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P11216

- PYGB_HUMAN

UniProt

P11216 - PYGB_HUMAN

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Protein

Glycogen phosphorylase, brain form

Gene

PYGB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Pyridoxal phosphate.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761AMPBy similarity
Sitei109 – 1091Involved in the association of subunitsBy similarity
Sitei143 – 1431Involved in the association of subunitsBy similarity
Sitei156 – 1561May be involved in allosteric controlBy similarity

GO - Molecular functioni

  1. glycogen phosphorylase activity Source: UniProtKB
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glucose metabolic process Source: Reactome
  3. glycogen catabolic process Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS02178-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase, brain form (EC:2.4.1.1)
Gene namesi
Name:PYGB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9723. PYGB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34066.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 843842Glycogen phosphorylase, brain formPRO_0000188535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase ACurated
Modified residuei197 – 1971PhosphotyrosineBy similarity
Modified residuei473 – 4731PhosphotyrosineBy similarity
Modified residuei681 – 6811N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11216.
PaxDbiP11216.
PeptideAtlasiP11216.
PRIDEiP11216.

PTM databases

PhosphoSiteiP11216.

Expressioni

Gene expression databases

BgeeiP11216.
CleanExiHS_PYGB.
ExpressionAtlasiP11216. baseline and differential.
GenevestigatoriP11216.

Organism-specific databases

HPAiHPA031067.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi111792. 29 interactions.
IntActiP11216. 1 interaction.
STRINGi9606.ENSP00000216962.

Structurei

3D structure databases

ProteinModelPortaliP11216.
SMRiP11216. Positions 14-839.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0058.
GeneTreeiENSGT00390000016886.
HOVERGENiHBG006848.
InParanoidiP11216.
KOiK00688.
OMAiMDQISSG.
OrthoDBiEOG7JQBMK.
PhylomeDBiP11216.
TreeFamiTF300309.

Family and domain databases

InterProiIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERiPTHR11468. PTHR11468. 1 hit.
PfamiPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsiTIGR02093. P_ylase. 1 hit.
PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11216-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR
60 70 80 90 100
DYFFALAHTV RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM
110 120 130 140 150
VNLGLQNACD EAIYQLGLDL EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA DDWLRYGNPW EKARPEYMLP
210 220 230 240 250
VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN TMRLWSAKAP
260 270 280 290 300
NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
310 320 330 340 350
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL
360 370 380 390 400
MRILVDVEKV DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH
410 420 430 440 450
LEIIYAINQR HLDHVAALFP GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS
460 470 480 490 500
HAVNGVARIH SEIVKQSVFK DFYELEPEKF QNKTNGITPR RWLLLCNPGL
510 520 530 540 550
ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ ENKLKFSAFL
560 570 580 590 600
EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV
610 620 630 640 650
PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR
660 670 680 690 700
VSLAEKVIPA ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGAENLF IFGLRVEDVE ALDRKGYNAR EYYDHLPELK QAVDQISSGF
760 770 780 790 800
FSPKEPDCFK DIVNMLMHHD RFKVFADYEA YMQCQAQVDQ LYRNPKEWTK
810 820 830 840
KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI PRD
Length:843
Mass (Da):96,696
Last modified:January 23, 2007 - v5
Checksum:i810BFAD3002CACB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AK → GE(PubMed:3346228)Curated
Sequence conflicti2 – 32AK → GE(PubMed:2615594)Curated
Sequence conflicti248 – 2481K → R in AAA59597. (PubMed:3346228)Curated
Sequence conflicti302 – 3021A → G in AAA59597. (PubMed:3346228)Curated
Sequence conflicti835 – 8439IPPPNIPRD → LQHLPHPEWESGGATCWAPP ELCTHLAMY in AAA59597. (PubMed:3346228)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031A → S.
Corresponds to variant rs2228976 [ dbSNP | Ensembl ].
VAR_034428
Natural varianti502 – 5021D → N.
Corresponds to variant rs2227891 [ dbSNP | Ensembl ].
VAR_020212

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13171.1.
PIRiA40138.
RefSeqiNP_002853.2. NM_002862.3.
XP_006723664.1. XM_006723601.1.
UniGeneiHs.368157.

Genome annotation databases

EnsembliENST00000216962; ENSP00000216962; ENSG00000100994.
GeneIDi5834.
KEGGihsa:5834.
UCSCiuc002wup.3. human.

Polymorphism databases

DMDMi20178317.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13171.1.
PIRi A40138.
RefSeqi NP_002853.2. NM_002862.3.
XP_006723664.1. XM_006723601.1.
UniGenei Hs.368157.

3D structure databases

ProteinModelPortali P11216.
SMRi P11216. Positions 14-839.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111792. 29 interactions.
IntActi P11216. 1 interaction.
STRINGi 9606.ENSP00000216962.

Chemistry

BindingDBi P11216.
ChEMBLi CHEMBL3856.

Protein family/group databases

CAZyi GT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSitei P11216.

Polymorphism databases

DMDMi 20178317.

Proteomic databases

MaxQBi P11216.
PaxDbi P11216.
PeptideAtlasi P11216.
PRIDEi P11216.

Protocols and materials databases

DNASUi 5834.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216962 ; ENSP00000216962 ; ENSG00000100994 .
GeneIDi 5834.
KEGGi hsa:5834.
UCSCi uc002wup.3. human.

Organism-specific databases

CTDi 5834.
GeneCardsi GC20P025228.
HGNCi HGNC:9723. PYGB.
HPAi HPA031067.
MIMi 138550. gene.
neXtProti NX_P11216.
PharmGKBi PA34066.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0058.
GeneTreei ENSGT00390000016886.
HOVERGENi HBG006848.
InParanoidi P11216.
KOi K00688.
OMAi MDQISSG.
OrthoDBi EOG7JQBMK.
PhylomeDBi P11216.
TreeFami TF300309.

Enzyme and pathway databases

BioCyci MetaCyc:HS02178-MONOMER.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

ChiTaRSi PYGB. human.
GenomeRNAii 5834.
NextBioi 22736.
PROi P11216.
SOURCEi Search...

Gene expression databases

Bgeei P11216.
CleanExi HS_PYGB.
ExpressionAtlasi P11216. baseline and differential.
Genevestigatori P11216.

Family and domain databases

InterProi IPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view ]
PANTHERi PTHR11468. PTHR11468. 1 hit.
Pfami PF00343. Phosphorylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsi TIGR02093. P_ylase. 1 hit.
PROSITEi PS00102. PHOSPHORYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYGB_HUMAN
AccessioniPrimary (citable) accession number: P11216
Secondary accession number(s): Q96AK1, Q9NPX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 170 of the entry and version 5 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

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3