Reviewed, UniProtKB/Swiss-Prot P11216 (PYGB_HUMAN)

Names and origin

Protein names

Recommended name:
    Glycogen phosphorylase, brain form
    EC=2.4.1.1

Gene names

Name:

PYGB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	843 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Carbohydrate metabolism Glycogen metabolism
Coding sequence diversity	Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	glycogen catabolic process Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	glycogen 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 843	842	Glycogen phosphorylase, brain form		PRO_0000188535
Sites
	Binding site	76	1	AMP By similarity
	Binding site	681	1	Pyridoxal phosphate (covalent) By similarity
	Site	109	1	Involved in the association of subunits By similarity
	Site	143	1	Involved in the association of subunits By similarity
	Site	156	1	May be involved in allosteric control By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	15	1	Phosphoserine; by PHK; in form phosphorylase A
	Modified residue	76	1	Phosphotyrosine
	Modified residue	197	1	Phosphotyrosine
	Modified residue	473	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	303	1	A → S: dbSNP rs2228976.		VAR_034428
	Natural variant	502	1	D → N: dbSNP rs2227891.		VAR_020212
Experimental info
	Sequence conflict	2 – 3	2	AK → GE Ref.1 Ref.2
	Sequence conflict	248	1	K → R in AAA59597. Ref.1
	Sequence conflict	302	1	A → G in AAA59597. Ref.1
	Sequence conflict	835 – 843	9	IPPPNIPRD → LQHLPHPEWESGGATCWAPP ELCTHLAMY in AAA59597. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P11216-1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 810BFAD3002CACB0	FASTA	843	96,696
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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
EMBLGenBankDDBJ	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.
PIR	A40138.
RefSeq	NP_002853.2.
UniGene	Hs.368157
3D structure databases
HSSP	HSSP built from PDB template 1A8I based on UniProtKB P00489.
SMR	P11216. Positions 13-838.
ModBase	Search...
PTM databases
PhosphoSite	P11216.
Proteomic databases
PeptideAtlas	P11216.
Genome annotation databases
Ensembl	ENSG00000100994. Homo sapiens. [Contig view]
GeneID	5834.
KEGG	hsa:5834.
NMPDR	fig|9606.3.peg.20003.
Organism-specific databases
HGNC	HGNC:9723. PYGB.
MIM	138550. gene.
PharmGKB	PA34066.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	P11216.
Gene expression databases
ArrayExpress	P11216.
CleanEx	HS_PYGB.
GermOnline	ENSG00000100994. Homo sapiens.
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
PANTHER	PTHR11468. Glyco_trans_35. 1 hit.
Pfam	PF00343. Phosphorylase. 1 hit. [Graphical view]
PIRSF	PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMs	TIGR02093. P_ylase. 1 hit.
PROSITE	PS00102. PHOSPHORYLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00114. Pyridoxal Phosphate.
NextBio	22736.
SOURCE	Search...

Entry information

Entry name

PYGB_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)