| Tag | Content |
|---|
| CPLM ID | CPLM-015865 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphorylase b kinase regulatory subunit beta |
Protein Synonyms/Alias | Phosphorylase kinase subunit beta |
Gene Name | Phkb |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 670 | LRISDTEKLPEFKSF | ubiquitination | [1] | | 1039 | SRLKEIEKQDDMTSF | 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 | 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 760 787 Calmodulin-binding (Potential).
REGION 912 943 Calmodulin-binding (Potential).
MOD_RES 10 10 Phosphoserine (By similarity).
MOD_RES 19 19 Phosphoserine.
MOD_RES 693 693 Phosphoserine.
LIPID 1082 1082 S-farnesyl cysteine (By similarity). |
Keyword | Calmodulin-binding; Carbohydrate metabolism; Cell membrane; Complete proteome; Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein; Prenylation; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1085 AA |
Protein Sequence | MANSPDAAFS SPALLRSGSV YEPLKSINLP RPDNETLWDK LDHYYRIVKS TMLMYQSPTT 60
GLFPTKTCGG EEKSKVHESL YCAAGAWALA LAYRRIDDDK GRTHELEHSA IKCMRGILYC 120
YMRQADKVQQ FKQDPRPTTC LHSVFSVHTG DELLSYEEYG HLQINAVSLF LLYLVEMISS 180
GLQIIYNTDE VSFIQNLVFC VERVYRVPDF GVWERGSKYN NGSTELHSSS VGLAKAALEA 240
INGFNLFGNQ GCSWSVIFVD LDAHNRNRQT LCSLLPRESR SHNTDAALLP CISYPAFALD 300
DEALFSQTLD KVIRKLKGKY GFKRFLRDGY RTPLEDPNRR YYKPAEIKLF DGIECEFPIF 360
FLYMMIDGVF RGNLEQVKEY QDLLTPLLHQ TTEGYPVVPK YYYVPADFVE CEKRNPGSQK 420
RFPSNCGRDG KLFLWGQALY IIAKLLADEL ISPKDIDPVQ RFVPLQNQRN VSMRYSNQGP 480
LENDLVVHVA LVAESQRLQV FLNTYGIQTQ TPQQVEPIQI WPQQELVKAY FHLGINEKLG 540
LSGRPDRPIG CLGTSKIYRI LGKTVVCYPI IFDLSDFYMS QDVLLLIDDI KNALQFIKQY 600
WKMHGRPLFL VLIREDNIRG SRFNPILDML AAFKKGIIGG VKVHVDRLQT LISGAVVEQL 660
DFLRISDTEK LPEFKSFEEL EFPKHSKVKR QSSTADAPEA QHEPGITITE WKNKSTHEIL 720
QKLNDCGCLA GQTILLGILL KREGPNFITM EGTVSDHIER VYRRAGSKKL WSVVRRAASL 780
LNKVVDSLAP SITNVLVQGK QVTLGAFGHE EEVISNPLSP RVIKNIIYYK CNTHDEREAV 840
IQQELVIHIG WIISNSPELF SGMLKIRIGW IIHAMEYELQ VRGGDKPAVD LYQLSPSEVK 900
QLLLDILQPQ QSGRCWLNRR QIDGSLNRTP PEFYDRVWQI LERTPNGIVV AGKHLPQQPT 960
LSDMTMYEMN FSLLVEDMLG NIDQPKYRQI IVELLMVVSI VLERNPELEF QDKVDLDRLV 1020
KEAFHEFQKD ESRLKEIEKQ DDMTSFYNTP PLGKRGTCSY LTKVVMNSLL EGEVKPSNED 1080
SCLVS 1085 |
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 | |