| Tag | Content |
|---|
| CPLM ID | CPLM-023400 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable phosphorylase b kinase regulatory subunit beta |
Protein Synonyms/Alias | Phosphorylase kinase subunit beta |
Gene Name | CG8475 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 929 | VPKHFYNKIWEILQR | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation (By similarity). |
Sequence Annotation | REGION 6 27 Calmodulin-binding (Potential).
REGION 751 778 Calmodulin-binding (Potential).
REGION 905 936 Calmodulin-binding (Potential).
LIPID 1090 1090 S-farnesyl cysteine (By similarity). |
Keyword | Alternative splicing; Calmodulin-binding; Carbohydrate metabolism; Cell membrane; Complete proteome; Glycogen metabolism; Lipoprotein; Membrane; Prenylation; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1093 AA |
Protein Sequence | MRDVPKSLGL SVTTPGGSSG APDSGRHNSL EEINLDQFLK TSNYEDTVKQ LDIYYGIVKR 60
QLLRYQSPIT GLFPVMSTDQ VVGSVRDSVY CASAVWSLYQ AYRRIDDDRG KSYELGQSTV 120
KCMRGILECW VKQASRVELF KQRQSNQHAL HSKFQLHTGE KIYPDEFYNH LQIDCVSLYL 180
LFLVQMITSG LQIIYTHDEV AFVQNLVYYV ERAYRTPDFG MWERGSKYNN GTPEIHASSI 240
GMAKSALEAI NGCNLFGEKG ASWSVVYVDI DAHNRNRSIF ETMLPRESSS KGVDASLLLT 300
LSFPAFASHE DRLVEQTKQN VVNRLRCKMG FKRFTRDGFL SKNEDKSRRY YHSGELKEFE 360
GLECEWPLFF IAMIIDGVFK NNNEQIEEFQ NDLRRCLRTD VNGDPVVTMY YAPDGDGSYM 420
RAPSQSLFLW GQSFFIIAQL LTAGLLHINE LDPIRRYLPS YNRPRRAGRY SAFQGTATDL 480
VVQIVLIAES MRLQAMMATY GIQTQTPHEV EPVQIWSSTE LIKVYQHLGV NNKVGLSGRP 540
CRPVGSLGTS KVYRICGMTV LCYPLIFEVS DFYLYRDMAL LIDDIKTELQ FVGKYWRLSG 600
RPTVCLLIRE EHMRDPQFKE MLDLLAMLKK GYCDGMKVRI GRLQNLISSS CIEHLDFMNQ 660
SDLTDNENAF SQINHEYIGY QSLTDVPKAL TYVEEKISVA HFDTKPTPDI INALRSTDSI 720
YCLCQLWGII LNREGPHFEV NGLNVNTALT QLYHRAGSLR YWRAVRYCSS LLHHIVDSIS 780
PFITTVLVNG KELTVGIIGQ KETVFDKPMT PAEIQNVMYT SVQPYDVIQA VLQQEVVLYC 840
GRLIATNPSM FRGILKIRIG WVLEAMRIYL QISGQQSIDV DNLSPFQVRI LLQKVLTVSE 900
WAVEEKLTTL QRRQLEGCLC RVPKHFYNKI WEILQRTPQG ILTQGHHLPA TPTLTNMSRG 960
ELTFNLLVEE TLICIDRPER RQITVELLCI VATILNRNPE LHFKQALDLD GILAEAFAMY 1020
CKDNNIQHQP KPEHEQTKNE DLKAFYSLPY SETTGYLARA AVNKVLQGGI FSTNEEDVQL 1080
DGDRLHDDNC KVS 1093 |
Gene Ontology | GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |