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P11217 (PYGM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen phosphorylase, muscle form

EC=2.4.1.1
Alternative name(s):
Myophosphorylase
Gene names
Name:PYGM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length842 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Catalytic activity

((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.

Subunit structure

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

Post-translational modification

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. Ref.10

Involvement in disease

Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the glycogen phosphorylase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11217-1)

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: P11217-2)

The sequence of this isoform differs from the canonical sequence as follows:
     82-169: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 842841Glycogen phosphorylase, muscle form
PRO_0000188529

Sites

Binding site761AMP By similarity
Site1091Involved in the association of subunits By similarity
Site1431Involved in the association of subunits By similarity
Site1561May be involved in allosteric control By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue151Phosphoserine; by PHK; in form phosphorylase A Ref.10
Modified residue4731Phosphotyrosine By similarity
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence82 – 16988Missing in isoform 2.
VSP_043047
Natural variant1161L → P in GSD5. Ref.15 Ref.22
VAR_014002
Natural variant1941R → W in GSD5. Ref.22
VAR_014003
Natural variant2051G → S in GSD5. Ref.11 Ref.13 Ref.16 Ref.17 Ref.22
Corresponds to variant rs119103251 [ dbSNP | Ensembl ].
VAR_003431
Natural variant2921L → P in GSD5; rare mutation. Ref.13
VAR_014004
Natural variant3491E → K in GSD5. Ref.22
VAR_014005
Natural variant3971L → P in GSD5. Ref.12 Ref.13
VAR_003432
Natural variant4141R → G.
Corresponds to variant rs11231866 [ dbSNP | Ensembl ].
VAR_061198
Natural variant4881T → N in GSD5. Ref.20 Ref.22
VAR_014006
Natural variant5431K → T in GSD5. Ref.11 Ref.13
VAR_003433
Natural variant6021R → W in GSD5. Ref.22
VAR_014007
Natural variant6551E → K in GSD5. Ref.12 Ref.13
VAR_003434
Natural variant6601A → D in GSD5. Ref.21 Ref.22
VAR_014008
Natural variant6661Q → E in GSD5. Ref.14
VAR_014009
Natural variant6851N → Y in GSD5. Ref.16 Ref.22
VAR_014010
Natural variant6861G → R in GSD5. Ref.14
VAR_014011
Natural variant6871A → P in GSD5. Ref.23
VAR_014012
Natural variant7041A → V in GSD5. Ref.22
VAR_014013
Natural variant7091Missing in GSD5; common in Japanese patients. Ref.13
VAR_014014
Natural variant7981W → R in GSD5. Ref.18 Ref.19 Ref.22
VAR_014015

Experimental info

Sequence conflict7911L → W in AAA60231. Ref.1

Secondary structure

......................................................................................................................................... 842
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 6.
Checksum: EBDB7D80D740B68F

FASTA84297,092
        10         20         30         40         50         60 
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM 

       130        140        150        160        170        180 
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA 

       190        200        210        220        230        240 
DDWLRYGNPW EKARPEFTLP VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 

       250        260        270        280        290        300 
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERM 

       370        380        390        400        410        420 
DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP 

       430        440        450        460        470        480 
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLVLCNPGL AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ 

       550        560        570        580        590        600 
ENKLKFAAYL EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV 

       610        620        630        640        650        660 
PRTVMIGGKA APGYHMAKMI IRLVTAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD 

       730        740        750        760        770        780 
KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYED 

       790        800        810        820        830        840 
YIKCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE 


AI 

« Hide

Isoform 2 [UniParc].

Checksum: F5C64CA460DA3FC9
Show »

FASTA75487,317

References

« Hide 'large scale' references
[1]"Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase."
Burke J., Hwang P.K., Anderson L., Lebo R., Gorin F., Fletterick R.J.
Proteins 2:177-187(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation."
Kubisch C., Wicklein E.M., Jentsch T.J.
Hum. Mutat. 12:27-32(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Carty M.D., Clancy Y.C., Soeller W.C.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[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] (ISOFORM 2).
Tissue: Tongue.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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] (ISOFORM 1).
[8]"Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs."
Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., Crerar M.M.
Eur. J. Biochem. 152:267-274(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-842 (ISOFORM 1).
[9]"Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis."
Gautron S., Daegelen D., Mennecier F., Dubocq D., Kahn A., Dreyfus J.-C.
J. Clin. Invest. 79:275-281(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 455-676 (ISOFORM 1).
[10]"Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties."
Carty T.J., Tu J., Graves D.J.
J. Biol. Chem. 250:4980-4985(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-15.
[11]"Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease)."
Tsujino S., Shanske S., Dimauro S.
N. Engl. J. Med. 329:241-245(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD5 SER-205 AND THR-543.
[12]"Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease)."
Tsujino S., Shanske S., Martinuzzi A., Heiman-Patterson T., Dimauro S.
Hum. Mutat. 6:276-277(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD5 PRO-397 AND LYS-655.
[13]"The molecular genetic basis of myophosphorylase deficiency (McArdle's disease)."
Tsujino S., Shanske S., Nonaka I., DiMauro S.
Muscle Nerve 3:S23-S27(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD5 SER-205; PRO-292; PRO-397; THR-543; LYS-655 AND PHE-709 DEL.
[14]"Mutation analysis in myophosphorylase deficiency (McArdle's disease)."
Vorgerd M., Kubisch C., Burwinkel B., Reichmann H., Mortier W., Tettenborn B., Pongratz D., Lindemuth R., Tegenthoff M., Malin J.P., Kilimann M.W.
Ann. Neurol. 43:326-331(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD5 GLU-666 AND ARG-686.
[15]"A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact."
Gamez J., Fernandez R., Bruno C., Andreu A.L., Cervera C., Navarro C., Schwartz S., Dimauro S.
Muscle Nerve 22:1136-1138(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 PRO-116.
[16]"A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease."
Andreu A.L., Bruno C., Tamburino L., Gamez J., Shanske S., Cervera C., Navarro C., DiMauro S.
Neuromuscul. Disord. 9:171-173(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD5 SER-205 AND TYR-685.
[17]"McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient."
Rubio J.C., Martin M.A., Garcia A., Campos Y., Cabello A., Culebras J.M., Arenas J.
Neuromuscul. Disord. 9:174-175(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 SER-205.
[18]"A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease."
Fernandez R., Navarro C., Andreu A.L., Bruno C., Shanske S., Gamez J., Teijeira S., Hernandez I., Teijeiro A., Fernandez J.M., Musumeci O., DiMauro S.
Arch. Neurol. 57:217-219(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 ARG-798.
[19]"A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease."
Rubio J.C., Martin M.A., Campos Y., Auciello R., Cabello A., Arenas J.
Muscle Nerve 23:129-131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 ARG-798.
[20]"A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease."
Rubio J.C., Martin M.A., Campos Y., Cabello A., Arenas J.
Neuromuscul. Disord. 10:138-140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 ASN-488.
[21]"A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease."
Martin M.A., Rubio J.C., Campos Y., Ricoy J.R., Cabello A., Arenas J.
Neuromuscul. Disord. 10:447-449(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 ASP-660.
[22]"Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study."
Martin M.A., Rubio J.C., Buchbinder J., Fernandez-Hojas R., del Hoyo P., Teijeira S., Gamez J., Navarro C., Fernandez J.M., Cabello A., Campos Y., Cervera C., Culebras J.M., Andreu A.L., Fletterick R.J., Arenas J.
Ann. Neurol. 50:574-581(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD5 PRO-116; TRP-194; SER-205; LYS-349; ASN-488; TRP-602; ASP-660; TYR-685; VAL-704 AND ARG-798.
[23]"Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease."
Bruno C., Lanzillo R., Biedi C., Iadicicco L., Minetti C., Santoro L.
Neuromuscul. Disord. 12:498-500(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD5 PRO-687.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32598 expand/collapse EMBL AC list , M32579, M32580, M32581, M32582, M32583, M32584, M32585, M32586, M32587, M32588, M32589, M32590, M32591, M32592, M32593, M32594, M32595, M32596, M32597 Genomic DNA. Translation: AAA60231.1.
U94777 expand/collapse EMBL AC list , U94774, U94775, U94776 Genomic DNA. Translation: AAC52081.1.
AF066859 mRNA. Translation: AAC17451.1.
AK056607 mRNA. Translation: BAG51762.1.
AP001462 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74284.1.
BC126392 mRNA. Translation: AAI26393.1.
BC130514 mRNA. Translation: AAI30515.1.
X03031 mRNA. Translation: CAA26834.1.
M16013 mRNA. Translation: AAA36216.1.
CCDSCCDS53659.1. [P11217-2]
CCDS8079.1. [P11217-1]
PIRA27335.
RefSeqNP_001158188.1. NM_001164716.1. [P11217-2]
NP_005600.1. NM_005609.2. [P11217-1]
UniGeneHs.154084.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z8DX-ray2.30A1-842[»]
ProteinModelPortalP11217.
SMRP11217. Positions 3-837.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111795. 8 interactions.
IntActP11217. 21 interactions.
MINTMINT-1134630.
STRING9606.ENSP00000164139.

Chemistry

BindingDBP11217.
ChEMBLCHEMBL3526.
DrugBankDB00114. Pyridoxal Phosphate.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSiteP11217.

Polymorphism databases

DMDM3041717.

Proteomic databases

MaxQBP11217.
PaxDbP11217.
PRIDEP11217.

Protocols and materials databases

DNASU5837.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000164139; ENSP00000164139; ENSG00000068976. [P11217-1]
ENST00000377432; ENSP00000366650; ENSG00000068976. [P11217-2]
GeneID5837.
KEGGhsa:5837.
UCSCuc001oax.4. human. [P11217-1]
uc001oay.4. human. [P11217-2]

Organism-specific databases

CTD5837.
GeneCardsGC11M064513.
GeneReviewsPYGM.
HGNCHGNC:9726. PYGM.
HPAHPA056003.
MIM232600. phenotype.
608455. gene.
neXtProtNX_P11217.
Orphanet368. Glycogen storage disease due to muscle glycogen phosphorylase deficiency.
PharmGKBPA34069.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0058.
HOGENOMHOG000278444.
HOVERGENHBG006848.
InParanoidP11217.
KOK00688.
OMACHTVNGV.
OrthoDBEOG7JQBMK.
PhylomeDBP11217.
TreeFamTF300309.

Enzyme and pathway databases

BioCycMetaCyc:HS00949-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP11217.
CleanExHS_PYGM.
GenevestigatorP11217.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. PTHR11468. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11217.
GenomeRNAi5837.
NextBio22746.
PROP11217.
SOURCESearch...

Entry information

Entry namePYGM_HUMAN
AccessionPrimary (citable) accession number: P11217
Secondary accession number(s): A0AVK1, A6NDY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 175 of the entry and version 6 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 11

Human chromosome 11: entries, gene names and cross-references to MIM