Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform

Gene

PHKA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  • phosphorylase kinase activity Source: ProtInc

GO - Biological processi

  • carbohydrate metabolic process Source: Reactome
  • generation of precursor metabolites and energy Source: ProtInc
  • glucose metabolic process Source: Reactome
  • glycogen catabolic process Source: Reactome
  • glycogen metabolic process Source: ProtInc
  • protein phosphorylation Source: GOC
  • 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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8925. PHKA1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 9D (GSD9D)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:300559
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.

Polymorphism and mutation databases

BioMutaiPHKA1.
DMDMi110282976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12231223Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoformPRO_0000057726Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei729 – 7291PhosphoserineBy similarity
Modified residuei735 – 7351Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine1 Publication
Modified residuei972 – 9721Phosphoserine2 Publications
Modified residuei985 – 9851Phosphoserine2 Publications
Modified residuei1007 – 10071Phosphoserine; by autocatalysisBy similarity
Modified residuei1018 – 10181Phosphoserine; by PKABy similarity
Modified residuei1020 – 10201PhosphoserineBy similarity
Modified residuei1023 – 10231PhosphoserineBy similarity
Lipidationi1220 – 12201S-farnesyl cysteineBy 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

BgeeiP46020.
CleanExiHS_PHKA1.
ExpressionAtlasiP46020. baseline and differential.
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. 11 interactions.
IntActiP46020. 1 interaction.
STRINGi9606.ENSP00000362643.

Structurei

3D structure databases

ProteinModelPortaliP46020.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni810 – 84031Calmodulin-bindingSequence AnalysisAdd
BLAST
Regioni1046 – 108641Calmodulin-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG82518.
GeneTreeiENSGT00520000055553.
HOGENOMiHOG000231478.
HOVERGENiHBG000273.
InParanoidiP46020.
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. AlignAdd to basket

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

        10         20         30         40         50
MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS
60 70 80 90 100
ILAVWGLGLA YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE
110 120 130 140 150
SFKYSQSTKD SLHAKYNTKT CATVVGDDQW GHLQLDATSV YLLFLAQMTA
160 170 180 190 200
SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD FGIWERGDKT NQGISELNAS
210 220 230 240 250
SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS ILNSLLPRAS
260 270 280 290 300
TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG
310 320 330 340 350
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE
360 370 380 390 400
YKEALEAVLI KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH
410 420 430 440 450
MWGQSLYILG SLMAEGFLAP GEIDPLNRRF STVPKPDVVV QVSILAETEE
460 470 480 490 500
IKTILKDKGI YVETIAEVYP IRVQPARILS HIYSSLGCNN RMKLSGRPYR
510 520 530 540 550
HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV EMLRTDLSYL
560 570 580 590 600
CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ
610 620 630 640 650
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS
660 670 680 690 700
TSHARCGDEV ARYLDHLLAH TAPHPKLAPT SQKGGLDRFQ AAVQTTCDLM
710 720 730 740 750
SLVTKAKELH VQNVHMYLPT KLFQASRPSF NLLDSPHPRQ ENQVPSVRVE
760 770 780 790 800
IHLPRDQSGE VDFKALVLQL KETSSLQEQA DILYMLYTMK GPDWNTELYN
810 820 830 840 850
ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL DEACTDLLSH
860 870 880 890 900
QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMSI SILTQEIMVY
910 920 930 940 950
LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS
960 970 980 990 1000
PSAMKNLLHH ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT
1010 1020 1030 1040 1050
GIMQLKSEIK QVEFRRLSIS AESQSPGTSM TPSSGSFPSA YDQQSSKDSR
1060 1070 1080 1090 1100
QGQWQRRRRL DGALNRVPVG FYQKVWKVLQ KCHGLSVEGF VLPSSTTREM
1110 1120 1130 1140 1150
TPGEIKFSVH VESVLNRVPQ PEYRQLLVEA ILVLTMLADI EIHSIGSIIA
1160 1170 1180 1190 1200
VEKIVHIAND LFLQEQKTLG ADDTMLAKDP ASGICTLLYD SAPSGRFGTM
1210 1220
TYLSKAAATY VQEFLPHSIC AMQ
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti568 – 5681H → Y in CAA52083 (PubMed:8226841).Curated

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. 1 PublicationVSP_042517Add
BLAST
Alternative sequencei1011 – 102313Missing in isoform 3. 1 PublicationVSP_042518Add
BLAST
Alternative sequencei1012 – 102413Missing in isoform 2. 2 PublicationsVSP_004697Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
GeneIDi5255.
KEGGihsa:5255.
UCSCiuc004eax.4. human. [P46020-1]
uc004eay.4. human. [P46020-2]
uc011mqi.2. human. [P46020-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP46020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111273. 11 interactions.
IntActiP46020. 1 interaction.
STRINGi9606.ENSP00000362643.

Chemistry

ChEMBLiCHEMBL2111324.

PTM databases

PhosphoSiteiP46020.

Polymorphism and mutation databases

BioMutaiPHKA1.
DMDMi110282976.

Proteomic databases

MaxQBiP46020.
PaxDbiP46020.
PRIDEiP46020.

Protocols and materials databases

DNASUi5255.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339490; ENSP00000342469; ENSG00000067177. [P46020-2]
ENST00000373542; ENSP00000362643; ENSG00000067177. [P46020-1]
ENST00000541944; ENSP00000441251; ENSG00000067177. [P46020-3]
GeneIDi5255.
KEGGihsa:5255.
UCSCiuc004eax.4. human. [P46020-1]
uc004eay.4. human. [P46020-2]
uc011mqi.2. human. [P46020-3]

Organism-specific databases

CTDi5255.
GeneCardsiGC0XM071798.
GeneReviewsiPHKA1.
HGNCiHGNC:8925. PHKA1.
HPAiHPA001081.
MIMi300559. phenotype.
311870. gene.
neXtProtiNX_P46020.
Orphaneti715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKBiPA33266.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG82518.
GeneTreeiENSGT00520000055553.
HOGENOMiHOG000231478.
HOVERGENiHBG000273.
InParanoidiP46020.
KOiK07190.
PhylomeDBiP46020.
TreeFamiTF313970.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPHKA1. human.
GeneWikiiPhosphorylase_kinase,_alpha_1.
GenomeRNAii5255.
NextBioi20300.
PROiP46020.
SOURCEiSearch...

Gene expression databases

BgeeiP46020.
CleanExiHS_PHKA1.
ExpressionAtlasiP46020. baseline and differential.
GenevestigatoriP46020.

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.
ProtoNetiSearch...

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: May 27, 2015
This is version 144 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.