P53778 (MK12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence 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 co-localizes 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 process	Cell cycle Stress response Transcription Transcription regulation
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP 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
PKN1	Q16512	2	EBI-602406,EBI-602382

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Mitogen-activated protein kinase 12

PRO_0000186282

Regions

Domain

27 – 311

285

Protein kinase

Nucleotide binding

33 – 41

9

ATP By similarity

Motif

183 – 185

3

TXY

Sites

Active site

153

1

Proton acceptor By similarity

Binding site

56

1

ATP By similarity

Amino acid modifications

Modified residue

183

1

Phosphothreonine; by MAP2K3 and MAP2K6 By similarity

Modified residue

185

1

Phosphotyrosine; by MAP2K3 and MAP2K6

Natural variations

Natural variant

103

1

T → M. Ref.21
Corresponds to variant rs34422484 [ dbSNP | Ensembl ].

VAR_042265

Natural variant

230

1

D → N. Ref.21
Corresponds to variant rs35396905 [ dbSNP | Ensembl ].

VAR_042266

Natural variant

244

1

T → M.
Corresponds to variant rs2066776 [ dbSNP | Ensembl ].

VAR_012002

Experimental info

Mutagenesis

179

1

D → A: Emulation of the active state. Ref.13

Mutagenesis

185

1

Y → F: Loss of activity. Ref.1

Mutagenesis

330

1

F → S: No effect. Ref.13

Sequence conflict

7

1

A → T in CAA55984. Ref.1

Sequence conflict

70

1

R → L in CAA55984. Ref.1

Sequence conflict

138

1

L → M in CAA55984. Ref.1

Sequence conflict

201 – 202

2

MR → IA in CAA55984. Ref.1

Sequence conflict

261

1

Y → N in AAB40118. Ref.3

Sequence conflict

297 – 298

2

EQ → DI in CAA55984. Ref.1

Sequence conflict

300

1

V → L in CAA55984. Ref.1

Sequence conflict

305

1

A → F in CAA55984. Ref.1

Sequence conflict

307

1

A → S in CAA55984. Ref.1

Sequence conflict

332 – 333

2

DV → YF in CAA55984. Ref.1

Secondary structure

1

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367

Helix Strand Turn

Details...

Beta strand

17 – 21

5

Beta strand

24 – 32

9

Beta strand

41 – 46

6

Turn

47 – 49

3

Beta strand

52 – 57

6

Helix

65 – 80

16

Beta strand

90 – 93

4

Turn

99 – 101

3

Beta strand

106 – 110

5

Beta strand

113 – 115

3

Helix

116 – 122

7

Helix

127 – 146

20

Helix

156 – 158

3

Beta strand

159 – 161

3

Beta strand

167 – 169

3

Helix

189 – 191

3

Helix

195 – 198

4

Turn

199 – 201

3

Helix

207 – 221

15

Helix

231 – 242

12

Helix

247 – 251

5

Helix

256 – 264

9

Helix

273 – 275

3

Helix

282 – 291

10

Turn

296 – 298

3

Helix

302 – 307

6

Helix

309 – 311

3

Turn

312 – 314

3

Helix

337 – 349

13

Sequences

	Sequence		Length	Mass (Da)
	P53778 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: EF680401D8E40610	FASTA	367	41,940
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00296283.

PIR

JC5252.
JC6138.

RefSeq

NP_002960.2. NM_002969.3.

UniGene

Hs.432642.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CM8	X-ray	2.40	A/B	1-367	[»]

ProteinModelPortal

P53778.

ModBase

Search...

Protein-protein interaction databases

IntAct

P53778. 2 interactions.

MINT

MINT-90266.

STRING

9606.ENSP00000215659.

PTM databases

PhosphoSite

P53778.

Polymorphism databases

DMDM

2851522.

Proteomic databases

PaxDb

P53778.

PRIDE

P53778.

Protocols and materials databases

DNASU

6300.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215659; ENSP00000215659; ENSG00000188130.

GeneID

6300.

KEGG

hsa:6300.

UCSC

uc003bkm.1. human.

Organism-specific databases

CTD

6300.

GeneCards

GC22M050684.

HGNC

HGNC:6874. MAPK12.

HPA

CAB025483.

MIM

602399. gene.

neXtProt

NX_P53778.

PharmGKB

PA30619.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

P53778.

KO

K04441.

OMA

HEKLGED.

OrthoDB

EOG4R23V4.

PhylomeDB

P53778.

Enzyme and pathway databases

Pathway_Interaction_DB

p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.

SignaLink

P53778.

Gene expression databases

ArrayExpress

P53778.

Bgee

P53778.

CleanEx

HS_MAPK12.

Genevestigator

P53778.

GermOnline

ENSG00000188130. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01773. P38MAPKINASE.

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P53778.

ChEMBL

CHEMBL4674.

EvolutionaryTrace

P53778.

GenomeRNAi

6300.

NextBio

24459.

SOURCE

Search...

Entry information

Entry name

MK12_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.