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P46020

- KPB1_HUMAN

UniProt

P46020 - KPB1_HUMAN

Protein

Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform

Gene

PHKA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (11 Jul 2006)
      Previous versions | rss
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    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

    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

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

    GO - Cellular componenti

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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 isoformPRO_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 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

    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.
    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.
    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

    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:
    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]
    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 ]
    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

    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: October 1, 2014
    This is version 138 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