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Reviewed, UniProtKB/Swiss-Prot P11216 (PYGB_HUMAN)

Last modified November 25, 2008. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycogen phosphorylase, brain form
    EC=2.4.1.1
Gene names
Name: PYGB
OrganismHomo sapiens (Human)
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.

Ontologies

Keywords

   Biological processCarbohydrate metabolism
Glycogen metabolism
   Coding sequence diversityPolymorphism
   LigandPyridoxal phosphate
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
Direct protein sequencing

Gene Ontology (GO)

   Biological processglycogen catabolic process Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from direct assay. Source: UniProtKB

   Molecular functionglycogen phosphorylase activity Ref.1

Non-traceable author statement. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 843842Glycogen phosphorylase, brain form
PRO_0000188535

Sites

Binding site761AMP By similarity
Binding site6811Pyridoxal phosphate (covalent) 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
Modified residue151Phosphoserine; by PHK; in form phosphorylase A
Modified residue761Phosphotyrosine
Modified residue1971Phosphotyrosine
Modified residue4731Phosphotyrosine By similarity

Natural variations

Natural variant3031A → S: dbSNP rs2228976.
VAR_034428
Natural variant5021D → N: dbSNP rs2227891.
VAR_020212

Experimental info

Sequence conflict2 – 32AK → GE Ref.1 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
P11216-1 [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: 3346228] [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: 2615594] [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: 11780052] [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: 15489334] [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: 12665801] [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, MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76 AND TYR-197, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRA40138.
RefSeqNP_002853.2.
UniGeneHs.368157

3D structure databases

HSSPHSSP built from PDB template 1A8I based on UniProtKB P00489.
SMRP11216. Positions 13-838.
ModBaseSearch...

PTM databases

PhosphoSiteP11216.

Proteomic databases

PeptideAtlasP11216.

Genome annotation databases

EnsemblENSG00000100994. Homo sapiens. [Contig view]
GeneID5834.
KEGGhsa:5834.
NMPDRfig|9606.3.peg.20003.

Organism-specific databases

HGNCHGNC:9723. PYGB.
MIM138550. gene.
PharmGKBPA34066.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP11216.

Gene expression databases

ArrayExpressP11216.
CleanExHS_PYGB.
GermOnlineENSG00000100994. Homo sapiens.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. Glyco_trans_35. 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 Resources

DrugBankDB00114. Pyridoxal Phosphate.
NextBio22736.
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: November 25, 2008
This is version 111 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 20

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents