Reviewed, UniProtKB/Swiss-Prot P07205 (PGK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphoglycerate kinase 2
    EC=2.7.2.3
Alternative name(s):
    Phosphoglycerate kinase, testis specific

Gene names

Name:	PGK2
Synonyms:	PGKB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Testis specific.
Sequence similarities	Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Ref.1 Non-traceable author statement. Source: UniProtKB phosphorylation Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoglycerate kinase 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 417	416	Phosphoglycerate kinase 2		PRO_0000145832
Regions
	Nucleotide binding	373 – 376	4	ATP By similarity
	Region	24 – 26	3	Substrate binding By similarity
	Region	63 – 66	4	Substrate binding By similarity
Sites
	Binding site	39	1	Substrate By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	220	1	ATP By similarity
	Binding site	313	1	ATP; via carbonyl oxygen By similarity
	Binding site	344	1	ATP By similarity
Amino acid modifications
	Modified residue	91	1	N6-acetyllysine Ref.6
	Modified residue	156	1	N6-acetyllysine Ref.6
	Modified residue	196	1	Phosphotyrosine By similarity
	Modified residue	267	1	N6-acetyllysine Ref.6
	Modified residue	390	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	396	1	G → R in CAA28872. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07205-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0CD5C71C2D3A9272	FASTA	417	44,796
	10 20 30 40 50 60 MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGAKAVVL 70 80 90 100 110 120 MSHLGRPDGV PMPDKYSLAP VAVELKSLLG KDVLFLKDCV GAEVEKACAN PAPGSVILLE 130 140 150 160 170 180 NLRFHVEEEG KGQDPSGKKI KAEPDKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN 190 200 210 220 230 240 LPHKASGFLM KKELDYFAKA LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM 250 260 270 280 290 300 AYTFLKVLNN MEIGASLFDE EGAKIVKDIM AKAQKNGVRI TFPVDFVTGD KFDENAQVGK 310 320 330 340 350 360 ATVASGISPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK GTKALMDEIV 370 380 390 400 410 KATSKGCITV IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human testis-specific PGK gene lacks introns and possesses characteristics of a processed gene." McCarrey J.R., Thomas K. Nature 326:501-504(1987) [PubMed: 3453121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-156 AND LYS-267, MASS SPECTROMETRY.

Web resources

Wikipedia

Phosphoglycerate kinase entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	X05246 Genomic DNA. Translation: CAA28872.1. AK312770 mRNA. Translation: BAG35635.1. AL121974 Genomic DNA. Translation: CAC19655.1. BC038843 mRNA. Translation: AAH38843.1.
IPI	IPI00219568.
PIR	A24030. A27816.
RefSeq	NP_620061.2.
UniGene	Hs.367727
3D structure databases
HSSP	HSSP built from PDB template 1FW8 based on UniProtKB P00560.
SMR	P07205. Positions 6-417.
ModBase	Search...
Protein-protein interaction databases
STRING	P07205.
Proteomic databases
PeptideAtlas	P07205.
PRIDE	P07205.
Genome annotation databases
Ensembl	ENST00000304801; ENSP00000305995; ENSG00000170950; Homo sapiens. [Genome view]
GeneID	5232.
KEGG	hsa:5232.
UCSC	uc003ozu.1. human.
Organism-specific databases
CTD	5232.
GeneCards	GC06M049861.
H-InvDB	HIX0025213.
HGNC	HGNC:8898. PGK2.
MIM	172270. gene.
PharmGKB	PA33237.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P07205.
HOVERGEN	P07205.
OMA	EGKGQDP.
Enzyme and pathway databases
BRENDA	2.7.2.3. 247.
Gene expression databases
ArrayExpress	P07205.
Bgee	P07205.
CleanEx	HS_PGK2.
Genevestigator	P07205.
GermOnline	ENSG00000170950. Homo sapiens.
Family and domain databases
InterPro	IPR001576. Phosphoglycerate_kinase. IPR015901. Phosphoglycerate_kinase_C. IPR015911. Phosphoglycerate_kinase_CS. IPR015824. Phosphoglycerate_kinase_N. [Graphical view]
Gene3D	G3DSA:3.40.50.1270. Phosphoglycerate_kinase_C. 1 hit. G3DSA:3.40.50.1260. Phosphoglycerate_kinase_N. 1 hit.
PANTHER	PTHR11406. PGK. 1 hit.
Pfam	PF00162. PGK. 1 hit. [Graphical view]
PRINTS	PR00477. PHGLYCKINASE.
PROSITE	PS00111. PGLYCERATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	20224.
SOURCE	Search...

Entry information

Entry name

PGK2_HUMAN

Accession

Primary (citable) accession number: P07205
Secondary accession number(s): B2R6Y8, Q9H107

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.