Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P06737 (PYGL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 176. 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, liver form

EC=2.4.1.1
Gene names
Name:PYGL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length847 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. Interacts with PPP1R3B By similarity.

Post-translational modification

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. Ref.14

Involvement in disease

Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4

Sequence similarities

Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glycogen metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Glycogen storage disease
   LigandNucleotide-binding
Pyridoxal phosphate
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process5-phosphoribose 1-diphosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

glucose homeostasis

Inferred from mutant phenotype PubMed 17705025. Source: UniProtKB

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen catabolic process

Traceable author statement. Source: Reactome

glycogen metabolic process

Inferred from mutant phenotype Ref.13PubMed 17705025. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionAMP binding

Inferred from direct assay Ref.14Ref.13. Source: UniProtKB

ATP binding

Inferred from direct assay Ref.14. Source: UniProtKB

bile acid binding

Inferred from direct assay Ref.15. Source: UniProtKB

drug binding

Inferred from direct assay Ref.13Ref.15. Source: UniProtKB

glucose binding

Non-traceable author statement Ref.15. Source: UniProtKB

glycogen phosphorylase activity

Inferred from mutant phenotype Ref.13PubMed 17705025Ref.4. Source: UniProtKB

protein homodimerization activity

Non-traceable author statement PubMed 17705025. Source: UniProtKB

purine nucleobase binding

Inferred from direct assay Ref.15. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

vitamin binding

Inferred from direct assay Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06737-1)

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: P06737-2)

The sequence of this isoform differs from the canonical sequence as follows:
     82-115: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 847846Glycogen phosphorylase, liver form
PRO_0000188524

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-acetylalanine Ref.10
Modified residue151Phosphoserine; by PHK; in form phosphorylase A Ref.14
Modified residue3641N6-succinyllysine By similarity
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence82 – 11534Missing in isoform 2.
VSP_045339
Natural variant2221V → I. Ref.4
Corresponds to variant rs946616 [ dbSNP | Ensembl ].
VAR_007907
Natural variant2311V → E.
Corresponds to variant rs1042195 [ dbSNP | Ensembl ].
VAR_013095
Natural variant3391N → S in GSD6. Ref.4
VAR_007908
Natural variant3771N → K in GSD6. Ref.4
VAR_007909
Natural variant4251R → P. Ref.1
Corresponds to variant rs2228499 [ dbSNP | Ensembl ].
VAR_034425
Natural variant6981V → G.
Corresponds to variant rs35831273 [ dbSNP | Ensembl ].
VAR_034426
Natural variant7151R → S.
Corresponds to variant rs1042210 [ dbSNP | Ensembl ].
VAR_013096
Natural variant8061I → L.
Corresponds to variant rs34313873 [ dbSNP | Ensembl ].
VAR_034427
Natural variant8451N → S. Ref.5
Corresponds to variant rs78558135 [ dbSNP | Ensembl ].
VAR_069054

Experimental info

Sequence conflict2 – 32AK → GE in AAA52577. Ref.1
Sequence conflict2 – 32AK → GE in AAC18079. Ref.3
Sequence conflict831V → E in AAA52577. Ref.1
Sequence conflict3231A → Q in AAA52577. Ref.1
Sequence conflict344 – 3452AL → RI in AAA52577. Ref.1
Sequence conflict3691T → N in AAA52577. Ref.1
Sequence conflict3691T → N in AAC18079. Ref.3
Sequence conflict5701R → S in AAC17450. Ref.2
Sequence conflict6831Missing in AAH09895. Ref.8
Sequence conflict7151R → G in BAG62279. Ref.5

Secondary structure

.......................................................................................................................................................... 847
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: 74017E8125FB5735

FASTA84797,149
        10         20         30         40         50         60 
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR DYYFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDI 

       130        140        150        160        170        180 
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA 

       190        200        210        220        230        240 
DDWLRYGNPW EKSRPEFMLP VHFYGKVEHT NTGTKWIDTQ VVLALPYDTP VPGYMNNTVN 

       250        260        270        280        290        300 
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKASKFGST RGAGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL 

       370        380        390        400        410        420 
PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH LEIIYEINQK HLDRIVALFP 

       430        440        450        460        470        480 
KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS HAVNGVAKIH SDIVKTKVFK DFSELEPDKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ 

       550        560        570        580        590        600 
ENKLKFSQFL ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV 

       610        620        630        640        650        660 
PRTVIIGGKA APGYHMAKMI IKLITSVADV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRIDDVA 

       730        740        750        760        770        780 
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPKQPDLFK DIINMLFYHD RFKVFADYEA 

       790        800        810        820        830        840 
YVKCQDKVSQ LYMNPKAWNT MVLKNIAASG KFSSDRTIKE YAQNIWNVEP SDLKISLSNE 


SNKVNGN 

« Hide

Isoform 2 [UniParc].

Checksum: 40B7DB0528A64AAA
Show »

FASTA81393,134

References

« Hide 'large scale' references
[1]"Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage."
Newgard C.B., Nakano K., Hwang P.K., Fletterick R.J.
Proc. Natl. Acad. Sci. U.S.A. 83:8132-8136(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-425.
Tissue: Liver.
[2]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: Liver.
[3]"Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI."
Chang S., Rosenberg M.J., Morton H., Francomano C.A., Biesecker L.G.
Hum. Mol. Genet. 7:865-870(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Mutations in the liver glycogen phosphorylase gene 'PYGL' underlying glycogenosis type VI."
Burwinkel B., Bakker H.D., Herschkovitz E., Moses S.W., Shin Y.S., Kilimann M.W.
Am. J. Hum. Genet. 62:785-791(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GSD6 SER-339 AND LYS-377, VARIANT ILE-222.
Tissue: Blood.
[5]"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), VARIANT SER-845.
[6]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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).
Tissue: Placenta, Skin and Uterus.
[9]"McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues."
Gorin F.A., Mullinax R.L., Ignacio P.C., Neve R.L., Kurnit D.M.
J. Neurogenet. 4:293-308(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 482-847 (ISOFORM 1).
Tissue: Fetal brain.
[10]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"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].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Human liver glycogen phosphorylase inhibitors bind at a new allosteric site."
Rath V.L., Ammirati M., Danley D.E., Ekstrom J.L., Gibbs E.M., Hynes T.R., Mathiowetz A.M., McPherson R.K., Olson T.V., Treadway J.L., Hoover D.J.
Chem. Biol. 7:677-682(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[14]"Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core."
Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N., Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., Pandit J.
Mol. Cell 6:139-148(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), PHOSPHORYLATION AT SER-15.
[15]"Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase."
Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J., Danley D.E., Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J., Day Y.S., Myszka D.G., Rath V.L.
Chem. Biol. 9:915-924(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14636 mRNA. Translation: AAA52577.1.
AF066858 mRNA. Translation: AAC17450.1.
AF046798 expand/collapse EMBL AC list , AF046787, AF046788, AF046789, AF046790, AF046791, AF046792, AF046793, AF046794, AF046795, AF046796, AF046797 Genomic DNA. Translation: AAC18079.1.
AF046785 mRNA. Translation: AAC23504.1.
Y15233 mRNA. Translation: CAA75517.1.
AK300580 mRNA. Translation: BAG62279.1.
AL358334 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65685.1.
BC009895 mRNA. Translation: AAH09895.3.
BC082229 mRNA. Translation: AAH82229.2.
BC095850 mRNA. Translation: AAH95850.2.
BC110791 mRNA. Translation: AAI10792.2.
M36807 mRNA. Translation: AAA35906.1.
CCDSCCDS32080.1. [P06737-1]
CCDS53894.1. [P06737-2]
PIRA25518.
RefSeqNP_001157412.1. NM_001163940.1. [P06737-2]
NP_002854.3. NM_002863.4. [P06737-1]
UniGeneHs.282417.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EM6X-ray2.20A/B1-847[»]
1EXVX-ray2.40A/B1-847[»]
1FA9X-ray2.40A2-847[»]
1FC0X-ray2.40A/B2-847[»]
1L5QX-ray2.25A/B1-847[»]
1L5RX-ray2.10A/B1-847[»]
1L5SX-ray2.10A/B1-847[»]
1L7XX-ray2.30A/B1-847[»]
1XOIX-ray2.10A/B2-847[»]
2ATIX-ray1.90A/B2-847[»]
2QLLX-ray2.56A1-847[»]
2ZB2X-ray2.45A/B1-847[»]
3CEHX-ray2.80A/B24-832[»]
3CEJX-ray3.30A/B24-832[»]
3CEMX-ray2.47A/B24-832[»]
3DD1X-ray2.57A/B2-847[»]
3DDSX-ray1.80A/B2-847[»]
3DDWX-ray1.90A/B2-847[»]
ProteinModelPortalP06737.
SMRP06737. Positions 6-839.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111794. 21 interactions.
IntActP06737. 7 interactions.
MINTMINT-1208599.
STRING9606.ENSP00000216392.

Chemistry

BindingDBP06737.
ChEMBLCHEMBL2568.
DrugBankDB00131. Adenosine monophosphate.
DB00114. Pyridoxal Phosphate.
DB00140. Riboflavin.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSiteP06737.

Polymorphism databases

DMDM6648082.

Proteomic databases

MaxQBP06737.
PaxDbP06737.
PeptideAtlasP06737.
PRIDEP06737.

Protocols and materials databases

DNASU5836.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216392; ENSP00000216392; ENSG00000100504. [P06737-1]
ENST00000544180; ENSP00000443787; ENSG00000100504. [P06737-2]
GeneID5836.
KEGGhsa:5836.
UCSCuc001wyu.3. human. [P06737-1]

Organism-specific databases

CTD5836.
GeneCardsGC14M051324.
HGNCHGNC:9725. PYGL.
HPAHPA000962.
HPA004119.
MIM232700. phenotype.
613741. gene.
neXtProtNX_P06737.
Orphanet369. Glycogen storage disease due to liver glycogen phosphorylase deficiency.
PharmGKBPA34068.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0058.
HOVERGENHBG006848.
InParanoidP06737.
KOK00688.
OMADLVNMLF.
PhylomeDBP06737.
TreeFamTF300309.

Enzyme and pathway databases

BioCycMetaCyc:HS02099-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP06737.
BgeeP06737.
CleanExHS_PYGL.
GenevestigatorP06737.

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

ChiTaRSPYGL. human.
EvolutionaryTraceP06737.
GenomeRNAi5836.
NextBio22742.
PROP06737.
SOURCESearch...

Entry information

Entry namePYGL_HUMAN
AccessionPrimary (citable) accession number: P06737
Secondary accession number(s): A6NDQ4 expand/collapse secondary AC list , B4DUB7, F5H816, O60567, O60752, O60913, Q501V9, Q641R5, Q96G82
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 176 of the entry and version 4 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 14

Human chromosome 14: entries, gene names and cross-references to MIM