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P09041 (PGK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase 2
EC=2.7.2.3
Alternative name(s):
Phosphoglycerate kinase, testis specific
Gene names
Name:Pgk2
Synonyms:Pgk-2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoglycerate kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 417416Phosphoglycerate kinase 2
PRO_0000145836

Regions

Nucleotide binding373 – 3764ATP By similarity
Region24 – 263Substrate binding By similarity
Region63 – 664Substrate binding By similarity

Sites

Binding site391Substrate By similarity
Binding site1231Substrate By similarity
Binding site1711Substrate By similarity
Binding site2201ATP By similarity
Binding site3131ATP; via carbonyl oxygen By similarity
Binding site3441ATP By similarity

Amino acid modifications

Modified residue911N6-acetyllysine By similarity
Modified residue1561N6-acetyllysine By similarity
Modified residue2671N6-acetyllysine By similarity

Experimental info

Sequence conflict1511Q → R in AAA39920. Ref.1
Sequence conflict1761T → M in AAA39920. Ref.1
Sequence conflict1761T → M in AAA39921. Ref.1

Secondary structure

1 .................................................................................. 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09041 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: BC3FACE559798B53

FASTA41744,853
        10         20         30         40         50         60 
MALSAKLTLD KVDLKGKRVI MRVDFNVPMK NNQITNNQRI KAAIPSIKHC LDNGAKSVVL 

        70         80         90        100        110        120 
MSHLGRPDGI PMPDKYSLEP VADELKSLLN KDVIFLKDCV GPEVEQACAN PDNGSIILLE 

       130        140        150        160        170        180 
NLRFHVEEEG KGKDSSGKKI SADPAKVEAF QASLSKLGDV YVNDAFGTAH RAHSSTVGVN 

       190        200        210        220        230        240 
LPQKASGFLM KKELDYFSKA LEKPERPFLA ILGGAKVKDK IQLIKNMLDK VNFMIIGGGM 

       250        260        270        280        290        300 
AYTFLKELKN MQIGASLFDE EGATIVKEIM EKAEKNGVKI VFPVDFVTGD KFDENAKVGQ 

       310        320        330        340        350        360 
ATIESGIPSG WMGLDCGPES IKINAQIVAQ AKLIVWNGPI GVFEWDAFAK GTKALMDEVV 

       370        380        390        400        410 
KATSNGCVTI IGGGDTATCC AKWGTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM

« Hide

References

« Hide 'large scale' references
[1]"The testis-specific phosphoglycerate kinase gene pgk-2 is a recruited retroposon."
Boer P.H., Adra C.N., Lau Y.-F.C., McBurney M.W.
Mol. Cell. Biol. 7:3107-3112(1987) [PubMed: 2823118] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"Selective activation of testis-specific genes in cultured rat spermatogenic cells."
Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.
Biochim. Biophys. Acta 1049:331-338(1990) [PubMed: 2166582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M17299 Genomic DNA. Translation: AAA39920.1.
M18654 mRNA. Translation: AAA39921.1.
AK133436 mRNA. Translation: BAE21656.1.
CH466559 Genomic DNA. Translation: EDL23381.1.
BC052343 mRNA. Translation: AAH52343.1.
BC061054 mRNA. Translation: AAH61054.1.
X55310 Genomic DNA. Translation: CAA39014.1.
IPIIPI00555060.
PIRA27775.
RefSeqNP_112467.2. NM_031190.2.
UniGeneMm.717.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P9QX-ray2.70A/B2-417[»]
2P9TX-ray2.00A2-417[»]
2PAAX-ray2.70A/B2-417[»]
ProteinModelPortalP09041.
SMRP09041. Positions 5-417.
ModBaseSearch...

Protein-protein interaction databases

IntActP09041. 1 interaction.
STRINGP09041.

PTM databases

PhosphoSiteP09041.

2D gel databases

REPRODUCTION-2DPAGEIPI00555060.
P09041.

Proteomic databases

PRIDEP09041.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033585; ENSMUSP00000033585; ENSMUSG00000031233.
GeneID18663.
KEGGmmu:18663.

Organism-specific databases

CTD5232.
MGIMGI:97563. Pgk2.

Phylogenomic databases

eggNOGroNOG09572.
HOGENOMHBG453500.
HOVERGENHBG008177.
InParanoidP09041.
OrthoDBEOG4GB780.
PhylomeDBP09041.

Gene expression databases

ArrayExpressP09041.
BgeeP09041.
CleanExMM_PGK2.
GenevestigatorP09041.
GermOnlineENSMUSG00000031233. Mus musculus.

Family and domain databases

InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.1270. Phosphoglycerate_kinase_C. 1 hit.
G3DSA:3.40.50.1260. Phosphoglycerate_kinase_N. 1 hit.
KOK00927.
PANTHERPTHR11406. PGK. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. PGK. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294668.
SOURCESearch...

Entry information

Entry namePGK2_MOUSE
AccessionPrimary (citable) accession number: P09041
Secondary accession number(s): Q5RKV3, Q6P8V2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: November 16, 2011
This is version 97 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents