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Reviewed, UniProtKB/Swiss-Prot Q16659 (MK06_HUMAN)

Last modified November 3, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase 6
    EC=2.7.11.24
Alternative name(s):
    Extracellular signal-regulated kinase 3
      Short name=ERK-3
    MAP kinase isoform p97
    p97-MAPK
Gene names
Name: MAPK6
Synonyms: ERK3, PRKM6
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Phosphorylates microtubule-associated protein 2 (MAP2). May promote entry in the cell cycle By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation By similarity.

Tissue specificity

Highest expression in the skeletal muscle, followed by the brain. Also found in heart, placenta, lung, liver, pancreas, kidney and skin fibroblasts.

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-626 and Tyr-628, which activates the enzyme By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

protein amino acid phosphorylation

Traceable author statement. Source: ProtInc

signal transduction

Traceable author statement. Source: ProtInc

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Mitogen-activated protein kinase 6
PRO_0000186257

Regions

Domain20 – 316297Protein kinase
Nucleotide binding26 – 349ATP By similarity
Motif626 – 6283TXY

Sites

Active site1521Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1891Phosphoserine Ref.6
Modified residue3861Phosphoserine Ref.6
Modified residue3891Phosphothreonine Ref.6
Modified residue6261Phosphothreonine By similarity
Modified residue6281Phosphotyrosine By similarity
Modified residue6651Phosphoserine Ref.6

Natural variations

Natural variant2901L → V
VAR_042256

Secondary structure

................................................ 721
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16659-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DAA3AAA9B98BB31F

FASTA72182,681
        10         20         30         40         50         60 
MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK IVLTDPQSVK 

        70         80         90        100        110        120 
HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE LNSVYIVQEY METDLANVLE 

       130        140        150        160        170        180 
QGPLLEEHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP 

       190        200        210        220        230        240 
HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ 

       250        260        270        280        290        300 
MQLILESIPV VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS 

       310        320        330        340        350        360 
PMDRLTAEEA LSHPYMSIYS FPMDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC 

       370        380        390        400        410        420 
QFSEHDWPVH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTNYS 

       430        440        450        460        470        480 
TEPCWQYSDH HENKYCDLEC SHTCNYKTRS SSYLDNLVWR ESEVNHYYEP KLIIDLSNWK 

       490        500        510        520        530        540 
EQSKEKSDKK GKSKCERNGL VKAQIALEEA SQQLAGKERE KNQGFDFDSF IAGTIQLSSQ 

       550        560        570        580        590        600 
HEPTDVVDKL NDLNSSVSQL ELKSLISKSV SQEKQEKGMA NLAQLEALYQ SSWDSQFVSG 

       610        620        630        640        650        660 
GEDCFFINQF CEVRKDEQVE KENTYTSYLD KFFSRKEDTE MLETEPVEDG KLGERGHEEG 

       670        680        690        700        710        720 
FLNNSGEFLF NKQLESIGIP QFHSPVGSPL KSIQATLTPS AMKSSPQIPH QTYSSILKHL 


N 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of p97MAPK, a novel human homolog of rat ERK-3."
Zhu A.X., Zhao Y., Moller D.E., Flier J.S.
Mol. Cell. Biol. 14:8202-8211(1994) [PubMed: 7969157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal skeletal muscle.
[2]"Primary structure, expression and chromosomal locus of a human homolog of rat ERK3."
Meloche S., Beatty B.G., Pellerin J.
Oncogene 13:1575-1579(1996) [PubMed: 8875998] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Smooth muscle.
[3]"ERK-3 cDNA clone isolated from human oral cancer."
Saranath D., Mahale A., Rai R., Dedhia P.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Oral cancer.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Oesophageal carcinoma.
[5]"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], VARIANT VAL-290.
Tissue: Placenta.
[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-189; SER-386; THR-389 AND SER-665, MASS SPECTROMETRY.
[7]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-290.
+Additional computationally mapped references.

Cross-references

Sequence databases

X80692 mRNA. Translation: CAA56709.1.
L77964 mRNA. Translation: AAA98769.1.
AF420474 mRNA. Translation: AAL17605.1.
CR749401 mRNA. Translation: CAH18246.1.
BC035492 mRNA. Translation: AAH35492.1.
IPIIPI00003431.
PIRA56352.
RefSeqNP_002739.1.
UniGeneHs.411847

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2I6LX-ray2.25A/B9-327[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ16659.

PTM databases

PhosphoSiteQ16659.

Proteomic databases

PRIDEQ16659.

Genome annotation databases

EnsemblENST00000261845; ENSP00000261845; ENSG00000069956; Homo sapiens. [Genome view]
GeneID5597.
KEGGhsa:5597.
NMPDRfig|9606.3.peg.10716.
UCSCuc002abp.1. human.

Organism-specific databases

CTD5597.
GeneCardsGC15P050098.
H-InvDBHIX0026784.
HIX0058579.
HIX0060074.
HGNCHGNC:6879. MAPK6.
HPACAB005184.
MIM602904. gene.
PharmGKBPA30624.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ16659.
HOVERGENQ16659.
OMAPAFDTSY.

Enzyme and pathway databases

BRENDA2.7.11.24. 247.

Gene expression databases

ArrayExpressQ16659.
BgeeQ16659.
CleanExHS_MAPK6.
GenevestigatorQ16659.
GermOnlineENSG00000069956. Homo sapiens.

Family and domain databases

InterProIPR008350. Erk_3_4_MAPK.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01771. ERK3ERK4MAPK.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21724.
SOURCESearch...

Entry information

Entry nameMK06_HUMAN
AccessionPrimary (citable) accession number: Q16659
Secondary accession number(s): Q68DH4, Q8IYN8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 3, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents