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Q13164

- MK07_HUMAN

UniProt

Q13164 - MK07_HUMAN

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Protein

Mitogen-activated protein kinase 7

Gene

MAPK7

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

Functioni

Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation (By similarity). Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841ATPPROSITE-ProRule annotation
Active sitei182 – 1821Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 699ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: ProtInc
  3. mitogen-activated protein kinase binding Source: BHF-UCL

GO - Biological processi

  1. cAMP-mediated signaling Source: BHF-UCL
  2. cell cycle Source: UniProtKB-KW
  3. cell differentiation Source: UniProtKB-KW
  4. cellular response to growth factor stimulus Source: BHF-UCL
  5. cellular response to hydrogen peroxide Source: BHF-UCL
  6. cellular response to laminar fluid shear stress Source: BHF-UCL
  7. cellular response to transforming growth factor beta stimulus Source: UniProtKB
  8. innate immune response Source: Reactome
  9. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  11. negative regulation of cAMP catabolic process Source: BHF-UCL
  12. negative regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
  13. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  14. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  15. negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  16. negative regulation of inflammatory response Source: BHF-UCL
  17. negative regulation of NFAT protein import into nucleus Source: Ensembl
  18. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  19. negative regulation of response to cytokine stimulus Source: BHF-UCL
  20. neurotrophin TRK receptor signaling pathway Source: Reactome
  21. peptidyl-serine phosphorylation Source: Ensembl
  22. positive regulation of protein metabolic process Source: BHF-UCL
  23. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  24. positive regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL
  25. regulation of angiogenesis Source: Ensembl
  26. signal transduction Source: ProtInc
  27. stress-activated MAPK cascade Source: Reactome
  28. toll-like receptor 10 signaling pathway Source: Reactome
  29. toll-like receptor 2 signaling pathway Source: Reactome
  30. toll-like receptor 3 signaling pathway Source: Reactome
  31. toll-like receptor 4 signaling pathway Source: Reactome
  32. toll-like receptor 5 signaling pathway Source: Reactome
  33. toll-like receptor 9 signaling pathway Source: Reactome
  34. toll-like receptor signaling pathway Source: Reactome
  35. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  36. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  37. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 2681.
ReactomeiREACT_12020. Signalling to ERK5.
REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
SignaLinkiQ13164.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 7 (EC:2.7.11.24)
Short name:
MAP kinase 7
Short name:
MAPK 7
Alternative name(s):
Big MAP kinase 1
Short name:
BMK-1
Extracellular signal-regulated kinase 5
Short name:
ERK-5
Gene namesi
Name:MAPK7
Synonyms:BMK1, ERK5, PRKM7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6880. MAPK7.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: BHF-UCL
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2213TEY → AEF: Loss activation by MAP2K5. 1 Publication

Organism-specific databases

PharmGKBiPA30625.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 816815Mitogen-activated protein kinase 7PRO_0000186260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei720 – 7201Phosphoserine1 Publication
Modified residuei733 – 7331Phosphothreonine1 Publication

Post-translational modificationi

Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme (By similarity). Autophosphorylated in vitro on threonine and tyrosine residues when the C-terminal part of the kinase, which could have a regulatory role, is absent.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13164.
PaxDbiQ13164.
PRIDEiQ13164.

PTM databases

PhosphoSiteiQ13164.

Expressioni

Tissue specificityi

Expressed in many adult tissues. Abundant in heart, placenta, lung, kidney and skeletal muscle. Not detectable in liver.1 Publication

Gene expression databases

BgeeiQ13164.
CleanExiHS_MAPK7.
ExpressionAtlasiQ13164. baseline and differential.
GenevestigatoriQ13164.

Organism-specific databases

HPAiCAB018561.
HPA031031.

Interactioni

Subunit structurei

Interacts with MAP2K5. Forms oligomers (By similarity). Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D (By similarity). Interacts with SGK1. Preferentially interacts with PML isoform PML-4 but shows interaction also with its other isoforms: isoform PML-1, isoform PML-2, isoform PML-3 and isoform PML-6.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAP2K5Q131632EBI-1213983,EBI-307294
PMLP295906EBI-1213983,EBI-295890

Protein-protein interaction databases

BioGridi111584. 57 interactions.
IntActiQ13164. 28 interactions.
STRINGi9606.ENSP00000311005.

Structurei

Secondary structure

1
816
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni45 – 484
Turni52 – 543
Beta strandi55 – 584
Beta strandi68 – 747
Turni75 – 773
Beta strandi80 – 867
Turni87 – 904
Helixi93 – 10816
Beta strandi117 – 1204
Turni127 – 1293
Beta strandi133 – 1386
Beta strandi141 – 1433
Helixi144 – 1485
Beta strandi149 – 1524
Helixi156 – 17520
Helixi185 – 1873
Beta strandi188 – 1903
Beta strandi196 – 1983
Helixi216 – 2183
Beta strandi226 – 2283
Helixi230 – 2345
Helixi242 – 25716
Helixi267 – 27812
Helixi283 – 2864
Beta strandi288 – 2903
Turni292 – 2943
Helixi295 – 2984
Beta strandi299 – 3013
Helixi309 – 3124
Beta strandi314 – 3163
Helixi318 – 32710
Helixi332 – 3343
Helixi338 – 3414
Helixi345 – 3473
Turni348 – 3503
Helixi353 – 3553
Helixi366 – 3694
Beta strandi370 – 3723
Helixi374 – 38310
Helixi386 – 3905
Beta strandi396 – 3983

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q8YX-ray2.00B215-223[»]
4B99X-ray2.80A1-397[»]
4IC7X-ray2.60A/D1-431[»]
4IC8X-ray2.80A/B1-431[»]
ProteinModelPortaliQ13164.
SMRiQ13164. Positions 46-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 347293Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7776Required for cytoplasmic targetingBy similarityAdd
BLAST
Regioni78 – 13962Required for binding to MAP2K5By similarityAdd
BLAST
Regioni140 – 406267Necessary for oligomerizationBy similarityAdd
BLAST
Regioni407 – 806400May not be required for kinase activity; required to stimulate MEF2C activityBy similarityAdd
BLAST
Regioni505 – 53935Nuclear localization signalBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi219 – 2213TXY

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi338 – 3414Poly-Ala
Compositional biasi403 – 694292Pro-richAdd
BLAST
Compositional biasi513 – 54331Arg-richAdd
BLAST

Domaini

The second proline-rich region may interact with actin targeting the kinase to a specific location in the cell.
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOVERGENiHBG108137.
InParanoidiQ13164.
KOiK04464.
OMAiIIETIGT.
OrthoDBiEOG70PBX2.
PhylomeDBiQ13164.
TreeFamiTF105099.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13164-1) [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
MAEPLKEEDG EDGSAEPPGP VKAEPAHTAA SVAAKNLALL KARSFDVTFD
60 70 80 90 100
VGDEYEIIET IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL
110 120 130 140 150
RELKILKHFK HDNIIAIKDI LRPTVPYGEF KSVYVVLDLM ESDLHQIIHS
160 170 180 190 200
SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH RDLKPSNLLV NENCELKIGD
210 220 230 240 250
FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT QAIDLWSVGC
260 270 280 290 300
IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS
310 320 330 340 350
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY
360 370 380 390 400
HDPDDEPDCA PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR
410 420 430 440 450
FQPSLQPVAS EPGCPDVEMP SPWAPSGDCA MESPPPAPPP CPGPAPDTID
460 470 480 490 500
LTLQPPPPVS EPAPPKKDGA ISDNTKAALK AALLKSLRSR LRDGPSAPLE
510 520 530 540 550
APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER KERGAGASGG
560 570 580 590 600
PSTDPLAGLV LSDNDRSLLE RWTRMARPAA PALTSVPAPA PAPTPTPTPV
610 620 630 640 650
QPTSPPPGPV AQPTGPQPQS AGSTSGPVPQ PACPPPGPAP HPTGPPGPIP
660 670 680 690 700
VPAPPQIATS TSLLAAQSLV PPPGLPGSST PGVLPYFPPG LPPPDAGGAP
710 720 730 740 750
QSSMSESPDV NLVTQQLSKS QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF
760 770 780 790 800
LNQSFDMGVA DGPQDGQADS ASLSASLLAD WLEGHGMNPA DIESLQREIQ
810
MDSPMLLADL PDLQDP
Length:816
Mass (Da):88,386
Last modified:September 2, 2008 - v2
Checksum:i27729FE31658CE3B
GO
Isoform 2 (identifier: Q13164-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Note: No experimental confirmation available.

Show »
Length:677
Mass (Da):73,218
Checksum:iEC01D3784EB8AAB0
GO
Isoform 3 (identifier: Q13164-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS

Show »
Length:533
Mass (Da):59,328
Checksum:i6E654D7CA1287E32
GO
Isoform 4 (identifier: Q13164-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: MAEPLKEEDG...TVPYGEFKSV → MLFFHTMPSA...HASLLPSPSS
     493-816: DGPSAPLEAP...LADLPDLQDP → GALWAGRVGR...KWPQRTPGGS

Note: No experimental confirmation available.

Show »
Length:451
Mass (Da):50,152
Checksum:iE0FAC412C3DE60F9
GO

Sequence cautioni

The sequence AAA81381.1 differs from that shown. Reason: Frameshift at positions 19 and 32.
The sequence BAD92848.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti610 – 6101V → L in AAA81381. (PubMed:7646528)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti535 – 5351R → H.1 Publication
VAR_046225
Natural varianti550 – 5501G → A.1 Publication
Corresponds to variant rs56388327 [ dbSNP | Ensembl ].
VAR_042257

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 139139Missing in isoform 2. 1 PublicationVSP_035198Add
BLAST
Alternative sequencei1 – 133133MAEPL…EFKSV → MLFFHTMPSAPMGSQGKAVT CLESEGCGEDGACPWSVIRP THASLLPSPSS in isoform 4. 1 PublicationVSP_035199Add
BLAST
Alternative sequencei493 – 816324DGPSA…DLQDP → GALWAGRVGRGETWTWTRLQ AFTFSPAQLPRKWPQRTPGG S in isoform 3 and isoform 4. 2 PublicationsVSP_035200Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29725 mRNA. Translation: AAA82931.1.
U29726 mRNA. Translation: AAA82932.1.
U29727 Genomic DNA. Translation: AAA82933.1.
U25278 mRNA. Translation: AAA81381.1. Frameshift.
AY534741 mRNA. Translation: AAS38577.1.
AB209611 mRNA. Translation: BAD92848.1. Different initiation.
CH471212 Genomic DNA. Translation: EAW50883.1.
CH471212 Genomic DNA. Translation: EAW50886.1.
BC007404 mRNA. Translation: AAH07404.1.
BC007992 mRNA. Translation: AAH07992.1.
BC009963 mRNA. Translation: AAH09963.1.
BC030134 mRNA. Translation: AAH30134.1.
CCDSiCCDS11206.1. [Q13164-1]
CCDS11207.1. [Q13164-2]
PIRiB56708.
RefSeqiNP_002740.2. NM_002749.3. [Q13164-1]
NP_620601.1. NM_139032.2. [Q13164-2]
NP_620602.2. NM_139033.2. [Q13164-1]
NP_620603.2. NM_139034.2. [Q13164-1]
XP_005256776.1. XM_005256719.1. [Q13164-2]
XP_006721623.1. XM_006721560.1. [Q13164-1]
UniGeneiHs.150136.

Genome annotation databases

EnsembliENST00000299612; ENSP00000299612; ENSG00000166484. [Q13164-2]
ENST00000308406; ENSP00000311005; ENSG00000166484. [Q13164-1]
ENST00000395602; ENSP00000378966; ENSG00000166484. [Q13164-1]
ENST00000395604; ENSP00000378968; ENSG00000166484. [Q13164-1]
GeneIDi5598.
KEGGihsa:5598.
UCSCiuc002gvn.3. human. [Q13164-1]

Polymorphism databases

DMDMi205371766.

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:
EMBL
GenBank
DDBJ
Links Updated
U29725 mRNA. Translation: AAA82931.1 .
U29726 mRNA. Translation: AAA82932.1 .
U29727 Genomic DNA. Translation: AAA82933.1 .
U25278 mRNA. Translation: AAA81381.1 . Frameshift.
AY534741 mRNA. Translation: AAS38577.1 .
AB209611 mRNA. Translation: BAD92848.1 . Different initiation.
CH471212 Genomic DNA. Translation: EAW50883.1 .
CH471212 Genomic DNA. Translation: EAW50886.1 .
BC007404 mRNA. Translation: AAH07404.1 .
BC007992 mRNA. Translation: AAH07992.1 .
BC009963 mRNA. Translation: AAH09963.1 .
BC030134 mRNA. Translation: AAH30134.1 .
CCDSi CCDS11206.1. [Q13164-1 ]
CCDS11207.1. [Q13164-2 ]
PIRi B56708.
RefSeqi NP_002740.2. NM_002749.3. [Q13164-1 ]
NP_620601.1. NM_139032.2. [Q13164-2 ]
NP_620602.2. NM_139033.2. [Q13164-1 ]
NP_620603.2. NM_139034.2. [Q13164-1 ]
XP_005256776.1. XM_005256719.1. [Q13164-2 ]
XP_006721623.1. XM_006721560.1. [Q13164-1 ]
UniGenei Hs.150136.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q8Y X-ray 2.00 B 215-223 [» ]
4B99 X-ray 2.80 A 1-397 [» ]
4IC7 X-ray 2.60 A/D 1-431 [» ]
4IC8 X-ray 2.80 A/B 1-431 [» ]
ProteinModelPortali Q13164.
SMRi Q13164. Positions 46-400.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111584. 57 interactions.
IntActi Q13164. 28 interactions.
STRINGi 9606.ENSP00000311005.

Chemistry

BindingDBi Q13164.
ChEMBLi CHEMBL5332.
GuidetoPHARMACOLOGYi 2093.

PTM databases

PhosphoSitei Q13164.

Polymorphism databases

DMDMi 205371766.

Proteomic databases

MaxQBi Q13164.
PaxDbi Q13164.
PRIDEi Q13164.

Protocols and materials databases

DNASUi 5598.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299612 ; ENSP00000299612 ; ENSG00000166484 . [Q13164-2 ]
ENST00000308406 ; ENSP00000311005 ; ENSG00000166484 . [Q13164-1 ]
ENST00000395602 ; ENSP00000378966 ; ENSG00000166484 . [Q13164-1 ]
ENST00000395604 ; ENSP00000378968 ; ENSG00000166484 . [Q13164-1 ]
GeneIDi 5598.
KEGGi hsa:5598.
UCSCi uc002gvn.3. human. [Q13164-1 ]

Organism-specific databases

CTDi 5598.
GeneCardsi GC17P019281.
HGNCi HGNC:6880. MAPK7.
HPAi CAB018561.
HPA031031.
MIMi 602521. gene.
neXtProti NX_Q13164.
PharmGKBi PA30625.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074298.
HOVERGENi HBG108137.
InParanoidi Q13164.
KOi K04464.
OMAi IIETIGT.
OrthoDBi EOG70PBX2.
PhylomeDBi Q13164.
TreeFami TF105099.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
Reactomei REACT_12020. Signalling to ERK5.
REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
SignaLinki Q13164.

Miscellaneous databases

GeneWikii MAPK7.
GenomeRNAii 5598.
NextBioi 21728.
PROi Q13164.
SOURCEi Search...

Gene expression databases

Bgeei Q13164.
CleanExi HS_MAPK7.
ExpressionAtlasi Q13164. baseline and differential.
Genevestigatori Q13164.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of BMK1: a new mammalian map kinase."
    Lee J.-D., Ulevitch R.J., Han J.
    Biochem. Biophys. Res. Commun. 213:715-724(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Placenta.
  2. "Components of a new human protein kinase signal transduction pathway."
    Zhou G., Bao Z.Q., Dixon J.E.
    J. Biol. Chem. 270:12665-12669(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAP2K5, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  3. "Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice variant."
    McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R.
    Gene 345:183-190(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Placenta.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Spleen.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Muscle and Pancreas.
  7. Bienvenut W.V., Fleming J., Leug H.Y.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-35; 75-98; 119-131; 198-205; 296-343; 377-392; 468-485; 489-505; 544-571; 720-735 AND 798-816, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  8. "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C."
    Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D.
    EMBO J. 16:7054-7066(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 219-THR--TYR-221.
  9. "Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor."
    Kato Y., Tapping R.I., Huang S., Watson M.H., Ulevitch R.J., Lee J.-D.
    Nature 395:713-716(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  10. "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase."
    Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y., Lee J.D.
    J. Biol. Chem. 276:8631-8634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SGK1.
  11. "Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival."
    Dong F., Gutkind J.S., Larner A.C.
    J. Biol. Chem. 276:10811-10816(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720 AND THR-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction."
    Yang Q., Liao L., Deng X., Chen R., Gray N.S., Yates J.R. III, Lee J.D.
    Oncogene 32:3156-3164(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PML.
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-535 AND ALA-550.

Entry informationi

Entry nameiMK07_HUMAN
AccessioniPrimary (citable) accession number: Q13164
Secondary accession number(s): Q16634
, Q59F50, Q6QLU7, Q7L4P4, Q969G1, Q96G51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 2, 2008
Last modified: October 29, 2014
This is version 146 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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