P11217 (PYGM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen phosphorylase, muscle form
EC=2.4.1.1

Alternative name(s):
Myophosphorylase

Gene names

Name:

PYGM

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	842 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.
Post-translational modification	Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. Ref.10
Involvement in disease	Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
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	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
Molecular_function	glycogen phosphorylase activity Traceable author statement Ref.2. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11217-1)

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: P11217-2)

The sequence of this isoform differs from the canonical sequence as follows:
     82-169: 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 – 842

841

Glycogen phosphorylase, muscle form

PRO_0000188529

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-acetylserine By similarity

Modified residue

15

1

Phosphoserine; by PHK; in form phosphorylase A Ref.10

Modified residue

473

1

Phosphotyrosine By similarity

Modified residue

681

1

N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence

82 – 169

88

Missing in isoform 2.

VSP_043047

Natural variant

116

1

L → P in GSD5. Ref.15 Ref.22

VAR_014002

Natural variant

194

1

R → W in GSD5. Ref.22

VAR_014003

Natural variant

205

1

G → S in GSD5. Ref.11 Ref.13 Ref.16 Ref.17 Ref.22

VAR_003431

Natural variant

292

1

L → P in GSD5; rare mutation. Ref.13

VAR_014004

Natural variant

349

1

E → K in GSD5. Ref.22

VAR_014005

Natural variant

397

1

L → P in GSD5. Ref.12 Ref.13

VAR_003432

Natural variant

414

1

R → G.
Corresponds to variant rs11231866 [ dbSNP | Ensembl ].

VAR_061198

Natural variant

488

1

T → N in GSD5. Ref.20 Ref.22

VAR_014006

Natural variant

543

1

K → T in GSD5. Ref.11 Ref.13

VAR_003433

Natural variant

602

1

R → W in GSD5. Ref.22

VAR_014007

Natural variant

655

1

E → K in GSD5. Ref.12 Ref.13

VAR_003434

Natural variant

660

1

A → D in GSD5. Ref.21 Ref.22

VAR_014008

Natural variant

666

1

Q → E in GSD5. Ref.14

VAR_014009

Natural variant

685

1

N → Y in GSD5. Ref.16 Ref.22

VAR_014010

Natural variant

686

1

G → R in GSD5. Ref.14

VAR_014011

Natural variant

687

1

A → P in GSD5. Ref.23

VAR_014012

Natural variant

704

1

A → V in GSD5. Ref.22

VAR_014013

Natural variant

709

1

Missing in GSD5; common in Japanese patients. Ref.13

VAR_014014

Natural variant

798

1

W → R in GSD5. Ref.18 Ref.19 Ref.22

VAR_014015

Experimental info

Sequence conflict

791

1

L → W in AAA60231. Ref.1

Secondary structure

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842

Helix Strand Turn

Details...

Helix

7 – 10

4

Helix

11 – 13

3

Helix

25 – 38

14

Turn

44 – 46

3

Helix

49 – 78

30

Beta strand

82 – 86

5

Helix

96 – 102

7

Helix

106 – 114

9

Turn

115 – 117

3

Helix

120 – 126

7

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 – 236

3

Beta strand

239 – 248

10

Helix

263 – 270

8

Helix

271 – 277

7

Helix

291 – 313

23

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

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 – 514

4

Helix

516 – 525

10

Helix

529 – 553

25

Beta strand

562 – 569

8

Turn

573 – 576

4

Helix

577 – 593

17

Beta strand

602 – 607

6

Helix

615 – 631

17

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

730 – 733

4

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 6. Checksum: EBDB7D80D740B68F	FASTA	842	97,092
	10 20 30 40 50 60 MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA 190 200 210 220 230 240 DDWLRYGNPW EKARPEFTLP VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 250 260 270 280 290 300 TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERM 370 380 390 400 410 420 DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP 430 440 450 460 470 480 GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 490 500 510 520 530 540 QNKTNGITPR RWLVLCNPGL AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ 550 560 570 580 590 600 ENKLKFAAYL EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV 610 620 630 640 650 660 PRTVMIGGKA APGYHMAKMI IRLVTAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA 670 680 690 700 710 720 ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD 730 740 750 760 770 780 KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYED 790 800 810 820 830 840 YIKCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE AI
	Isoform 2 [UniParc]. Checksum: F5C64CA460DA3FC9	FASTA	754	87,317
	10 20 30 40 50 60 MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYEKDP KKISGGWQME EADDWLRYGN PWEKARPEFT LPVHFYGHVE 130 140 150 160 170 180 HTSQGAKWVD TQVVLAMPYD TPVPGYRNNV VNTMRLWSAK APNDFNLKDF NVGGYIQAVL 190 200 210 220 230 240 DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKSSKFG CRDPVRTNFD 250 260 270 280 290 300 AFPDKVAIQL NDTHPSLAIP ELMRILVDLE RMDWDKAWDV TVRTCAYTNH TVLPEALERW 310 320 330 340 350 360 PVHLLETLLP RHLQIIYEIN QRFLNRVAAA FPGDVDRLRR MSLVEEGAVK RINMAHLCIA 370 380 390 400 410 420 GSHAVNGVAR IHSEILKKTI FKDFYELEPH KFQNKTNGIT PRRWLVLCNP GLAEVIAERI 430 440 450 460 470 480 GEDFISDLDQ LRKLLSFVDD EAFIRDVAKV KQENKLKFAA YLEREYKVHI NPNSLFDIQV 490 500 510 520 530 540 KRIHEYKRQL LNCLHVITLY NRIKREPNKF FVPRTVMIGG KAAPGYHMAK MIIRLVTAIG 550 560 570 580 590 600 DVVNHDPAVG DRLRVIFLEN YRVSLAEKVI PAADLSEQIS TAGTEASGTG NMKFMLNGAL 610 620 630 640 650 660 TIGTMDGANV EMAEEAGEEN FFIFGMRVED VDKLDQRGYN AQEYYDRIPE LRQVIEQLSS 670 680 690 700 710 720 GFFSPKQPDL FKDIVNMLMH HDRFKVFADY EDYIKCQEKV SALYKNPREW TRMVIRNIAT 730 740 750 SGKFSSDRTI AQYAREIWGV EPSRQRLPAP DEAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase." Burke J., Hwang P.K., Anderson L., Lebo R., Gorin F., Fletterick R.J. Proteins 2:177-187(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation." Kubisch C., Wicklein E.M., Jentsch T.J. Hum. Mutat. 12:27-32(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	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: Muscle.
[4]	"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). Tissue: Tongue.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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).
[8]	"Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs." Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., Crerar M.M. Eur. J. Biochem. 152:267-274(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-842 (ISOFORM 1).
[9]	"Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis." Gautron S., Daegelen D., Mennecier F., Dubocq D., Kahn A., Dreyfus J.-C. J. Clin. Invest. 79:275-281(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 455-676 (ISOFORM 1).
[10]	"Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties." Carty T.J., Tu J., Graves D.J. J. Biol. Chem. 250:4980-4985(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15.
[11]	"Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease)." Tsujino S., Shanske S., Dimauro S. N. Engl. J. Med. 329:241-245(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD5 SER-205 AND THR-543.
[12]	"Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease)." Tsujino S., Shanske S., Martinuzzi A., Heiman-Patterson T., Dimauro S. Hum. Mutat. 6:276-277(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD5 PRO-397 AND LYS-655.
[13]	"The molecular genetic basis of myophosphorylase deficiency (McArdle's disease)." Tsujino S., Shanske S., Nonaka I., DiMauro S. Muscle Nerve 3:S23-S27(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD5 SER-205; PRO-292; PRO-397; THR-543; LYS-655 AND PHE-709 DEL.
[14]	"Mutation analysis in myophosphorylase deficiency (McArdle's disease)." Vorgerd M., Kubisch C., Burwinkel B., Reichmann H., Mortier W., Tettenborn B., Pongratz D., Lindemuth R., Tegenthoff M., Malin J.P., Kilimann M.W. Ann. Neurol. 43:326-331(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD5 GLU-666 AND ARG-686.
[15]	"A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact." Gamez J., Fernandez R., Bruno C., Andreu A.L., Cervera C., Navarro C., Schwartz S., Dimauro S. Muscle Nerve 22:1136-1138(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 PRO-116.
[16]	"A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease." Andreu A.L., Bruno C., Tamburino L., Gamez J., Shanske S., Cervera C., Navarro C., DiMauro S. Neuromuscul. Disord. 9:171-173(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD5 SER-205 AND TYR-685.
[17]	"McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient." Rubio J.C., Martin M.A., Garcia A., Campos Y., Cabello A., Culebras J.M., Arenas J. Neuromuscul. Disord. 9:174-175(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 SER-205.
[18]	"A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease." Fernandez R., Navarro C., Andreu A.L., Bruno C., Shanske S., Gamez J., Teijeira S., Hernandez I., Teijeiro A., Fernandez J.M., Musumeci O., DiMauro S. Arch. Neurol. 57:217-219(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 ARG-798.
[19]	"A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease." Rubio J.C., Martin M.A., Campos Y., Auciello R., Cabello A., Arenas J. Muscle Nerve 23:129-131(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 ARG-798.
[20]	"A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease." Rubio J.C., Martin M.A., Campos Y., Cabello A., Arenas J. Neuromuscul. Disord. 10:138-140(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 ASN-488.
[21]	"A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease." Martin M.A., Rubio J.C., Campos Y., Ricoy J.R., Cabello A., Arenas J. Neuromuscul. Disord. 10:447-449(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 ASP-660.
[22]	"Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study." Martin M.A., Rubio J.C., Buchbinder J., Fernandez-Hojas R., del Hoyo P., Teijeira S., Gamez J., Navarro C., Fernandez J.M., Cabello A., Campos Y., Cervera C., Culebras J.M., Andreu A.L., Fletterick R.J., Arenas J. Ann. Neurol. 50:574-581(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD5 PRO-116; TRP-194; SER-205; LYS-349; ASN-488; TRP-602; ASP-660; TYR-685; VAL-704 AND ARG-798.
[23]	"Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease." Bruno C., Lanzillo R., Biedi C., Iadicicco L., Minetti C., Santoro L. Neuromuscul. Disord. 12:498-500(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD5 PRO-687.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32598 , M32579, M32580, M32581, M32582, M32583, M32584, M32585, M32586, M32587, M32588, M32589, M32590, M32591, M32592, M32593, M32594, M32595, M32596, M32597 Genomic DNA. Translation: AAA60231.1.
U94777 , U94774, U94775, U94776 Genomic DNA. Translation: AAC52081.1.
AF066859 mRNA. Translation: AAC17451.1.
AK056607 mRNA. Translation: BAG51762.1.
AP001462 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74284.1.
BC126392 mRNA. Translation: AAI26393.1.
BC130514 mRNA. Translation: AAI30515.1.
X03031 mRNA. Translation: CAA26834.1.
M16013 mRNA. Translation: AAA36216.1.

IPI

IPI00218130.
IPI00657751.

PIR

A27335.

RefSeq

NP_001158188.1. NM_001164716.1.
NP_005600.1. NM_005609.2.

UniGene

Hs.154084.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z8D	X-ray	2.30	A	1-842	[»]

ProteinModelPortal

P11217.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11217. 21 interactions.

MINT

MINT-1134630.

STRING

9606.ENSP00000164139.

Protein family/group databases

CAZy

GT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSite

P11217.

Polymorphism databases

DMDM

3041717.

Proteomic databases

PaxDb

P11217.

PRIDE

P11217.

Protocols and materials databases

DNASU

5837.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000164139; ENSP00000164139; ENSG00000068976.
ENST00000377432; ENSP00000366650; ENSG00000068976.

GeneID

5837.

KEGG

hsa:5837.

UCSC

uc001oax.4. human.

Organism-specific databases

CTD

5837.

GeneCards

GC11M064513.

HGNC

HGNC:9726. PYGM.

HPA

HPA056003.

MIM

232600. phenotype.
608455. gene.

neXtProt

NX_P11217.

Orphanet

368. Myophosphorylase deficiency.

PharmGKB

PA34069.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0058.

HOGENOM

HOG000278444.

HOVERGEN

HBG006848.

InParanoid

P11217.

KO

K00688.

OMA

FGVIHRY.

OrthoDB

EOG4S1T6F.

PhylomeDB

P11217.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P11217.

CleanEx

HS_PYGM.

Genevestigator

P11217.

GermOnline

ENSG00000068976. 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

P11217.

ChEMBL

CHEMBL3526.

DrugBank

DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

P11217.

GenomeRNAi

5837.

NextBio

22746.

SOURCE

Search...

Entry information

Entry name

PYGM_HUMAN

Accession

Primary (citable) accession number: P11217
Secondary accession number(s): A0AVK1, A6NDY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 162 of the entry and version 6 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.