Full text data of PGK2
PGK2
(PGKB)
[Confidence: low (only semi-automatic identification from reviews)]
Phosphoglycerate kinase 2; 2.7.2.3 (Phosphoglycerate kinase, testis specific)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphoglycerate kinase 2; 2.7.2.3 (Phosphoglycerate kinase, testis specific)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P07205
ID PGK2_HUMAN Reviewed; 417 AA.
AC P07205; B2R6Y8; Q9H107;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3;
DE AltName: Full=Phosphoglycerate kinase, testis specific;
GN Name=PGK2; Synonyms=PGKB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3453121; DOI=10.1038/326501a0;
RA McCarrey J.R., Thomas K.;
RT "Human testis-specific PGK gene lacks introns and possesses
RT characteristics of a processed gene.";
RL Nature 326:501-504(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC D-glyceroyl phosphate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="http://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X05246; CAA28872.1; -; Genomic_DNA.
DR EMBL; AK312770; BAG35635.1; -; mRNA.
DR EMBL; AL121974; CAC19655.1; -; Genomic_DNA.
DR EMBL; BC038843; AAH38843.1; -; mRNA.
DR PIR; A24030; A24030.
DR PIR; A27816; A27816.
DR RefSeq; NP_620061.2; NM_138733.4.
DR UniGene; Hs.367727; -.
DR ProteinModelPortal; P07205; -.
DR SMR; P07205; 6-417.
DR STRING; 9606.ENSP00000305995; -.
DR BindingDB; P07205; -.
DR ChEMBL; CHEMBL2096677; -.
DR PhosphoSite; P07205; -.
DR DMDM; 21264485; -.
DR UCD-2DPAGE; P07205; -.
DR PaxDb; P07205; -.
DR PeptideAtlas; P07205; -.
DR PRIDE; P07205; -.
DR DNASU; 5232; -.
DR Ensembl; ENST00000304801; ENSP00000305995; ENSG00000170950.
DR GeneID; 5232; -.
DR KEGG; hsa:5232; -.
DR UCSC; uc003ozu.3; human.
DR CTD; 5232; -.
DR GeneCards; GC06M049753; -.
DR HGNC; HGNC:8898; PGK2.
DR HPA; HPA045385; -.
DR MIM; 172270; gene.
DR neXtProt; NX_P07205; -.
DR PharmGKB; PA33237; -.
DR eggNOG; COG0126; -.
DR HOGENOM; HOG000227107; -.
DR HOVERGEN; HBG008177; -.
DR InParanoid; P07205; -.
DR KO; K00927; -.
DR OMA; ESNKNHA; -.
DR OrthoDB; EOG74R1QN; -.
DR PhylomeDB; P07205; -.
DR BioCyc; MetaCyc:HS10215-MONOMER; -.
DR UniPathway; UPA00109; UER00185.
DR GenomeRNAi; 5232; -.
DR NextBio; 20224; -.
DR PRO; PR:P07205; -.
DR Bgee; P07205; -.
DR CleanEx; HS_PGK2; -.
DR Genevestigator; P07205; -.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolysis; NAS:UniProtKB.
DR Gene3D; 3.40.50.1260; -; 1.
DR Gene3D; 3.40.50.1270; -; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1 417 Phosphoglycerate kinase 2.
FT /FTId=PRO_0000145832.
FT NP_BIND 373 376 ATP (By similarity).
FT REGION 24 26 Substrate binding (By similarity).
FT REGION 63 66 Substrate binding (By similarity).
FT BINDING 39 39 Substrate (By similarity).
FT BINDING 123 123 Substrate (By similarity).
FT BINDING 171 171 Substrate (By similarity).
FT BINDING 220 220 ATP (By similarity).
FT BINDING 313 313 ATP; via carbonyl oxygen (By similarity).
FT BINDING 344 344 ATP (By similarity).
FT CONFLICT 396 396 G -> R (in Ref. 1; CAA28872).
SQ SEQUENCE 417 AA; 44796 MW; 0CD5C71C2D3A9272 CRC64;
MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGAKAVVL
MSHLGRPDGV PMPDKYSLAP VAVELKSLLG KDVLFLKDCV GAEVEKACAN PAPGSVILLE
NLRFHVEEEG KGQDPSGKKI KAEPDKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPHKASGFLM KKELDYFAKA LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM
AYTFLKVLNN MEIGASLFDE EGAKIVKDIM AKAQKNGVRI TFPVDFVTGD KFDENAQVGK
ATVASGISPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK GTKALMDEIV
KATSKGCITV IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM
//
ID PGK2_HUMAN Reviewed; 417 AA.
AC P07205; B2R6Y8; Q9H107;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3;
DE AltName: Full=Phosphoglycerate kinase, testis specific;
GN Name=PGK2; Synonyms=PGKB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3453121; DOI=10.1038/326501a0;
RA McCarrey J.R., Thomas K.;
RT "Human testis-specific PGK gene lacks introns and possesses
RT characteristics of a processed gene.";
RL Nature 326:501-504(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC D-glyceroyl phosphate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="http://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X05246; CAA28872.1; -; Genomic_DNA.
DR EMBL; AK312770; BAG35635.1; -; mRNA.
DR EMBL; AL121974; CAC19655.1; -; Genomic_DNA.
DR EMBL; BC038843; AAH38843.1; -; mRNA.
DR PIR; A24030; A24030.
DR PIR; A27816; A27816.
DR RefSeq; NP_620061.2; NM_138733.4.
DR UniGene; Hs.367727; -.
DR ProteinModelPortal; P07205; -.
DR SMR; P07205; 6-417.
DR STRING; 9606.ENSP00000305995; -.
DR BindingDB; P07205; -.
DR ChEMBL; CHEMBL2096677; -.
DR PhosphoSite; P07205; -.
DR DMDM; 21264485; -.
DR UCD-2DPAGE; P07205; -.
DR PaxDb; P07205; -.
DR PeptideAtlas; P07205; -.
DR PRIDE; P07205; -.
DR DNASU; 5232; -.
DR Ensembl; ENST00000304801; ENSP00000305995; ENSG00000170950.
DR GeneID; 5232; -.
DR KEGG; hsa:5232; -.
DR UCSC; uc003ozu.3; human.
DR CTD; 5232; -.
DR GeneCards; GC06M049753; -.
DR HGNC; HGNC:8898; PGK2.
DR HPA; HPA045385; -.
DR MIM; 172270; gene.
DR neXtProt; NX_P07205; -.
DR PharmGKB; PA33237; -.
DR eggNOG; COG0126; -.
DR HOGENOM; HOG000227107; -.
DR HOVERGEN; HBG008177; -.
DR InParanoid; P07205; -.
DR KO; K00927; -.
DR OMA; ESNKNHA; -.
DR OrthoDB; EOG74R1QN; -.
DR PhylomeDB; P07205; -.
DR BioCyc; MetaCyc:HS10215-MONOMER; -.
DR UniPathway; UPA00109; UER00185.
DR GenomeRNAi; 5232; -.
DR NextBio; 20224; -.
DR PRO; PR:P07205; -.
DR Bgee; P07205; -.
DR CleanEx; HS_PGK2; -.
DR Genevestigator; P07205; -.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolysis; NAS:UniProtKB.
DR Gene3D; 3.40.50.1260; -; 1.
DR Gene3D; 3.40.50.1270; -; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1 417 Phosphoglycerate kinase 2.
FT /FTId=PRO_0000145832.
FT NP_BIND 373 376 ATP (By similarity).
FT REGION 24 26 Substrate binding (By similarity).
FT REGION 63 66 Substrate binding (By similarity).
FT BINDING 39 39 Substrate (By similarity).
FT BINDING 123 123 Substrate (By similarity).
FT BINDING 171 171 Substrate (By similarity).
FT BINDING 220 220 ATP (By similarity).
FT BINDING 313 313 ATP; via carbonyl oxygen (By similarity).
FT BINDING 344 344 ATP (By similarity).
FT CONFLICT 396 396 G -> R (in Ref. 1; CAA28872).
SQ SEQUENCE 417 AA; 44796 MW; 0CD5C71C2D3A9272 CRC64;
MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGAKAVVL
MSHLGRPDGV PMPDKYSLAP VAVELKSLLG KDVLFLKDCV GAEVEKACAN PAPGSVILLE
NLRFHVEEEG KGQDPSGKKI KAEPDKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPHKASGFLM KKELDYFAKA LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM
AYTFLKVLNN MEIGASLFDE EGAKIVKDIM AKAQKNGVRI TFPVDFVTGD KFDENAQVGK
ATVASGISPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK GTKALMDEIV
KATSKGCITV IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM
//
MIM
172270
*RECORD*
*FIELD* NO
172270
*FIELD* TI
*172270 PHOSPHOGLYCERATE KINASE 2; PGK2
;;PHOSPHOGLYCERATE KINASE OF SPERMATOZOA; PGKB;;
read morePGK, TESTICULAR
*FIELD* TX
DESCRIPTION
The PGK2 gene encodes a testis-specific form of phosphoglycerate kinase
(EC 2.7.2.3), which catalyzes the reversible conversion of
1,3-diphosphoglycerate to 3-phosphoglycerate during glycolysis,
generating one molecule of ATP.
See also PGK1 (311800), which is ubiquitously expressed in all somatic
tissues and maps to chromosome Xq13.
CLONING
Chen et al. (1976) identified a form of phosphoglycerate kinase unique
to spermatozoa, PGK2, which was immunologically and electrophoretically
distinct from erythrocyte PGK1.
McCarrey and Thomas (1987) isolated a cDNA clone corresponding to the
human testis-specific PGK gene. The deduced 417-residue protein showed
87% amino acid identity to PGK1.
GENE STRUCTURE
McCarrey and Thomas (1987) found that the PGK2 gene lacks introns and
contains characteristics of a processed gene, or 'retroposon,' including
the remnants of a poly(A) tail and bounding direct repeats. The
structural features were consistent with the notion that this locus
arose by reverse transcriptase-mediated processing of a tailored mRNA
transcript originally produced by the PGK1 gene. McCarrey and Thomas
(1987) concluded that the unusual conservation of function in this
processed PGK2 gene and its tissue-specific expression in
spermatogenesis may be best explained as a compensatory response to the
inactivation of the X-linked PGK1 gene in spermatogenic cells before
meiosis.
McCarrey (1990) studied further the evolution of the functional,
intronless PGK2 gene as well as the intronless PGK1 pseudogene, both of
which are retroposons of the intron-containing PGK1 gene.
MAPPING
Szabo et al. (1984) used a human cDNA probe of PGK1 (Singer-Sam et al.,
1983) to isolate a sequence subclone of the autosomal locus for PGK.
Somatic cell hybridization studies mapped the PGK2 gene to chromosome
6p23-q12. The authors concluded that this gene, located in the same
chromosome segment as HLA, was the human homolog of mouse Pgk2.
Michelson et al. (1985) mapped the human PGK2 gene to 6p21.1-p12,
proximal to the major histocompatibility complex (MHC), by use of a
panel of human-rodent somatic cell hybrids and by chromosomal in situ
hybridization.
In the mouse, testicular PGK is autosomal (VandeBerg et al., 1973).
Eicher et al. (1978) found that testis-specific mouse Pgk was closely
linked to the MHC on chromosome 17. They termed the locus Pgk2. The
kangaroo and the owl monkey show location of PGK2 on the chromosome
homologous to human chromosome 6 (Michelson et al., 1985).
HISTORY
Several early reports indicated that the functional testis-specific PGK2
gene was located on chromosome 19 and that the locus on chromosome 6 was
a pseudogene (Tani et al., 1985; Gartler et al., 1985, 1986; Willard et
al., 1985); it was later determined, however, that the functional PGK2
gene is in fact on chromosome 6p (Szabo et al., 1984). A PGK pseudogene
(PGK1P2, see 311800) maps to chromosome 19.
ANIMAL MODEL
Silver et al. (1983) showed that, in the mouse, allelic variants of the
T complex protein TCP2 (products of the Pgk2 locus) are distributed
nonrandomly among a series of T haplotypes.
*FIELD* RF
1. Chen, S.-H.; Donahue, R. P.; Scott, C. R.: Characterization of
phosphoglycerate kinase for human spermatozoa. Fertil. Steril. 27:
699-701, 1976.
2. Eicher, E. M.; Cherry, M.; Flaherty, L.: Autosomal phosphoglycerate
kinase linked to mouse major histocompatibility complex. Molec. Gen.
Genet. 158: 225-228, 1978.
3. Gartler, S.; Riley, D.; Eddy, R.; Shows, T.: A human autosomal
phosphoglycerate kinase gene has been assigned to chromosome 19. (Abstract) Cytogenet.
Cell Genet. 40: 635-636, 1985.
4. Gartler, S. M.; Riley, D. E.; Lebo, R. V.; Cheung, M.-C.; Eddy,
R. L.; Shows, T. B.: Mapping of human autosomal phosphoglycerate
kinase sequence to chromosome 19. Somat. Cell Molec. Genet. 12:
395-401, 1986.
5. McCarrey, J. R.: Molecular evolution of the human Pgk-2 retroposon. Nucleic
Acids Res. 18: 949-955, 1990.
6. McCarrey, J. R.; Thomas, K.: Human testis-specific PGK lacks introns
and possesses characteristics of a processed gene. Nature 326: 501-505,
1987.
7. Michelson, A. M.; Bruns, G. A. P.; Morton, C. C.; Orkin, S. H.
: The human phosphoglycerate kinase multigene family: HLA-associated
sequences and an X-linked locus containing a processed pseudogene
and its functional counterpart. J. Biol. Chem. 260: 6982-6992, 1985.
8. Silver, L. M.; Uman, J.; Danska, J.; Garrels, J. I.: A diversified
set of testicular cell proteins specified by genes within the mouse
T complex. Cell 35: 35-45, 1983.
9. Singer-Sam, J.; Simmer, R. L.; Keith, D. H.; Shively, L.; Teplitz,
M.; Itakura, K.; Gartler, S. M.; Riggs, A. D.: Isolation of a cDNA
clone for human X-linked 3-phosphoglycerate kinase by use of a mixture
of synthetic oligodeoxyribonucleotides as a detection probe. Proc.
Nat. Acad. Sci. 80: 802-806, 1983.
10. Szabo, P.; Grzeschik, K.-H.; Siniscalco, M.: A human autosomal
phosphoglycerate kinase locus maps near the HLA cluster. Proc. Nat.
Acad. Sci. 81: 3167-3169, 1984.
11. Tani, K.; Singer-Sam, J.; Munns, M.; Yoshida, A.: Molecular cloning
and structure of an autosomal processed gene for human phosphoglycerate
kinase. Gene 35: 11-18, 1985.
12. VandeBerg, J. L.; Cooper, D. W.; Close, P. J.: Mammalian testis
phosphoglycerate kinase. Nature N.B. 243: 48-50, 1973.
13. Willard, H. F.; Goss, S. J.; Holmes, M. T.; Munroe, D. L.: Regional
localization of the phosphoglycerate kinase gene and pseudogene on
the human X chromosome and assignment of a related DNA sequence to
chromosome 19. Hum. Genet. 71: 138-143, 1985.
*FIELD* CN
Cassandra L. Kniffin - reorganized: 07/02/2007
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/02/2007
ckniffin: 7/2/2007
ckniffin: 10/31/2006
carol: 7/2/2002
alopez: 6/2/1997
mark: 4/10/1997
carol: 10/20/1992
supermim: 3/16/1992
supermim: 8/6/1991
carol: 3/26/1991
carol: 6/8/1990
supermim: 3/20/1990
*RECORD*
*FIELD* NO
172270
*FIELD* TI
*172270 PHOSPHOGLYCERATE KINASE 2; PGK2
;;PHOSPHOGLYCERATE KINASE OF SPERMATOZOA; PGKB;;
read morePGK, TESTICULAR
*FIELD* TX
DESCRIPTION
The PGK2 gene encodes a testis-specific form of phosphoglycerate kinase
(EC 2.7.2.3), which catalyzes the reversible conversion of
1,3-diphosphoglycerate to 3-phosphoglycerate during glycolysis,
generating one molecule of ATP.
See also PGK1 (311800), which is ubiquitously expressed in all somatic
tissues and maps to chromosome Xq13.
CLONING
Chen et al. (1976) identified a form of phosphoglycerate kinase unique
to spermatozoa, PGK2, which was immunologically and electrophoretically
distinct from erythrocyte PGK1.
McCarrey and Thomas (1987) isolated a cDNA clone corresponding to the
human testis-specific PGK gene. The deduced 417-residue protein showed
87% amino acid identity to PGK1.
GENE STRUCTURE
McCarrey and Thomas (1987) found that the PGK2 gene lacks introns and
contains characteristics of a processed gene, or 'retroposon,' including
the remnants of a poly(A) tail and bounding direct repeats. The
structural features were consistent with the notion that this locus
arose by reverse transcriptase-mediated processing of a tailored mRNA
transcript originally produced by the PGK1 gene. McCarrey and Thomas
(1987) concluded that the unusual conservation of function in this
processed PGK2 gene and its tissue-specific expression in
spermatogenesis may be best explained as a compensatory response to the
inactivation of the X-linked PGK1 gene in spermatogenic cells before
meiosis.
McCarrey (1990) studied further the evolution of the functional,
intronless PGK2 gene as well as the intronless PGK1 pseudogene, both of
which are retroposons of the intron-containing PGK1 gene.
MAPPING
Szabo et al. (1984) used a human cDNA probe of PGK1 (Singer-Sam et al.,
1983) to isolate a sequence subclone of the autosomal locus for PGK.
Somatic cell hybridization studies mapped the PGK2 gene to chromosome
6p23-q12. The authors concluded that this gene, located in the same
chromosome segment as HLA, was the human homolog of mouse Pgk2.
Michelson et al. (1985) mapped the human PGK2 gene to 6p21.1-p12,
proximal to the major histocompatibility complex (MHC), by use of a
panel of human-rodent somatic cell hybrids and by chromosomal in situ
hybridization.
In the mouse, testicular PGK is autosomal (VandeBerg et al., 1973).
Eicher et al. (1978) found that testis-specific mouse Pgk was closely
linked to the MHC on chromosome 17. They termed the locus Pgk2. The
kangaroo and the owl monkey show location of PGK2 on the chromosome
homologous to human chromosome 6 (Michelson et al., 1985).
HISTORY
Several early reports indicated that the functional testis-specific PGK2
gene was located on chromosome 19 and that the locus on chromosome 6 was
a pseudogene (Tani et al., 1985; Gartler et al., 1985, 1986; Willard et
al., 1985); it was later determined, however, that the functional PGK2
gene is in fact on chromosome 6p (Szabo et al., 1984). A PGK pseudogene
(PGK1P2, see 311800) maps to chromosome 19.
ANIMAL MODEL
Silver et al. (1983) showed that, in the mouse, allelic variants of the
T complex protein TCP2 (products of the Pgk2 locus) are distributed
nonrandomly among a series of T haplotypes.
*FIELD* RF
1. Chen, S.-H.; Donahue, R. P.; Scott, C. R.: Characterization of
phosphoglycerate kinase for human spermatozoa. Fertil. Steril. 27:
699-701, 1976.
2. Eicher, E. M.; Cherry, M.; Flaherty, L.: Autosomal phosphoglycerate
kinase linked to mouse major histocompatibility complex. Molec. Gen.
Genet. 158: 225-228, 1978.
3. Gartler, S.; Riley, D.; Eddy, R.; Shows, T.: A human autosomal
phosphoglycerate kinase gene has been assigned to chromosome 19. (Abstract) Cytogenet.
Cell Genet. 40: 635-636, 1985.
4. Gartler, S. M.; Riley, D. E.; Lebo, R. V.; Cheung, M.-C.; Eddy,
R. L.; Shows, T. B.: Mapping of human autosomal phosphoglycerate
kinase sequence to chromosome 19. Somat. Cell Molec. Genet. 12:
395-401, 1986.
5. McCarrey, J. R.: Molecular evolution of the human Pgk-2 retroposon. Nucleic
Acids Res. 18: 949-955, 1990.
6. McCarrey, J. R.; Thomas, K.: Human testis-specific PGK lacks introns
and possesses characteristics of a processed gene. Nature 326: 501-505,
1987.
7. Michelson, A. M.; Bruns, G. A. P.; Morton, C. C.; Orkin, S. H.
: The human phosphoglycerate kinase multigene family: HLA-associated
sequences and an X-linked locus containing a processed pseudogene
and its functional counterpart. J. Biol. Chem. 260: 6982-6992, 1985.
8. Silver, L. M.; Uman, J.; Danska, J.; Garrels, J. I.: A diversified
set of testicular cell proteins specified by genes within the mouse
T complex. Cell 35: 35-45, 1983.
9. Singer-Sam, J.; Simmer, R. L.; Keith, D. H.; Shively, L.; Teplitz,
M.; Itakura, K.; Gartler, S. M.; Riggs, A. D.: Isolation of a cDNA
clone for human X-linked 3-phosphoglycerate kinase by use of a mixture
of synthetic oligodeoxyribonucleotides as a detection probe. Proc.
Nat. Acad. Sci. 80: 802-806, 1983.
10. Szabo, P.; Grzeschik, K.-H.; Siniscalco, M.: A human autosomal
phosphoglycerate kinase locus maps near the HLA cluster. Proc. Nat.
Acad. Sci. 81: 3167-3169, 1984.
11. Tani, K.; Singer-Sam, J.; Munns, M.; Yoshida, A.: Molecular cloning
and structure of an autosomal processed gene for human phosphoglycerate
kinase. Gene 35: 11-18, 1985.
12. VandeBerg, J. L.; Cooper, D. W.; Close, P. J.: Mammalian testis
phosphoglycerate kinase. Nature N.B. 243: 48-50, 1973.
13. Willard, H. F.; Goss, S. J.; Holmes, M. T.; Munroe, D. L.: Regional
localization of the phosphoglycerate kinase gene and pseudogene on
the human X chromosome and assignment of a related DNA sequence to
chromosome 19. Hum. Genet. 71: 138-143, 1985.
*FIELD* CN
Cassandra L. Kniffin - reorganized: 07/02/2007
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/02/2007
ckniffin: 7/2/2007
ckniffin: 10/31/2006
carol: 7/2/2002
alopez: 6/2/1997
mark: 4/10/1997
carol: 10/20/1992
supermim: 3/16/1992
supermim: 8/6/1991
carol: 3/26/1991
carol: 6/8/1990
supermim: 3/20/1990