P46019 (KPB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphorylase b kinase regulatory subunit alpha, liver isoform
Short name=Phosphorylase kinase alpha L subunit

Gene names

Name:	PHKA2
Synonyms:	PHKLA, PYK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1235 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Glycogen storage disease
Ligand	Calmodulin-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucose metabolic process Traceable author statement. Source: Reactome glycogen catabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome phosphorylase kinase complex Traceable author statement Ref.2. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro phosphorylase kinase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1235	1235	Phosphorylase b kinase regulatory subunit alpha, liver isoform		PRO_0000057730
Regions
	Region	807 – 837	31	Calmodulin-binding Potential
	Region	1059 – 1099	41	Calmodulin-binding Potential
Amino acid modifications
	Modified residue	729	1	Phosphoserine Ref.11 Ref.13 Ref.14 Ref.15
	Modified residue	735	1	Phosphoserine Ref.11 Ref.15
	Modified residue	1015	1	Phosphoserine Ref.11 Ref.12 Ref.14
	Modified residue	1048	1	Phosphothreonine By similarity
	Lipidation	1232	1	S-farnesyl cysteine By similarity
Natural variations
	Natural variant	38	1	E → Q. Corresponds to variant rs17313469 [ dbSNP | Ensembl ].		VAR_024563
	Natural variant	120	1	T → TYNTAT in GSD9A.		VAR_062393
	Natural variant	132	1	H → P in GSD9A; type 2. Ref.18		VAR_006177
	Natural variant	132	1	H → Y in GSD9A; type 2. Ref.18		VAR_006178
	Natural variant	141	1	Missing in GSD9A; type 1. Ref.1		VAR_006179
	Natural variant	186	1	R → C in GSD9A; type 2. Ref.3 Ref.17		VAR_006180
	Natural variant	186	1	R → H in GSD9A; type 2. Ref.3 Ref.18		VAR_006181
	Natural variant	189 – 190	2	Missing in GSD9A; type 2.		VAR_012270
	Natural variant	189	1	K → E in GSD9A; type 2. Ref.8		VAR_012269
	Natural variant	193	1	G → V in GSD9A; type 2. Ref.2		VAR_012271
	Natural variant	251	1	Missing in GSD9A; type 2. Ref.17		VAR_006182
	Natural variant	295	1	R → H in GSD9A; type 1 and type 2. Ref.3		VAR_012272
	Natural variant	299	1	D → G in GSD9A; type 2. Ref.18 Ref.19		VAR_006183
	Natural variant	399	1	P → S in GSD9A; type 1. Ref.8		VAR_012273
	Natural variant	416	1	G → R. Corresponds to variant rs16980929 [ dbSNP | Ensembl ].		VAR_050518
	Natural variant	498	1	P → L in GSD9A. Ref.19		VAR_062394
	Natural variant	818 – 825	8	Missing in GSD9A; type 1.		VAR_012274
	Natural variant	869	1	P → R in GSD9A. Ref.19		VAR_062395
	Natural variant	916	1	R → W in GSD9A. Ref.19		VAR_062396
	Natural variant	953 – 954	2	NL → I in GSD9A; type 1.		VAR_012275
	Natural variant	1070	1	Missing in GSD9A. Ref.19		VAR_062397
	Natural variant	1111	1	R → RTR in GSD9A; type 2.		VAR_006184
	Natural variant	1113	1	M → I in GSD9A. Ref.19		VAR_062398
	Natural variant	1114	1	T → I in GSD9A; type 2. Ref.17		VAR_006185
	Natural variant	1125	1	E → K in GSD9A; type 1. Ref.3		VAR_012276
	Natural variant	1205	1	P → L in GSD9A; type 1. Ref.1		VAR_006186
	Natural variant	1207	1	G → W in GSD9A; type 1. Ref.8		VAR_012277
Experimental info
	Sequence conflict	527	1	Q → E in AAH14036. Ref.7
	Sequence conflict	756	1	G → S in AAH14036. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P46019 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 6CA10CFFA86A582A	FASTA	1,235	138,408
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY.
[14]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[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

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80497 mRNA. Translation: CAA56662.1. D38616 mRNA. Translation: BAA07606.1. AF044572 , 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.
IPI	IPI00004237.
RefSeq	NP_000283.1. NM_000292.2.
UniGene	Hs.54941.
3D structure databases
ProteinModelPortal	P46019.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46019. 3 interactions.
MINT	MINT-1185164.
STRING	9606.ENSP00000369274.
PTM databases
PhosphoSite	P46019.
Polymorphism databases
DMDM	1170685.
Proteomic databases
PaxDb	P46019.
PRIDE	P46019.
Protocols and materials databases
DNASU	5256.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379942; ENSP00000369274; ENSG00000044446.
GeneID	5256.
KEGG	hsa:5256.
UCSC	uc004cyv.4. human.
Organism-specific databases
CTD	5256.
GeneCards	GC0XM018910.
H-InvDB	HIX0176778.
HGNC	HGNC:8926. PHKA2.
HPA	HPA002912.
MIM	300798. gene. 306000. phenotype.
neXtProt	NX_P46019.
Orphanet	264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKB	PA33267.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG82518.
HOGENOM	HOG000231478.
HOVERGEN	HBG000273.
InParanoid	P46019.
KO	K07190.
OMA	SHHKQLT.
OrthoDB	EOG4ZPDTH.
PhylomeDB	P46019.
Enzyme and pathway databases
BioCyc	MetaCyc:HS00576-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00163.
Gene expression databases
Bgee	P46019.
CleanEx	HS_PHKA2.
Genevestigator	P46019.
GermOnline	ENSG00000044446. Homo sapiens.
Family and domain databases
Gene3D	1.50.10.10. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR011613. Glyco_hydro_15. IPR008734. PHK_A/B_su. [Graphical view]
PANTHER	PTHR10749. PTHR10749. 1 hit.
Pfam	PF00723. Glyco_hydro_15. 1 hit. [Graphical view]
SUPFAM	SSF48208. Glyco_trans_6hp. 1 hit.
ProtoNet	Search...
Other
BindingDB	P46019.
ChEMBL	CHEMBL2906.
GenomeRNAi	5256.
NextBio	20304.
SOURCE	Search...

Entry information

Entry name

KPB2_HUMAN

Accession

Primary (citable) accession number: P46019
Secondary accession number(s): A8K1T1 , Q6LAJ5, Q7Z6W0, Q96CR3, Q9UDA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.