Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 181 (17 Jun 2020)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Glycogen phosphorylase, muscle form

Gene

PYGM

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphate

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei76AMP1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Glycosyltransferase, Transferase
Biological processCarbohydrate metabolism, Glycogen metabolism
LigandNucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.1 1749

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00489

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT35 Glycosyltransferase Family 35

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glycogen phosphorylase, muscle form (EC:2.4.1.1)
Alternative name(s):
Myophosphorylase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PYGM
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOryctolagus cuniculus (Rabbit)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4696

DrugCentral

More...
DrugCentrali
P00489

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001885322 – 843Glycogen phosphorylase, muscle formAdd BLAST842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1
Modified residuei15Phosphoserine; by PHK; in form phosphorylase ABy similarity1
Modified residuei204PhosphotyrosineBy similarity1
Modified residuei227PhosphotyrosineBy similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei473PhosphotyrosineBy similarity1
Modified residuei514PhosphoserineBy similarity1
Modified residuei681N6-(pyridoxal phosphate)lysine1
Modified residuei747PhosphoserineBy similarity1
Modified residuei748PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P00489

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00489

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-38240N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P00489

Protein interaction database and analysis system

More...
IntActi
P00489, 5 interactors

Molecular INTeraction database

More...
MINTi
P00489

STRING: functional protein association networks

More...
STRINGi
9986.ENSOCUP00000001880

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00489

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1843
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P00489

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00489

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2099 Eukaryota
COG0058 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00489

KEGG Orthology (KO)

More...
KOi
K00688

Database of Orthologous Groups

More...
OrthoDBi
240595at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011833 Glycg_phsphrylas
IPR000811 Glyco_trans_35
IPR035090 Pyridoxal_P_attach_site

The PANTHER Classification System

More...
PANTHERi
PTHR11468 PTHR11468, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00343 Phosphorylase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000460 Pprylas_GlgP, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02093 P_ylase, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00102 PHOSPHORYLASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9884F06FDD3AE9D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D00040 mRNA Translation: BAA00027.1
X04265 mRNA Translation: CAA27816.1
X03030 mRNA Translation: CAA26833.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A24302 PHRBG

NCBI Reference Sequences

More...
RefSeqi
NP_001075653.1, NM_001082184.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100008972

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100008972

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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-ray2.00A2-843[»]
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[»]
5LRCX-ray2.00A2-843[»]
5LRDX-ray1.80A1-843[»]
5LREX-ray1.80A2-843[»]
5LRFX-ray1.75A2-843[»]
5MCBX-ray1.95A13-837[»]
5MEMX-ray1.78A1-843[»]
5O50X-ray1.90A2-843[»]
5O52X-ray1.90A1-843[»]
5O54X-ray2.45A1-843[»]
5O56X-ray2.45A1-843[»]
5OWYX-ray1.90A1-843[»]
5OWZX-ray1.85A1-843[»]
5OX0X-ray1.90A1-843[»]
5OX1X-ray1.85A1-843[»]
5OX3X-ray1.90A1-843[»]
5OX4X-ray1.80A1-843[»]
6F3JX-ray2.20A1-843[»]
6F3LX-ray1.90A1-843[»]
6F3RX-ray1.90A1-843[»]
6F3SX-ray1.90A1-843[»]
6F3UX-ray2.20A1-843[»]
6GPBX-ray2.86A2-843[»]
6QA6X-ray2.40A1-843[»]
6QA7X-ray2.36A1-843[»]
6QA8X-ray2.35A1-843[»]
6R0HX-ray2.50A1-843[»]
6R0IX-ray2.40A1-843[»]
6S4HX-ray2.45A1-843[»]
6S4KX-ray2.43A1-843[»]
6S4OX-ray2.35A1-843[»]
6S4PX-ray2.37A1-843[»]
6S4RX-ray2.30A1-843[»]
6S51X-ray2.37A1-843[»]
6S52X-ray2.37A1-843[»]
7GPBX-ray2.90A/B/C/D2-843[»]
8GPBX-ray2.20A2-843[»]
9GPBX-ray2.90A/B/C/D2-843[»]
SMRiP00489
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-38240N
ELMiP00489
IntActiP00489, 5 interactors
MINTiP00489
STRINGi9986.ENSOCUP00000001880

Chemistry databases

BindingDBiP00489
ChEMBLiCHEMBL4696
DrugCentraliP00489

Protein family/group databases

CAZyiGT35 Glycosyltransferase Family 35

PTM databases

iPTMnetiP00489

Proteomic databases

PRIDEiP00489

Genome annotation databases

GeneIDi100008972
KEGGiocu:100008972

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5837

Phylogenomic databases

eggNOGiKOG2099 Eukaryota
COG0058 LUCA
InParanoidiP00489
KOiK00688
OrthoDBi240595at2759

Enzyme and pathway databases

BRENDAi2.4.1.1 1749
SABIO-RKiP00489

Miscellaneous databases

EvolutionaryTraceiP00489

Protein Ontology

More...
PROi
PR:P00489

Family and domain databases

InterProiView protein in InterPro
IPR011833 Glycg_phsphrylas
IPR000811 Glyco_trans_35
IPR035090 Pyridoxal_P_attach_site
PANTHERiPTHR11468 PTHR11468, 1 hit
PfamiView protein in Pfam
PF00343 Phosphorylase, 1 hit
PIRSFiPIRSF000460 Pprylas_GlgP, 1 hit
TIGRFAMsiTIGR02093 P_ylase, 1 hit
PROSITEiView protein in PROSITE
PS00102 PHOSPHORYLASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPYGM_RABIT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00489
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 17, 2020
This is version 181 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again