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Protein

Pyruvate kinase

Gene

PKM

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. potassium ion binding Source: InterPro
  3. pyruvate kinase activity Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, PyruvateImported

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinaseUniRule annotation (EC:2.7.1.40UniRule annotation)
Gene namesi
Name:PKMImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9021. PKM.

PTM / Processingi

Proteomic databases

PRIDEiB4DNK4.

Expressioni

Gene expression databases

ExpressionAtlasiB4DNK4. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliB4DNK4.
SMRiB4DNK4. Positions 7-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
KOiK00873.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4DNK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT
60 70 80 90 100
IGPASRSVEL KKGATLKITL DNAYMEKCDE NILWLDYKNI CKVVEVGSKI
110 120 130 140 150
YVDDGLISLQ VKQKGADFLV TEVENGGSLG SKKGVNLPGA AVDLPAVSEK
160 170 180 190 200
DIQDLKFGVE QDVDMVFASF IRKASDVHEV RKVLGEKGKN IKIISKIENH
210 220 230 240 250
EGVRRFDEIL EASDGIMVAR GDLGIEIPAE KVFLAQKMMI GRCNRAGKPV
260 270 280 290 300
ICATQMLESM IKKPRPTRAE GSDVANAVLD GADCIMLSGE TAKGDYPLEA
310 320 330 340 350
VRMQHLIARE AEAAIYHLQL FEELRRLAPI TSDPTEATAV GAVEASFKCC
360 370 380 390 400
SGAIIVLTKS GRSAHQVARY RPRAPIIAVT RNPQTARQAH LYRGIFPVLC
410 420 430 440 450
KDPVQEAWAE DVDLRVNFAM NVGKARGFFK KGDVVIVLTG WRPGSGFTNT

MRVVPVP
Length:457
Mass (Da):49,898
Last modified:September 23, 2008 - v1
Checksum:iFC7B2566EEDC7096
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC020779 Genomic DNA. No translation available.
AK297951 mRNA. Translation: BAG60266.1.
RefSeqiNP_001193726.1. NM_001206797.1.
UniGeneiHs.534770.

Genome annotation databases

EnsembliENST00000389093; ENSP00000373745; ENSG00000067225.
GeneIDi5315.
KEGGihsa:5315.
UCSCiuc010ukk.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC020779 Genomic DNA. No translation available.
AK297951 mRNA. Translation: BAG60266.1.
RefSeqiNP_001193726.1. NM_001206797.1.
UniGeneiHs.534770.

3D structure databases

ProteinModelPortaliB4DNK4.
SMRiB4DNK4. Positions 7-457.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB4DNK4.

Protocols and materials databases

DNASUi5315.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389093; ENSP00000373745; ENSG00000067225.
GeneIDi5315.
KEGGihsa:5315.
UCSCiuc010ukk.2. human.

Organism-specific databases

CTDi5315.
HGNCiHGNC:9021. PKM.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
KOiK00873.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Miscellaneous databases

GenomeRNAii5315.
NextBioi20554.

Gene expression databases

ExpressionAtlasiB4DNK4. baseline and differential.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  2. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "NEDO human cDNA sequencing project focused on splicing variants."
    Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.
    , Sugano S., Nomura N., Isogai T.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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].
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Ensembl
    Submitted (NOV-2014) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB4DNK4_HUMAN
AccessioniPrimary (citable) accession number: B4DNK4
Entry historyi
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: April 29, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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, Proteomics identificationCombined sources, Reference proteomeImported

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.