ID PGAM4_HUMAN Reviewed; 254 AA.
AC Q8N0Y7; Q5JPN2; Q8NI24; Q8NI25; Q8NI26;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Probable phosphoglycerate mutase 4;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669};
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669};
GN Name=PGAM4; Synonyms=PGAM3;
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], AND VARIANTS CYS-40; GLN-90 AND THR-175.
RX PubMed=11961099; DOI=10.1093/oxfordjournals.molbev.a004124;
RA Betran E., Wang W., Jin L., Long M.;
RT "Evolution of the phosphoglycerate mutase processed gene in human and
RT chimpanzee revealing the origin of a new primate gene.";
RL Mol. Biol. Evol. 19:654-663(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P18669};
CC -!- MISCELLANEOUS: This is the product of a processed gene created by
CC retroposition from mRNA of an expressed gene. This gene seems to be
CC expressed.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; AF465731; AAM27282.1; -; Genomic_DNA.
DR EMBL; AF465732; AAM27283.1; -; Genomic_DNA.
DR EMBL; AF465733; AAM27284.1; -; Genomic_DNA.
DR EMBL; AF465734; AAM27285.1; -; Genomic_DNA.
DR EMBL; AF465735; AAM27286.1; -; Genomic_DNA.
DR EMBL; AF465736; AAM27287.1; -; Genomic_DNA.
DR EMBL; AF465737; AAM27288.1; -; Genomic_DNA.
DR EMBL; AF465738; AAM27289.1; -; Genomic_DNA.
DR EMBL; AF465739; AAM27290.1; -; Genomic_DNA.
DR EMBL; AF465740; AAM27291.1; -; Genomic_DNA.
DR EMBL; AF465741; AAM27292.1; -; Genomic_DNA.
DR EMBL; AF465742; AAM27293.1; -; Genomic_DNA.
DR EMBL; AF465743; AAM27294.1; -; Genomic_DNA.
DR EMBL; AF465744; AAM27295.1; -; Genomic_DNA.
DR EMBL; AF465745; AAM27296.1; -; Genomic_DNA.
DR EMBL; DQ120647; ABB92432.1; -; Genomic_DNA.
DR EMBL; AL772330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS35338.1; -.
DR RefSeq; NP_001025062.1; NM_001029891.2.
DR AlphaFoldDB; Q8N0Y7; -.
DR SMR; Q8N0Y7; -.
DR BioGRID; 137555; 40.
DR IntAct; Q8N0Y7; 3.
DR STRING; 9606.ENSP00000412189; -.
DR DEPOD; PGAM4; -.
DR GlyGen; Q8N0Y7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N0Y7; -.
DR PhosphoSitePlus; Q8N0Y7; -.
DR BioMuta; PGAM4; -.
DR DMDM; 26006838; -.
DR EPD; Q8N0Y7; -.
DR jPOST; Q8N0Y7; -.
DR MassIVE; Q8N0Y7; -.
DR MaxQB; Q8N0Y7; -.
DR PaxDb; 9606-ENSP00000412189; -.
DR PeptideAtlas; Q8N0Y7; -.
DR PRIDE; Q8N0Y7; -.
DR ProteomicsDB; 71490; -.
DR Antibodypedia; 67001; 133 antibodies from 14 providers.
DR DNASU; 441531; -.
DR Ensembl; ENST00000458128.3; ENSP00000412189.1; ENSG00000226784.3.
DR GeneID; 441531; -.
DR KEGG; hsa:441531; -.
DR MANE-Select; ENST00000458128.3; ENSP00000412189.1; NM_001029891.3; NP_001025062.1.
DR UCSC; uc004ecy.2; human.
DR AGR; HGNC:21731; -.
DR CTD; 441531; -.
DR DisGeNET; 441531; -.
DR GeneCards; PGAM4; -.
DR HGNC; HGNC:21731; PGAM4.
DR HPA; ENSG00000226784; Not detected.
DR MIM; 300567; gene.
DR neXtProt; NX_Q8N0Y7; -.
DR OpenTargets; ENSG00000226784; -.
DR PharmGKB; PA142671183; -.
DR VEuPathDB; HostDB:ENSG00000226784; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; Q8N0Y7; -.
DR OMA; PMESDHD; -.
DR OrthoDB; 5480493at2759; -.
DR PhylomeDB; Q8N0Y7; -.
DR TreeFam; TF300007; -.
DR PathwayCommons; Q8N0Y7; -.
DR SignaLink; Q8N0Y7; -.
DR BioGRID-ORCS; 441531; 316 hits in 707 CRISPR screens.
DR GenomeRNAi; 441531; -.
DR Pharos; Q8N0Y7; Tbio.
DR PRO; PR:Q8N0Y7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N0Y7; Protein.
DR Bgee; ENSG00000226784; Expressed in stromal cell of endometrium and 51 other cell types or tissues.
DR Genevisible; Q8N0Y7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IMP:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IMP:UniProtKB.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; NAS:UniProtKB.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF14; PHOSPHOGLYCERATE MUTASE 4-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Probable phosphoglycerate mutase 4"
FT /id="PRO_0000179832"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 251
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 251
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18669"
FT VARIANT 40
FT /note="R -> C (in dbSNP:rs782408548)"
FT /evidence="ECO:0000269|PubMed:11961099"
FT /id="VAR_014355"
FT VARIANT 90
FT /note="R -> Q (in dbSNP:rs5959129)"
FT /evidence="ECO:0000269|PubMed:11961099"
FT /id="VAR_014356"
FT VARIANT 175
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:11961099"
FT /id="VAR_014357"
SQ SEQUENCE 254 AA; 28777 MW; BB589CDEAAC2E706 CRC64;
MAAYKLVLIR HGESTWNLEN RFSCWYDADL SPAGHEEAKR GGQALRDAGY EFDICLTSVQ
KRVIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSYESPKDTI ARALPFWNEE IVPQIKEGKR
VLIAAHGNSL QGIAKHVEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVC
KAIEAVAAQG KAKK
//
