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Protein

Phosphoglycerate kinase 2

Gene

PGK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391SubstrateBy similarity
Binding sitei123 – 1231SubstrateBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei220 – 2201ATPBy similarity
Binding sitei313 – 3131ATP; via carbonyl oxygenBy similarity
Binding sitei344 – 3441ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi373 – 3764ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. phosphoglycerate kinase activity Source: UniProtKB

GO - Biological processi

  1. glycolytic process Source: UniProtKB
  2. phosphorylation Source: UniProtKB
  3. sperm motility Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10215-MONOMER.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase 2 (EC:2.7.2.3)
Alternative name(s):
Phosphoglycerate kinase, testis specific
Gene namesi
Name:PGK2
Synonyms:PGKB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:8898. PGK2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. sperm fibrous sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417Phosphoglycerate kinase 2PRO_0000145832Add
BLAST

Proteomic databases

MaxQBiP07205.
PaxDbiP07205.
PeptideAtlasiP07205.
PRIDEiP07205.

2D gel databases

UCD-2DPAGEP07205.

PTM databases

PhosphoSiteiP07205.

Expressioni

Tissue specificityi

Testis specific.

Gene expression databases

BgeeiP07205.
CleanExiHS_PGK2.
GenevestigatoriP07205.

Organism-specific databases

HPAiHPA045385.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi111253. 2 interactions.
STRINGi9606.ENSP00000305995.

Structurei

3D structure databases

ProteinModelPortaliP07205.
SMRiP07205. Positions 6-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 263Substrate bindingBy similarity
Regioni63 – 664Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0126.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP07205.
KOiK00927.
OMAiESNKNHA.
OrthoDBiEOG74R1QN.
PhylomeDBiP07205.
TreeFamiTF300489.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07205-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC
60 70 80 90 100
LDNGAKAVVL MSHLGRPDGV PMPDKYSLAP VAVELKSLLG KDVLFLKDCV
110 120 130 140 150
GAEVEKACAN PAPGSVILLE NLRFHVEEEG KGQDPSGKKI KAEPDKIEAF
160 170 180 190 200
RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPHKASGFLM KKELDYFAKA
210 220 230 240 250
LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM AYTFLKVLNN
260 270 280 290 300
MEIGASLFDE EGAKIVKDIM AKAQKNGVRI TFPVDFVTGD KFDENAQVGK
310 320 330 340 350
ATVASGISPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK
360 370 380 390 400
GTKALMDEIV KATSKGCITV IGGGDTATCC AKWNTEDKVS HVSTGGGASL
410
ELLEGKILPG VEALSNM
Length:417
Mass (Da):44,796
Last modified:January 23, 2007 - v3
Checksum:i0CD5C71C2D3A9272
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961G → R in CAA28872. (PubMed:3453121)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05246 Genomic DNA. Translation: CAA28872.1.
AK312770 mRNA. Translation: BAG35635.1.
AL121974 Genomic DNA. Translation: CAC19655.1.
BC038843 mRNA. Translation: AAH38843.1.
CCDSiCCDS4930.1.
PIRiA24030.
A27816.
RefSeqiNP_620061.2. NM_138733.4.
UniGeneiHs.367727.

Genome annotation databases

EnsembliENST00000304801; ENSP00000305995; ENSG00000170950.
GeneIDi5232.
KEGGihsa:5232.
UCSCiuc003ozu.3. human.

Polymorphism databases

DMDMi21264485.

Cross-referencesi

Web resourcesi

Wikipedia

Phosphoglycerate kinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05246 Genomic DNA. Translation: CAA28872.1.
AK312770 mRNA. Translation: BAG35635.1.
AL121974 Genomic DNA. Translation: CAC19655.1.
BC038843 mRNA. Translation: AAH38843.1.
CCDSiCCDS4930.1.
PIRiA24030.
A27816.
RefSeqiNP_620061.2. NM_138733.4.
UniGeneiHs.367727.

3D structure databases

ProteinModelPortaliP07205.
SMRiP07205. Positions 6-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111253. 2 interactions.
STRINGi9606.ENSP00000305995.

Chemistry

ChEMBLiCHEMBL2096677.

PTM databases

PhosphoSiteiP07205.

Polymorphism databases

DMDMi21264485.

2D gel databases

UCD-2DPAGEP07205.

Proteomic databases

MaxQBiP07205.
PaxDbiP07205.
PeptideAtlasiP07205.
PRIDEiP07205.

Protocols and materials databases

DNASUi5232.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304801; ENSP00000305995; ENSG00000170950.
GeneIDi5232.
KEGGihsa:5232.
UCSCiuc003ozu.3. human.

Organism-specific databases

CTDi5232.
GeneCardsiGC06M049753.
HGNCiHGNC:8898. PGK2.
HPAiHPA045385.
MIMi172270. gene.
neXtProtiNX_P07205.
PharmGKBiPA33237.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0126.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP07205.
KOiK00927.
OMAiESNKNHA.
OrthoDBiEOG74R1QN.
PhylomeDBiP07205.
TreeFamiTF300489.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
BioCyciMetaCyc:HS10215-MONOMER.

Miscellaneous databases

GenomeRNAii5232.
NextBioi20224.
PROiP07205.
SOURCEiSearch...

Gene expression databases

BgeeiP07205.
CleanExiHS_PGK2.
GenevestigatoriP07205.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPGK2_HUMAN
AccessioniPrimary (citable) accession number: P07205
Secondary accession number(s): B2R6Y8, Q9H107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.