDLTEL PKCTVCLERM DESVNGILTT LCNHSFHSQC LQRWDDTTCP 300
VCRYCQTPEP VEENKCFECG VQENLWICLI CGHIGCGRYV SRHAYKHFEE TQHTYAMQLT 360
NHRVWDYAGD NYVHRLVASK TDGKIVQYEC EGDTCQEEKI DALQLEYSYL LTSQLESQRI 420
YWENKIVRIE KDTAEEINNM KTKFKETIEK CDSLELRLSD LLKEKQSVER KCTQLNTRVA 480
KLSTELQEEQ ELNKCLRANQ LVLQNQLKEE EKLLKETCAQ KDLQITEIQE QLRDVMFYLE 540
TQQQISHLPA ETRQEIQEGQ INIAMASAPN PPSSGAGGKL QSRKGRSKRG K 591 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0000151; C:ubiquitin ligase complex; IEA:Compara. GO:0008139; F:nuclear localization sequence binding; IEA:Compara. GO:0000166; F:nucleotide binding; IEA:InterPro. GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0000165; P:MAPK cascade; IEA:Compara. GO:0009968; P:negative regulation of signal transduction; IEA:Compara. GO:0007265; P:Ras protein signal transduction; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |