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   07-JUL-2009, entry version 57.
DE   RecName: Full=Probable phosphoglycerate mutase 4;
DE            EC=5.4.2.1;
DE            EC=5.4.2.4;
DE            EC=3.1.3.13;
GN   Name=PGAM4; Synonyms=PGAM3;
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], AND VARIANTS CYS-40; GLN-90 AND
RP   THR-175.
RX   MEDLINE=21959328; PubMed=11961099;
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. 3:1970-1979(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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   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.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   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.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   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.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   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.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92; TYR-119 AND TYR-133,
RP   AND MASS SPECTROMETRY.
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-
CC       bisphospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H(2)O = 3-
CC       phospho-D-glycerate + phosphate.
CC   -!- MISCELLANEOUS: This is the product of a processed gene created by
CC       retroposition from mRNA of an expressed gene. This gene seems to
CC       be expressed.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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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; CAI42111.1; -; Genomic_DNA.
DR   IPI; IPI00374975; -.
DR   RefSeq; NP_001025062.1; -.
DR   RefSeq; XP_001126103.1; -.
DR   UniGene; Hs.632822; -.
DR   HSSP; P31217; 1E58.
DR   SMR; Q8N0Y7; 2-246.
DR   PRIDE; Q8N0Y7; -.
DR   Ensembl; ENSG00000186076; Homo sapiens.
DR   GeneID; 441531; -.
DR   GeneID; 728188; -.
DR   KEGG; hsa:441531; -.
DR   KEGG; hsa:728188; -.
DR   UCSC; uc004ecy.1; human.
DR   GeneCards; GC0XM077110; -.
DR   GeneCards; GC0XM077111; -.
DR   HGNC; HGNC:21731; PGAM4.
DR   PharmGKB; PA142671183; -.
DR   HOGENOM; Q8N0Y7; -.
DR   HOVERGEN; Q8N0Y7; -.
DR   OMA; Q8N0Y7; RVLPYWY.
DR   BRENDA; 3.1.3.13; 247.
DR   BRENDA; 5.4.2.1; 247.
DR   BRENDA; 5.4.2.4; 247.
DR   NextBio; 110285; -.
DR   CleanEx; HS_PGAM4; -.
DR   GermOnline; ENSG00000186076; Homo sapiens.
DR   GO; GO:0004083; F:2,3-bisphospho-D-glycerate 2-phosphohydrola...; IEA:EC.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; NAS:UniProtKB.
DR   GO; GO:0006096; P:glycolysis; NAS:UniProtKB.
DR   InterPro; IPR001345; PG/BPGM_mutase.
DR   InterPro; IPR013078; PG_mutase.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Glycolysis; Hydrolase; Isomerase;
KW   Phosphoprotein; Polymorphism.
FT   CHAIN         1    254       Probable phosphoglycerate mutase 4.
FT                                /FTId=PRO_0000179832.
FT   COMPBIAS    122    131       Pro-rich.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    186    186       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
FT   MOD_RES      92     92       Phosphotyrosine.
FT   MOD_RES     106    106       N6-acetyllysine.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     119    119       Phosphotyrosine.
FT   MOD_RES     133    133       Phosphotyrosine.
FT   VARIANT      40     40       R -> C.
FT                                /FTId=VAR_014355.
FT   VARIANT      90     90       R -> Q.
FT                                /FTId=VAR_014356.
FT   VARIANT     175    175       I -> T.
FT                                /FTId=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
//