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P00489

- PYGM_RABIT

UniProt

P00489 - PYGM_RABIT

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Protein
Glycogen phosphorylase, muscle form
Gene
PYGM
Organism
Oryctolagus cuniculus (Rabbit)
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 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761AMP
Sitei109 – 1091Involved in the association of subunits
Sitei143 – 1431Involved in the association of subunits
Sitei156 – 1561Can be labeled by an AMP analog; may be involved in allosteric regulation

GO - Molecular functioni

  1. glycogen phosphorylase activity Source: Ensembl
  2. nucleotide binding Source: UniProtKB-KW
  3. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glycogen catabolic process Source: Ensembl
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
ProteomesiUP000001811: Unplaced

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 843842Glycogen phosphorylase, muscle form
PRO_0000188532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase A1 Publication
Modified residuei473 – 4731Phosphotyrosine By similarity
Modified residuei681 – 6811N6-(pyridoxal phosphate)lysine

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00489.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-38240N.
IntActiP00489. 2 interactions.
MINTiMINT-6368963.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 135
Helixi15 – 173
Helixi22 – 3817
Turni44 – 463
Helixi49 – 6214
Helixi65 – 7814
Beta strandi82 – 865
Beta strandi90 – 934
Helixi96 – 1027
Helixi106 – 11510
Helixi120 – 1245
Beta strandi130 – 1323
Helixi136 – 15015
Beta strandi155 – 1606
Beta strandi168 – 1725
Beta strandi175 – 1795
Turni183 – 1864
Helixi195 – 1973
Beta strandi199 – 2046
Beta strandi206 – 2094
Beta strandi211 – 2188
Beta strandi220 – 23213
Beta strandi234 – 2374
Beta strandi239 – 24810
Helixi253 – 2564
Beta strandi259 – 2613
Helixi263 – 2686
Helixi270 – 2745
Helixi275 – 2773
Beta strandi284 – 2863
Helixi291 – 31323
Turni315 – 3195
Beta strandi322 – 3254
Helixi327 – 3293
Helixi330 – 3334
Beta strandi334 – 3418
Turni342 – 3454
Helixi346 – 35611
Helixi362 – 37211
Beta strandi373 – 3764
Helixi382 – 3843
Beta strandi387 – 3893
Helixi390 – 3967
Helixi398 – 41821
Beta strandi419 – 4213
Helixi423 – 4297
Beta strandi431 – 4333
Beta strandi435 – 4373
Beta strandi439 – 4413
Helixi442 – 4487
Beta strandi453 – 4575
Helixi458 – 4669
Turni467 – 4693
Helixi470 – 4756
Helixi477 – 4793
Beta strandi480 – 4823
Helixi490 – 4956
Helixi498 – 50811
Helixi511 – 5144
Helixi516 – 52510
Helixi529 – 55426
Beta strandi562 – 5698
Turni573 – 5764
Helixi577 – 59317
Beta strandi602 – 6076
Helixi615 – 63117
Turni635 – 6373
Helixi638 – 6403
Beta strandi641 – 6466
Helixi651 – 6577
Helixi658 – 6603
Beta strandi662 – 6665
Turni670 – 6723
Beta strandi673 – 6753
Helixi678 – 6847
Beta strandi688 – 6914
Helixi697 – 7048
Helixi706 – 7083
Beta strandi709 – 7113
Helixi716 – 72510
Helixi729 – 7357
Helixi737 – 74812
Turni749 – 7513
Beta strandi753 – 7553
Turni756 – 7594
Helixi760 – 7689
Helixi775 – 7773
Helixi778 – 79215
Helixi795 – 80612
Helixi810 – 8123
Helixi814 – 82411

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4EJ2X-ray2.65A13-837[»]
4EKEX-ray2.60A13-837[»]
4EKYX-ray2.45A13-837[»]
4EL0X-ray2.40A13-837[»]
4EL5X-ray2.00A13-837[»]
4GPBX-ray2.30A2-843[»]
4MRAX-ray2.34A13-837[»]
5GPBX-ray2.30A2-843[»]
6GPBX-ray2.86A2-843[»]
7GPBX-ray2.90A/B/C/D2-843[»]
8GPBX-ray2.20A2-843[»]
9GPBX-ray2.90A/B/C/D2-843[»]
ProteinModelPortaliP00489.
SMRiP00489. Positions 15-843.

Miscellaneous databases

EvolutionaryTraceiP00489.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0058.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.

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.

P00489-1 [UniParc]FASTAAdd to Basket

« Hide

MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR    50
DYYFALAHTV RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM 100
VNLALENACD EATYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT 150
LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA DDWLRYGNPW EKARPEFTLP 200
VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN TMRLWSAKAP 250
NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL 350
MRVLVDLERL DWDKAWEVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH 400
LQIIYEINQR FLNRVAAAFP GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS 450
HAVNGVARIH SEILKKTIFK DFYELEPHKF QNKTNGITPR RWLVLCNPGL 500
AEIIAERIGE EYISDLDQLR KLLSYVDDEA FIRDVAKVKQ ENKLKFAAYL 550
EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFVV 600
PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR 650
VSLAEKVIPA ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 700
AEEAGEENFF IFGMRVEDVD RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF 750
FSPKQPDLFK DIVNMLMHHD RFKVFADYEE YVKCQERVSA LYKNPREWTR 800
MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE KIP 843
Length:843
Mass (Da):97,289
Last modified:January 23, 2007 - v3
Checksum:i9884F06FDD3AE9D3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 333NFN → DFD AA sequence 1 Publication
Sequence conflicti43 – 431D → N AA sequence 1 Publication
Sequence conflicti56 – 583LAH → HAL AA sequence 1 Publication
Sequence conflicti89 – 891E → Q AA sequence 1 Publication
Sequence conflicti113 – 1131T → D AA sequence 1 Publication
Sequence conflicti309 – 3091Missing AA sequence 1 Publication
Sequence conflicti578 – 5792LL → FF in CAA26833. 1 Publication
Sequence conflicti610 – 6101A → P in BAA00027. 1 Publication
Sequence conflicti610 – 6101A → P in CAA27816. 1 Publication
Sequence conflicti713 – 7131G → C in CAA26833. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Web resourcesi

ProZyme technical fact sheet

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00040 mRNA. Translation: BAA00027.1 .
X04265 mRNA. Translation: CAA27816.1 .
X03030 mRNA. Translation: CAA26833.1 .
PIRi A24302. PHRBG.
RefSeqi NP_001075653.1. NM_001082184.1.
UniGenei Ocu.2087.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A8I X-ray 1.78 A 2-843 [» ]
1ABB X-ray 2.80 A/B/C/D 11-838 [» ]
1AXR X-ray 2.30 A 2-843 [» ]
1B4D X-ray 2.00 A 2-843 [» ]
1BX3 X-ray 2.30 A 2-843 [» ]
1C50 X-ray 2.30 A 14-843 [» ]
1C8K X-ray 1.76 A 2-843 [» ]
1C8L X-ray 2.30 A 2-843 [» ]
1E1Y X-ray 2.23 A 2-843 [» ]
1FS4 X-ray 2.38 A 2-843 [» ]
1FTQ X-ray 2.35 A 2-843 [» ]
1FTW X-ray 2.36 A 2-843 [» ]
1FTY X-ray 2.38 A 2-843 [» ]
1FU4 X-ray 2.36 A 2-843 [» ]
1FU7 X-ray 2.36 A 2-843 [» ]
1FU8 X-ray 2.35 A 2-843 [» ]
1GFZ X-ray 2.30 A 2-843 [» ]
1GG8 X-ray 2.31 A 2-843 [» ]
1GGN X-ray 2.36 A 2-843 [» ]
1GPA X-ray 2.90 A/B/C/D 2-843 [» ]
1GPB X-ray 1.90 A 2-843 [» ]
1GPY X-ray 2.40 A 2-843 [» ]
1H5U X-ray 1.76 A 2-843 [» ]
1HLF X-ray 2.26 A 2-843 [» ]
1K06 X-ray 1.80 A 2-843 [» ]
1K08 X-ray 2.26 A 2-843 [» ]
1KTI X-ray 1.97 A 2-843 [» ]
1LWN X-ray 2.00 A 2-843 [» ]
1LWO X-ray 2.00 A 2-843 [» ]
1NOI X-ray 2.50 A/B/C/D 2-843 [» ]
1NOJ X-ray 2.40 A 2-843 [» ]
1NOK X-ray 2.40 A 2-843 [» ]
1P29 X-ray 2.20 A 2-843 [» ]
1P2B X-ray 2.20 A 2-843 [» ]
1P2D X-ray 1.94 A 2-843 [» ]
1P2G X-ray 2.30 A 2-843 [» ]
1P4G X-ray 2.10 A 2-843 [» ]
1P4H X-ray 2.06 A 2-843 [» ]
1P4J X-ray 2.00 A 2-843 [» ]
1PYG X-ray 2.87 A/B/C/D 2-843 [» ]
1UZU X-ray 2.30 A 2-843 [» ]
1WUT X-ray 2.26 A 2-843 [» ]
1WUY X-ray 2.26 A 2-843 [» ]
1WV0 X-ray 2.26 A 2-843 [» ]
1WV1 X-ray 2.26 A 2-843 [» ]
1WW2 X-ray 1.90 A 2-843 [» ]
1WW3 X-ray 1.80 A 2-843 [» ]
1XC7 X-ray 1.83 A 2-843 [» ]
1XKX X-ray 1.93 A 2-843 [» ]
1XL0 X-ray 1.92 A 2-843 [» ]
1XL1 X-ray 2.10 A 2-843 [» ]
1Z62 X-ray 1.90 A 2-843 [» ]
1Z6P X-ray 2.40 A 2-843 [» ]
1Z6Q X-ray 2.03 A 2-843 [» ]
2AMV X-ray 2.30 A 2-843 [» ]
2F3P X-ray 1.94 A 2-843 [» ]
2F3Q X-ray 1.96 A 2-843 [» ]
2F3S X-ray 1.96 A 2-843 [» ]
2F3U X-ray 1.93 A 2-843 [» ]
2FET X-ray 2.03 A 2-843 [» ]
2FF5 X-ray 2.03 A 2-843 [» ]
2FFR X-ray 2.03 A 13-837 [» ]
2G9Q X-ray 2.50 A 2-843 [» ]
2G9R X-ray 2.07 A 2-843 [» ]
2G9U X-ray 2.15 A 2-843 [» ]
2G9V X-ray 2.15 A 2-843 [» ]
2GJ4 X-ray 1.60 A 13-836 [» ]
2GM9 X-ray 2.30 A 13-837 [» ]
2GPA X-ray 2.00 A 2-839 [» ]
2GPB X-ray 2.30 A 2-843 [» ]
2GPN X-ray 1.99 A 2-843 [» ]
2IEG X-ray 1.90 A/B 2-843 [» ]
2IEI X-ray 1.91 A/B 2-843 [» ]
2OFF X-ray 2.20 A 2-843 [» ]
2PRI X-ray 2.30 A 2-843 [» ]
2PRJ X-ray 2.30 A 2-843 [» ]
2PYD X-ray 1.93 A 1-843 [» ]
2PYI X-ray 1.88 A 1-843 [» ]
2QLM X-ray 2.10 A 2-843 [» ]
2QLN X-ray 2.15 A 2-843 [» ]
2QN1 X-ray 2.40 A 2-843 [» ]
2QN2 X-ray 2.70 A 2-843 [» ]
2QN3 X-ray 1.96 A 2-843 [» ]
2QN7 X-ray 1.83 A 2-843 [» ]
2QN8 X-ray 1.90 A 2-843 [» ]
2QN9 X-ray 2.00 A 2-843 [» ]
2QNB X-ray 1.80 A 2-843 [» ]
2QRG X-ray 1.85 A 2-843 [» ]
2QRH X-ray 1.83 A 2-843 [» ]
2QRM X-ray 1.90 A 2-843 [» ]
2QRP X-ray 1.86 A 2-843 [» ]
2QRQ X-ray 1.80 A 2-843 [» ]
2SKC X-ray 2.40 A 2-843 [» ]
2SKD X-ray 2.40 A 2-843 [» ]
2SKE X-ray 2.46 A 2-843 [» ]
3AMV X-ray 2.10 A 2-843 [» ]
3BCR X-ray 2.14 A 2-843 [» ]
3BCS X-ray 2.00 A 2-843 [» ]
3BCU X-ray 2.03 A 2-843 [» ]
3BD6 X-ray 2.00 A 2-843 [» ]
3BD7 X-ray 1.90 A 2-843 [» ]
3BD8 X-ray 2.10 A 2-843 [» ]
3BDA X-ray 2.00 A 2-843 [» ]
3CUT X-ray 2.30 A 2-843 [» ]
3CUU X-ray 2.30 A 2-843 [» ]
3CUV X-ray 1.93 A 2-843 [» ]
3CUW X-ray 2.00 A 2-843 [» ]
3E3L X-ray 2.59 A/B/C/D 2-843 [» ]
3E3N X-ray 2.70 A/B/C/D/E/F/G/H 2-843 [» ]
3E3O X-ray 2.60 A/B/C/D 2-843 [» ]
3EBO X-ray 1.90 A 2-843 [» ]
3EBP X-ray 2.00 A 2-843 [» ]
3G2H X-ray 2.03 A 2-843 [» ]
3G2I X-ray 2.00 A 2-843 [» ]
3G2J X-ray 2.14 A 2-843 [» ]
3G2K X-ray 2.00 A 2-843 [» ]
3G2L X-ray 2.30 A 2-843 [» ]
3G2N X-ray 2.10 A 2-843 [» ]
3GPB X-ray 2.30 A 2-843 [» ]
3L79 X-ray 1.86 A 1-843 [» ]
3L7A X-ray 1.90 A 1-843 [» ]
3L7B X-ray 2.00 A 1-843 [» ]
3L7C X-ray 1.93 A 1-843 [» ]
3L7D X-ray 2.00 A 1-843 [» ]
3MQF X-ray 1.95 A 2-843 [» ]
3MRT X-ray 1.98 A 2-843 [» ]
3MRV X-ray 1.94 A 2-843 [» ]
3MRX X-ray 1.95 A 2-843 [» ]
3MS2 X-ray 2.10 A 2-843 [» ]
3MS4 X-ray 2.07 A 2-843 [» ]
3MS7 X-ray 1.95 A 2-843 [» ]
3MSC X-ray 1.95 A 2-843 [» ]
3MT7 X-ray 2.00 A 2-843 [» ]
3MT8 X-ray 2.00 A 2-843 [» ]
3MT9 X-ray 2.05 A 2-843 [» ]
3MTA X-ray 2.23 A 2-843 [» ]
3MTB X-ray 1.95 A 2-843 [» ]
3MTD X-ray 2.10 A 2-843 [» ]
3NC4 X-ray 2.07 A 3-843 [» ]
3NP7 X-ray 2.05 A 2-843 [» ]
3NP9 X-ray 2.00 A 2-843 [» ]
3NPA X-ray 1.97 A 2-843 [» ]
3S0J X-ray 2.00 A 2-843 [» ]
3SYM X-ray 2.40 A 2-843 [» ]
3SYR X-ray 2.40 A 2-843 [» ]
3T3D X-ray 2.50 A 2-843 [» ]
3T3E X-ray 2.15 A 2-843 [» ]
3T3G X-ray 2.40 A 2-843 [» ]
3T3H X-ray 2.60 A 2-843 [» ]
3T3I X-ray 2.65 A 2-843 [» ]
3ZCP X-ray 1.83 A 1-843 [» ]
3ZCQ X-ray 2.15 A 1-843 [» ]
3ZCR X-ray 2.07 A 1-843 [» ]
3ZCS X-ray 2.03 A 1-843 [» ]
3ZCT X-ray 2.00 A 1-843 [» ]
3ZCU X-ray 2.05 A 1-843 [» ]
3ZCV X-ray 1.83 A 1-843 [» ]
4EJ2 X-ray 2.65 A 13-837 [» ]
4EKE X-ray 2.60 A 13-837 [» ]
4EKY X-ray 2.45 A 13-837 [» ]
4EL0 X-ray 2.40 A 13-837 [» ]
4EL5 X-ray 2.00 A 13-837 [» ]
4GPB X-ray 2.30 A 2-843 [» ]
4MRA X-ray 2.34 A 13-837 [» ]
5GPB X-ray 2.30 A 2-843 [» ]
6GPB X-ray 2.86 A 2-843 [» ]
7GPB X-ray 2.90 A/B/C/D 2-843 [» ]
8GPB X-ray 2.20 A 2-843 [» ]
9GPB X-ray 2.90 A/B/C/D 2-843 [» ]
ProteinModelPortali P00489.
SMRi P00489. Positions 15-843.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-38240N.
IntActi P00489. 2 interactions.
MINTi MINT-6368963.

Chemistry

BindingDBi P00489.
ChEMBLi CHEMBL4696.
DrugBanki DB00131. Adenosine monophosphate.

Protein family/group databases

CAZyi GT35. Glycosyltransferase Family 35.

Proteomic databases

PRIDEi P00489.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100008972.

Organism-specific databases

CTDi 5837.

Phylogenomic databases

eggNOGi COG0058.
HOGENOMi HOG000278444.
HOVERGENi HBG006848.

Enzyme and pathway databases

BRENDAi 2.4.1.1. 1749.
SABIO-RK P00489.

Miscellaneous databases

EvolutionaryTracei P00489.

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

  1. "Complete cDNA sequence for rabbit muscle glycogen phosphorylase."
    Nakano K., Hwang P.K., Fletterick R.J.
    FEBS Lett. 204:283-287(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of the amino-terminal 349 residues of rabbit muscle glycogen phosphorylase including the sites of covalent and allosteric control."
    Koide A., Titani K., Ericsson L.H., Kumar S., Neurath H., Walsh K.A.
    Biochemistry 17:5657-5672(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-351.
  3. "Amino acid sequence of two cyanogen bromide fragments of glycogen phosphorylase."
    Hermann J., Titani K., Ericsson L.H., Wade R.D., Neurath H., Walsh K.A.
    Biochemistry 17:5672-5679(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 352-429 AND 443-605.
  4. "Sequence of the carboxyl-terminal 492 residues of rabbit muscle glycogen phosphorylase including the pyridoxal 5'-phosphate binding site."
    Titani K., Koide A., Ericsson L.H., Kumar S., Hermann J., Wade R.D., Walsh K.A., Neurath H., Fischer E.H.
    Biochemistry 17:5680-5693(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 352-843.
  5. "Inactivation of phosphorylase b by potassium ferrate. Identification of a tyrosine residue involved in the binding of adenosine 5'-monophosphate."
    Lee Y.M., Benisek W.F.
    J. Biol. Chem. 253:5460-5463(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 71-81.
  6. "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 575-843.
  7. "Crystallographic analysis of phosphorylase alpha at 2.5-A resolution, a comment on the chemical sequence."
    Sprang S.R., Fletterick R.J.
    Biochemistry 17:5693-5694(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A.
  8. "Domain separation in the activation of glycogen phosphorylase a."
    Goldsmith E.J., Sprang S.R., Hamlin R., Xuong N.-H., Fletterick R.J.
    Science 245:528-532(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF PHOSPHORYLASE A.
  9. "Structure of the nucleotide activation switch in glycogen phosphorylase a."
    Sprang S.R., Goldsmith E.J., Fletterick R.J.
    Science 237:1012-1019(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A WITH AMP.
  10. "Assignment of the amino acid sequence to the crystal structure of glycogen phosphorylase b."
    Jenkins J.A., Johnson L.N., Wilson K.S.
    Biochemistry 17:5694-5695(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PHOSPHORYLASE B.
  11. "The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b: kinetic and crystallographic studies."
    Oikonomakos N.G., Zographos S.E., Johnson L.N., Papageorgiou A.C., Acharya K.R.
    J. Mol. Biol. 254:900-917(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF PHOSPHORYLASE B.
  12. "Activator anion binding site in pyridoxal phosphorylase b: the binding of phosphite, phosphate, and fluorophosphate in the crystal."
    Oikonomakos N.G., Zographos S.E., Tsitsanou K.E., Johnson L.N., Acharya K.R.
    Protein Sci. 5:2416-2428(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PHOSPHORYLASE B.
  13. "The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8-A resolution and 100 K: the role of the water structure and its contribution to binding."
    Gregoriou M., Noble M.E.M., Watson K.A., Garman E.F., Krulle T.M., de la Fuente C., Fleet G.W., Oikonomakos N.G., Johnson L.N.
    Protein Sci. 7:915-927(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF PHOSPHORYLASE B.

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: July 9, 2014
This is version 141 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

External Data

Dasty 3

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