P46020 (KPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
Short name=Phosphorylase kinase alpha M subunit

Gene names

Name:	PHKA1
Synonyms:	PHKA

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	1223 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. Allosteric regulation 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	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.
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 9D (GSD9D) [MIM:300559]: A metabolic disorder characterized by slowly progressive, predominantly distal muscle weakness and atrophy. Clinical features include exercise intolerance with early fatigability, pain, cramps and occasionally myoglobinuria. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8
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	Alternative splicing
Disease	Disease mutation Glycogen storage disease
Ligand	Calmodulin-binding
Molecular function	Muscle protein
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 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.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P46020-1)

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.

Isoform 2 (identifier: P46020-2)

Also known as: C;

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

Isoform 3 (identifier: P46020-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1223	1223	Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform		PRO_0000057726
Regions
	Region	810 – 840	31	Calmodulin-binding Potential
	Region	1046 – 1086	41	Calmodulin-binding Potential
Sites
	Site	1220	1	Not methylated
Amino acid modifications
	Modified residue	200	1	Phosphoserine By similarity
	Modified residue	201	1	Phosphoserine By similarity
	Modified residue	735	1	Phosphoserine Ref.4
	Modified residue	758	1	Phosphoserine Ref.6
	Modified residue	972	1	Phosphoserine Ref.5 Ref.6
	Modified residue	985	1	Phosphoserine Ref.5 Ref.6
	Modified residue	1007	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	1018	1	Phosphoserine; by PKA By similarity
	Modified residue	1020	1	Phosphoserine By similarity
	Modified residue	1023	1	Phosphoserine By similarity
	Lipidation	1220	1	S-farnesyl cysteine By similarity
Natural variations
	Alternative sequence	654 – 713	60	ARCGD…LHVQN → D in isoform 3.		VSP_042517
	Alternative sequence	1011 – 1023	13	Missing in isoform 3.		VSP_042518
	Alternative sequence	1012 – 1024	13	Missing in isoform 2.		VSP_004697
	Natural variant	299	1	D → V in GSD9D. Ref.8		VAR_020856
Experimental info
	Sequence conflict	568	1	H → Y in CAA52083. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AC) [UniParc]. Last modified July 11, 2006. Version 2. Checksum: 48511719C0BFE40F	FASTA	1,223	137,312
	10 20 30 40 50 60 MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA 70 80 90 100 110 120 YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT 130 140 150 160 170 180 CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD 190 200 210 220 230 240 FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS 250 260 270 280 290 300 ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG 310 320 330 340 350 360 YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE YKEALEAVLI 370 380 390 400 410 420 KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP 430 440 450 460 470 480 GEIDPLNRRF STVPKPDVVV QVSILAETEE IKTILKDKGI YVETIAEVYP IRVQPARILS 490 500 510 520 530 540 HIYSSLGCNN RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV 550 560 570 580 590 600 EMLRTDLSYL CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ 610 620 630 640 650 660 TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS TSHARCGDEV 670 680 690 700 710 720 ARYLDHLLAH TAPHPKLAPT SQKGGLDRFQ AAVQTTCDLM SLVTKAKELH VQNVHMYLPT 730 740 750 760 770 780 KLFQASRPSF NLLDSPHPRQ ENQVPSVRVE IHLPRDQSGE VDFKALVLQL KETSSLQEQA 790 800 810 820 830 840 DILYMLYTMK GPDWNTELYN ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL 850 860 870 880 890 900 DEACTDLLSH QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMSI SILTQEIMVY 910 920 930 940 950 960 LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS PSAMKNLLHH 970 980 990 1000 1010 1020 ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT GIMQLKSEIK QVEFRRLSIS 1030 1040 1050 1060 1070 1080 AESQSPGTSM TPSSGSFPSA YDQQSSKDSR QGQWQRRRRL DGALNRVPVG FYQKVWKVLQ 1090 1100 1110 1120 1130 1140 KCHGLSVEGF VLPSSTTREM TPGEIKFSVH VESVLNRVPQ PEYRQLLVEA ILVLTMLADI 1150 1160 1170 1180 1190 1200 EIHSIGSIIA VEKIVHIAND LFLQEQKTLG ADDTMLAKDP ASGICTLLYD SAPSGRFGTM 1210 1220 TYLSKAAATY VQEFLPHSIC AMQ
	Isoform 2 (C) [UniParc]. Checksum: 6D79FA1069CE6D25	FASTA	1,210	135,808
	10 20 30 40 50 60 MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA 70 80 90 100 110 120 YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT 130 140 150 160 170 180 CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD 190 200 210 220 230 240 FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS 250 260 270 280 290 300 ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG 310 320 330 340 350 360 YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE YKEALEAVLI 370 380 390 400 410 420 KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP 430 440 450 460 470 480 GEIDPLNRRF STVPKPDVVV QVSILAETEE IKTILKDKGI YVETIAEVYP IRVQPARILS 490 500 510 520 530 540 HIYSSLGCNN RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV 550 560 570 580 590 600 EMLRTDLSYL CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ 610 620 630 640 650 660 TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS TSHARCGDEV 670 680 690 700 710 720 ARYLDHLLAH TAPHPKLAPT SQKGGLDRFQ AAVQTTCDLM SLVTKAKELH VQNVHMYLPT 730 740 750 760 770 780 KLFQASRPSF NLLDSPHPRQ ENQVPSVRVE IHLPRDQSGE VDFKALVLQL KETSSLQEQA 790 800 810 820 830 840 DILYMLYTMK GPDWNTELYN ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL 850 860 870 880 890 900 DEACTDLLSH QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMSI SILTQEIMVY 910 920 930 940 950 960 LAMYMRTQPG LFAEMFRLRI GLIIQVMATE LAHSLRCSAE EATEGLMNLS PSAMKNLLHH 970 980 990 1000 1010 1020 ILSGKEFGVE RSVRPTDSNV SPAISIHEIG AVGATKTERT GIMQLKSEIK QSPGTSMTPS 1030 1040 1050 1060 1070 1080 SGSFPSAYDQ QSSKDSRQGQ WQRRRRLDGA LNRVPVGFYQ KVWKVLQKCH GLSVEGFVLP 1090 1100 1110 1120 1130 1140 SSTTREMTPG EIKFSVHVES VLNRVPQPEY RQLLVEAILV LTMLADIEIH SIGSIIAVEK 1150 1160 1170 1180 1190 1200 IVHIANDLFL QEQKTLGADD TMLAKDPASG ICTLLYDSAP SGRFGTMTYL SKAAATYVQE 1210 FLPHSICAMQ
	Isoform 3 [UniParc]. Checksum: F8E38DBD42155D47	FASTA	1,151	129,388
	10 20 30 40 50 60 MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA 70 80 90 100 110 120 YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT 130 140 150 160 170 180 CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD 190 200 210 220 230 240 FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS 250 260 270 280 290 300 ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSQLVELTK QEIITKLQGR YGCCRFLRDG 310 320 330 340 350 360 YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGV FSGNAEQVQE YKEALEAVLI 370 380 390 400 410 420 KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP 430 440 450 460 470 480 GEIDPLNRRF STVPKPDVVV QVSILAETEE IKTILKDKGI YVETIAEVYP IRVQPARILS 490 500 510 520 530 540 HIYSSLGCNN RMKLSGRPYR HMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNKMIV 550 560 570 580 590 600 EMLRTDLSYL CSRWRMTGQP TITFPISHSM LDEDGTSLNS SILAALRKMQ DGYFGGARVQ 610 620 630 640 650 660 TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDDNYDYLE SGNWMNDYDS TSHDVHMYLP 670 680 690 700 710 720 TKLFQASRPS FNLLDSPHPR QENQVPSVRV EIHLPRDQSG EVDFKALVLQ LKETSSLQEQ 730 740 750 760 770 780 ADILYMLYTM KGPDWNTELY NERSATVREL LTELYGKVGE IRHWGLIRYI SGILRKKVEA 790 800 810 820 830 840 LDEACTDLLS HQKHLTVGLP PEPREKTISA PLPYEALTQL IDEASEGDMS ISILTQEIMV 850 860 870 880 890 900 YLAMYMRTQP GLFAEMFRLR IGLIIQVMAT ELAHSLRCSA EEATEGLMNL SPSAMKNLLH 910 920 930 940 950 960 HILSGKEFGV ERSVRPTDSN VSPAISIHEI GAVGATKTER TGIMQLKSEI KQSPGTSMTP 970 980 990 1000 1010 1020 SSGSFPSAYD QQSSKDSRQG QWQRRRRLDG ALNRVPVGFY QKVWKVLQKC HGLSVEGFVL 1030 1040 1050 1060 1070 1080 PSSTTREMTP GEIKFSVHVE SVLNRVPQPE YRQLLVEAIL VLTMLADIEI HSIGSIIAVE 1090 1100 1110 1120 1130 1140 KIVHIANDLF LQEQKTLGAD DTMLAKDPAS GICTLLYDSA PSGRFGTMTY LSKAAATYVQ 1150 EFLPHSICAM Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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-972 AND SER-985, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"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].
[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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00004247. IPI00216725. IPI00446678.
PIR	I38111.
RefSeq	NP_001116142.1. NM_001122670.1. NP_001165907.1. NM_001172436.1. NP_002628.2. NM_002637.3.
UniGene	Hs.201379.
3D structure databases
ProteinModelPortal	P46020.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46020. 2 interactions.
STRING	9606.ENSP00000362643.
PTM databases
PhosphoSite	P46020.
Polymorphism databases
DMDM	110282976.
Proteomic databases
PaxDb	P46020.
PRIDE	P46020.
Protocols and materials databases
DNASU	5255.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000339490; ENSP00000342469; ENSG00000067177. ENST00000373542; ENSP00000362643; ENSG00000067177. ENST00000541944; ENSP00000441251; ENSG00000067177. ENST00000593378; ENSP00000471521; ENSG00000268579. ENST00000600891; ENSP00000471771; ENSG00000268579. ENST00000601371; ENSP00000472984; ENSG00000268579.
GeneID	5255.
KEGG	hsa:5255.
UCSC	uc004eax.4. human. uc004eay.4. human. uc011mqi.2. human.
Organism-specific databases
CTD	5255.
GeneCards	GC0XM071715.
HGNC	HGNC:8925. PHKA1.
HPA	HPA001081.
MIM	300559. phenotype. 311870. gene.
neXtProt	NX_P46020.
Orphanet	715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKB	PA33266.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG82518.
HOGENOM	HOG000231478.
HOVERGEN	HBG000273.
KO	K07190.
OrthoDB	EOG4ZPDTH.
PhylomeDB	P46020.
Enzyme and pathway databases
BioCyc	MetaCyc:HS00901-MONOMER.
BRENDA	2.7.11.19. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00163.
Gene expression databases
ArrayExpress	P46020.
Bgee	P46020.
CleanEx	HS_PHKA1.
Genevestigator	P46020.
GermOnline	ENSG00000067177. 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	P46020.
ChEMBL	CHEMBL2905.
ChiTaRS	PHKA1. human.
GenomeRNAi	5255.
NextBio	20300.
SOURCE	Search...

Entry information

Entry name

KPB1_HUMAN

Accession

Primary (citable) accession number: P46020
Secondary accession number(s): B7ZL05, B7ZL07, Q2M3D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	July 11, 2006
Last modified:	May 29, 2013
This is version 125 of the entry and version 2 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.