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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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 843842Glycogen phosphorylase, muscle formPRO_0000188532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase A
Modified residuei473 – 4731PhosphotyrosineBy 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

1
843
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 135Combined sources
Helixi15 – 173Combined sources
Helixi22 – 3817Combined sources
Turni44 – 463Combined sources
Helixi49 – 6214Combined sources
Helixi65 – 7814Combined sources
Beta strandi82 – 865Combined sources
Beta strandi90 – 934Combined sources
Helixi96 – 1027Combined sources
Helixi106 – 11510Combined sources
Helixi120 – 1245Combined sources
Beta strandi130 – 1323Combined sources
Helixi136 – 15015Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi175 – 1795Combined sources
Turni183 – 1864Combined sources
Helixi195 – 1973Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi211 – 2188Combined sources
Beta strandi220 – 23213Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi239 – 24810Combined sources
Helixi253 – 2564Combined sources
Beta strandi259 – 2613Combined sources
Helixi263 – 2686Combined sources
Helixi270 – 2745Combined sources
Helixi275 – 2773Combined sources
Beta strandi284 – 2863Combined sources
Helixi291 – 31323Combined sources
Turni315 – 3195Combined sources
Beta strandi322 – 3254Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 3334Combined sources
Beta strandi334 – 3418Combined sources
Turni342 – 3454Combined sources
Helixi346 – 35611Combined sources
Helixi362 – 37211Combined sources
Beta strandi373 – 3764Combined sources
Helixi382 – 3843Combined sources
Beta strandi387 – 3893Combined sources
Helixi390 – 3967Combined sources
Helixi398 – 41821Combined sources
Beta strandi419 – 4213Combined sources
Helixi423 – 4297Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi439 – 4413Combined sources
Helixi442 – 4487Combined sources
Beta strandi453 – 4575Combined sources
Helixi458 – 4669Combined sources
Turni467 – 4693Combined sources
Helixi470 – 4756Combined sources
Helixi477 – 4793Combined sources
Beta strandi480 – 4823Combined sources
Helixi490 – 4956Combined sources
Helixi498 – 50811Combined sources
Helixi511 – 5144Combined sources
Helixi516 – 52510Combined sources
Helixi529 – 55426Combined sources
Beta strandi562 – 5698Combined sources
Turni573 – 5764Combined sources
Helixi577 – 59317Combined sources
Beta strandi602 – 6076Combined sources
Helixi615 – 63117Combined sources
Turni635 – 6373Combined sources
Helixi638 – 6403Combined sources
Beta strandi641 – 6466Combined sources
Helixi651 – 6577Combined sources
Helixi658 – 6603Combined sources
Beta strandi662 – 6665Combined sources
Turni670 – 6723Combined sources
Beta strandi673 – 6753Combined sources
Helixi678 – 6847Combined sources
Beta strandi688 – 6914Combined sources
Helixi697 – 7048Combined sources
Helixi706 – 7083Combined sources
Beta strandi709 – 7113Combined sources
Helixi716 – 72510Combined sources
Helixi729 – 7357Combined sources
Helixi737 – 74812Combined sources
Turni749 – 7513Combined sources
Beta strandi753 – 7553Combined sources
Turni756 – 7594Combined sources
Helixi760 – 7689Combined sources
Helixi775 – 7773Combined sources
Helixi778 – 79215Combined sources
Helixi795 – 80612Combined sources
Helixi810 – 8123Combined sources
Helixi814 – 82411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
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[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00489.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0058.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP00489.

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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 333NFN → DFD AA sequence (PubMed:728424)Curated
Sequence conflicti43 – 431D → N AA sequence (PubMed:728424)Curated
Sequence conflicti56 – 583LAH → HAL AA sequence (PubMed:728424)Curated
Sequence conflicti89 – 891E → Q AA sequence (PubMed:728424)Curated
Sequence conflicti113 – 1131T → D AA sequence (PubMed:728424)Curated
Sequence conflicti309 – 3091Missing AA sequence (PubMed:728424)Curated
Sequence conflicti578 – 5792LL → FF in CAA26833. (PubMed:3840433)Curated
Sequence conflicti610 – 6101A → P in BAA00027. (PubMed:3015680)Curated
Sequence conflicti610 – 6101A → P in CAA27816. (PubMed:3015680)Curated
Sequence conflicti713 – 7131G → C in CAA26833. (PubMed:3840433)Curated

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.

Cross-referencesi

Web resourcesi

ProZyme technical fact sheet

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 .
PIRi A24302. PHRBG.
RefSeqi NP_001075653.1. NM_001082184.1.
UniGenei Ocu.2087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4CTM X-ray 1.95 A 1-843 [» ]
4CTN X-ray 2.10 A 1-843 [» ]
4CTO X-ray 1.90 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 [» ]
4MHO X-ray 2.00 A 13-837 [» ]
4MHS X-ray 2.00 A 13-837 [» ]
4MI3 X-ray 2.15 A 13-837 [» ]
4MI6 X-ray 1.90 A 13-837 [» ]
4MI9 X-ray 1.85 A 13-837 [» ]
4MIC X-ray 2.45 A 13-837 [» ]
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.

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.
InParanoidi P00489.

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: November 26, 2014
This is version 144 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