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P46019

- KPB2_HUMAN

UniProt

P46019 - KPB2_HUMAN

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Protein
Phosphorylase b kinase regulatory subunit alpha, liver isoform
Gene
PHKA2, PHKLA, PYK
Organism
Homo sapiens (Human)
Status
Reviewed - 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 and by calcium.

Pathwayi

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  2. phosphorylase kinase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular protein modification process Source: ProtInc
  3. generation of precursor metabolites and energy Source: ProtInc
  4. glucose metabolic process Source: Reactome
  5. glycogen catabolic process Source: Reactome
  6. protein phosphorylation Source: GOC
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00576-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
UniPathwayiUPA00163.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphorylase b kinase regulatory subunit alpha, liver isoform
Short name:
Phosphorylase kinase alpha L subunit
Gene namesi
Name:PHKA2
Synonyms:PHKLA, PYK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8926. PHKA2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. phosphorylase kinase complex Source: ProtInc
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.7 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201T → TYNTAT in GSD9A.
VAR_062393
Natural varianti132 – 1321H → P in GSD9A; type 2. 1 Publication
VAR_006177
Natural varianti132 – 1321H → Y in GSD9A; type 2. 1 Publication
VAR_006178
Natural varianti141 – 1411Missing in GSD9A; type 1. 1 Publication
VAR_006179
Natural varianti186 – 1861R → C in GSD9A; type 2. 2 Publications
VAR_006180
Natural varianti186 – 1861R → H in GSD9A; type 2. 2 Publications
VAR_006181
Natural varianti189 – 1902Missing in GSD9A; type 2.
VAR_012270
Natural varianti189 – 1891K → E in GSD9A; type 2. 1 Publication
VAR_012269
Natural varianti193 – 1931G → V in GSD9A; type 2. 1 Publication
VAR_012271
Natural varianti251 – 2511Missing in GSD9A; type 2. 1 Publication
VAR_006182
Natural varianti295 – 2951R → H in GSD9A; type 1 and type 2. 1 Publication
VAR_012272
Natural varianti299 – 2991D → G in GSD9A; type 2. 2 Publications
VAR_006183
Natural varianti399 – 3991P → S in GSD9A; type 1. 1 Publication
VAR_012273
Natural varianti498 – 4981P → L in GSD9A. 1 Publication
VAR_062394
Natural varianti818 – 8258Missing in GSD9A; type 1.
VAR_012274
Natural varianti869 – 8691P → R in GSD9A. 1 Publication
VAR_062395
Natural varianti916 – 9161R → W in GSD9A. 1 Publication
VAR_062396
Natural varianti953 – 9542NL → I in GSD9A; type 1.
VAR_012275
Natural varianti1070 – 10701Missing in GSD9A. 1 Publication
VAR_062397
Natural varianti1111 – 11111R → RTR in GSD9A; type 2.
VAR_006184
Natural varianti1113 – 11131M → I in GSD9A. 1 Publication
VAR_062398
Natural varianti1114 – 11141T → I in GSD9A; type 2. 1 Publication
VAR_006185
Natural varianti1125 – 11251E → K in GSD9A; type 1. 1 Publication
VAR_012276
Natural varianti1205 – 12051P → L in GSD9A; type 1. 1 Publication
VAR_006186
Natural varianti1207 – 12071G → W in GSD9A; type 1. 1 Publication
VAR_012277

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi306000. phenotype.
Orphaneti264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKBiPA33267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12351235Phosphorylase b kinase regulatory subunit alpha, liver isoform
PRO_0000057730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei729 – 7291Phosphoserine4 Publications
Modified residuei735 – 7351Phosphoserine2 Publications
Modified residuei1015 – 10151Phosphoserine3 Publications
Lipidationi1232 – 12321S-farnesyl cysteine By 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

MaxQBiP46019.
PaxDbiP46019.
PRIDEiP46019.

PTM databases

PhosphoSiteiP46019.

Expressioni

Tissue specificityi

Predominantly expressed in liver and other non-muscle tissues.

Gene expression databases

BgeeiP46019.
CleanExiHS_PHKA2.
GenevestigatoriP46019.

Organism-specific databases

HPAiHPA002912.

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

BioGridi111274. 10 interactions.
IntActiP46019. 4 interactions.
MINTiMINT-1185164.
STRINGi9606.ENSP00000369274.

Structurei

3D structure databases

ProteinModelPortaliP46019.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni807 – 83731Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni1059 – 109941Calmodulin-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG82518.
HOGENOMiHOG000231478.
HOVERGENiHBG000273.
InParanoidiP46019.
KOiK07190.
OMAiPRDDHGD.
OrthoDBiEOG73V6JF.
PhylomeDBiP46019.
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.

Sequencei

Sequence statusi: Complete.

P46019-1 [UniParc]FASTAAdd to Basket

« Hide

MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHEQK DAWVRDNIYS     50
ILAVWGLGMA YRKNADRDED KAKAYELEQN VVKLMRGLLQ CMMRQVAKVE 100
KFKHTQSTKD SLHAKYNTAT CGTVVGDDQW GHLQVDATSL FLLFLAQMTA 150
SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD YGMWERGDKT NQGIPELNAS 200
SVGMAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS ILFSMLPRAS 250
TSKEIDAGLL SIISFPAFAV EDVNLVNVTK NEIISKLQGR YGCCRFLRDG 300
YKTPREDPNR LHYDPAELKL FENIECEWPV FWTYFIIDGV FSGDAVQVQE 350
YREALEGILI RGKNGIRLVP ELYAVPPNKV DEEYKNPHTV DRVPMGKVPH 400
LWGQSLYILS SLLAEGFLAA GEIDPLNRRF STSVKPDVVV QVTVLAENNH 450
IKDLLRKHGV NVQSIADIHP IQVQPGRILS HIYAKLGRNK NMNLSGRPYR 500
HIGVLGTSKL YVIRNQIFTF TPQFTDQHHF YLALDNEMIV EMLRIELAYL 550
CTCWRMTGRP TLTFPISRTM LTNDGSDIHS AVLSTIRKLE DGYFGGARVK 600
LGNLSEFLTT SFYTYLTFLD PDCDEKLFDN ASEGTFSPDS DSDLVGYLED 650
TCNQESQDEL DHYINHLLQS TSLRSYLPPL CKNTEDRHVF SAIHSTRDIL 700
SVMAKAKGLE VPFVPMTLPT KVLSAHRKSL NLVDSPQPLL EKVPESDFQW 750
PRDDHGDVDC EKLVEQLKDC SNLQDQADIL YILYVIKGPS WDTNLSGQHG 800
VTVQNLLGEL YGKAGLNQEW GLIRYISGLL RKKVEVLAEA CTDLLSHQKQ 850
LTVGLPPEPR EKIISAPLPP EELTKLIYEA SGQDISIAVL TQEIVVYLAM 900
YVRAQPSLFV EMLRLRIGLI IQVMATELAR SLNCSGEEAS ESLMNLSPFD 950
MKNLLHHILS GKEFGVERSV RPIHSSTSSP TISIHEVGHT GVTKTERSGI 1000
NRLRSEMKQM TRRFSADEQF FSVGQAASSS AHSSKSARSS TPSSPTGTSS 1050
SDSGGHHIGW GERQGQWLRR RRLDGAINRV PVGFYQRVWK ILQKCHGLSI 1100
DGYVLPSSTT REMTPHEIKF AVHVESVLNR VPQPEYRQLL VEAIMVLTLL 1150
SDTEMTSIGG IIHVDQIVQM ASQLFLQDQV SIGAMDTLEK DQATGICHFF 1200
YDSAPSGAYG TMTYLTRAVA SYLQELLPNS GCQMQ 1235
Length:1,235
Mass (Da):138,408
Last modified:November 1, 1995 - v1
Checksum:i6CA10CFFA86A582A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381E → Q.
Corresponds to variant rs17313469 [ dbSNP | Ensembl ].
VAR_024563
Natural varianti120 – 1201T → TYNTAT in GSD9A.
VAR_062393
Natural varianti132 – 1321H → P in GSD9A; type 2. 1 Publication
VAR_006177
Natural varianti132 – 1321H → Y in GSD9A; type 2. 1 Publication
VAR_006178
Natural varianti141 – 1411Missing in GSD9A; type 1. 1 Publication
VAR_006179
Natural varianti186 – 1861R → C in GSD9A; type 2. 2 Publications
VAR_006180
Natural varianti186 – 1861R → H in GSD9A; type 2. 2 Publications
VAR_006181
Natural varianti189 – 1902Missing in GSD9A; type 2.
VAR_012270
Natural varianti189 – 1891K → E in GSD9A; type 2. 1 Publication
VAR_012269
Natural varianti193 – 1931G → V in GSD9A; type 2. 1 Publication
VAR_012271
Natural varianti251 – 2511Missing in GSD9A; type 2. 1 Publication
VAR_006182
Natural varianti295 – 2951R → H in GSD9A; type 1 and type 2. 1 Publication
VAR_012272
Natural varianti299 – 2991D → G in GSD9A; type 2. 2 Publications
VAR_006183
Natural varianti399 – 3991P → S in GSD9A; type 1. 1 Publication
VAR_012273
Natural varianti416 – 4161G → R.
Corresponds to variant rs16980929 [ dbSNP | Ensembl ].
VAR_050518
Natural varianti498 – 4981P → L in GSD9A. 1 Publication
VAR_062394
Natural varianti818 – 8258Missing in GSD9A; type 1.
VAR_012274
Natural varianti869 – 8691P → R in GSD9A. 1 Publication
VAR_062395
Natural varianti916 – 9161R → W in GSD9A. 1 Publication
VAR_062396
Natural varianti953 – 9542NL → I in GSD9A; type 1.
VAR_012275
Natural varianti1070 – 10701Missing in GSD9A. 1 Publication
VAR_062397
Natural varianti1111 – 11111R → RTR in GSD9A; type 2.
VAR_006184
Natural varianti1113 – 11131M → I in GSD9A. 1 Publication
VAR_062398
Natural varianti1114 – 11141T → I in GSD9A; type 2. 1 Publication
VAR_006185
Natural varianti1125 – 11251E → K in GSD9A; type 1. 1 Publication
VAR_012276
Natural varianti1205 – 12051P → L in GSD9A; type 1. 1 Publication
VAR_006186
Natural varianti1207 – 12071G → W in GSD9A; type 1. 1 Publication
VAR_012277

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti527 – 5271Q → E in AAH14036. 1 Publication
Sequence conflicti756 – 7561G → S in AAH14036. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14190.1.
RefSeqiNP_000283.1. NM_000292.2.
UniGeneiHs.54941.

Genome annotation databases

EnsembliENST00000379942; ENSP00000369274; ENSG00000044446.
GeneIDi5256.
KEGGihsa:5256.
UCSCiuc004cyv.4. human.

Polymorphism databases

DMDMi1170685.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14190.1.
RefSeqi NP_000283.1. NM_000292.2.
UniGenei Hs.54941.

3D structure databases

ProteinModelPortali P46019.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111274. 10 interactions.
IntActi P46019. 4 interactions.
MINTi MINT-1185164.
STRINGi 9606.ENSP00000369274.

Chemistry

BindingDBi P46019.
ChEMBLi CHEMBL2111324.

PTM databases

PhosphoSitei P46019.

Polymorphism databases

DMDMi 1170685.

Proteomic databases

MaxQBi P46019.
PaxDbi P46019.
PRIDEi P46019.

Protocols and materials databases

DNASUi 5256.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379942 ; ENSP00000369274 ; ENSG00000044446 .
GeneIDi 5256.
KEGGi hsa:5256.
UCSCi uc004cyv.4. human.

Organism-specific databases

CTDi 5256.
GeneCardsi GC0XM018910.
GeneReviewsi PHKA2.
H-InvDBi HIX0176778.
HGNCi HGNC:8926. PHKA2.
HPAi HPA002912.
MIMi 300798. gene.
306000. phenotype.
neXtProti NX_P46019.
Orphaneti 264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKBi PA33267.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG82518.
HOGENOMi HOG000231478.
HOVERGENi HBG000273.
InParanoidi P46019.
KOi K07190.
OMAi PRDDHGD.
OrthoDBi EOG73V6JF.
PhylomeDBi P46019.
TreeFami TF313970.

Enzyme and pathway databases

UniPathwayi UPA00163 .
BioCyci MetaCyc:HS00576-MONOMER.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

GeneWikii PHKA2.
GenomeRNAii 5256.
NextBioi 20304.
PROi P46019.
SOURCEi Search...

Gene expression databases

Bgeei P46019.
CleanExi HS_PHKA2.
Genevestigatori P46019.

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

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiKPB2_HUMAN
AccessioniPrimary (citable) accession number: P46019
Secondary accession number(s): A8K1T1
, Q6LAJ5, Q7Z6W0, Q96CR3, Q9UDA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 149 of the entry and version 1 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

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