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P46019 (KPB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=Phosphorylase kinase alpha L subunit
Gene names
Name:PHKA2
Synonyms:PHKLA, PYK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1235 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 and 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

Predominantly expressed in liver and other non-muscle tissues.

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 9A (GSD9A) [MIM:306000]: A metabolic disorder resulting in a mild liver glycogenosis with clinical symptoms that include hepatomegaly, growth retardation, muscle weakness, elevation of glutamate-pyruvate transaminase and glutamate-oxaloacetate transaminase, hypercholesterolemia, hypertriglyceridemia, and fasting hyperketosis. Two subtypes are known: type 1 or classic type with no phosphorylase kinase activity in liver or erythrocytes, and type 2 or variant type with no phosphorylase kinase activity in liver, but normal activity in erythrocytes. Unlike other glycogenosis diseases, glycogen storage disease type 9A is generally a benign condition. Patients improve with age and are often asymptomatic as adults. Accurate diagnosis is therefore also of prognostic interest.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.3 Ref.8 Ref.17 Ref.18 Ref.19

Sequence similarities

Belongs to the phosphorylase b kinase regulatory chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235Phosphorylase b kinase regulatory subunit alpha, liver isoform
PRO_0000057730

Regions

Region807 – 83731Calmodulin-binding Potential
Region1059 – 109941Calmodulin-binding Potential

Amino acid modifications

Modified residue7291Phosphoserine Ref.11 Ref.14 Ref.15 Ref.16
Modified residue7351Phosphoserine Ref.11 Ref.16
Modified residue10151Phosphoserine Ref.11 Ref.12 Ref.15
Lipidation12321S-farnesyl cysteine By similarity

Natural variations

Natural variant381E → Q.
Corresponds to variant rs17313469 [ dbSNP | Ensembl ].
VAR_024563
Natural variant1201T → TYNTAT in GSD9A.
VAR_062393
Natural variant1321H → P in GSD9A; type 2. Ref.18
VAR_006177
Natural variant1321H → Y in GSD9A; type 2. Ref.18
VAR_006178
Natural variant1411Missing in GSD9A; type 1. Ref.1
VAR_006179
Natural variant1861R → C in GSD9A; type 2. Ref.3 Ref.17
VAR_006180
Natural variant1861R → H in GSD9A; type 2. Ref.3 Ref.18
VAR_006181
Natural variant189 – 1902Missing in GSD9A; type 2.
VAR_012270
Natural variant1891K → E in GSD9A; type 2. Ref.8
VAR_012269
Natural variant1931G → V in GSD9A; type 2. Ref.2
VAR_012271
Natural variant2511Missing in GSD9A; type 2. Ref.17
VAR_006182
Natural variant2951R → H in GSD9A; type 1 and type 2. Ref.3
VAR_012272
Natural variant2991D → G in GSD9A; type 2. Ref.18 Ref.19
VAR_006183
Natural variant3991P → S in GSD9A; type 1. Ref.8
VAR_012273
Natural variant4161G → R.
Corresponds to variant rs16980929 [ dbSNP | Ensembl ].
VAR_050518
Natural variant4981P → L in GSD9A. Ref.19
VAR_062394
Natural variant818 – 8258Missing in GSD9A; type 1.
VAR_012274
Natural variant8691P → R in GSD9A. Ref.19
VAR_062395
Natural variant9161R → W in GSD9A. Ref.19
VAR_062396
Natural variant953 – 9542NL → I in GSD9A; type 1.
VAR_012275
Natural variant10701Missing in GSD9A. Ref.19
VAR_062397
Natural variant11111R → RTR in GSD9A; type 2.
VAR_006184
Natural variant11131M → I in GSD9A. Ref.19
VAR_062398
Natural variant11141T → I in GSD9A; type 2. Ref.17
VAR_006185
Natural variant11251E → K in GSD9A; type 1. Ref.3
VAR_012276
Natural variant12051P → L in GSD9A; type 1. Ref.1
VAR_006186
Natural variant12071G → W in GSD9A; type 1. Ref.8
VAR_012277

Experimental info

Sequence conflict5271Q → E in AAH14036. Ref.7
Sequence conflict7561G → S in AAH14036. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P46019 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 6CA10CFFA86A582A

FASTA1,235138,408
        10         20         30         40         50         60 
MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHEQK DAWVRDNIYS ILAVWGLGMA 

        70         80         90        100        110        120 
YRKNADRDED KAKAYELEQN VVKLMRGLLQ CMMRQVAKVE KFKHTQSTKD SLHAKYNTAT 

       130        140        150        160        170        180 
CGTVVGDDQW GHLQVDATSL FLLFLAQMTA SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD 

       190        200        210        220        230        240 
YGMWERGDKT NQGIPELNAS SVGMAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS 

       250        260        270        280        290        300 
ILFSMLPRAS TSKEIDAGLL SIISFPAFAV EDVNLVNVTK NEIISKLQGR YGCCRFLRDG 

       310        320        330        340        350        360 
YKTPREDPNR LHYDPAELKL FENIECEWPV FWTYFIIDGV FSGDAVQVQE YREALEGILI 

       370        380        390        400        410        420 
RGKNGIRLVP ELYAVPPNKV DEEYKNPHTV DRVPMGKVPH LWGQSLYILS SLLAEGFLAA 

       430        440        450        460        470        480 
GEIDPLNRRF STSVKPDVVV QVTVLAENNH IKDLLRKHGV NVQSIADIHP IQVQPGRILS 

       490        500        510        520        530        540 
HIYAKLGRNK NMNLSGRPYR HIGVLGTSKL YVIRNQIFTF TPQFTDQHHF YLALDNEMIV 

       550        560        570        580        590        600 
EMLRIELAYL CTCWRMTGRP TLTFPISRTM LTNDGSDIHS AVLSTIRKLE DGYFGGARVK 

       610        620        630        640        650        660 
LGNLSEFLTT SFYTYLTFLD PDCDEKLFDN ASEGTFSPDS DSDLVGYLED TCNQESQDEL 

       670        680        690        700        710        720 
DHYINHLLQS TSLRSYLPPL CKNTEDRHVF SAIHSTRDIL SVMAKAKGLE VPFVPMTLPT 

       730        740        750        760        770        780 
KVLSAHRKSL NLVDSPQPLL EKVPESDFQW PRDDHGDVDC EKLVEQLKDC SNLQDQADIL 

       790        800        810        820        830        840 
YILYVIKGPS WDTNLSGQHG VTVQNLLGEL YGKAGLNQEW GLIRYISGLL RKKVEVLAEA 

       850        860        870        880        890        900 
CTDLLSHQKQ LTVGLPPEPR EKIISAPLPP EELTKLIYEA SGQDISIAVL TQEIVVYLAM 

       910        920        930        940        950        960 
YVRAQPSLFV EMLRLRIGLI IQVMATELAR SLNCSGEEAS ESLMNLSPFD MKNLLHHILS 

       970        980        990       1000       1010       1020 
GKEFGVERSV RPIHSSTSSP TISIHEVGHT GVTKTERSGI NRLRSEMKQM TRRFSADEQF 

      1030       1040       1050       1060       1070       1080 
FSVGQAASSS AHSSKSARSS TPSSPTGTSS SDSGGHHIGW GERQGQWLRR RRLDGAINRV 

      1090       1100       1110       1120       1130       1140 
PVGFYQRVWK ILQKCHGLSI DGYVLPSSTT REMTPHEIKF AVHVESVLNR VPQPEYRQLL 

      1150       1160       1170       1180       1190       1200 
VEAIMVLTLL SDTEMTSIGG IIHVDQIVQM ASQLFLQDQV SIGAMDTLEK DQATGICHFF 

      1210       1220       1230 
YDSAPSGAYG TMTYLTRAVA SYLQELLPNS GCQMQ 

« Hide

References

« Hide 'large scale' references
[1]"X-linked liver phosphorylase kinase deficiency is associated with mutations in the human liver phosphorylase kinase alpha subunit."
van den Berg I.E.T., van Beurden E.A.C.M., Malingre H.E.M., Ploos van Amstel H.K., Poll-The B.T., Smeitink J.A.M., Lamers W.H., Berger R.
Am. J. Hum. Genet. 56:381-387(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GSD9A PHE-141 DEL AND LEU-1205.
Tissue: Liver.
[2]"Isolation of cDNA encoding the human liver phosphorylase kinase alpha subunit (PHKA2) and identification of a missense mutation of the PHKA2 gene in a family with liver phosphorylase kinase deficiency."
Hirono H., Hayasaka K., Sato W., Takahashi T., Takada G.
Biochem. Mol. Biol. Int. 36:505-511(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD9A VAL-193.
Tissue: Liver.
[3]"Complete genomic structure and mutational spectrum of PHKA2 in patients with X-linked liver glycogenosis type I and II."
Hendrickx J., Lee P., Keating J.P., Carton D., Sardharwalla I.B., Tuchman M., Baussan C., Willems P.J.
Am. J. Hum. Genet. 64:1541-1549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GSD9A CYS-186; HIS-186; 189-LYS-THR-190 DEL; HIS-295 AND LYS-1125.
Tissue: Liver.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus.
[5]"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].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Colon.
[8]"Variability of biochemical and clinical phenotype in X-linked liver glycogenosis with mutations in the phosphorylase kinase PHKA2 gene."
Burwinkel B., Amat L., Gray R.G., Matsuo N., Muroya K., Narisawa K., Sokol R.J., Vilaseca M.A., Kilimann M.W.
Hum. Genet. 102:423-429(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-206, VARIANTS GSD9A GLU-189; SER-399; 818-GLN--TYR-825 DEL; 953-ASN--LEU-954 DELINS ILE AND TRP-1207.
[9]"X-linked liver glycogenosis: localization and isolation of a candidate gene."
Hendrickx J., Coucke P., Bossuyt P., Wauters J., Raeymaekers P., Marchau F., Smit G.P., Stolte I., Sardharwalla I.B., Berthelot J.
Hum. Mol. Genet. 2:583-589(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 750-1126.
Tissue: Liver.
[10]"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] OF 977-1080.
Tissue: Liver.
[11]"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-729; SER-735 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-729 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"X-linked liver glycogenosis type II (XLG II) is caused by mutations in PHKA2, the gene encoding the liver alpha subunit of phosphorylase kinase."
Hendrickx J., Dams E., Coucke P., Lee P., Fernandes J., Willems P.J.
Hum. Mol. Genet. 5:649-652(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD9A CYS-186; THR-251 DEL; THR-ARG-1111 INS AND ILE-1114.
[18]"Mutation hotspots in the PHKA2 gene in X-linked liver glycogenosis due to phosphorylase kinase deficiency with atypical activity in blood cells (XLG2)."
Burwinkel B., Shin Y.S., Bakker H.D., Deutsch J., Lozano M.J., Maire I., Kilimann M.W.
Hum. Mol. Genet. 5:653-658(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD9A PRO-132; TYR-132; HIS-186 AND GLY-299.
[19]"Glycogen storage disease type IX: High variability in clinical phenotype."
Beauchamp N.J., Dalton A., Ramaswami U., Niinikoski H., Mention K., Kenny P., Kolho K.L., Raiman J., Walter J., Treacy E., Tanner S., Sharrard M.
Mol. Genet. Metab. 92:88-99(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD9A TYR-ASN-THR-ALA-THR-120 INS; GLY-299; LEU-498; ARG-869; TRP-916; ARG-1070 DEL AND ILE-1113.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80497 mRNA. Translation: CAA56662.1.
D38616 mRNA. Translation: BAA07606.1.
AF044572 expand/collapse EMBL AC list , AF044540, AF044541, AF044542, AF044543, AF044544, AF044545, AF044546, AF044547, AF044548, AF044549, AF044550, AF044551, AF044552, AF044553, AF044554, AF044555, AF044556, AF044557, AF044558, AF044559, AF044560, AF044561, AF044562, AF044563, AF044564, AF044565, AF044566, AF044567, AF044568, AF044569, AF044570, AF044571 Genomic DNA. Translation: AAD32846.1.
AK289996 mRNA. Translation: BAF82685.1.
AL096700, AL732509 Genomic DNA. Translation: CAB86408.2.
AL732509, AL096700 Genomic DNA. Translation: CAI41680.1.
CH471074 Genomic DNA. Translation: EAW98951.1.
BC014036 mRNA. Translation: AAH14036.1.
Y15154 Genomic DNA. Translation: CAA75421.1.
X73875 mRNA. Translation: CAA52084.1.
RefSeqNP_000283.1. NM_000292.2.
UniGeneHs.54941.

3D structure databases

ProteinModelPortalP46019.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111274. 10 interactions.
IntActP46019. 4 interactions.
MINTMINT-1185164.
STRING9606.ENSP00000369274.

Chemistry

BindingDBP46019.
ChEMBLCHEMBL2111324.

PTM databases

PhosphoSiteP46019.

Polymorphism databases

DMDM1170685.

Proteomic databases

PaxDbP46019.
PRIDEP46019.

Protocols and materials databases

DNASU5256.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379942; ENSP00000369274; ENSG00000044446.
GeneID5256.
KEGGhsa:5256.
UCSCuc004cyv.4. human.

Organism-specific databases

CTD5256.
GeneCardsGC0XM018910.
H-InvDBHIX0176778.
HGNCHGNC:8926. PHKA2.
HPAHPA002912.
MIM300798. gene.
306000. phenotype.
neXtProtNX_P46019.
Orphanet264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKBPA33267.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82518.
HOGENOMHOG000231478.
HOVERGENHBG000273.
InParanoidP46019.
KOK07190.
OMATEMNSIG.
OrthoDBEOG73V6JF.
PhylomeDBP46019.
TreeFamTF313970.

Enzyme and pathway databases

BioCycMetaCyc:HS00576-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00163.

Gene expression databases

BgeeP46019.
CleanExHS_PHKA2.
GenevestigatorP46019.

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

GeneWikiPHKA2.
GenomeRNAi5256.
NextBio20304.
PROP46019.
SOURCESearch...

Entry information

Entry nameKPB2_HUMAN
AccessionPrimary (citable) accession number: P46019
Secondary accession number(s): A8K1T1 expand/collapse secondary AC list , Q6LAJ5, Q7Z6W0, Q96CR3, Q9UDA1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 146 of the entry and version 1 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