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O15264

- MK13_HUMAN

UniProt

O15264 - MK13_HUMAN

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Protein

Mitogen-activated protein kinase 13

Gene

MAPK13

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. MAPK13 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. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated by phosphorylation on threonine and tyrosine by dual specificity kinases, MAP2K3/MKK3, MAP2K6/MKK6, MAP2K4/MKK4 and MAP2K7/MKK7. Activation by ultraviolet radiation, hyperosmotic shock, anisomycin or by TNF-alpha is mediated by MAP2K3/MKK3. Inhibited by dual specificity phosphatase DUSP1.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: BHF-UCL

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. intracellular signal transduction Source: UniProtKB
  3. MAPK cascade Source: GOC
  4. neurotrophin TRK receptor signaling pathway Source: Reactome
  5. peptidyl-serine phosphorylation Source: BHF-UCL
  6. positive regulation of inflammatory response Source: BHF-UCL
  7. positive regulation of interleukin-6 production Source: BHF-UCL
  8. Ras protein signal transduction Source: Reactome
  9. regulation of transcription, DNA-templated Source: UniProtKB-KW
  10. response to osmotic stress Source: UniProtKB
  11. response to stress Source: UniProtKB
  12. 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, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 2681.
ReactomeiREACT_12065. p38MAPK events.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiO15264.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 13 (EC:2.7.11.24)
Short name:
MAP kinase 13
Short name:
MAPK 13
Alternative name(s):
Mitogen-activated protein kinase p38 delta
Short name:
MAP kinase p38 delta
Stress-activated protein kinase 4
Gene namesi
Name:MAPK13
Synonyms:PRKM13, SAPK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6875. MAPK13.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801T → A: Loss of kinase activity. 1 Publication
Mutagenesisi182 – 1821Y → A: Loss of kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA30620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Mitogen-activated protein kinase 13PRO_0000186286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Phosphoserine1 Publication
Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K71 Publication
Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K71 Publication
Modified residuei350 – 3501Phosphoserine1 Publication

Post-translational modificationi

Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15264.
PaxDbiO15264.
PRIDEiO15264.

PTM databases

PhosphoSiteiO15264.

Expressioni

Tissue specificityi

Expressed in testes, pancreas, small intestine, lung and kidney. Abundant in macrophages, also present in neutrophils, CD4+ T-cells, and endothelial cells.2 Publications

Gene expression databases

BgeeiO15264.
CleanExiHS_MAPK13.
ExpressionAtlasiO15264. baseline and differential.
GenevestigatoriO15264.

Organism-specific databases

HPAiCAB025854.
HPA007667.

Interactioni

Subunit structurei

Interacts with MAPK8IP2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FPR1P214623EBI-2116951,EBI-2869495
PRKD1Q151396EBI-2116951,EBI-1181072

Protein-protein interaction databases

BioGridi111589. 16 interactions.
IntActiO15264. 90 interactions.
MINTiMINT-1183220.
STRINGi9606.ENSP00000211287.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85Combined sources
Beta strandi9 – 146Combined sources
Beta strandi17 – 226Combined sources
Beta strandi25 – 339Combined sources
Beta strandi35 – 4410Combined sources
Turni45 – 473Combined sources
Beta strandi50 – 567Combined sources
Helixi63 – 7816Combined sources
Beta strandi88 – 914Combined sources
Beta strandi95 – 973Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 1174Combined sources
Helixi124 – 14320Combined sources
Helixi153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi164 – 1663Combined sources
Helixi191 – 1944Combined sources
Helixi204 – 21815Combined sources
Beta strandi222 – 2265Combined sources
Helixi228 – 23912Combined sources
Helixi244 – 2474Combined sources
Helixi253 – 2619Combined sources
Helixi270 – 2734Combined sources
Helixi279 – 28810Combined sources
Turni293 – 2953Combined sources
Helixi299 – 3035Combined sources
Helixi306 – 3083Combined sources
Turni309 – 3113Combined sources
Helixi314 – 3163Combined sources
Turni327 – 3304Combined sources
Helixi335 – 34814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3COIX-ray2.09A2-352[»]
4EXUX-ray1.70A1-352[»]
4EYJX-ray2.10A1-352[»]
4EYMX-ray2.35A1-352[»]
ProteinModelPortaliO15264.
SMRiO15264. Positions 2-351.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15264.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 308284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1823TXY

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.
InParanoidiO15264.
KOiK04441.
OMAiEHPYFDN.
OrthoDBiEOG7PCJGV.
PhylomeDBiO15264.
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: O15264-1) [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
MSLIRKKGFY KQDVNKTAWE LPKTYVSPTH VGSGAYGSVC SAIDKRSGEK
60 70 80 90 100
VAIKKLSRPF QSEIFAKRAY RELLLLKHMQ HENVIGLLDV FTPASSLRNF
110 120 130 140 150
YDFYLVMPFM QTDLQKIMGM EFSEEKIQYL VYQMLKGLKY IHSAGVVHRD
160 170 180 190 200
LKPGNLAVNE DCELKILDFG LARHADAEMT GYVVTRWYRA PEVILSWMHY
210 220 230 240 250
NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG VPGTEFVQKL
260 270 280 290 300
NDKAAKSYIQ SLPQTPRKDF TQLFPRASPQ AADLLEKMLE LDVDKRLTAA
310 320 330 340 350
QALTHPFFEP FRDPEEETEA QQPFDDSLEH EKLTVDEWKQ HIYKEIVNFS
360
PIARKDSRRR SGMKL
Length:365
Mass (Da):42,090
Last modified:January 1, 1998 - v1
Checksum:i52E749EDB2973DDF
GO
Isoform 2 (identifier: O15264-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     204-256: VDIWSVGCIM...VQKLNDKAAK → GQILHPVPAT...DGRAGPHPSL
     257-364: Missing.

Note: No experimental confirmation available.

Show »
Length:257
Mass (Da):28,779
Checksum:iBDCA13CF80344118
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142DV → EL in AAC51374. (PubMed:9207191)Curated
Sequence conflicti39 – 391V → W in AAC51374. (PubMed:9207191)Curated
Sequence conflicti56 – 561L → P in AAC51758. (PubMed:9295308)Curated
Sequence conflicti166 – 1661I → V in AAC51758. (PubMed:9295308)Curated
Sequence conflicti224 – 2241K → R in AAC51758. (PubMed:9295308)Curated
Sequence conflicti224 – 2241K → R in AAD23377. (PubMed:10066767)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411S → L.1 Publication
Corresponds to variant rs55776345 [ dbSNP | Ensembl ].
VAR_042267
Natural varianti282 – 2821A → V.1 Publication
Corresponds to variant rs55990045 [ dbSNP | Ensembl ].
VAR_042268
Natural varianti300 – 3001A → T.1 Publication
Corresponds to variant rs41270090 [ dbSNP | Ensembl ].
VAR_042269

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei204 – 25653VDIWS…DKAAK → GQILHPVPATDPQEGFHSAV PTGQPPGCGPAGEDAGARRG QAPDGRAGPHPSL in isoform 2. 1 PublicationVSP_056558Add
BLAST
Alternative sequencei257 – 364108Missing in isoform 2. 1 PublicationVSP_056559Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10488 mRNA. Translation: CAA71512.1.
U93232 mRNA. Translation: AAB87639.1.
AF015256 mRNA. Translation: AAC51758.1.
AF004709 mRNA. Translation: AAC51374.1.
AF092535 mRNA. Translation: AAD23377.1.
AF100546 mRNA. Translation: AAF36772.1.
BT007221 mRNA. Translation: AAP35885.1.
CR536490 mRNA. Translation: CAG38729.1.
Z95152 Genomic DNA. Translation: CAB08438.1.
CH471081 Genomic DNA. Translation: EAX03874.1.
CH471081 Genomic DNA. Translation: EAX03875.1.
BC000433 mRNA. Translation: AAH00433.1.
BC001641 mRNA. Translation: AAH01641.1.
BC004428 mRNA. Translation: AAH04428.1.
BC085196 mRNA. Translation: AAH85196.1.
CCDSiCCDS4818.1. [O15264-1]
PIRiJC5528.
RefSeqiNP_002745.1. NM_002754.4. [O15264-1]
UniGeneiHs.178695.

Genome annotation databases

EnsembliENST00000211287; ENSP00000211287; ENSG00000156711. [O15264-1]
ENST00000373766; ENSP00000362871; ENSG00000156711. [O15264-2]
GeneIDi5603.
KEGGihsa:5603.
UCSCiuc003ols.4. human. [O15264-1]

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
Y10488 mRNA. Translation: CAA71512.1 .
U93232 mRNA. Translation: AAB87639.1 .
AF015256 mRNA. Translation: AAC51758.1 .
AF004709 mRNA. Translation: AAC51374.1 .
AF092535 mRNA. Translation: AAD23377.1 .
AF100546 mRNA. Translation: AAF36772.1 .
BT007221 mRNA. Translation: AAP35885.1 .
CR536490 mRNA. Translation: CAG38729.1 .
Z95152 Genomic DNA. Translation: CAB08438.1 .
CH471081 Genomic DNA. Translation: EAX03874.1 .
CH471081 Genomic DNA. Translation: EAX03875.1 .
BC000433 mRNA. Translation: AAH00433.1 .
BC001641 mRNA. Translation: AAH01641.1 .
BC004428 mRNA. Translation: AAH04428.1 .
BC085196 mRNA. Translation: AAH85196.1 .
CCDSi CCDS4818.1. [O15264-1 ]
PIRi JC5528.
RefSeqi NP_002745.1. NM_002754.4. [O15264-1 ]
UniGenei Hs.178695.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3COI X-ray 2.09 A 2-352 [» ]
4EXU X-ray 1.70 A 1-352 [» ]
4EYJ X-ray 2.10 A 1-352 [» ]
4EYM X-ray 2.35 A 1-352 [» ]
ProteinModelPortali O15264.
SMRi O15264. Positions 2-351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111589. 16 interactions.
IntActi O15264. 90 interactions.
MINTi MINT-1183220.
STRINGi 9606.ENSP00000211287.

Chemistry

BindingDBi O15264.
ChEMBLi CHEMBL2939.
GuidetoPHARMACOLOGYi 1502.

PTM databases

PhosphoSitei O15264.

Proteomic databases

MaxQBi O15264.
PaxDbi O15264.
PRIDEi O15264.

Protocols and materials databases

DNASUi 5603.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000211287 ; ENSP00000211287 ; ENSG00000156711 . [O15264-1 ]
ENST00000373766 ; ENSP00000362871 ; ENSG00000156711 . [O15264-2 ]
GeneIDi 5603.
KEGGi hsa:5603.
UCSCi uc003ols.4. human. [O15264-1 ]

Organism-specific databases

CTDi 5603.
GeneCardsi GC06P036095.
HGNCi HGNC:6875. MAPK13.
HPAi CAB025854.
HPA007667.
MIMi 602899. gene.
neXtProti NX_O15264.
PharmGKBi PA30620.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi O15264.
KOi K04441.
OMAi EHPYFDN.
OrthoDBi EOG7PCJGV.
PhylomeDBi O15264.
TreeFami TF105100.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
Reactomei REACT_12065. p38MAPK events.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki O15264.

Miscellaneous databases

EvolutionaryTracei O15264.
GeneWikii MAPK13.
GenomeRNAii 5603.
NextBioi 21772.
PROi O15264.
SOURCEi Search...

Gene expression databases

Bgeei O15264.
CleanExi HS_MAPK13.
ExpressionAtlasi O15264. baseline and differential.
Genevestigatori O15264.

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. "Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases."
    Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.
    EMBO J. 16:3563-3571(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION.
    Tissue: Pituitary.
  2. "Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta."
    Jiang Y., Gram H., Zhao M., New L., Gu J., Feng L., Di Padova F., Ulevitch R.J., Han J.
    J. Biol. Chem. 272:30122-30128(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-180 AND TYR-182, MUTAGENESIS OF THR-180 AND TYR-182, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Liver.
  3. "Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase."
    Wang X.S., Diener K., Manthey C.L., Wang S.-W., Rosenzweig B., Bray J., Delaney J., Cole C., Zukowski M., Yao Z.
    J. Biol. Chem. 272:23668-23674(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles."
    Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R.
    Biochem. Biophys. Res. Commun. 235:533-538(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Murine p38-delta mitogen-activated protein kinase, a developmentally regulated protein kinase that is activated by stress and proinflammatory cytokines."
    Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R., Tan T.-H.
    J. Biol. Chem. 274:7095-7102(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "Structure and polymorphism of two stress-activated protein kinase genes centromeric of the MHC: SAPK2a and SAPK4."
    Herbison C.E., Sayer D.C., Bellgard M., Allcock R.J.N., Christiansen F.T., Price P.
    DNA Seq. 10:229-243(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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: Lung and Pancreas.
  12. Cited for: FUNCTION IN PHOSPHORYLATION OF STMN1.
  13. "Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages."
    Hale K.K., Trollinger D., Rihanek M., Manthey C.L.
    J. Immunol. 162:4246-4252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "Fibroblast growth factor homologous factors are intracellular signaling proteins."
    Schoorlemmer J., Goldfarb M.
    Curr. Biol. 11:793-797(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8IP2.
  15. "A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta."
    Knebel A., Morrice N., Cohen P.
    EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  16. "Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells."
    Buee-Scherrer V., Goedert M.
    FEBS Lett. 515:151-154(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
  17. "Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly."
    Feijoo C., Campbell D.G., Jakes R., Goedert M., Cuenda A.
    J. Cell Sci. 118:397-408(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
  18. "Activation of PKCdelta and p38delta MAPK during okadaic acid dependent keratinocyte apoptosis."
    Kraft C.A., Efimova T., Eckert R.L.
    Arch. Dermatol. Res. 299:71-83(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KERATINOCYTE APOPTOSIS.
  19. "p38MAPK delta controls c-Myb degradation in response to stress."
    Pani E., Ferrari S.
    Blood Cells Mol. Dis. 40:388-394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MYB.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  21. "MKP-1 inhibits high NaCl-induced activation of p38 but does not inhibit the activation of TonEBP/OREBP: opposite roles of p38alpha and p38delta."
    Zhou X., Ferraris J.D., Dmitrieva N.I., Liu Y., Burg M.B.
    Proc. Natl. Acad. Sci. U.S.A. 105:5620-5625(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY DUSP1, FUNCTION.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Human p38 delta MAP kinase mediates UV irradiation induced up-regulation of the gene expression of chemokine BRAK/CXCL14."
    Ozawa S., Ito S., Kato Y., Kubota E., Hata R.
    Biochem. Biophys. Res. Commun. 396:1060-1064(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "p38delta mitogen-activated protein kinase regulates skin homeostasis and tumorigenesis."
    Efimova T.
    Cell Cycle 9:498-505(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  25. "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.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Crystal structure of p38delta kinase."
    New York structural genomix research consortium (NYSGXRC)
    Submitted (JUN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-352.
  28. "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] LEU-41; VAL-282 AND THR-300.

Entry informationi

Entry nameiMK13_HUMAN
AccessioniPrimary (citable) accession number: O15264
Secondary accession number(s): O14739
, O15124, Q5U4A5, Q6FI46, Q9UNU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 157 of the entry and version 1 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 6
    Human chromosome 6: 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