| Tag |
Content |
LipidDB ID |
LipidDB-9986-00492 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.95 |
Molecular Weight |
125295.01 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Phosphorylase b kinase regulatory subunit beta |
Protein Synonyms/Alias |
Phosphorylase kinase subunit beta; |
Gene Name |
PHKB |
Gene Synonyms/Alias |
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Created Date |
01-OCT-1989 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
1090 | Canonical | KPSNEDSCLVS**** | [1] | S-Farnesylation |
|
Organism |
Oryctolagus cuniculus (Rabbit) |
NCBI Taxa ID |
9986 |
Reference |
[1] Heilmeyer LM Jr, Serwe M, Weber C, Metzger J, Hoffmann-Posorske E, Meyer HE.Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit skeletalmuscle phosphorylase kinase: localization by conversion to S-ethylcysteine and bytandem mass spectrometry. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9554-8.[ PMID:1409665]
|
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. |
Sequence Annotation |
Region: 7 29 Calmodulin-binding.
Region: 768 795 Calmodulin-binding.
Region: 920 951 Calmodulin-binding.
Functional site: 1090 1090 Not methylated.
Modified residue: 2 2 N-acetylalanine.
Modified residue: 12 12 Phosphoserine; by autocatalysis.
Modified residue: 27 27 Phosphoserine; by PKA.
Modified residue: 701 701 Phosphoserine; by PKA.
|
Protein Length |
1093 AA. |
Protein Sequence
(Canonical) |
MAGATGLMAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD YYYKIVKSTL 60
LLYQSPTTGL FPTKTCGGDQ TAKIHDSLYC AAGAWALALA YRRIDDDKGR THELEHSAIK 120
CMRGILYCYM RQADKVQQFK QDPRPTTCLH SLFNVHTGDE LLSYEEYGHL QINAVSLYLL 180
YLVEMISSGL QIIYNTDEVS FIQNLVFCVE RVYRVPDFGV WERGSKYNNG STELHSSSVG 240
LAKAALEAIN GFNLFGNQGC SWSVIFVDLD AHNRNRQTLC SLLPRESRSH NTDAALLPCI 300
SYPAFALDDD VLYNQTLDKV IRKLKGKYGF KRFLRDGYRT SLEDPKRRYY KPAEIKLFDG 360
IECEFPIFFL YMMIDGVFRG NPKQVKEYQD LLTPVLHQTT EGYPVVPKYY YVPADFVEYE 420
KRNPGSQKRF PSNCGRDGKL FLWGQALYII AKLLADELIS PKDIDPVQRY VPLQNQRNVS 480
MRYSNQGPLE NDLVVHVALV AESQRLQVFL NTYGIQTQTP QQVEPIQIWP QQELVKAYFH 540
LGINEKLGLS GRPDRPIGCL GTSKIYRILG KTVVCYPIIF DLSDFYMSQD VLLLIDDIKN 600
ALQFIKQYWK MHGRPLFLVL IREDNIRGSR FNPMLDMLAA LKNGMIGGVK VHVDRLQTLI 660
SGAVVEQLDF LRISDTEELP EFKSFEELEP PKHSKVKRQS STSNAPELEQ QPEVSVTEWR 720
NKPTHEILQK LNDCSCLASQ TILLGILLKR EGPNFITQEG TVSDHIERLY RRAGSKKLWL 780
AVRYGAAFTQ KFSSSIAPHI TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IKNIIYYKCN 840
THDEREAVIQ QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQIR SGDKPAKDLY 900
QLSPSEVKQL LLDILQPQQN GRCWLNKRQI DGSLNRTPTG FYDRVWQILE RTPNGIIVAG 960
KHLPQQPTLS DMTMYEMNFS LLVEDMLGNI DQPKYRQIVV ELLMVVSIVL ERNPELEFQD 1020
KVDLDKLVKE AFHEFQKDES RLKEIEKQDD MTSFYNTPPL GKRGTCSYLT KVVMNLLLEG 1080
EVKPSNEDSC LVS 1093
|
FASTA
(Canonical) |
>LipidDB-9986-00492|P12798
MAGATGLMAEVSWKVLERRARTKRSGSVYEPLKSINLPRPDNETLWDKLDYYYKIVKSTL
LLYQSPTTGLFPTKTCGGDQTAKIHDSLYCAAGAWALALAYRRIDDDKGRTHELEHSAIK
CMRGILYCYMRQADKVQQFKQDPRPTTCLHSLFNVHTGDELLSYEEYGHLQINAVSLYLL
YLVEMISSGLQIIYNTDEVSFIQNLVFCVERVYRVPDFGVWERGSKYNNGSTELHSSSVG
LAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLCSLLPRESRSHNTDAALLPCI
SYPAFALDDDVLYNQTLDKVIRKLKGKYGFKRFLRDGYRTSLEDPKRRYYKPAEIKLFDG
IECEFPIFFLYMMIDGVFRGNPKQVKEYQDLLTPVLHQTTEGYPVVPKYYYVPADFVEYE
KRNPGSQKRFPSNCGRDGKLFLWGQALYIIAKLLADELISPKDIDPVQRYVPLQNQRNVS
MRYSNQGPLENDLVVHVALVAESQRLQVFLNTYGIQTQTPQQVEPIQIWPQQELVKAYFH
LGINEKLGLSGRPDRPIGCLGTSKIYRILGKTVVCYPIIFDLSDFYMSQDVLLLIDDIKN
ALQFIKQYWKMHGRPLFLVLIREDNIRGSRFNPMLDMLAALKNGMIGGVKVHVDRLQTLI
SGAVVEQLDFLRISDTEELPEFKSFEELEPPKHSKVKRQSSTSNAPELEQQPEVSVTEWR
NKPTHEILQKLNDCSCLASQTILLGILLKREGPNFITQEGTVSDHIERLYRRAGSKKLWL
AVRYGAAFTQKFSSSIAPHITTFLVHGKQVTLGAFGHEEEVISNPLSPRVIKNIIYYKCN
THDEREAVIQQELVIHIGWIISNNPELFSGMLKIRIGWIIHAMEYELQIRSGDKPAKDLY
QLSPSEVKQLLLDILQPQQNGRCWLNKRQIDGSLNRTPTGFYDRVWQILERTPNGIIVAG
KHLPQQPTLSDMTMYEMNFSLLVEDMLGNIDQPKYRQIVVELLMVVSIVLERNPELEFQD
KVDLDKLVKEAFHEFQKDESRLKEIEKQDDMTSFYNTPPLGKRGTCSYLTKVVMNLLLEG
EVKPSNEDSCLVS
|
Gene Ontology |
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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