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P53778

- MK12_HUMAN

UniProt

P53778 - MK12_HUMAN

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Protein

Mitogen-activated protein kinase 12

Gene

MAPK12

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

Functioni

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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions.1 Publication

Enzyme regulationi

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.2 Publications

Kineticsi

  1. KM=37 µM for ATP1 Publication
  2. KM=313 µM for EGFR substrate peptide1 Publication
  3. KM=254 µM for GST-ATF21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561ATPPROSITE-ProRule annotation
Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 419ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: UniProtKB
  3. MAP kinase activity Source: ProtInc
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle arrest Source: ProtInc
  2. DNA damage induced protein phosphorylation Source: ProtInc
  3. muscle cell differentiation Source: Reactome
  4. muscle organ development Source: ProtInc
  5. myoblast differentiation Source: UniProtKB
  6. neurotrophin TRK receptor signaling pathway Source: Reactome
  7. peptidyl-serine phosphorylation Source: BHF-UCL
  8. positive regulation of muscle cell differentiation Source: Reactome
  9. positive regulation of peptidase activity Source: ParkinsonsUK-UCL
  10. Ras protein signal transduction Source: Reactome
  11. regulation of transcription, DNA-templated Source: UniProtKB-KW
  12. signal transduction Source: ProtInc
  13. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21402. CDO in myogenesis.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiP53778.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 12 (EC:2.7.11.24)
Short name:
MAP kinase 12
Short name:
MAPK 12
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 namesi
Name:MAPK12
Synonyms:ERK6, SAPK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6874. MAPK12.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. mitochondrion Source: UniProtKB-KW
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi179 – 1791D → A: Emulation of the active state. 1 Publication
Mutagenesisi185 – 1851Y → F: Loss of activity. 1 Publication
Mutagenesisi330 – 3301F → S: No effect. 1 Publication

Organism-specific databases

PharmGKBiPA30619.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Mitogen-activated protein kinase 12PRO_0000186282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphothreonine; by MAP2K3 and MAP2K6By similarity
Modified residuei185 – 1851Phosphotyrosine; by MAP2K3 and MAP2K6By similarity

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme.2 Publications
Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP53778.
PaxDbiP53778.
PRIDEiP53778.

PTM databases

PhosphoSiteiP53778.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle and heart.2 Publications

Inductioni

Expression of MAPK12 is down-regulation by MAPK14 activation.1 Publication

Gene expression databases

BgeeiP53778.
CleanExiHS_MAPK12.
ExpressionAtlasiP53778. baseline and differential.
GenevestigatoriP53778.

Organism-specific databases

HPAiCAB025483.
HPA018841.
HPA054562.

Interactioni

Subunit structurei

Monomer. Interacts with the PDZ domain of the syntrophin SNTA1. Interacts with SH3BP5. Interacts with LIN7C, SCRIB and SYNJ2BP (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PKN1Q165122EBI-602406,EBI-602382
PTPN4P290742EBI-602406,EBI-710431

Protein-protein interaction databases

BioGridi112207. 22 interactions.
IntActiP53778. 10 interactions.
MINTiMINT-90266.
STRINGi9606.ENSP00000215659.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 215Combined sources
Beta strandi24 – 329Combined sources
Beta strandi41 – 466Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 576Combined sources
Helixi65 – 8016Combined sources
Beta strandi90 – 934Combined sources
Turni99 – 1013Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi113 – 1153Combined sources
Helixi116 – 1227Combined sources
Helixi127 – 14620Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi167 – 1693Combined sources
Helixi189 – 1913Combined sources
Helixi195 – 1984Combined sources
Turni199 – 2013Combined sources
Helixi207 – 22115Combined sources
Helixi231 – 24212Combined sources
Helixi247 – 2515Combined sources
Helixi256 – 2649Combined sources
Helixi273 – 2753Combined sources
Helixi282 – 29110Combined sources
Turni296 – 2983Combined sources
Helixi302 – 3076Combined sources
Helixi309 – 3113Combined sources
Turni312 – 3143Combined sources
Helixi337 – 34913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM8X-ray2.40A/B1-367[»]
ProteinModelPortaliP53778.
SMRiP53778. Positions 8-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53778.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 311285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP53778.
KOiK04441.
OMAiWEVRERY.
PhylomeDBiP53778.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. 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.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P53778-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSPPPARSG FYRQEVTKTA WEVRAVYRDL QPVGSGAYGA VCSAVDGRTG
60 70 80 90 100
AKVAIKKLYR PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD
110 120 130 140 150
DFTDFYLVMP FMGTDLGKLM KHEKLGEDRI QFLVYQMLKG LRYIHAAGII
160 170 180 190 200
HRDLKPGNLA VNEDCELKIL DFGLARQADS EMTGYVVTRW YRAPEVILNW
210 220 230 240 250
MRYTQTVDIW SVGCIMAEMI TGKTLFKGSD HLDQLKEIMK VTGTPPAEFV
260 270 280 290 300
QRLQSDEAKN YMKGLPELEK KDFASILTNA SPLAVNLLEK MLVLDAEQRV
310 320 330 340 350
TAGEALAHPY FESLHDTEDE PQVQKYDDSF DDVDRTLDEW KRVTYKEVLS
360
FKPPRQLGAR VSKETPL
Length:367
Mass (Da):41,940
Last modified:July 15, 1998 - v3
Checksum:iEF680401D8E40610
GO
Isoform 2 (identifier: P53778-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-151: Missing.

Note: No experimental confirmation available.

Show »
Length:357
Mass (Da):40,808
Checksum:i35F0C4A10EB77B20
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71A → T in CAA55984. (PubMed:8633070)Curated
Sequence conflicti70 – 701R → L in CAA55984. (PubMed:8633070)Curated
Sequence conflicti138 – 1381L → M in CAA55984. (PubMed:8633070)Curated
Sequence conflicti201 – 2022MR → IA in CAA55984. (PubMed:8633070)Curated
Sequence conflicti261 – 2611Y → N in AAB40118. (PubMed:8920915)Curated
Sequence conflicti297 – 2982EQ → DI in CAA55984. (PubMed:8633070)Curated
Sequence conflicti300 – 3001V → L in CAA55984. (PubMed:8633070)Curated
Sequence conflicti305 – 3051A → F in CAA55984. (PubMed:8633070)Curated
Sequence conflicti307 – 3071A → S in CAA55984. (PubMed:8633070)Curated
Sequence conflicti332 – 3332DV → YF in CAA55984. (PubMed:8633070)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031T → M.2 Publications
Corresponds to variant rs34422484 [ dbSNP | Ensembl ].
VAR_042265
Natural varianti230 – 2301D → N.1 Publication
Corresponds to variant rs35396905 [ dbSNP | Ensembl ].
VAR_042266
Natural varianti244 – 2441T → M.
Corresponds to variant rs2066776 [ dbSNP | Ensembl ].
VAR_012002

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 15110Missing in isoform 2. 1 PublicationVSP_055224

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79483 mRNA. Translation: CAA55984.1.
Y10487 mRNA. Translation: CAA71511.1.
U66243 mRNA. Translation: AAB40118.1.
CR456515 mRNA. Translation: CAG30401.1.
AL022328 Genomic DNA. No translation available.
BC015741 mRNA. Translation: AAH15741.1.
CCDSiCCDS14089.1. [P53778-1]
PIRiJC5252.
JC6138.
RefSeqiNP_002960.2. NM_002969.3. [P53778-1]
UniGeneiHs.432642.

Genome annotation databases

EnsembliENST00000215659; ENSP00000215659; ENSG00000188130. [P53778-1]
ENST00000622558; ENSP00000479972; ENSG00000188130. [P53778-2]
GeneIDi6300.
KEGGihsa:6300.
UCSCiuc003bkm.1. human. [P53778-1]

Polymorphism databases

DMDMi2851522.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79483 mRNA. Translation: CAA55984.1 .
Y10487 mRNA. Translation: CAA71511.1 .
U66243 mRNA. Translation: AAB40118.1 .
CR456515 mRNA. Translation: CAG30401.1 .
AL022328 Genomic DNA. No translation available.
BC015741 mRNA. Translation: AAH15741.1 .
CCDSi CCDS14089.1. [P53778-1 ]
PIRi JC5252.
JC6138.
RefSeqi NP_002960.2. NM_002969.3. [P53778-1 ]
UniGenei Hs.432642.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CM8 X-ray 2.40 A/B 1-367 [» ]
ProteinModelPortali P53778.
SMRi P53778. Positions 8-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112207. 22 interactions.
IntActi P53778. 10 interactions.
MINTi MINT-90266.
STRINGi 9606.ENSP00000215659.

Chemistry

BindingDBi P53778.
ChEMBLi CHEMBL2094115.
GuidetoPHARMACOLOGYi 1501.

PTM databases

PhosphoSitei P53778.

Polymorphism databases

DMDMi 2851522.

Proteomic databases

MaxQBi P53778.
PaxDbi P53778.
PRIDEi P53778.

Protocols and materials databases

DNASUi 6300.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215659 ; ENSP00000215659 ; ENSG00000188130 . [P53778-1 ]
ENST00000622558 ; ENSP00000479972 ; ENSG00000188130 . [P53778-2 ]
GeneIDi 6300.
KEGGi hsa:6300.
UCSCi uc003bkm.1. human. [P53778-1 ]

Organism-specific databases

CTDi 6300.
GeneCardsi GC22M050684.
HGNCi HGNC:6874. MAPK12.
HPAi CAB025483.
HPA018841.
HPA054562.
MIMi 602399. gene.
neXtProti NX_P53778.
PharmGKBi PA30619.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P53778.
KOi K04441.
OMAi WEVRERY.
PhylomeDBi P53778.
TreeFami TF105100.

Enzyme and pathway databases

Reactomei REACT_12065. p38MAPK events.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21402. CDO in myogenesis.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki P53778.

Miscellaneous databases

EvolutionaryTracei P53778.
GeneWikii MAPK12.
GenomeRNAii 6300.
NextBioi 24459.
PROi P53778.
SOURCEi Search...

Gene expression databases

Bgeei P53778.
CleanExi HS_MAPK12.
ExpressionAtlasi P53778. baseline and differential.
Genevestigatori P53778.

Family and domain databases

InterProi IPR011009. 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.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT MET-103.
  5. "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].
  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] (ISOFORM 1).
    Tissue: Pancreas.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.

Entry informationi

Entry nameiMK12_HUMAN
AccessioniPrimary (citable) accession number: P53778
Secondary accession number(s): Q14260
, Q6IC53, Q99588, Q99672
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3