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Protein

Mitogen-activated protein kinase 7

Gene

MAPK7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Mg2+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)DescriptionActionsGraphical viewLength
Binding sitei84ATPPROSITE-ProRule annotation1
Active sitei182Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi61 – 69ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: ProtInc
  • mitogen-activated protein kinase binding Source: BHF-UCL
  • protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  • cAMP-mediated signaling Source: BHF-UCL
  • cell cycle Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cellular response to growth factor stimulus Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: BHF-UCL
  • cellular response to laminar fluid shear stress Source: BHF-UCL
  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • negative regulation of cAMP catabolic process Source: BHF-UCL
  • negative regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
  • negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  • negative regulation of ERK5 cascade Source: Ensembl
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • negative regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  • negative regulation of inflammatory response Source: BHF-UCL
  • negative regulation of MAP kinase activity Source: Ensembl
  • negative regulation of NFAT protein import into nucleus Source: Ensembl
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of response to cytokine stimulus Source: BHF-UCL
  • peptidyl-serine phosphorylation Source: Ensembl
  • positive regulation of protein metabolic process Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL
  • regulation of angiogenesis Source: Ensembl
  • signal transduction Source: ProtInc
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

BioCyciZFISH:HS09407-MONOMER.
BRENDAi2.7.11.24. 2681.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-198765. Signalling to ERK5.
R-HSA-202670. ERKs are inactivated.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
R-HSA-8853659. RET signaling.
SignaLinkiQ13164.
SIGNORiQ13164.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6880. MAPK7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi219 – 221TEY → AEF: Loss activation by MAP2K5. 1 Publication3

Organism-specific databases

DisGeNETi5598.
OpenTargetsiENSG00000166484.
PharmGKBiPA30625.

Chemistry databases

ChEMBLiCHEMBL5332.
GuidetoPHARMACOLOGYi2093.

Polymorphism and mutation databases

BioMutaiMAPK7.
DMDMi205371766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001862602 – 816Mitogen-activated protein kinase 7Add BLAST815

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei720PhosphoserineCombined sources1
Modified residuei733PhosphothreonineCombined sources1

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 similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13164.
MaxQBiQ13164.
PaxDbiQ13164.
PeptideAtlasiQ13164.
PRIDEiQ13164.

PTM databases

iPTMnetiQ13164.
PhosphoSitePlusiQ13164.

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

BgeeiENSG00000166484.
CleanExiHS_MAPK7.
ExpressionAtlasiQ13164. baseline and differential.
GenevisibleiQ13164. HS.

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
MAP2K5Q131634EBI-1213983,EBI-307294
PMLP295906EBI-1213983,EBI-295890
UBE2CQ5TZN33EBI-1213983,EBI-10247554

GO - Molecular functioni

  • mitogen-activated protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111584. 64 interactors.
IntActiQ13164. 34 interactors.
STRINGi9606.ENSP00000311005.

Chemistry databases

BindingDBiQ13164.

Structurei

Secondary structure

1816
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni45 – 48Combined sources4
Beta strandi53 – 64Combined sources12
Beta strandi67 – 74Combined sources8
Turni75 – 77Combined sources3
Beta strandi80 – 86Combined sources7
Turni87 – 90Combined sources4
Helixi93 – 108Combined sources16
Beta strandi117 – 120Combined sources4
Helixi127 – 129Combined sources3
Beta strandi133 – 137Combined sources5
Beta strandi141 – 143Combined sources3
Helixi144 – 148Combined sources5
Beta strandi150 – 152Combined sources3
Helixi156 – 175Combined sources20
Helixi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi196 – 198Combined sources3
Helixi214 – 216Combined sources3
Helixi219 – 221Combined sources3
Helixi225 – 227Combined sources3
Helixi230 – 234Combined sources5
Helixi242 – 257Combined sources16
Helixi267 – 278Combined sources12
Helixi283 – 287Combined sources5
Beta strandi288 – 290Combined sources3
Helixi292 – 300Combined sources9
Helixi309 – 312Combined sources4
Beta strandi313 – 316Combined sources4
Helixi318 – 327Combined sources10
Helixi332 – 334Combined sources3
Helixi338 – 342Combined sources5
Helixi345 – 347Combined sources3
Turni348 – 350Combined sources3
Helixi353 – 355Combined sources3
Helixi366 – 369Combined sources4
Beta strandi370 – 372Combined sources3
Helixi374 – 393Combined sources20
Beta strandi396 – 398Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q8YX-ray2.00B215-223[»]
4B99X-ray2.80A1-397[»]
4IC7X-ray2.60A/D1-431[»]
4IC8X-ray2.80A/B1-431[»]
4ZSGX-ray1.79A47-393[»]
4ZSJX-ray2.48A50-393[»]
4ZSLX-ray2.25A53-393[»]
5BYYX-ray2.79A49-394[»]
5BYZX-ray1.65A48-395[»]
ProteinModelPortaliQ13164.
SMRiQ13164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 347Protein kinasePROSITE-ProRule annotationAdd BLAST293

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 77Required for cytoplasmic targetingBy similarityAdd BLAST76
Regioni78 – 139Required for binding to MAP2K5By similarityAdd BLAST62
Regioni140 – 406Necessary for oligomerizationBy similarityAdd BLAST267
Regioni407 – 806May not be required for kinase activity; required to stimulate MEF2C activityBy similarityAdd BLAST400

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi219 – 221TXY3
Motifi505 – 539Nuclear localization signalBy similarityAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi338 – 341Poly-Ala4
Compositional biasi403 – 694Pro-richAdd BLAST292
Compositional biasi513 – 543Arg-richAdd BLAST31

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

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074298.
HOVERGENiHBG108137.
InParanoidiQ13164.
KOiK04464.
OMAiQCESATP.
OrthoDBiEOG091G08QL.
PhylomeDBiQ13164.
TreeFamiTF105099.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti610V → L in AAA81381 (PubMed:7646528).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_046225535R → H.1 Publication1
Natural variantiVAR_042257550G → A.1 PublicationCorresponds to variant rs56388327dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0351981 – 139Missing in isoform 2. 1 PublicationAdd BLAST139
Alternative sequenceiVSP_0351991 – 133MAEPL…EFKSV → MLFFHTMPSAPMGSQGKAVT CLESEGCGEDGACPWSVIRP THASLLPSPSS in isoform 4. 1 PublicationAdd BLAST133
Alternative sequenceiVSP_035200493 – 816DGPSA…DLQDP → GALWAGRVGRGETWTWTRLQ AFTFSPAQLPRKWPQRTPGG S in isoform 3 and isoform 4. 2 PublicationsAdd BLAST324

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_011522259.1. XM_011523957.2. [Q13164-2]
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.4. human. [Q13164-1]

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
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_011522259.1. XM_011523957.2. [Q13164-2]
UniGeneiHs.150136.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q8YX-ray2.00B215-223[»]
4B99X-ray2.80A1-397[»]
4IC7X-ray2.60A/D1-431[»]
4IC8X-ray2.80A/B1-431[»]
4ZSGX-ray1.79A47-393[»]
4ZSJX-ray2.48A50-393[»]
4ZSLX-ray2.25A53-393[»]
5BYYX-ray2.79A49-394[»]
5BYZX-ray1.65A48-395[»]
ProteinModelPortaliQ13164.
SMRiQ13164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111584. 64 interactors.
IntActiQ13164. 34 interactors.
STRINGi9606.ENSP00000311005.

Chemistry databases

BindingDBiQ13164.
ChEMBLiCHEMBL5332.
GuidetoPHARMACOLOGYi2093.

PTM databases

iPTMnetiQ13164.
PhosphoSitePlusiQ13164.

Polymorphism and mutation databases

BioMutaiMAPK7.
DMDMi205371766.

Proteomic databases

EPDiQ13164.
MaxQBiQ13164.
PaxDbiQ13164.
PeptideAtlasiQ13164.
PRIDEiQ13164.

Protocols and materials databases

DNASUi5598.
Structural Biology KnowledgebaseSearch...

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.4. human. [Q13164-1]

Organism-specific databases

CTDi5598.
DisGeNETi5598.
GeneCardsiMAPK7.
HGNCiHGNC:6880. MAPK7.
HPAiCAB018561.
HPA031031.
MIMi602521. gene.
neXtProtiNX_Q13164.
OpenTargetsiENSG00000166484.
PharmGKBiPA30625.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074298.
HOVERGENiHBG108137.
InParanoidiQ13164.
KOiK04464.
OMAiQCESATP.
OrthoDBiEOG091G08QL.
PhylomeDBiQ13164.
TreeFamiTF105099.

Enzyme and pathway databases

BioCyciZFISH:HS09407-MONOMER.
BRENDAi2.7.11.24. 2681.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-198765. Signalling to ERK5.
R-HSA-202670. ERKs are inactivated.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
R-HSA-8853659. RET signaling.
SignaLinkiQ13164.
SIGNORiQ13164.

Miscellaneous databases

ChiTaRSiMAPK7. human.
GeneWikiiMAPK7.
GenomeRNAii5598.
PROiQ13164.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166484.
CleanExiHS_MAPK7.
ExpressionAtlasiQ13164. baseline and differential.
GenevisibleiQ13164. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 170 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.