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P12798

- KPBB_RABIT

UniProt

P12798 - KPBB_RABIT

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Protein
Phosphorylase b kinase regulatory subunit beta
Gene
PHKB
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Enzyme regulationi

By phosphorylation of various serine residues.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1090 – 10901Not methylated

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glycogen metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

UniPathwayiUPA00163.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphorylase b kinase regulatory subunit beta
Short name:
Phosphorylase kinase subunit beta
Gene namesi
Name:PHKB
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10931092Phosphorylase b kinase regulatory subunit beta
PRO_0000057738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei12 – 121Phosphoserine; by autocatalysis2 Publications
Modified residuei27 – 271Phosphoserine; by PKA2 Publications
Modified residuei701 – 7011Phosphoserine; by PKA2 Publications
Lipidationi1090 – 10901S-farnesyl cysteine1 Publication

Post-translational modificationi

Cys-1090 is farnesylated, but the terminal tripeptide is not removed and the cysteine carboxyl is not methylated.

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein, Prenylation

Interactioni

Subunit structurei

Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin.

Protein-protein interaction databases

DIPiDIP-48333N.
IntActiP12798. 1 interaction.
MINTiMINT-8146705.
STRINGi9986.ENSOCUP00000013584.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 2923Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni768 – 79528Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni920 – 95132Calmodulin-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG82518.
HOGENOMiHOG000231477.
HOVERGENiHBG097309.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR011613. Glyco_hydro_15.
IPR008734. PHK_A/B_su.
[Graphical view]
PANTHERiPTHR10749. PTHR10749. 1 hit.
PfamiPF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P12798-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAGATGLMAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD     50
YYYKIVKSTL LLYQSPTTGL FPTKTCGGDQ TAKIHDSLYC AAGAWALALA 100
YRRIDDDKGR THELEHSAIK CMRGILYCYM RQADKVQQFK QDPRPTTCLH 150
SLFNVHTGDE LLSYEEYGHL QINAVSLYLL YLVEMISSGL QIIYNTDEVS 200
FIQNLVFCVE RVYRVPDFGV WERGSKYNNG STELHSSSVG LAKAALEAIN 250
GFNLFGNQGC SWSVIFVDLD AHNRNRQTLC SLLPRESRSH NTDAALLPCI 300
SYPAFALDDD VLYNQTLDKV IRKLKGKYGF KRFLRDGYRT SLEDPKRRYY 350
KPAEIKLFDG IECEFPIFFL YMMIDGVFRG NPKQVKEYQD LLTPVLHQTT 400
EGYPVVPKYY YVPADFVEYE KRNPGSQKRF PSNCGRDGKL FLWGQALYII 450
AKLLADELIS PKDIDPVQRY VPLQNQRNVS MRYSNQGPLE NDLVVHVALV 500
AESQRLQVFL NTYGIQTQTP QQVEPIQIWP QQELVKAYFH LGINEKLGLS 550
GRPDRPIGCL GTSKIYRILG KTVVCYPIIF DLSDFYMSQD VLLLIDDIKN 600
ALQFIKQYWK MHGRPLFLVL IREDNIRGSR FNPMLDMLAA LKNGMIGGVK 650
VHVDRLQTLI SGAVVEQLDF LRISDTEELP EFKSFEELEP PKHSKVKRQS 700
STSNAPELEQ QPEVSVTEWR NKPTHEILQK LNDCSCLASQ TILLGILLKR 750
EGPNFITQEG TVSDHIERLY RRAGSKKLWL AVRYGAAFTQ KFSSSIAPHI 800
TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IKNIIYYKCN THDEREAVIQ 850
QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQIR SGDKPAKDLY 900
QLSPSEVKQL LLDILQPQQN GRCWLNKRQI DGSLNRTPTG FYDRVWQILE 950
RTPNGIIVAG KHLPQQPTLS DMTMYEMNFS LLVEDMLGNI DQPKYRQIVV 1000
ELLMVVSIVL ERNPELEFQD KVDLDKLVKE AFHEFQKDES RLKEIEKQDD 1050
MTSFYNTPPL GKRGTCSYLT KVVMNLLLEG EVKPSNEDSC LVS 1093
Length:1,093
Mass (Da):125,295
Last modified:January 23, 2007 - v3
Checksum:i5954A72A50CD6F3C
GO
Isoform 2 (identifier: P12798-2) [UniParc]FASTAAdd to Basket

Also known as: Brain

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MAGATGLMAEVSWKVLERRARTK → MASSADAVVSSPPAFL

Show »
Length:1,086
Mass (Da):124,283
Checksum:i5163CA948AF0479B
GO
Isoform 3 (identifier: P12798-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     780-806: LAVRYGAAFTQKFSSSIAPHITTFLVH → SVVRRAASLLNKVVDSLAPSITNVLVQ

Show »
Length:1,093
Mass (Da):125,182
Checksum:i07F26602E742B485
GO
Isoform 4 (identifier: P12798-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MAGATGLMAEVSWKVLERRARTK → MASSADAVVSSPPAFL
     780-806: LAVRYGAAFTQKFSSSIAPHITTFLVH → SVVRRAASLLNKVVDSLAPSITNVLVQ

Show »
Length:1,086
Mass (Da):124,170
Checksum:i0FC50BBC3D7F9C22
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281V → I.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MAGAT…RARTK → MASSADAVVSSPPAFL in isoform 2 and isoform 4.
VSP_004702Add
BLAST
Alternative sequencei780 – 80627LAVRY…TFLVH → SVVRRAASLLNKVVDSLAPS ITNVLVQ in isoform 3 and isoform 4.
VSP_004703Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241R → Q AA sequence 1 Publication
Sequence conflicti30 – 301Missing AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04120 mRNA. Translation: AAA31447.1.
M64657 mRNA. Translation: AAA31450.1.
M64658 mRNA. Translation: AAA31448.1.
PIRiA31758.
B40793.
RefSeqiNP_001075770.1. NM_001082301.1. [P12798-4]
UniGeneiOcu.1949.

Genome annotation databases

GeneIDi100009137.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04120 mRNA. Translation: AAA31447.1 .
M64657 mRNA. Translation: AAA31450.1 .
M64658 mRNA. Translation: AAA31448.1 .
PIRi A31758.
B40793.
RefSeqi NP_001075770.1. NM_001082301.1. [P12798-4 ]
UniGenei Ocu.1949.

3D structure databases

ModBasei Search...

Protein-protein interaction databases

DIPi DIP-48333N.
IntActi P12798. 1 interaction.
MINTi MINT-8146705.
STRINGi 9986.ENSOCUP00000013584.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009137.

Organism-specific databases

CTDi 5257.

Phylogenomic databases

eggNOGi NOG82518.
HOGENOMi HOG000231477.
HOVERGENi HBG097309.

Enzyme and pathway databases

UniPathwayi UPA00163 .

Family and domain databases

InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR011613. Glyco_hydro_15.
IPR008734. PHK_A/B_su.
[Graphical view ]
PANTHERi PTHR10749. PTHR10749. 1 hit.
Pfami PF00723. Glyco_hydro_15. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The alpha and beta subunits of phosphorylase kinase are homologous: cDNA cloning and primary structure of the beta subunit."
    Kilimann M.W., Zander N.F., Kuhn C.C., Crabb J.W., Meyer H.E., Heilmeyer L.M.G. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 85:9381-9385(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Skeletal muscle.
  2. "Isoform diversity of phosphorylase kinase alpha and beta subunits generated by alternative RNA splicing."
    Harmann B., Zander N.F., Kilimann M.W.
    J. Biol. Chem. 266:15631-15637(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  3. "Localization of phosphoserine residues in the alpha subunit of rabbit skeletal muscle phosphorylase kinase."
    Meyer H.E., Meyer G.F., Dirks H., Heilmeyer L.M.G. Jr.
    Eur. J. Biochem. 188:367-376(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-18; 25-33; 688-709 AND 1072-1093, PHOSPHORYLATION AT SER-12; SER-27 AND SER-701.
  4. "Electrophoretic purification of the alpha and beta subunits of phosphorylase kinase and evidence in support of the deduced amino acid sequences."
    Crabb J.W., Harris W.R., Johnson C.M., Sotiroudis T.G., Kuhn C.C., Heilmeyer L.M. Jr.
    Electrophoresis 11:133-140(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-1081.
  5. "The hormonal control of activity of skeletal muscle phosphorylase kinase. Amino-acid sequences at the two sites of action of adenosine-3':5'-monophosphate-dependent protein kinase."
    Cohen P., Watson D.C., Dixon G.H.
    Eur. J. Biochem. 51:79-92(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Skeletal muscle.
  6. "Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit skeletal muscle phosphorylase kinase: localization by conversion to S-ethylcysteine and by tandem mass spectrometry."
    Heilmeyer L.M. Jr., Serwe M., Weber C., Metzger J., Hoffmann-Posorske E., Meyer H.E.
    Proc. Natl. Acad. Sci. U.S.A. 89:9554-9558(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1073-1093, ISOPRENYLATION AT CYS-1090, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiKPBB_RABIT
AccessioniPrimary (citable) accession number: P12798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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