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P46020 (KPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform

Short name=Phosphorylase kinase alpha M subunit
Gene names
Name:PHKA1
Synonyms:PHKA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1223 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.

Enzyme regulation

By phosphorylation of various serine residues. Allosteric regulation by calcium.

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.

Tissue specificity

Muscle specific. Isoform 1 is predominant in vastus lateralis muscle. Isoform 2 predominates slightly in heart, and it predominates clearly in the other tissues tested.

Post-translational modification

Although the final Cys may be farnesylated, the terminal tripeptide is probably not removed, and the C-terminus is not methylated By similarity.

Involvement in disease

Glycogen storage disease 9D (GSD9D) [MIM:300559]: A metabolic disorder characterized by slowly progressive, predominantly distal muscle weakness and atrophy. Clinical features include exercise intolerance with early fatigability, pain, cramps and occasionally myoglobinuria.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the phosphorylase b kinase regulatory chain family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P46020-1)

Also known as: AC;

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: P46020-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     1012-1024: Missing.
Isoform 3 (identifier: P46020-3)

The sequence of this isoform differs from the canonical sequence as follows:
     654-713: ARCGDEVARYLDHLLAHTAPHPKLAPTSQKGGLDRFQAAVQTTCDLMSLVTKAKELHVQN → D
     1011-1023: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12231223Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
PRO_0000057726

Regions

Region810 – 84031Calmodulin-binding Potential
Region1046 – 108641Calmodulin-binding Potential

Sites

Site12201Not methylated

Amino acid modifications

Modified residue7351Phosphoserine Ref.4
Modified residue7581Phosphoserine Ref.6
Modified residue9721Phosphoserine Ref.5 Ref.6
Modified residue9851Phosphoserine Ref.5 Ref.6
Modified residue10071Phosphoserine; by autocatalysis By similarity
Modified residue10181Phosphoserine; by PKA By similarity
Modified residue10201Phosphoserine By similarity
Modified residue10231Phosphoserine By similarity
Lipidation12201S-farnesyl cysteine By similarity

Natural variations

Alternative sequence654 – 71360ARCGD…LHVQN → D in isoform 3.
VSP_042517
Alternative sequence1011 – 102313Missing in isoform 3.
VSP_042518
Alternative sequence1012 – 102413Missing in isoform 2.
VSP_004697
Natural variant2991D → V in GSD9D. Ref.8
VAR_020856

Experimental info

Sequence conflict5681H → Y in CAA52083. Ref.1

Sequences

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

Last modified July 11, 2006. Version 2.
Checksum: 48511719C0BFE40F

FASTA1,223137,312
        10         20         30         40         50         60 
MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA 

        70         80         90        100        110        120 
YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT 

       130        140        150        160        170        180 
CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD 

       190        200        210        220        230        240 
FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS 

       250        260        270        280        290        300 
ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG 

       310        320        330        340        350        360 
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE YKEALEAVLI 

       370        380        390        400        410        420 
KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP 

       430        440        450        460        470        480 
GEIDPLNRRF STVPKPDVVV QVSILAETEE IKTILKDKGI YVETIAEVYP IRVQPARILS 

       490        500        510        520        530        540 
HIYSSLGCNN RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV 

       550        560        570        580        590        600 
EMLRTDLSYL CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ 

       610        620        630        640        650        660 
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS TSHARCGDEV 

       670        680        690        700        710        720 
ARYLDHLLAH TAPHPKLAPT SQKGGLDRFQ AAVQTTCDLM SLVTKAKELH VQNVHMYLPT 

       730        740        750        760        770        780 
KLFQASRPSF NLLDSPHPRQ ENQVPSVRVE IHLPRDQSGE VDFKALVLQL KETSSLQEQA 

       790        800        810        820        830        840 
DILYMLYTMK GPDWNTELYN ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL 

       850        860        870        880        890        900 
DEACTDLLSH QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMSI SILTQEIMVY 

       910        920        930        940        950        960 
LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS PSAMKNLLHH 

       970        980        990       1000       1010       1020 
ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT GIMQLKSEIK QVEFRRLSIS 

      1030       1040       1050       1060       1070       1080 
AESQSPGTSM TPSSGSFPSA YDQQSSKDSR QGQWQRRRRL DGALNRVPVG FYQKVWKVLQ 

      1090       1100       1110       1120       1130       1140 
KCHGLSVEGF VLPSSTTREM TPGEIKFSVH VESVLNRVPQ PEYRQLLVEA ILVLTMLADI 

      1150       1160       1170       1180       1190       1200 
EIHSIGSIIA VEKIVHIAND LFLQEQKTLG ADDTMLAKDP ASGICTLLYD SAPSGRFGTM 

      1210       1220 
TYLSKAAATY VQEFLPHSIC AMQ 

« Hide

Isoform 2 (C) [UniParc].

Checksum: 6D79FA1069CE6D25
Show »

FASTA1,210135,808
Isoform 3 [UniParc].

Checksum: F8E38DBD42155D47
Show »

FASTA1,151129,388

References

« Hide 'large scale' references
[1]"The multiphosphorylation domain of the phosphorylase kinase alpha M and alpha L subunits is a hotspot of differential mRNA processing and of molecular evolution."
Wuellrich A., Hamacher C., Schneider A., Kilimann M.W.
J. Biol. Chem. 268:23208-23214(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Muscle.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-972 AND SER-985, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758; SER-972 AND SER-985, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases."
Burwinkel B., Hu B., Schroers A., Clemens P.R., Moses S.W., Shin Y.S., Pongratz D., Vorgerd M., Kilimann M.W.
Eur. J. Hum. Genet. 11:516-526(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD9D VAL-299.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73874 mRNA. Translation: CAA52083.1.
BX295541 Genomic DNA. No translation available.
BX295542 Genomic DNA. No translation available.
BC104944 mRNA. Translation: AAI04945.1.
BC143499 mRNA. Translation: AAI43500.1.
BC143501 mRNA. Translation: AAI43502.1.
PIRI38111.
RefSeqNP_001116142.1. NM_001122670.1.
NP_001165907.1. NM_001172436.1.
NP_002628.2. NM_002637.3.
UniGeneHs.201379.

3D structure databases

ProteinModelPortalP46020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111273. 4 interactions.
IntActP46020. 1 interaction.
STRING9606.ENSP00000362643.

Chemistry

BindingDBP46020.
ChEMBLCHEMBL2111324.

PTM databases

PhosphoSiteP46020.

Polymorphism databases

DMDM110282976.

Proteomic databases

PaxDbP46020.
PRIDEP46020.

Protocols and materials databases

DNASU5255.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339490; ENSP00000342469; ENSG00000067177. [P46020-2]
ENST00000373542; ENSP00000362643; ENSG00000067177. [P46020-1]
ENST00000541944; ENSP00000441251; ENSG00000067177. [P46020-3]
ENST00000593378; ENSP00000471521; ENSG00000268579. [P46020-1]
ENST00000600891; ENSP00000471771; ENSG00000268579. [P46020-2]
ENST00000601371; ENSP00000472984; ENSG00000268579. [P46020-3]
GeneID5255.
KEGGhsa:5255.
UCSCuc004eax.4. human. [P46020-1]
uc004eay.4. human. [P46020-2]
uc011mqi.2. human. [P46020-3]

Organism-specific databases

CTD5255.
GeneCardsGC0XM071715.
HGNCHGNC:8925. PHKA1.
HPAHPA001081.
MIM300559. phenotype.
311870. gene.
neXtProtNX_P46020.
Orphanet715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKBPA33266.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82518.
HOGENOMHOG000231478.
HOVERGENHBG000273.
KOK07190.
PhylomeDBP46020.
TreeFamTF313970.

Enzyme and pathway databases

BioCycMetaCyc:HS00901-MONOMER.
BRENDA2.7.11.19. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00163.

Gene expression databases

ArrayExpressP46020.
BgeeP46020.
CleanExHS_PHKA1.
GenevestigatorP46020.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
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...

Other

ChiTaRSPHKA1. human.
GeneWikiPhosphorylase_kinase,_alpha_1.
GenomeRNAi5255.
NextBio20300.
PROP46020.
SOURCESearch...

Entry information

Entry nameKPB1_HUMAN
AccessionPrimary (citable) accession number: P46020
Secondary accession number(s): B7ZL05, B7ZL07, Q2M3D7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2006
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM