P06737 (PYGL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen phosphorylase, liver form
EC=2.4.1.1

Gene names

Name:

PYGL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	847 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 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.
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 process	Carbohydrate metabolism Glycogen metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Glycogen storage disease
Ligand	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: Compara 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 small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	AMP binding Inferred from direct assay Ref.12Ref.11. Source: UniProtKB ATP binding Inferred from direct assay Ref.12. Source: UniProtKB bile acid binding Inferred from direct assay Ref.13. Source: UniProtKB drug binding Inferred from direct assay Ref.11Ref.13. Source: UniProtKB glucose binding Non-traceable author statement Ref.13. Source: UniProtKB glycogen phosphorylase activity Inferred from mutant phenotype Ref.11PubMed 17705025Ref.4. Source: UniProtKB protein homodimerization activity Non-traceable author statement PubMed 17705025. Source: UniProtKB purine nucleobase binding Inferred from direct assay Ref.13. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro vitamin binding Inferred from direct assay Ref.13. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 847

846

Glycogen phosphorylase, liver form

PRO_0000188524

Sites

Binding site

76

1

AMP 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 By similarity

Modified residue

15

1

Phosphoserine; by PHK; in form phosphorylase A

Modified residue

681

1

N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence

82 – 115

34

Missing in isoform 2.

VSP_045339

Natural variant

222

1

V → I. Ref.4
Corresponds to variant rs946616 [ dbSNP | Ensembl ].

VAR_007907

Natural variant

231

1

V → E.
Corresponds to variant rs1042195 [ dbSNP | Ensembl ].

VAR_013095

Natural variant

339

1

N → S in GSD6. Ref.4

VAR_007908

Natural variant

377

1

N → K in GSD6. Ref.4

VAR_007909

Natural variant

425

1

R → P. Ref.1
Corresponds to variant rs2228499 [ dbSNP | Ensembl ].

VAR_034425

Natural variant

698

1

V → G.
Corresponds to variant rs35831273 [ dbSNP | Ensembl ].

VAR_034426

Natural variant

715

1

R → S.
Corresponds to variant rs1042210 [ dbSNP | Ensembl ].

VAR_013096

Natural variant

806

1

I → L.
Corresponds to variant rs34313873 [ dbSNP | Ensembl ].

VAR_034427

Natural variant

845

1

N → S. Ref.5
Corresponds to variant rs78558135 [ dbSNP | Ensembl ].

VAR_069054

Experimental info

Sequence conflict

2 – 3

2

AK → GE in AAA52577. Ref.1

Sequence conflict

2 – 3

2

AK → GE in AAC18079. Ref.3

Sequence conflict

83

1

V → E in AAA52577. Ref.1

Sequence conflict

323

1

A → Q in AAA52577. Ref.1

Sequence conflict

344 – 345

2

AL → RI in AAA52577. Ref.1

Sequence conflict

369

1

T → N in AAA52577. Ref.1

Sequence conflict

369

1

T → N in AAC18079. Ref.3

Sequence conflict

570

1

R → S in AAC17450. Ref.2

Sequence conflict

683

1

Missing in AAH09895. Ref.8

Sequence conflict

715

1

R → G in BAG62279. Ref.5

Secondary structure

1

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847

Helix Strand Turn

Details...

Turn

8 – 10

3

Helix

11 – 13

3

Beta strand

14 – 17

4

Helix

19 – 38

20

Helix

44 – 46

3

Helix

49 – 62

14

Helix

65 – 78

14

Beta strand

82 – 86

5

Beta strand

90 – 93

4

Helix

96 – 102

7

Helix

106 – 115

10

Helix

120 – 125

6

Beta strand

130 – 135

6

Helix

136 – 150

15

Beta strand

155 – 160

6

Beta strand

168 – 172

5

Beta strand

175 – 179

5

Turn

183 – 186

4

Helix

195 – 197

3

Beta strand

199 – 204

6

Beta strand

206 – 210

5

Beta strand

213 – 218

6

Beta strand

220 – 232

13

Beta strand

234 – 237

4

Beta strand

239 – 248

10

Helix

255 – 260

6

Helix

263 – 268

6

Helix

270 – 274

5

Helix

275 – 277

3

Helix

291 – 314

24

Beta strand

315 – 317

3

Beta strand

322 – 325

4

Helix

327 – 329

3

Helix

330 – 333

4

Beta strand

334 – 341

8

Turn

342 – 345

4

Helix

346 – 356

11

Helix

362 – 372

11

Beta strand

373 – 376

4

Helix

382 – 384

3

Beta strand

387 – 389

3

Helix

390 – 396

7

Helix

398 – 418

21

Beta strand

419 – 421

3

Helix

423 – 429

7

Beta strand

431 – 433

3

Beta strand

435 – 437

3

Beta strand

439 – 441

3

Helix

442 – 448

7

Beta strand

451 – 457

7

Helix

458 – 466

9

Turn

467 – 469

3

Helix

470 – 475

6

Helix

477 – 479

3

Beta strand

480 – 482

3

Helix

490 – 495

6

Helix

498 – 508

11

Helix

511 – 513

3

Helix

516 – 525

10

Helix

529 – 553

25

Beta strand

554 – 556

3

Beta strand

562 – 569

8

Turn

573 – 576

4

Helix

577 – 593

17

Beta strand

595 – 597

3

Beta strand

602 – 607

6

Helix

615 – 633

19

Turn

635 – 637

3

Helix

638 – 640

3

Beta strand

641 – 646

6

Helix

651 – 657

7

Helix

658 – 660

3

Beta strand

662 – 666

5

Turn

670 – 672

3

Helix

678 – 684

7

Beta strand

688 – 691

4

Helix

697 – 704

8

Helix

706 – 708

3

Beta strand

709 – 711

3

Helix

716 – 725

10

Helix

729 – 735

7

Helix

737 – 748

12

Turn

749 – 751

3

Turn

756 – 759

4

Helix

760 – 768

9

Helix

774 – 792

19

Helix

795 – 806

12

Helix

810 – 812

3

Helix

814 – 824

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 74017E8125FB5735	FASTA	847	97,149
	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
	Isoform 2 [UniParc]. Checksum: 40B7DB0528A64AAA	FASTA	813	93,134
	10 20 30 40 50 60 MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR DYYFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYDKCP KLGLDIEELE EIEEDAGLGN GGLGRLAACF LDSMATLGLA 130 140 150 160 170 180 AYGYGIRYEY GIFNQKIRDG WQVEEADDWL RYGNPWEKSR PEFMLPVHFY GKVEHTNTGT 190 200 210 220 230 240 KWIDTQVVLA LPYDTPVPGY MNNTVNTMRL WSARAPNDFN LRDFNVGDYI QAVLDRNLAE 250 260 270 280 290 300 NISRVLYPND NFFEGKELRL KQEYFVVAAT LQDIIRRFKA SKFGSTRGAG TVFDAFPDQV 310 320 330 340 350 360 AIQLNDTHPA LAIPELMRIF VDIEKLPWSK AWELTQKTFA YTNHTVLPEA LERWPVDLVE 370 380 390 400 410 420 KLLPRHLEII YEINQKHLDR IVALFPKDVD RLRRMSLIEE EGSKRINMAH LCIVGSHAVN 430 440 450 460 470 480 GVAKIHSDIV KTKVFKDFSE LEPDKFQNKT NGITPRRWLL LCNPGLAELI AEKIGEDYVK 490 500 510 520 530 540 DLSQLTKLHS FLGDDVFLRE LAKVKQENKL KFSQFLETEY KVKINPSSMF DVQVKRIHEY 550 560 570 580 590 600 KRQLLNCLHV ITMYNRIKKD PKKLFVPRTV IIGGKAAPGY HMAKMIIKLI TSVADVVNND 610 620 630 640 650 660 PMVGSKLKVI FLENYRVSLA EKVIPATDLS EQISTAGTEA SGTGNMKFML NGALTIGTMD 670 680 690 700 710 720 GANVEMAEEA GEENLFIFGM RIDDVAALDK KGYEAKEYYE ALPELKLVID QIDNGFFSPK 730 740 750 760 770 780 QPDLFKDIIN MLFYHDRFKV FADYEAYVKC QDKVSQLYMN PKAWNTMVLK NIAASGKFSS 790 800 810 DRTIKEYAQN IWNVEPSDLK ISLSNESNKV NGN

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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].
[11]	"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).
[12]	"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).
[13]	"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.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14636 mRNA. Translation: AAA52577.1.
AF066858 mRNA. Translation: AAC17450.1.
AF046798 , 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.

IPI

IPI00783313.
IPI00943894.

PIR

A25518.

RefSeq

NP_001157412.1. NM_001163940.1.
NP_002854.3. NM_002863.4.

UniGene

Hs.282417.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EM6	X-ray	2.20	A/B	1-847	[»]
1EXV	X-ray	2.40	A/B	1-847	[»]
1FA9	X-ray	2.40	A	2-847	[»]
1FC0	X-ray	2.40	A/B	2-847	[»]
1L5Q	X-ray	2.25	A/B	1-847	[»]
1L5R	X-ray	2.10	A/B	1-847	[»]
1L5S	X-ray	2.10	A/B	1-847	[»]
1L7X	X-ray	2.30	A/B	1-847	[»]
1XOI	X-ray	2.10	A/B	2-846	[»]
2ATI	X-ray	1.90	A/B	2-846	[»]
2QLL	X-ray	2.56	A	1-847	[»]
2ZB2	X-ray	2.45	A/B	1-847	[»]
3CEH	X-ray	2.80	A/B	24-832	[»]
3CEJ	X-ray	3.30	A/B	24-832	[»]
3CEM	X-ray	2.47	A/B	24-832	[»]
3DD1	X-ray	2.57	A/B	2-847	[»]
3DDS	X-ray	1.80	A/B	2-847	[»]
3DDW	X-ray	1.90	A/B	2-847	[»]

ProteinModelPortal

P06737.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06737. 7 interactions.

MINT

MINT-1208599.

STRING

9606.ENSP00000216392.

Protein family/group databases

CAZy

GT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSite

P06737.

Polymorphism databases

DMDM

6648082.

Proteomic databases

PaxDb

P06737.

PeptideAtlas

P06737.

PRIDE

P06737.

Protocols and materials databases

DNASU

5836.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216392; ENSP00000216392; ENSG00000100504.
ENST00000544180; ENSP00000443787; ENSG00000100504.

GeneID

5836.

KEGG

hsa:5836.

UCSC

uc001wyu.3. human.

Organism-specific databases

CTD

5836.

GeneCards

GC14M051324.

HGNC

HGNC:9725. PYGL.

HPA

HPA000962.
HPA004119.

MIM

232700. phenotype.
613741. gene.

neXtProt

NX_P06737.

Orphanet

369. Liver phosphorylase deficiency.

PharmGKB

PA34068.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0058.

HOVERGEN

HBG006848.

InParanoid

P06737.

KO

K00688.

OMA

IVDVKLF.

OrthoDB

EOG4S1T6F.

PhylomeDB

P06737.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P06737.

Bgee

P06737.

CleanEx

HS_PYGL.

Genevestigator

P06737.

GermOnline

ENSG00000100504. Homo sapiens.

Family and domain databases

InterPro

IPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]

PANTHER

PTHR11468. PTHR11468. 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

BindingDB

P06737.

ChEMBL

CHEMBL2568.

ChiTaRS

PYGL. human.

DrugBank

DB00131. Adenosine monophosphate.
DB00114. Pyridoxal Phosphate.
DB00140. Riboflavin.

EvolutionaryTrace

P06737.

GenomeRNAi

5836.

NextBio

22742.

SOURCE

Search...

Entry information

Entry name

PYGL_HUMAN

Accession

Primary (citable) accession number: P06737
Secondary accession number(s): A6NDQ4 , 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:	May 1, 2013
This is version 163 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.