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Protein

Glycogen phosphorylase, muscle form

Gene

PYGM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: 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

Enzyme regulationi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76AMP1
Sitei109Involved in the association of subunits1
Sitei143Involved in the association of subunits1
Sitei156Can be labeled by an AMP analog; may be involved in allosteric regulation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.4.1.1. 1749.
SABIO-RKP00489.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase, muscle form (EC:2.4.1.1)
Alternative name(s):
Myophosphorylase
Gene namesi
Name:PYGM
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001885322 – 843Glycogen phosphorylase, muscle formAdd BLAST842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei15Phosphoserine; by PHK; in form phosphorylase ABy similarity1
Modified residuei204PhosphotyrosineBy similarity1
Modified residuei227PhosphotyrosineBy similarity1
Modified residuei364N6-succinyllysineBy similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei473PhosphotyrosineBy similarity1
Modified residuei514PhosphoserineBy similarity1
Modified residuei524PhosphoserineBy similarity1
Modified residuei681N6-(pyridoxal phosphate)lysine1
Modified residuei747PhosphoserineBy similarity1
Modified residuei748PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00489.

PTM databases

iPTMnetiP00489.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-38240N.
IntActiP00489. 2 interactors.
MINTiMINT-6368963.
STRINGi9986.ENSOCUP00000001880.

Chemistry databases

BindingDBiP00489.

Structurei

Secondary structure

1843
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 13Combined sources5
Helixi15 – 17Combined sources3
Helixi22 – 38Combined sources17
Turni44 – 46Combined sources3
Helixi49 – 62Combined sources14
Helixi65 – 78Combined sources14
Beta strandi82 – 86Combined sources5
Beta strandi90 – 93Combined sources4
Helixi96 – 102Combined sources7
Helixi106 – 115Combined sources10
Helixi120 – 124Combined sources5
Beta strandi130 – 132Combined sources3
Helixi136 – 150Combined sources15
Beta strandi155 – 160Combined sources6
Beta strandi168 – 172Combined sources5
Beta strandi175 – 179Combined sources5
Turni183 – 186Combined sources4
Helixi195 – 197Combined sources3
Beta strandi199 – 204Combined sources6
Beta strandi206 – 209Combined sources4
Beta strandi211 – 218Combined sources8
Beta strandi220 – 232Combined sources13
Beta strandi234 – 237Combined sources4
Beta strandi239 – 248Combined sources10
Helixi253 – 256Combined sources4
Beta strandi259 – 261Combined sources3
Helixi263 – 268Combined sources6
Helixi270 – 274Combined sources5
Helixi275 – 277Combined sources3
Beta strandi284 – 286Combined sources3
Helixi291 – 313Combined sources23
Turni315 – 319Combined sources5
Beta strandi322 – 325Combined sources4
Helixi327 – 329Combined sources3
Helixi330 – 333Combined sources4
Beta strandi334 – 341Combined sources8
Turni342 – 345Combined sources4
Helixi346 – 356Combined sources11
Helixi362 – 372Combined sources11
Beta strandi373 – 376Combined sources4
Helixi382 – 384Combined sources3
Beta strandi387 – 389Combined sources3
Helixi390 – 396Combined sources7
Helixi398 – 418Combined sources21
Beta strandi419 – 421Combined sources3
Helixi423 – 429Combined sources7
Beta strandi431 – 433Combined sources3
Beta strandi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Helixi442 – 448Combined sources7
Beta strandi453 – 457Combined sources5
Helixi458 – 466Combined sources9
Turni467 – 469Combined sources3
Helixi470 – 475Combined sources6
Helixi477 – 479Combined sources3
Beta strandi480 – 482Combined sources3
Helixi490 – 495Combined sources6
Helixi498 – 508Combined sources11
Helixi511 – 514Combined sources4
Helixi516 – 525Combined sources10
Helixi529 – 554Combined sources26
Beta strandi562 – 569Combined sources8
Turni573 – 576Combined sources4
Helixi577 – 593Combined sources17
Beta strandi602 – 607Combined sources6
Helixi615 – 631Combined sources17
Turni635 – 637Combined sources3
Helixi638 – 640Combined sources3
Beta strandi641 – 646Combined sources6
Helixi651 – 657Combined sources7
Helixi658 – 660Combined sources3
Beta strandi662 – 666Combined sources5
Turni670 – 672Combined sources3
Beta strandi673 – 675Combined sources3
Helixi678 – 684Combined sources7
Beta strandi688 – 691Combined sources4
Helixi697 – 704Combined sources8
Helixi706 – 708Combined sources3
Beta strandi709 – 711Combined sources3
Helixi716 – 725Combined sources10
Helixi729 – 735Combined sources7
Helixi737 – 748Combined sources12
Turni749 – 751Combined sources3
Beta strandi753 – 755Combined sources3
Turni756 – 759Combined sources4
Helixi760 – 768Combined sources9
Helixi775 – 777Combined sources3
Helixi778 – 792Combined sources15
Helixi795 – 806Combined sources12
Helixi810 – 812Combined sources3
Helixi814 – 824Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A8IX-ray1.78A2-843[»]
1ABBX-ray2.80A/B/C/D11-838[»]
1AXRX-ray2.30A2-843[»]
1B4DX-ray2.00A2-843[»]
1BX3X-ray2.30A2-843[»]
1C50X-ray2.30A14-843[»]
1C8KX-ray1.76A2-843[»]
1C8LX-ray2.30A2-843[»]
1E1YX-ray2.23A2-843[»]
1FS4X-ray2.38A2-843[»]
1FTQX-ray2.35A2-843[»]
1FTWX-ray2.36A2-843[»]
1FTYX-ray2.38A2-843[»]
1FU4X-ray2.36A2-843[»]
1FU7X-ray2.36A2-843[»]
1FU8X-ray2.35A2-843[»]
1GFZX-ray2.30A2-843[»]
1GG8X-ray2.31A2-843[»]
1GGNX-ray2.36A2-843[»]
1GPAX-ray2.90A/B/C/D2-843[»]
1GPBX-ray1.90A2-843[»]
1GPYX-ray2.40A2-843[»]
1H5UX-ray1.76A2-843[»]
1HLFX-ray2.26A2-843[»]
1K06X-ray1.80A2-843[»]
1K08X-ray2.26A2-843[»]
1KTIX-ray1.97A2-843[»]
1LWNX-ray2.00A2-843[»]
1LWOX-ray2.00A2-843[»]
1NOIX-ray2.50A/B/C/D2-843[»]
1NOJX-ray2.40A2-843[»]
1NOKX-ray2.40A2-843[»]
1P29X-ray2.20A2-843[»]
1P2BX-ray2.20A2-843[»]
1P2DX-ray1.94A2-843[»]
1P2GX-ray2.30A2-843[»]
1P4GX-ray2.10A2-843[»]
1P4HX-ray2.06A2-843[»]
1P4JX-ray2.00A2-843[»]
1PYGX-ray2.87A/B/C/D2-843[»]
1UZUX-ray2.30A2-843[»]
1WUTX-ray2.26A2-843[»]
1WUYX-ray2.26A2-843[»]
1WV0X-ray2.26A2-843[»]
1WV1X-ray2.26A2-843[»]
1WW2X-ray1.90A2-843[»]
1WW3X-ray1.80A2-843[»]
1XC7X-ray1.83A2-843[»]
1XKXX-ray1.93A2-843[»]
1XL0X-ray1.92A2-843[»]
1XL1X-ray2.10A2-843[»]
1Z62X-ray1.90A2-843[»]
1Z6PX-ray2.40A2-843[»]
1Z6QX-ray2.03A2-843[»]
2AMVX-ray2.30A2-843[»]
2F3PX-ray1.94A2-843[»]
2F3QX-ray1.96A2-843[»]
2F3SX-ray1.96A2-843[»]
2F3UX-ray1.93A2-843[»]
2FETX-ray2.03A2-843[»]
2FF5X-ray2.03A2-843[»]
2FFRX-ray2.03A13-837[»]
2G9QX-ray2.50A2-843[»]
2G9RX-ray2.07A2-843[»]
2G9UX-ray2.15A2-843[»]
2G9VX-ray2.15A2-843[»]
2GJ4X-ray1.60A13-836[»]
2GM9X-ray2.30A13-837[»]
2GPAX-ray2.00A2-839[»]
2GPBX-ray2.30A2-843[»]
2GPNX-ray1.99A2-843[»]
2IEGX-ray1.90A/B2-843[»]
2IEIX-ray1.91A/B2-843[»]
2OFFX-ray2.20A2-843[»]
2PRIX-ray2.30A2-843[»]
2PRJX-ray2.30A2-843[»]
2PYDX-ray1.93A1-843[»]
2PYIX-ray1.88A1-843[»]
2QLMX-ray2.10A2-843[»]
2QLNX-ray2.15A2-843[»]
2QN1X-ray2.40A2-843[»]
2QN2X-ray2.70A2-843[»]
2QN3X-ray1.96A2-843[»]
2QN7X-ray1.83A2-843[»]
2QN8X-ray1.90A2-843[»]
2QN9X-ray2.00A2-843[»]
2QNBX-ray1.80A2-843[»]
2QRGX-ray1.85A2-843[»]
2QRHX-ray1.83A2-843[»]
2QRMX-ray1.90A2-843[»]
2QRPX-ray1.86A2-843[»]
2QRQX-ray1.80A2-843[»]
2SKCX-ray2.40A2-843[»]
2SKDX-ray2.40A2-843[»]
2SKEX-ray2.46A2-843[»]
3AMVX-ray2.10A2-843[»]
3BCRX-ray2.14A2-843[»]
3BCSX-ray2.00A2-843[»]
3BCUX-ray2.03A2-843[»]
3BD6X-ray2.00A2-843[»]
3BD7X-ray1.90A2-843[»]
3BD8X-ray2.10A2-843[»]
3BDAX-ray2.00A2-843[»]
3CUTX-ray2.30A2-843[»]
3CUUX-ray2.30A2-843[»]
3CUVX-ray1.93A2-843[»]
3CUWX-ray2.00A2-843[»]
3E3LX-ray2.59A/B/C/D2-843[»]
3E3NX-ray2.70A/B/C/D/E/F/G/H2-843[»]
3E3OX-ray2.60A/B/C/D2-843[»]
3EBOX-ray1.90A2-843[»]
3EBPX-ray2.00A2-843[»]
3G2HX-ray2.03A2-843[»]
3G2IX-ray2.00A2-843[»]
3G2JX-ray2.14A2-843[»]
3G2KX-ray2.00A2-843[»]
3G2LX-ray2.30A2-843[»]
3G2NX-ray2.10A2-843[»]
3GPBX-ray2.30A2-843[»]
3L79X-ray1.86A1-843[»]
3L7AX-ray1.90A1-843[»]
3L7BX-ray2.00A1-843[»]
3L7CX-ray1.93A1-843[»]
3L7DX-ray2.00A1-843[»]
3MQFX-ray1.95A2-843[»]
3MRTX-ray1.98A2-843[»]
3MRVX-ray1.94A2-843[»]
3MRXX-ray1.95A2-843[»]
3MS2X-ray2.10A2-843[»]
3MS4X-ray2.07A2-843[»]
3MS7X-ray1.95A2-843[»]
3MSCX-ray1.95A2-843[»]
3MT7X-ray2.00A2-843[»]
3MT8X-ray2.00A2-843[»]
3MT9X-ray2.05A2-843[»]
3MTAX-ray2.23A2-843[»]
3MTBX-ray1.95A2-843[»]
3MTDX-ray2.10A2-843[»]
3NC4X-ray2.07A3-843[»]
3NP7X-ray2.05A2-843[»]
3NP9X-ray2.00A2-843[»]
3NPAX-ray1.97A2-843[»]
3S0JX-ray2.00A2-843[»]
3SYMX-ray2.40A2-843[»]
3SYRX-ray2.40A2-843[»]
3T3DX-ray2.50A2-843[»]
3T3EX-ray2.15A2-843[»]
3T3GX-ray2.40A2-843[»]
3T3HX-ray2.60A2-843[»]
3T3IX-ray2.65A2-843[»]
3ZCPX-ray1.83A1-843[»]
3ZCQX-ray2.15A1-843[»]
3ZCRX-ray2.07A1-843[»]
3ZCSX-ray2.03A1-843[»]
3ZCTX-ray2.00A1-843[»]
3ZCUX-ray2.05A1-843[»]
3ZCVX-ray1.83A1-843[»]
4CTMX-ray1.95A1-843[»]
4CTNX-ray2.10A1-843[»]
4CTOX-ray1.90A1-843[»]
4EJ2X-ray2.65A13-837[»]
4EKEX-ray2.60A13-837[»]
4EKYX-ray2.45A13-837[»]
4EL0X-ray2.40A13-837[»]
4EL5X-ray2.00A13-837[»]
4GPBX-ray2.30A2-843[»]
4MHOX-ray2.00A13-837[»]
4MHSX-ray2.00A13-837[»]
4MI3X-ray2.15A13-837[»]
4MI6X-ray1.90A13-837[»]
4MI9X-ray1.85A13-837[»]
4MICX-ray2.45A13-837[»]
4MRAX-ray2.34A13-837[»]
4YI3X-ray1.80A1-843[»]
4YI5X-ray1.80A1-843[»]
4YUAX-ray2.00A13-837[»]
4Z5XX-ray2.10A1-843[»]
5GPBX-ray2.30A2-843[»]
5JTTX-ray1.85A1-843[»]
5JTUX-ray1.85A1-843[»]
6GPBX-ray2.86A2-843[»]
7GPBX-ray2.90A/B/C/D2-843[»]
8GPBX-ray2.20A2-843[»]
9GPBX-ray2.90A/B/C/D2-843[»]
ProteinModelPortaliP00489.
SMRiP00489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00489.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP00489.
KOiK00688.

Family and domain databases

CDDicd04300. GT1_Glycogen_Phosphorylase. 1 hit.
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.

P00489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR
60 70 80 90 100
DYYFALAHTV RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM
110 120 130 140 150
VNLALENACD EATYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA DDWLRYGNPW EKARPEFTLP
210 220 230 240 250
VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN TMRLWSAKAP
260 270 280 290 300
NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
310 320 330 340 350
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL
360 370 380 390 400
MRVLVDLERL DWDKAWEVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH
410 420 430 440 450
LQIIYEINQR FLNRVAAAFP GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS
460 470 480 490 500
HAVNGVARIH SEILKKTIFK DFYELEPHKF QNKTNGITPR RWLVLCNPGL
510 520 530 540 550
AEIIAERIGE EYISDLDQLR KLLSYVDDEA FIRDVAKVKQ ENKLKFAAYL
560 570 580 590 600
EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFVV
610 620 630 640 650
PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR
660 670 680 690 700
VSLAEKVIPA ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGEENFF IFGMRVEDVD RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF
760 770 780 790 800
FSPKQPDLFK DIVNMLMHHD RFKVFADYEE YVKCQERVSA LYKNPREWTR
810 820 830 840
MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE KIP
Length:843
Mass (Da):97,289
Last modified:January 23, 2007 - v3
Checksum:i9884F06FDD3AE9D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31 – 33NFN → DFD AA sequence (PubMed:728424).Curated3
Sequence conflicti43D → N AA sequence (PubMed:728424).Curated1
Sequence conflicti56 – 58LAH → HAL AA sequence (PubMed:728424).Curated3
Sequence conflicti89E → Q AA sequence (PubMed:728424).Curated1
Sequence conflicti113T → D AA sequence (PubMed:728424).Curated1
Sequence conflicti309Missing AA sequence (PubMed:728424).Curated1
Sequence conflicti578 – 579LL → FF in CAA26833 (PubMed:3840433).Curated2
Sequence conflicti610A → P in BAA00027 (PubMed:3015680).Curated1
Sequence conflicti610A → P in CAA27816 (PubMed:3015680).Curated1
Sequence conflicti713G → C in CAA26833 (PubMed:3840433).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00040 mRNA. Translation: BAA00027.1.
X04265 mRNA. Translation: CAA27816.1.
X03030 mRNA. Translation: CAA26833.1.
PIRiA24302. PHRBG.
RefSeqiNP_001075653.1. NM_001082184.1.
UniGeneiOcu.2087.

Genome annotation databases

GeneIDi100008972.
KEGGiocu:100008972.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00040 mRNA. Translation: BAA00027.1.
X04265 mRNA. Translation: CAA27816.1.
X03030 mRNA. Translation: CAA26833.1.
PIRiA24302. PHRBG.
RefSeqiNP_001075653.1. NM_001082184.1.
UniGeneiOcu.2087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A8IX-ray1.78A2-843[»]
1ABBX-ray2.80A/B/C/D11-838[»]
1AXRX-ray2.30A2-843[»]
1B4DX-ray2.00A2-843[»]
1BX3X-ray2.30A2-843[»]
1C50X-ray2.30A14-843[»]
1C8KX-ray1.76A2-843[»]
1C8LX-ray2.30A2-843[»]
1E1YX-ray2.23A2-843[»]
1FS4X-ray2.38A2-843[»]
1FTQX-ray2.35A2-843[»]
1FTWX-ray2.36A2-843[»]
1FTYX-ray2.38A2-843[»]
1FU4X-ray2.36A2-843[»]
1FU7X-ray2.36A2-843[»]
1FU8X-ray2.35A2-843[»]
1GFZX-ray2.30A2-843[»]
1GG8X-ray2.31A2-843[»]
1GGNX-ray2.36A2-843[»]
1GPAX-ray2.90A/B/C/D2-843[»]
1GPBX-ray1.90A2-843[»]
1GPYX-ray2.40A2-843[»]
1H5UX-ray1.76A2-843[»]
1HLFX-ray2.26A2-843[»]
1K06X-ray1.80A2-843[»]
1K08X-ray2.26A2-843[»]
1KTIX-ray1.97A2-843[»]
1LWNX-ray2.00A2-843[»]
1LWOX-ray2.00A2-843[»]
1NOIX-ray2.50A/B/C/D2-843[»]
1NOJX-ray2.40A2-843[»]
1NOKX-ray2.40A2-843[»]
1P29X-ray2.20A2-843[»]
1P2BX-ray2.20A2-843[»]
1P2DX-ray1.94A2-843[»]
1P2GX-ray2.30A2-843[»]
1P4GX-ray2.10A2-843[»]
1P4HX-ray2.06A2-843[»]
1P4JX-ray2.00A2-843[»]
1PYGX-ray2.87A/B/C/D2-843[»]
1UZUX-ray2.30A2-843[»]
1WUTX-ray2.26A2-843[»]
1WUYX-ray2.26A2-843[»]
1WV0X-ray2.26A2-843[»]
1WV1X-ray2.26A2-843[»]
1WW2X-ray1.90A2-843[»]
1WW3X-ray1.80A2-843[»]
1XC7X-ray1.83A2-843[»]
1XKXX-ray1.93A2-843[»]
1XL0X-ray1.92A2-843[»]
1XL1X-ray2.10A2-843[»]
1Z62X-ray1.90A2-843[»]
1Z6PX-ray2.40A2-843[»]
1Z6QX-ray2.03A2-843[»]
2AMVX-ray2.30A2-843[»]
2F3PX-ray1.94A2-843[»]
2F3QX-ray1.96A2-843[»]
2F3SX-ray1.96A2-843[»]
2F3UX-ray1.93A2-843[»]
2FETX-ray2.03A2-843[»]
2FF5X-ray2.03A2-843[»]
2FFRX-ray2.03A13-837[»]
2G9QX-ray2.50A2-843[»]
2G9RX-ray2.07A2-843[»]
2G9UX-ray2.15A2-843[»]
2G9VX-ray2.15A2-843[»]
2GJ4X-ray1.60A13-836[»]
2GM9X-ray2.30A13-837[»]
2GPAX-ray2.00A2-839[»]
2GPBX-ray2.30A2-843[»]
2GPNX-ray1.99A2-843[»]
2IEGX-ray1.90A/B2-843[»]
2IEIX-ray1.91A/B2-843[»]
2OFFX-ray2.20A2-843[»]
2PRIX-ray2.30A2-843[»]
2PRJX-ray2.30A2-843[»]
2PYDX-ray1.93A1-843[»]
2PYIX-ray1.88A1-843[»]
2QLMX-ray2.10A2-843[»]
2QLNX-ray2.15A2-843[»]
2QN1X-ray2.40A2-843[»]
2QN2X-ray2.70A2-843[»]
2QN3X-ray1.96A2-843[»]
2QN7X-ray1.83A2-843[»]
2QN8X-ray1.90A2-843[»]
2QN9X-ray2.00A2-843[»]
2QNBX-ray1.80A2-843[»]
2QRGX-ray1.85A2-843[»]
2QRHX-ray1.83A2-843[»]
2QRMX-ray1.90A2-843[»]
2QRPX-ray1.86A2-843[»]
2QRQX-ray1.80A2-843[»]
2SKCX-ray2.40A2-843[»]
2SKDX-ray2.40A2-843[»]
2SKEX-ray2.46A2-843[»]
3AMVX-ray2.10A2-843[»]
3BCRX-ray2.14A2-843[»]
3BCSX-ray2.00A2-843[»]
3BCUX-ray2.03A2-843[»]
3BD6X-ray2.00A2-843[»]
3BD7X-ray1.90A2-843[»]
3BD8X-ray2.10A2-843[»]
3BDAX-ray2.00A2-843[»]
3CUTX-ray2.30A2-843[»]
3CUUX-ray2.30A2-843[»]
3CUVX-ray1.93A2-843[»]
3CUWX-ray2.00A2-843[»]
3E3LX-ray2.59A/B/C/D2-843[»]
3E3NX-ray2.70A/B/C/D/E/F/G/H2-843[»]
3E3OX-ray2.60A/B/C/D2-843[»]
3EBOX-ray1.90A2-843[»]
3EBPX-ray2.00A2-843[»]
3G2HX-ray2.03A2-843[»]
3G2IX-ray2.00A2-843[»]
3G2JX-ray2.14A2-843[»]
3G2KX-ray2.00A2-843[»]
3G2LX-ray2.30A2-843[»]
3G2NX-ray2.10A2-843[»]
3GPBX-ray2.30A2-843[»]
3L79X-ray1.86A1-843[»]
3L7AX-ray1.90A1-843[»]
3L7BX-ray2.00A1-843[»]
3L7CX-ray1.93A1-843[»]
3L7DX-ray2.00A1-843[»]
3MQFX-ray1.95A2-843[»]
3MRTX-ray1.98A2-843[»]
3MRVX-ray1.94A2-843[»]
3MRXX-ray1.95A2-843[»]
3MS2X-ray2.10A2-843[»]
3MS4X-ray2.07A2-843[»]
3MS7X-ray1.95A2-843[»]
3MSCX-ray1.95A2-843[»]
3MT7X-ray2.00A2-843[»]
3MT8X-ray2.00A2-843[»]
3MT9X-ray2.05A2-843[»]
3MTAX-ray2.23A2-843[»]
3MTBX-ray1.95A2-843[»]
3MTDX-ray2.10A2-843[»]
3NC4X-ray2.07A3-843[»]
3NP7X-ray2.05A2-843[»]
3NP9X-ray2.00A2-843[»]
3NPAX-ray1.97A2-843[»]
3S0JX-ray2.00A2-843[»]
3SYMX-ray2.40A2-843[»]
3SYRX-ray2.40A2-843[»]
3T3DX-ray2.50A2-843[»]
3T3EX-ray2.15A2-843[»]
3T3GX-ray2.40A2-843[»]
3T3HX-ray2.60A2-843[»]
3T3IX-ray2.65A2-843[»]
3ZCPX-ray1.83A1-843[»]
3ZCQX-ray2.15A1-843[»]
3ZCRX-ray2.07A1-843[»]
3ZCSX-ray2.03A1-843[»]
3ZCTX-ray2.00A1-843[»]
3ZCUX-ray2.05A1-843[»]
3ZCVX-ray1.83A1-843[»]
4CTMX-ray1.95A1-843[»]
4CTNX-ray2.10A1-843[»]
4CTOX-ray1.90A1-843[»]
4EJ2X-ray2.65A13-837[»]
4EKEX-ray2.60A13-837[»]
4EKYX-ray2.45A13-837[»]
4EL0X-ray2.40A13-837[»]
4EL5X-ray2.00A13-837[»]
4GPBX-ray2.30A2-843[»]
4MHOX-ray2.00A13-837[»]
4MHSX-ray2.00A13-837[»]
4MI3X-ray2.15A13-837[»]
4MI6X-ray1.90A13-837[»]
4MI9X-ray1.85A13-837[»]
4MICX-ray2.45A13-837[»]
4MRAX-ray2.34A13-837[»]
4YI3X-ray1.80A1-843[»]
4YI5X-ray1.80A1-843[»]
4YUAX-ray2.00A13-837[»]
4Z5XX-ray2.10A1-843[»]
5GPBX-ray2.30A2-843[»]
5JTTX-ray1.85A1-843[»]
5JTUX-ray1.85A1-843[»]
6GPBX-ray2.86A2-843[»]
7GPBX-ray2.90A/B/C/D2-843[»]
8GPBX-ray2.20A2-843[»]
9GPBX-ray2.90A/B/C/D2-843[»]
ProteinModelPortaliP00489.
SMRiP00489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38240N.
IntActiP00489. 2 interactors.
MINTiMINT-6368963.
STRINGi9986.ENSOCUP00000001880.

Chemistry databases

BindingDBiP00489.
ChEMBLiCHEMBL4696.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

PTM databases

iPTMnetiP00489.

Proteomic databases

PRIDEiP00489.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008972.
KEGGiocu:100008972.

Organism-specific databases

CTDi5837.

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP00489.
KOiK00688.

Enzyme and pathway databases

BRENDAi2.4.1.1. 1749.
SABIO-RKP00489.

Miscellaneous databases

EvolutionaryTraceiP00489.
PROiP00489.

Family and domain databases

CDDicd04300. GT1_Glycogen_Phosphorylase. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPYGM_RABIT
AccessioniPrimary (citable) accession number: P00489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.