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Q13164 (MK07_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 7

Short name=MAP kinase 7
Short name=MAPK 7
EC=2.7.11.24
Alternative name(s):
Big MAP kinase 1
Short name=BMK-1
Extracellular signal-regulated kinase 5
Short name=ERK-5
Gene names
Name:MAPK7
Synonyms:BMK1, ERK5, PRKM7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length816 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction. Ref.8 Ref.9 Ref.10 Ref.11 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation By similarity. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF). Ref.8 Ref.9

Subunit structure

Interacts with MAP2K5. Forms oligomers By similarity. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D By similarity. Interacts with SGK1. Preferentially interacts with PML isoform PML-4but shows interaction also with its other isoforms: isoform PML-1 isoform PML-2 isoform PML-3and isoform PML-6 Ref.2 Ref.10 Ref.14

Subcellular location

Cytoplasm. Nucleus. NucleusPML body. Note: Translocates to the nucleus upon activation. Ref.8 Ref.14

Tissue specificity

Expressed in many adult tissues. Abundant in heart, placenta, lung, kidney and skeletal muscle. Not detectable in liver. Ref.2

Domain

The second proline-rich region may interact with actin targeting the kinase to a specific location in the cell.

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

Post-translational modification

Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme By similarity. Autophosphorylated in vitro on threonine and tyrosine residues when the C-terminal part of the kinase, which could have a regulatory role, is absent. Ref.14

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence AAA81381.1 differs from that shown. Reason: Frameshift at positions 19 and 32.

The sequence BAD92848.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Differentiation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cAMP-mediated signaling

Non-traceable author statement PubMed 16177794. Source: BHF-UCL

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to growth factor stimulus

Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL

cellular response to hydrogen peroxide

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

cellular response to laminar fluid shear stress

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

cellular response to transforming growth factor beta stimulus

Inferred from direct assay PubMed 18588859. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

negative regulation of NFAT protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of cAMP catabolic process

Non-traceable author statement PubMed 16177794. Source: BHF-UCL

negative regulation of cyclic-nucleotide phosphodiesterase activity

Non-traceable author statement PubMed 16177794. Source: BHF-UCL

negative regulation of endothelial cell apoptotic process

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL

negative regulation of heterotypic cell-cell adhesion

Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL

negative regulation of inflammatory response

Traceable author statement PubMed 20551324. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

negative regulation of response to cytokine stimulus

Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein metabolic process

Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 20551324. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter in response to stress

Inferred from mutant phenotype PubMed 23043106. Source: BHF-UCL

regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentPML body

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 23043106. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 18588859Ref.14. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Traceable author statement Ref.1. Source: ProtInc

mitogen-activated protein kinase binding

Inferred from physical interaction PubMed 23043106. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13164-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q13164-3)

The sequence of this isoform differs from the canonical sequence as follows:
     493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS
Isoform 4 (identifier: Q13164-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: MAEPLKEEDG...TVPYGEFKSV → MLFFHTMPSA...HASLLPSPSS
     493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 816815Mitogen-activated protein kinase 7
PRO_0000186260

Regions

Domain55 – 347293Protein kinase
Nucleotide binding61 – 699ATP By similarity
Region2 – 7776Required for cytoplasmic targeting By similarity
Region78 – 13962Required for binding to MAP2K5 By similarity
Region140 – 406267Necessary for oligomerization By similarity
Region407 – 806400May not be required for kinase activity; required to stimulate MEF2C activity By similarity
Region505 – 53935Nuclear localization signal By similarity
Motif219 – 2213TXY
Compositional bias338 – 3414Poly-Ala
Compositional bias403 – 694292Pro-rich
Compositional bias513 – 54331Arg-rich

Sites

Active site1821Proton acceptor By similarity
Binding site841ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue7201Phosphoserine Ref.12
Modified residue7331Phosphothreonine Ref.12

Natural variations

Alternative sequence1 – 139139Missing in isoform 2.
VSP_035198
Alternative sequence1 – 133133MAEPL…EFKSV → MLFFHTMPSAPMGSQGKAVT CLESEGCGEDGACPWSVIRP THASLLPSPSS in isoform 4.
VSP_035199
Alternative sequence493 – 816324DGPSA…DLQDP → GALWAGRVGRGETWTWTRLQ AFTFSPAQLPRKWPQRTPGG S in isoform 3 and isoform 4.
VSP_035200
Natural variant5351R → H. Ref.15
VAR_046225
Natural variant5501G → A. Ref.15
Corresponds to variant rs56388327 [ dbSNP | Ensembl ].
VAR_042257

Experimental info

Mutagenesis219 – 2213TEY → AEF: Loss activation by MAP2K5. Ref.8
Sequence conflict6101V → L in AAA81381. Ref.1

Secondary structure

......................................................................... 816
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 27729FE31658CE3B

FASTA81688,386
        10         20         30         40         50         60 
MAEPLKEEDG EDGSAEPPGP VKAEPAHTAA SVAAKNLALL KARSFDVTFD VGDEYEIIET 

        70         80         90        100        110        120 
IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 

       130        140        150        160        170        180 
LRPTVPYGEF KSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH 

       190        200        210        220        230        240 
RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT 

       250        260        270        280        290        300 
QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 

       310        320        330        340        350        360 
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA 

       370        380        390        400        410        420 
PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPGCPDVEMP 

       430        440        450        460        470        480 
SPWAPSGDCA MESPPPAPPP CPGPAPDTID LTLQPPPPVS EPAPPKKDGA ISDNTKAALK 

       490        500        510        520        530        540 
AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER 

       550        560        570        580        590        600 
KERGAGASGG PSTDPLAGLV LSDNDRSLLE RWTRMARPAA PALTSVPAPA PAPTPTPTPV 

       610        620        630        640        650        660 
QPTSPPPGPV AQPTGPQPQS AGSTSGPVPQ PACPPPGPAP HPTGPPGPIP VPAPPQIATS 

       670        680        690        700        710        720 
TSLLAAQSLV PPPGLPGSST PGVLPYFPPG LPPPDAGGAP QSSMSESPDV NLVTQQLSKS 

       730        740        750        760        770        780 
QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDGQADS ASLSASLLAD 

       790        800        810 
WLEGHGMNPA DIESLQREIQ MDSPMLLADL PDLQDP 

« Hide

Isoform 2 [UniParc].

Checksum: EC01D3784EB8AAB0
Show »

FASTA67773,218
Isoform 3 [UniParc].

Checksum: 6E654D7CA1287E32
Show »

FASTA53359,328
Isoform 4 [UniParc].

Checksum: E0FAC412C3DE60F9
Show »

FASTA45150,152

References

« Hide 'large scale' references
[1]"Primary structure of BMK1: a new mammalian map kinase."
Lee J.-D., Ulevitch R.J., Han J.
Biochem. Biophys. Res. Commun. 213:715-724(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Placenta.
[2]"Components of a new human protein kinase signal transduction pathway."
Zhou G., Bao Z.Q., Dixon J.E.
J. Biol. Chem. 270:12665-12669(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAP2K5, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[3]"Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice variant."
McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R.
Gene 345:183-190(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Placenta.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Spleen.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Muscle and Pancreas.
[7]Bienvenut W.V., Fleming J., Leug H.Y.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-35; 75-98; 119-131; 198-205; 296-343; 377-392; 468-485; 489-505; 544-571; 720-735 AND 798-816, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[8]"BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C."
Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D.
EMBO J. 16:7054-7066(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 219-THR--TYR-221.
[9]"Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor."
Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J., Lee J.-D.
Nature 395:713-716(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[10]"BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase."
Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y., Lee J.D.
J. Biol. Chem. 276:8631-8634(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SGK1.
[11]"Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival."
Dong F., Gutkind J.S., Larner A.C.
J. Biol. Chem. 276:10811-10816(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction."
Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III, Lee J.D.
Oncogene 32:3156-3164(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PML.
[15]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-535 AND ALA-550.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29725 mRNA. Translation: AAA82931.1.
U29726 mRNA. Translation: AAA82932.1.
U29727 Genomic DNA. Translation: AAA82933.1.
U25278 mRNA. Translation: AAA81381.1. Frameshift.
AY534741 mRNA. Translation: AAS38577.1.
AB209611 mRNA. Translation: BAD92848.1. Different initiation.
CH471212 Genomic DNA. Translation: EAW50883.1.
CH471212 Genomic DNA. Translation: EAW50886.1.
BC007404 mRNA. Translation: AAH07404.1.
BC007992 mRNA. Translation: AAH07992.1.
BC009963 mRNA. Translation: AAH09963.1.
BC030134 mRNA. Translation: AAH30134.1.
PIRB56708.
RefSeqNP_002740.2. NM_002749.3.
NP_620601.1. NM_139032.2.
NP_620602.2. NM_139033.2.
NP_620603.2. NM_139034.2.
XP_005256776.1. XM_005256719.1.
UniGeneHs.150136.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q8YX-ray2.00B215-223[»]
4B99X-ray2.80A1-397[»]
4IC7X-ray2.60A/D1-431[»]
4IC8X-ray2.80A/B1-431[»]
ProteinModelPortalQ13164.
SMRQ13164. Positions 46-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111584. 55 interactions.
IntActQ13164. 27 interactions.
STRING9606.ENSP00000311005.

Chemistry

BindingDBQ13164.
ChEMBLCHEMBL5332.
GuidetoPHARMACOLOGY2093.

PTM databases

PhosphoSiteQ13164.

Polymorphism databases

DMDM205371766.

Proteomic databases

PaxDbQ13164.
PRIDEQ13164.

Protocols and materials databases

DNASU5598.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299612; ENSP00000299612; ENSG00000166484. [Q13164-2]
ENST00000308406; ENSP00000311005; ENSG00000166484. [Q13164-1]
ENST00000395602; ENSP00000378966; ENSG00000166484. [Q13164-1]
ENST00000395604; ENSP00000378968; ENSG00000166484. [Q13164-1]
GeneID5598.
KEGGhsa:5598.
UCSCuc002gvn.3. human. [Q13164-1]

Organism-specific databases

CTD5598.
GeneCardsGC17P019281.
HGNCHGNC:6880. MAPK7.
HPACAB018561.
HPA031031.
MIM602521. gene.
neXtProtNX_Q13164.
PharmGKBPA30625.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108137.
InParanoidQ13164.
KOK04464.
OMAIIETIGT.
OrthoDBEOG70PBX2.
PhylomeDBQ13164.
TreeFamTF105099.

Enzyme and pathway databases

BRENDA2.7.11.24. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkQ13164.

Gene expression databases

ArrayExpressQ13164.
BgeeQ13164.
CleanExHS_MAPK7.
GenevestigatorQ13164.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMAPK7.
GenomeRNAi5598.
NextBio21728.
PROQ13164.
SOURCESearch...

Entry information

Entry nameMK07_HUMAN
AccessionPrimary (citable) accession number: Q13164
Secondary accession number(s): Q16634 expand/collapse secondary AC list , Q59F50, Q6QLU7, Q7L4P4, Q969G1, Q96G51
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM