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P12798 (KPBB_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphorylase b kinase regulatory subunit beta

Short name=Phosphorylase kinase subunit beta
Gene names
Name:PHKB
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length1093 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 regulation

By phosphorylation of various serine residues.

Pathway

Glycan biosynthesis; glycogen metabolism.

Subunit structure

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.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Post-translational modification

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

Sequence similarities

Belongs to the phosphorylase b kinase regulatory chain family.

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12798-1)

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.
Isoform 2 (identifier: P12798-2)

Also known as: Brain;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MAGATGLMAEVSWKVLERRARTK → MASSADAVVSSPPAFL
Isoform 3 (identifier: P12798-3)

The sequence of this isoform differs from the canonical sequence as follows:
     780-806: LAVRYGAAFTQKFSSSIAPHITTFLVH → SVVRRAASLLNKVVDSLAPSITNVLVQ
Isoform 4 (identifier: P12798-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 10931092Phosphorylase b kinase regulatory subunit beta
PRO_0000057738

Regions

Region7 – 2923Calmodulin-binding Potential
Region768 – 79528Calmodulin-binding Potential
Region920 – 95132Calmodulin-binding Potential

Sites

Site10901Not methylated

Amino acid modifications

Modified residue21N-acetylalanine Ref.1
Modified residue121Phosphoserine; by autocatalysis Ref.1 Ref.3
Modified residue271Phosphoserine; by PKA Ref.1 Ref.3
Modified residue7011Phosphoserine; by PKA Ref.1 Ref.3
Lipidation10901S-farnesyl cysteine Ref.6

Natural variations

Alternative sequence1 – 2323MAGAT…RARTK → MASSADAVVSSPPAFL in isoform 2 and isoform 4.
VSP_004702
Alternative sequence780 – 80627LAVRY…TFLVH → SVVRRAASLLNKVVDSLAPS ITNVLVQ in isoform 3 and isoform 4.
VSP_004703
Natural variant281V → I.

Experimental info

Sequence conflict241R → Q AA sequence Ref.5
Sequence conflict301Missing AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5954A72A50CD6F3C

FASTA1,093125,295
        10         20         30         40         50         60 
MAGATGLMAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD YYYKIVKSTL 

        70         80         90        100        110        120 
LLYQSPTTGL FPTKTCGGDQ TAKIHDSLYC AAGAWALALA YRRIDDDKGR THELEHSAIK 

       130        140        150        160        170        180 
CMRGILYCYM RQADKVQQFK QDPRPTTCLH SLFNVHTGDE LLSYEEYGHL QINAVSLYLL 

       190        200        210        220        230        240 
YLVEMISSGL QIIYNTDEVS FIQNLVFCVE RVYRVPDFGV WERGSKYNNG STELHSSSVG 

       250        260        270        280        290        300 
LAKAALEAIN GFNLFGNQGC SWSVIFVDLD AHNRNRQTLC SLLPRESRSH NTDAALLPCI 

       310        320        330        340        350        360 
SYPAFALDDD VLYNQTLDKV IRKLKGKYGF KRFLRDGYRT SLEDPKRRYY KPAEIKLFDG 

       370        380        390        400        410        420 
IECEFPIFFL YMMIDGVFRG NPKQVKEYQD LLTPVLHQTT EGYPVVPKYY YVPADFVEYE 

       430        440        450        460        470        480 
KRNPGSQKRF PSNCGRDGKL FLWGQALYII AKLLADELIS PKDIDPVQRY VPLQNQRNVS 

       490        500        510        520        530        540 
MRYSNQGPLE NDLVVHVALV AESQRLQVFL NTYGIQTQTP QQVEPIQIWP QQELVKAYFH 

       550        560        570        580        590        600 
LGINEKLGLS GRPDRPIGCL GTSKIYRILG KTVVCYPIIF DLSDFYMSQD VLLLIDDIKN 

       610        620        630        640        650        660 
ALQFIKQYWK MHGRPLFLVL IREDNIRGSR FNPMLDMLAA LKNGMIGGVK VHVDRLQTLI 

       670        680        690        700        710        720 
SGAVVEQLDF LRISDTEELP EFKSFEELEP PKHSKVKRQS STSNAPELEQ QPEVSVTEWR 

       730        740        750        760        770        780 
NKPTHEILQK LNDCSCLASQ TILLGILLKR EGPNFITQEG TVSDHIERLY RRAGSKKLWL 

       790        800        810        820        830        840 
AVRYGAAFTQ KFSSSIAPHI TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IKNIIYYKCN 

       850        860        870        880        890        900 
THDEREAVIQ QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQIR SGDKPAKDLY 

       910        920        930        940        950        960 
QLSPSEVKQL LLDILQPQQN GRCWLNKRQI DGSLNRTPTG FYDRVWQILE RTPNGIIVAG 

       970        980        990       1000       1010       1020 
KHLPQQPTLS DMTMYEMNFS LLVEDMLGNI DQPKYRQIVV ELLMVVSIVL ERNPELEFQD 

      1030       1040       1050       1060       1070       1080 
KVDLDKLVKE AFHEFQKDES RLKEIEKQDD MTSFYNTPPL GKRGTCSYLT KVVMNLLLEG 

      1090 
EVKPSNEDSC LVS 

« Hide

Isoform 2 (Brain) [UniParc].

Checksum: 5163CA948AF0479B
Show »

FASTA1,086124,283
Isoform 3 [UniParc].

Checksum: 07F26602E742B485
Show »

FASTA1,093125,182
Isoform 4 [UniParc].

Checksum: 0FC50BBC3D7F9C22
Show »

FASTA1,086124,170

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04120 mRNA. Translation: AAA31447.1.
M64657 mRNA. Translation: AAA31450.1.
M64658 mRNA. Translation: AAA31448.1.
PIRA31758.
B40793.
RefSeqNP_001075770.1. NM_001082301.1. [P12798-4]
UniGeneOcu.1949.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48333N.
IntActP12798. 1 interaction.
MINTMINT-8146705.
STRING9986.ENSOCUP00000013584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009137.

Organism-specific databases

CTD5257.

Phylogenomic databases

eggNOGNOG82518.
HOGENOMHOG000231477.
HOVERGENHBG097309.

Enzyme and pathway databases

UniPathwayUPA00163.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
IPR011613. Glyco_hydro_15.
IPR008734. PHK_A/B_su.
[Graphical view]
PANTHERPTHR10749. PTHR10749. 1 hit.
PfamPF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKPBB_RABIT
AccessionPrimary (citable) accession number: P12798
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways