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P53778 (MK12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 157. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 12

Short name=MAP kinase 12
Short name=MAPK 12
EC=2.7.11.24
Alternative name(s):
Extracellular signal-regulated kinase 6
Short name=ERK-6
Mitogen-activated protein kinase p38 gamma
Short name=MAP kinase p38 gamma
Stress-activated protein kinase 3
Gene names
Name:MAPK12
Synonyms:ERK6, SAPK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. Ref.1 Ref.6 Ref.9 Ref.12 Ref.14 Ref.15 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Binds 2 magnesium ions. Ref.20

Enzyme regulation

Activated by phosphorylation on threonine and tyrosine. MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK12 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK12 activator in response to TNF-alpha. Ref.6 Ref.7

Subunit structure

Monomer. Interacts with the PDZ domain of the syntrophin SNTA1. Interacts with SH3BP5. Interacts with LIN7C, SCRIB and SYNJ2BP By similarity. Ref.7 Ref.11 Ref.20

Subcellular location

Cytoplasm. Nucleus. Mitochondrion. Note: Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma By similarity. Ref.10 Ref.11 Ref.14

Tissue specificity

Highly expressed in skeletal muscle and heart. Ref.1 Ref.10

Induction

Expression of MAPK12 is down-regulation by MAPK14 activation. Ref.6 Ref.7 Ref.14

Domain

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

Post-translational modification

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme. Ref.8 Ref.14

Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway. Ref.14

Involvement in disease

MAPK is overexpressed in highly metastatic breast cancer cell lines and its expression is preferentially associated with basal-like and metastatic phenotypes of breast tumor samples.

Sequence similarities

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

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=37 µM for ATP Ref.7

KM=313 µM for EGFR substrate peptide

KM=254 µM for GST-ATF2

Ontologies

Keywords
   Biological processCell cycle
Stress response
Transcription
Transcription regulation
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage induced protein phosphorylation

Traceable author statement Ref.9. Source: ProtInc

Ras protein signal transduction

Traceable author statement. Source: Reactome

cell cycle arrest

Traceable author statement Ref.9. Source: ProtInc

muscle organ development

Traceable author statement Ref.1. Source: ProtInc

myoblast differentiation

Inferred from direct assay Ref.1. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 15850461. Source: BHF-UCL

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Traceable author statement Ref.9. Source: ProtInc

magnesium ion binding

Inferred from direct assay Ref.20. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKN1Q165122EBI-602406,EBI-602382

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Mitogen-activated protein kinase 12
PRO_0000186282

Regions

Domain27 – 311285Protein kinase
Nucleotide binding33 – 419ATP By similarity
Motif183 – 1853TXY

Sites

Active site1531Proton acceptor By similarity
Binding site561ATP By similarity

Amino acid modifications

Modified residue1831Phosphothreonine; by MAP2K3 and MAP2K6 By similarity
Modified residue1851Phosphotyrosine; by MAP2K3 and MAP2K6

Natural variations

Natural variant1031T → M. Ref.21
Corresponds to variant rs34422484 [ dbSNP | Ensembl ].
VAR_042265
Natural variant2301D → N. Ref.21
Corresponds to variant rs35396905 [ dbSNP | Ensembl ].
VAR_042266
Natural variant2441T → M.
Corresponds to variant rs2066776 [ dbSNP | Ensembl ].
VAR_012002

Experimental info

Mutagenesis1791D → A: Emulation of the active state. Ref.13
Mutagenesis1851Y → F: Loss of activity. Ref.1
Mutagenesis3301F → S: No effect. Ref.13
Sequence conflict71A → T in CAA55984. Ref.1
Sequence conflict701R → L in CAA55984. Ref.1
Sequence conflict1381L → M in CAA55984. Ref.1
Sequence conflict201 – 2022MR → IA in CAA55984. Ref.1
Sequence conflict2611Y → N in AAB40118. Ref.3
Sequence conflict297 – 2982EQ → DI in CAA55984. Ref.1
Sequence conflict3001V → L in CAA55984. Ref.1
Sequence conflict3051A → F in CAA55984. Ref.1
Sequence conflict3071A → S in CAA55984. Ref.1
Sequence conflict332 – 3332DV → YF in CAA55984. Ref.1

Secondary structure

...................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53778 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: EF680401D8E40610

FASTA36741,940
        10         20         30         40         50         60 
MSSPPPARSG FYRQEVTKTA WEVRAVYRDL QPVGSGAYGA VCSAVDGRTG AKVAIKKLYR 

        70         80         90        100        110        120 
PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD DFTDFYLVMP FMGTDLGKLM 

       130        140        150        160        170        180 
KHEKLGEDRI QFLVYQMLKG LRYIHAAGII HRDLKPGNLA VNEDCELKIL DFGLARQADS 

       190        200        210        220        230        240 
EMTGYVVTRW YRAPEVILNW MRYTQTVDIW SVGCIMAEMI TGKTLFKGSD HLDQLKEIMK 

       250        260        270        280        290        300 
VTGTPPAEFV QRLQSDEAKN YMKGLPELEK KDFASILTNA SPLAVNLLEK MLVLDAEQRV 

       310        320        330        340        350        360 
TAGEALAHPY FESLHDTEDE PQVQKYDDSF DDVDRTLDEW KRVTYKEVLS FKPPRQLGAR 


VSKETPL 

« Hide

References

« Hide 'large scale' references
[1]"ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation."
Lechner C., Zahalka M.A., Giot J.-F., Moeller N.P.H., Ullrich A.
Proc. Natl. Acad. Sci. U.S.A. 93:4355-4359(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-185.
Tissue: Skeletal muscle.
[2]"Assignment of the human stress-activated protein kinase-3 gene (SAPK3) to chromosome 22q13.3 by fluorescence in situ hybridization."
Goedert M., Hasegawa J., Craxton M., Leversha M.A., Clegg S.
Genomics 41:501-502(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[3]"The primary structure of p38 gamma: a new member of p38 group of MAP kinases."
Li Z., Jiang Y., Ulevitch R.J., Han J.
Biochem. Biophys. Res. Commun. 228:334-340(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[6]"Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6."
Enslen H., Raingeaud J., Davis R.J.
J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, ENZYME REGULATION.
[7]"Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition."
Hasegawa M., Cuenda A., Spillantini M.G., Thomas G.M., Buee-Scherrer V., Cohen P., Goedert M.
J. Biol. Chem. 274:12626-12631(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNTA1, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"Differential activation of p38 mitogen-activated protein kinase isoforms depending on signal strength."
Alonso G., Ambrosino C., Jones M., Nebreda A.R.
J. Biol. Chem. 275:40641-40648(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY MAP2K6/MKK6.
[9]"Involvement of the MKK6-p38gamma cascade in gamma-radiation-induced cell cycle arrest."
Wang X., McGowan C.H., Zhao M., He L., Downey J.S., Fearns C., Wang Y., Huang S., Han J.
Mol. Cell. Biol. 20:4543-4552(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF THE G2 CHECKPOINT.
[10]"Cardiac expression and subcellular localization of the p38 mitogen-activated protein kinase member, stress-activated protein kinase-3 (SAPK3)."
Court N.W., dos Remedios C.G., Cordell J., Bogoyevitch M.A.
J. Mol. Cell. Cardiol. 34:413-426(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Heart.
[11]"A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria."
Wiltshire C., Matsushita M., Tsukada S., Gillespie D.A., May G.H.
Biochem. J. 367:577-585(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, SUBCELLULAR LOCATION, INTERACTION WITH SH3BP5.
[12]"p38gamma MAPK regulation of glucose transporter expression and glucose uptake in L6 myotubes and mouse skeletal muscle."
Ho R.C., Alcazar O., Fujii N., Hirshman M.F., Goodyear L.J.
Am. J. Physiol. 286:R342-R349(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Active mutants of the human p38alpha mitogen-activated protein kinase."
Diskin R., Askari N., Capone R., Engelberg D., Livnah O.
J. Biol. Chem. 279:47040-47049(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-179 AND PHE-330.
[14]"p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-proteasome pathways in regulating Ras transformation and stress response."
Qi X., Pohl N.M., Loesch M., Hou S., Li R., Qin J.Z., Cuenda A., Chen G.
J. Biol. Chem. 282:31398-31408(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, UBIQUITINATION.
[15]"p38gamma regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock."
Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A., Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A.
J. Cell Sci. 123:2596-2604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF DLG1.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Loss of p38gamma MAPK induces pleiotropic mitotic defects and massive cell death."
Kukkonen-Macchi A., Sicora O., Kaczynska K., Oetken-Lindholm C., Pouwels J., Laine L., Kallio M.J.
J. Cell Sci. 124:216-227(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"p38gamma mitogen-activated protein kinase contributes to oncogenic properties maintenance and resistance to poly (ADP-ribose)-polymerase-1 inhibition in breast cancer."
Meng F., Zhang H., Liu G., Kreike B., Chen W., Sethi S., Miller F.R., Wu G.
Neoplasia 13:472-482(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[19]"Mechanisms and functions of p38 MAPK signalling."
Cuadrado A., Nebreda A.R.
Biochem. J. 429:403-417(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
[20]"The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation."
Bellon S., Fitzgibbon M.J., Fox T., Hsiao H.M., Wilson K.P.
Structure 7:1057-1065(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), COFACTOR, SUBUNIT.
[21]"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] MET-103 AND ASN-230.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79483 mRNA. Translation: CAA55984.1.
Y10487 mRNA. Translation: CAA71511.1.
U66243 mRNA. Translation: AAB40118.1.
AL022328 Genomic DNA. No translation available.
BC015741 mRNA. Translation: AAH15741.1.
PIRJC5252.
JC6138.
RefSeqNP_002960.2. NM_002969.3.
UniGeneHs.432642.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM8X-ray2.40A/B1-367[»]
ProteinModelPortalP53778.
SMRP53778. Positions 8-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112207. 19 interactions.
IntActP53778. 6 interactions.
MINTMINT-90266.
STRING9606.ENSP00000215659.

Chemistry

BindingDBP53778.
ChEMBLCHEMBL4674.
GuidetoPHARMACOLOGY1501.

PTM databases

PhosphoSiteP53778.

Polymorphism databases

DMDM2851522.

Proteomic databases

PaxDbP53778.
PRIDEP53778.

Protocols and materials databases

DNASU6300.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215659; ENSP00000215659; ENSG00000188130.
GeneID6300.
KEGGhsa:6300.
UCSCuc003bkm.1. human.

Organism-specific databases

CTD6300.
GeneCardsGC22M050684.
HGNCHGNC:6874. MAPK12.
HPACAB025483.
HPA018841.
HPA054562.
MIM602399. gene.
neXtProtNX_P53778.
PharmGKBPA30619.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP53778.
KOK04441.
OMAWEVRERY.
PhylomeDBP53778.
TreeFamTF105100.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.
SignaLinkP53778.

Gene expression databases

ArrayExpressP53778.
BgeeP53778.
CleanExHS_MAPK12.
GenevestigatorP53778.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01773. P38MAPKINASE.
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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53778.
GeneWikiMAPK12.
GenomeRNAi6300.
NextBio24459.
PROP53778.
SOURCESearch...

Entry information

Entry nameMK12_HUMAN
AccessionPrimary (citable) accession number: P53778
Secondary accession number(s): Q14260, Q99588, Q99672
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: February 19, 2014
This is version 157 of the entry and version 3 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 22

Human chromosome 22: entries, gene names and cross-references to MIM