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P11216 (PYGB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen phosphorylase, brain form

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

Protein attributes

Sequence length843 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 non-covalent 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.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 843842Glycogen phosphorylase, brain form
PRO_0000188535

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.6 Ref.7 Ref.9
Modified residue151Phosphoserine; by PHK; in form phosphorylase A Probable
Modified residue1971Phosphotyrosine By similarity
Modified residue4731Phosphotyrosine By similarity
Modified residue6811N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant3031A → S.
Corresponds to variant rs2228976 [ dbSNP | Ensembl ].
VAR_034428
Natural variant5021D → N.
Corresponds to variant rs2227891 [ dbSNP | Ensembl ].
VAR_020212

Experimental info

Sequence conflict2 – 32AK → GE Ref.1
Sequence conflict2 – 32AK → GE Ref.2
Sequence conflict2481K → R in AAA59597. Ref.1
Sequence conflict3021A → G in AAA59597. Ref.1
Sequence conflict835 – 8439IPPPNIPRD → LQHLPHPEWESGGATCWAPP ELCTHLAMY in AAA59597. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11216 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 810BFAD3002CACB0

FASTA84396,696
        10         20         30         40         50         60 
MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL 

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

       190        200        210        220        230        240 
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN 

       250        260        270        280        290        300 
TMRLWSAKAP NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV 

       370        380        390        400        410        420 
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP 

       430        440        450        460        470        480 
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLLLCNPGL ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ 

       550        560        570        580        590        600 
ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV 

       610        620        630        640        650        660 
PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE 

       730        740        750        760        770        780 
ALDRKGYNAR EYYDHLPELK QAVDQISSGF FSPKEPDCFK DIVNMLMHHD RFKVFADYEA 

       790        800        810        820        830        840 
YMQCQAQVDQ LYRNPKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI 


PRD 

« Hide

References

« Hide 'large scale' references
[1]"Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes."
Newgard C.B., Littman D.R., van Genderen C., Smith M., Fletterick R.J.
J. Biol. Chem. 263:3850-3857(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences."
Gelinas R.P., Froman B.E., McElroy F., Tait R.C., Gorin F.A.
Brain Res. Mol. Brain Res. 6:177-185(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Lung and Skin.
[5]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Platelet.
[6]Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 18-30; 51-61; 71-78; 193-206; 271-278; 353-359; 388-395; 400-425; 508-520; 522-533; 546-552; 558-569; 577-590; 623-640; 657-681; 731-754 AND 817-823, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[7]"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].
[8]"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].
[9]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03544 mRNA. Translation: AAA59597.1.
U47025 mRNA. Translation: AAB60395.1.
AL121772 Genomic DNA. Translation: CAC00661.1.
BC017045 mRNA. Translation: AAH17045.1.
BC030795 mRNA. Translation: AAH30795.1.
CCDSCCDS13171.1.
PIRA40138.
RefSeqNP_002853.2. NM_002862.3.
XP_006723664.1. XM_006723601.1.
UniGeneHs.368157.

3D structure databases

ProteinModelPortalP11216.
SMRP11216. Positions 14-839.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111792. 17 interactions.
STRING9606.ENSP00000216962.

Chemistry

BindingDBP11216.
ChEMBLCHEMBL3856.
DrugBankDB00114. Pyridoxal Phosphate.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSiteP11216.

Polymorphism databases

DMDM20178317.

Proteomic databases

MaxQBP11216.
PaxDbP11216.
PeptideAtlasP11216.
PRIDEP11216.

Protocols and materials databases

DNASU5834.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216962; ENSP00000216962; ENSG00000100994.
GeneID5834.
KEGGhsa:5834.
UCSCuc002wup.3. human.

Organism-specific databases

CTD5834.
GeneCardsGC20P025228.
HGNCHGNC:9723. PYGB.
HPAHPA031067.
MIM138550. gene.
neXtProtNX_P11216.
PharmGKBPA34066.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0058.
HOVERGENHBG006848.
InParanoidP11216.
KOK00688.
OMAMDQISSG.
OrthoDBEOG7JQBMK.
PhylomeDBP11216.
TreeFamTF300309.

Enzyme and pathway databases

BioCycMetaCyc:HS02178-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP11216.
BgeeP11216.
CleanExHS_PYGB.
GenevestigatorP11216.

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

ChiTaRSPYGB. human.
GenomeRNAi5834.
NextBio22736.
PROP11216.
SOURCESearch...

Entry information

Entry namePYGB_HUMAN
AccessionPrimary (citable) accession number: P11216
Secondary accession number(s): Q96AK1, Q9NPX8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 167 of the entry and version 5 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

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 20

Human chromosome 20: entries, gene names and cross-references to MIM