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P46020

- KPB1_HUMAN

UniProt

P46020 - KPB1_HUMAN

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Protein
Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
Gene
PHKA1, PHKA
Organism
Homo sapiens (Human)
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 alpha chain may bind calmodulin.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1220 – 12201Not methylated

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  2. phosphorylase kinase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. generation of precursor metabolites and energy Source: ProtInc
  3. glucose metabolic process Source: Reactome
  4. glycogen catabolic process Source: Reactome
  5. glycogen metabolic process Source: ProtInc
  6. protein phosphorylation Source: GOC
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00901-MONOMER.
BRENDAi2.7.11.19. 2681.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
UniPathwayiUPA00163.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
Short name:
Phosphorylase kinase alpha M subunit
Gene namesi
Name:PHKA1
Synonyms:PHKA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8925. PHKA1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991D → V in GSD9D. 1 Publication
VAR_020856

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi300559. phenotype.
Orphaneti715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKBiPA33266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12231223Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
PRO_0000057726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei735 – 7351Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine1 Publication
Modified residuei972 – 9721Phosphoserine2 Publications
Modified residuei985 – 9851Phosphoserine2 Publications
Modified residuei1007 – 10071Phosphoserine; by autocatalysis By similarity
Modified residuei1018 – 10181Phosphoserine; by PKA By similarity
Modified residuei1020 – 10201Phosphoserine By similarity
Modified residuei1023 – 10231Phosphoserine By similarity
Lipidationi1220 – 12201S-farnesyl cysteine By similarity

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP46020.
PaxDbiP46020.
PRIDEiP46020.

PTM databases

PhosphoSiteiP46020.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiP46020.
BgeeiP46020.
CleanExiHS_PHKA1.
GenevestigatoriP46020.

Organism-specific databases

HPAiHPA001081.

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

BioGridi111273. 4 interactions.
IntActiP46020. 1 interaction.
STRINGi9606.ENSP00000362643.

Structurei

3D structure databases

ProteinModelPortaliP46020.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni810 – 84031Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni1046 – 108641Calmodulin-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG82518.
HOGENOMiHOG000231478.
HOVERGENiHBG000273.
KOiK07190.
PhylomeDBiP46020.
TreeFamiTF313970.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P46020-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS     50
ILAVWGLGLA YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE 100
SFKYSQSTKD SLHAKYNTKT CATVVGDDQW GHLQLDATSV YLLFLAQMTA 150
SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD FGIWERGDKT NQGISELNAS 200
SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS ILNSLLPRAS 250
TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG 300
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE 350
YKEALEAVLI KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH 400
MWGQSLYILG SLMAEGFLAP GEIDPLNRRF STVPKPDVVV QVSILAETEE 450
IKTILKDKGI YVETIAEVYP IRVQPARILS HIYSSLGCNN RMKLSGRPYR 500
HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV EMLRTDLSYL 550
CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ 600
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS 650
TSHARCGDEV ARYLDHLLAH TAPHPKLAPT SQKGGLDRFQ AAVQTTCDLM 700
SLVTKAKELH VQNVHMYLPT KLFQASRPSF NLLDSPHPRQ ENQVPSVRVE 750
IHLPRDQSGE VDFKALVLQL KETSSLQEQA DILYMLYTMK GPDWNTELYN 800
ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL DEACTDLLSH 850
QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMSI SILTQEIMVY 900
LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS 950
PSAMKNLLHH ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT 1000
GIMQLKSEIK QVEFRRLSIS AESQSPGTSM TPSSGSFPSA YDQQSSKDSR 1050
QGQWQRRRRL DGALNRVPVG FYQKVWKVLQ KCHGLSVEGF VLPSSTTREM 1100
TPGEIKFSVH VESVLNRVPQ PEYRQLLVEA ILVLTMLADI EIHSIGSIIA 1150
VEKIVHIAND LFLQEQKTLG ADDTMLAKDP ASGICTLLYD SAPSGRFGTM 1200
TYLSKAAATY VQEFLPHSIC AMQ 1223
Length:1,223
Mass (Da):137,312
Last modified:July 11, 2006 - v2
Checksum:i48511719C0BFE40F
GO
Isoform 2 (identifier: P46020-2) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     1012-1024: Missing.

Show »
Length:1,210
Mass (Da):135,808
Checksum:i6D79FA1069CE6D25
GO
Isoform 3 (identifier: P46020-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,151
Mass (Da):129,388
Checksum:iF8E38DBD42155D47
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991D → V in GSD9D. 1 Publication
VAR_020856

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei654 – 71360ARCGD…LHVQN → D in isoform 3.
VSP_042517Add
BLAST
Alternative sequencei1011 – 102313Missing in isoform 3.
VSP_042518Add
BLAST
Alternative sequencei1012 – 102413Missing in isoform 2.
VSP_004697Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti568 – 5681H → Y in CAA52083. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14421.1. [P46020-1]
CCDS48137.1. [P46020-2]
CCDS55453.1. [P46020-3]
PIRiI38111.
RefSeqiNP_001116142.1. NM_001122670.1. [P46020-2]
NP_001165907.1. NM_001172436.1. [P46020-3]
NP_002628.2. NM_002637.3. [P46020-1]
UniGeneiHs.201379.

Genome annotation databases

EnsembliENST00000339490; 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]
GeneIDi5255.
KEGGihsa:5255.
UCSCiuc004eax.4. human. [P46020-1]
uc004eay.4. human. [P46020-2]
uc011mqi.2. human. [P46020-3]

Polymorphism databases

DMDMi110282976.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14421.1. [P46020-1 ]
CCDS48137.1. [P46020-2 ]
CCDS55453.1. [P46020-3 ]
PIRi I38111.
RefSeqi NP_001116142.1. NM_001122670.1. [P46020-2 ]
NP_001165907.1. NM_001172436.1. [P46020-3 ]
NP_002628.2. NM_002637.3. [P46020-1 ]
UniGenei Hs.201379.

3D structure databases

ProteinModelPortali P46020.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111273. 4 interactions.
IntActi P46020. 1 interaction.
STRINGi 9606.ENSP00000362643.

Chemistry

BindingDBi P46020.
ChEMBLi CHEMBL2111324.

PTM databases

PhosphoSitei P46020.

Polymorphism databases

DMDMi 110282976.

Proteomic databases

MaxQBi P46020.
PaxDbi P46020.
PRIDEi P46020.

Protocols and materials databases

DNASUi 5255.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339490 ; 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 ]
GeneIDi 5255.
KEGGi hsa:5255.
UCSCi uc004eax.4. human. [P46020-1 ]
uc004eay.4. human. [P46020-2 ]
uc011mqi.2. human. [P46020-3 ]

Organism-specific databases

CTDi 5255.
GeneCardsi GC0XM071715.
GeneReviewsi PHKA1.
HGNCi HGNC:8925. PHKA1.
HPAi HPA001081.
MIMi 300559. phenotype.
311870. gene.
neXtProti NX_P46020.
Orphaneti 715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKBi PA33266.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG82518.
HOGENOMi HOG000231478.
HOVERGENi HBG000273.
KOi K07190.
PhylomeDBi P46020.
TreeFami TF313970.

Enzyme and pathway databases

UniPathwayi UPA00163 .
BioCyci MetaCyc:HS00901-MONOMER.
BRENDAi 2.7.11.19. 2681.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

ChiTaRSi PHKA1. human.
GeneWikii Phosphorylase_kinase,_alpha_1.
GenomeRNAii 5255.
NextBioi 20300.
PROi P46020.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46020.
Bgeei P46020.
CleanExi HS_PHKA1.
Genevestigatori P46020.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
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

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiKPB1_HUMAN
AccessioniPrimary (citable) accession number: P46020
Secondary accession number(s): B7ZL05, B7ZL07, Q2M3D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2006
Last modified: September 3, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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