PGK2_HUMAN
ID PGK2_HUMAN Reviewed; 417 AA.
AC P07205; B2R6Y8; Q9H107;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 characteristics
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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 project:
RT 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26677959; DOI=10.1093/humrep/dev301;
RA Liu X.X., Zhang H., Shen X.F., Liu F.J., Liu J., Wang W.J.;
RT "Characteristics of testis-specific phosphoglycerate kinase 2 and its
RT association with human sperm quality.";
RL Hum. Reprod. 31:273-279(2016).
CC -!- FUNCTION: Essential for sperm motility and male fertility
CC (PubMed:26677959). Not required for the completion of spermatogenesis
CC (By similarity). {ECO:0000250|UniProtKB:P09041,
CC ECO:0000269|PubMed:26677959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly found in round spermatids. Localized on the
CC principle piece in the sperm (at protein level). Testis-specific.
CC Expression significantly decreased in the testis of elderly men.
CC {ECO:0000269|PubMed:26677959}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglycerate kinase entry;
CC URL="https://en.wikipedia.org/wiki/Phosphoglycerate_kinase";
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DR EMBL; X05246; CAA28872.1; -; Genomic_DNA.
DR EMBL; AK312770; BAG35635.1; -; mRNA.
DR EMBL; AL121974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038843; AAH38843.1; -; mRNA.
DR CCDS; CCDS4930.1; -.
DR PIR; A24030; A24030.
DR PIR; A27816; A27816.
DR RefSeq; NP_620061.2; NM_138733.4.
DR AlphaFoldDB; P07205; -.
DR SMR; P07205; -.
DR BioGRID; 111253; 55.
DR IntAct; P07205; 22.
DR STRING; 9606.ENSP00000305995; -.
DR BindingDB; P07205; -.
DR ChEMBL; CHEMBL2096677; -.
DR DrugBank; DB00787; Acyclovir.
DR GlyGen; P07205; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07205; -.
DR PhosphoSitePlus; P07205; -.
DR SwissPalm; P07205; -.
DR BioMuta; PGK2; -.
DR DMDM; 21264485; -.
DR UCD-2DPAGE; P07205; -.
DR EPD; P07205; -.
DR jPOST; P07205; -.
DR MassIVE; P07205; -.
DR MaxQB; P07205; -.
DR PaxDb; P07205; -.
DR PeptideAtlas; P07205; -.
DR PRIDE; P07205; -.
DR ProteomicsDB; 51974; -.
DR Antibodypedia; 30847; 250 antibodies from 28 providers.
DR DNASU; 5232; -.
DR Ensembl; ENST00000304801.6; ENSP00000305995.3; ENSG00000170950.6.
DR GeneID; 5232; -.
DR KEGG; hsa:5232; -.
DR MANE-Select; ENST00000304801.6; ENSP00000305995.3; NM_138733.5; NP_620061.2.
DR UCSC; uc003ozu.4; human.
DR CTD; 5232; -.
DR DisGeNET; 5232; -.
DR GeneCards; PGK2; -.
DR HGNC; HGNC:8898; PGK2.
DR HPA; ENSG00000170950; Tissue enriched (testis).
DR MIM; 172270; gene.
DR neXtProt; NX_P07205; -.
DR OpenTargets; ENSG00000170950; -.
DR PharmGKB; PA33237; -.
DR VEuPathDB; HostDB:ENSG00000170950; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; P07205; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 838642at2759; -.
DR PhylomeDB; P07205; -.
DR TreeFam; TF300489; -.
DR BioCyc; MetaCyc:HS10215-MON; -.
DR BRENDA; 2.7.2.3; 2681.
DR PathwayCommons; P07205; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SignaLink; P07205; -.
DR SIGNOR; P07205; -.
DR UniPathway; UPA00109; UER00185.
DR BioGRID-ORCS; 5232; 22 hits in 1069 CRISPR screens.
DR GenomeRNAi; 5232; -.
DR Pharos; P07205; Tbio.
DR PRO; PR:P07205; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P07205; protein.
DR Bgee; ENSG00000170950; Expressed in sperm and 58 other tissues.
DR ExpressionAtlas; P07205; baseline and differential.
DR Genevisible; P07205; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0035686; C:sperm fibrous sheath; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
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 Acetylation; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT CHAIN 2..417
FT /note="Phosphoglycerate kinase 2"
FT /id="PRO_0000145832"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT CONFLICT 396
FT /note="G -> R (in Ref. 1; CAA28872)"
FT /evidence="ECO:0000305"
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
