Reviewed, UniProtKB/Swiss-Prot Q8N0Y7 (PGAM4_HUMAN)

Names and origin

Protein names

Recommended name:
    Probable phosphoglycerate mutase 4
    EC=5.4.2.1
    EC=5.4.2.4
    EC=3.1.3.13

Gene names

Name:	PGAM4
Synonyms:	PGAM3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. 2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.
Miscellaneous	This is the product of a processed gene created by retroposition from mRNA of an expressed gene. This gene seems to be expressed.
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Isomerase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	glycolysis Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	2,3-bisphospho-D-glycerate 2-phosphohydrolase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC phosphoglycerate mutase activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 254	254	Probable phosphoglycerate mutase 4		PRO_0000179832
Regions
	Compositional bias	122 – 131	10	Pro-rich
Sites
	Active site	11	1	Tele-phosphohistidine intermediate By similarity
	Active site	186	1	By similarity
	Site	62	1	Interaction with carboxyl group of phosphoglycerates By similarity
Amino acid modifications
	Modified residue	92	1	Phosphotyrosine Ref.5
	Modified residue	106	1	N6-acetyllysine Ref.4
	Modified residue	118	1	Phosphoserine Ref.6
	Modified residue	119	1	Phosphotyrosine Ref.5
	Modified residue	133	1	Phosphotyrosine Ref.5
Natural variations
	Natural variant	40	1	R → C Ref.1		VAR_014355
	Natural variant	90	1	R → Q Ref.1		VAR_014356
	Natural variant	175	1	I → T Ref.1		VAR_014357

Sequences

	Sequence		Length	Mass (Da)
	Q8N0Y7-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: BB589CDEAAC2E706	FASTA	254	28,777
	10 20 30 40 50 60 MAAYKLVLIR HGESTWNLEN RFSCWYDADL SPAGHEEAKR GGQALRDAGY EFDICLTSVQ 70 80 90 100 110 120 KRVIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD 130 140 150 160 170 180 VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSYESPKDTI ARALPFWNEE IVPQIKEGKR 190 200 210 220 230 240 VLIAAHGNSL QGIAKHVEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVC 250 KAIEAVAAQG KAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolution of the phosphoglycerate mutase processed gene in human and chimpanzee revealing the origin of a new primate gene." Betran E., Wang W., Jin L., Long M. Mol. Biol. Evol. 19:654-663(2002) [PubMed: 11961099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-40; GLN-90 AND THR-175.
[2]	"Emergence of young human genes after a burst of retroposition in primates." Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H. PLoS Biol. 3:1970-1979(2005) [PubMed: 16201836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92; TYR-119 AND TYR-133, MASS SPECTROMETRY.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF465731 Genomic DNA. Translation: AAM27282.1. AF465732 Genomic DNA. Translation: AAM27283.1. AF465733 Genomic DNA. Translation: AAM27284.1. AF465734 Genomic DNA. Translation: AAM27285.1. AF465735 Genomic DNA. Translation: AAM27286.1. AF465736 Genomic DNA. Translation: AAM27287.1. AF465737 Genomic DNA. Translation: AAM27288.1. AF465738 Genomic DNA. Translation: AAM27289.1. AF465739 Genomic DNA. Translation: AAM27290.1. AF465740 Genomic DNA. Translation: AAM27291.1. AF465741 Genomic DNA. Translation: AAM27292.1. AF465742 Genomic DNA. Translation: AAM27293.1. AF465743 Genomic DNA. Translation: AAM27294.1. AF465744 Genomic DNA. Translation: AAM27295.1. AF465745 Genomic DNA. Translation: AAM27296.1. DQ120647 Genomic DNA. Translation: ABB92432.1. AL772330 Genomic DNA. Translation: CAI42111.1.
IPI	IPI00374975.
RefSeq	NP_001025062.1. XP_001126103.1.
UniGene	Hs.632822
3D structure databases
HSSP	HSSP built from PDB template 1E58 based on UniProtKB P31217.
SMR	Q8N0Y7. Positions 2-246.
ModBase	Search...
Proteomic databases
PRIDE	Q8N0Y7.
Genome annotation databases
Ensembl	ENSG00000186076. Homo sapiens. [Contig view]
GeneID	441531. 728188.
KEGG	hsa:441531. hsa:728188.
Organism-specific databases
GeneCards	GC0XM077110. GC0XM077111.
HGNC	HGNC:21731. PGAM4.
PharmGKB	PA142671183.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8N0Y7.
HOVERGEN	Q8N0Y7.
OMA	Q8N0Y7. RVLPYWY.
Enzyme and pathway databases
BRENDA	3.1.3.13. 247. 5.4.2.1. 247. 5.4.2.4. 247.
Gene expression databases
CleanEx	HS_PGAM4.
GermOnline	ENSG00000186076. Homo sapiens.
Family and domain databases
InterPro	IPR001345. PG/BPGM_mutase. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. Phosphogly_mut1. 1 hit.
Pfam	PF00300. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01258. pgm_1. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	110285.

Entry information

Entry name

PGAM4_HUMAN

Accession

Primary (citable) accession number: Q8N0Y7
Secondary accession number(s): Q5JPN2 , Q8NI24, Q8NI25, Q8NI26

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)