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O14733 (MP2K7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity mitogen-activated protein kinase kinase 7

Short name=MAP kinase kinase 7
Short name=MAPKK 7
EC=2.7.12.2
Alternative name(s):
JNK-activating kinase 2
MAPK/ERK kinase 7
Short name=MEK 7
Stress-activated protein kinase kinase 4
Short name=SAPK kinase 4
Short name=SAPKK-4
Short name=SAPKK4
c-Jun N-terminal kinase kinase 2
Short name=JNK kinase 2
Short name=JNKK 2
Gene names
Name:MAP2K7
Synonyms:JNKK2, MEK7, MKK7, PRKMK7, SKK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Ref.1 Ref.2 Ref.3 Ref.5

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Activated by phosphorylation by specific MAP kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3, MAP3K11/MLK3 and MAP3K12/DLK. Ref.2 Ref.4

Subunit structure

Interacts with isoform 1 of VRK2. Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 By similarity. Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1 and MAP3K1/MEKK1 By similarity. Interacts with MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold proteins. Interacts with RASSF7, the interaction promotes phosphorylation. Ref.10 Ref.12 Ref.14 Ref.18

Subcellular location

Nucleus. Cytoplasm By similarity.

Tissue specificity

Ubiquitous; with highest level of expression in skeletal muscle. Isoform 3 is found at low levels in placenta, fetal liver, and skeletal muscle. Ref.1 Ref.3 Ref.4

Domain

The DVD domain (residues 377-400) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation. Ref.13

The D domain (residues 37-57) contains a conserved docking site and is required for the binding to MAPK substrates. Ref.13

Post-translational modification

Activated by phosphorylation on Ser-271 and Thr-275 by MAP kinase kinase kinases (MAP3Ks) By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAB97813.1 differs from that shown. Reason: Erroneous termination at position 420. Translated as stop.

The sequence AAB97813.1 differs from that shown. Reason: Frameshift at positions 402 and 410.

Ontologies

Keywords
   Biological processApoptosis
Stress response
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

JNK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of JUN kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to sorbitol

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

response to stress

Inferred from direct assay Ref.3. Source: UniProtKB

signal transduction

Traceable author statement Ref.3. Source: ProtInc

stress-activated MAPK cascade

Inferred from direct assay Ref.3. Source: UniProtKB

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

JUN kinase kinase activity

Inferred from electronic annotation. Source: Ensembl

MAP kinase kinase activity

Inferred from direct assay Ref.3. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.3. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 14697235. Source: UniProtKB

protein phosphatase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14733-1)

Also known as: A;

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.
Isoform 2 (identifier: O14733-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     111-111: Q → QVPPSLWRGEGGGPARLDPSWERQWGAGGGGRAPGTLQPSLSSQ
Note: May be due to intron retention.
Isoform 3 (identifier: O14733-3)

Also known as: gamma1;

The sequence of this isoform differs from the canonical sequence as follows:
     42-42: T → IIVITLSPAPAPSQRAA
Isoform 4 (identifier: O14733-4)

The sequence of this isoform differs from the canonical sequence as follows:
     312-312: L → LPCPSPSQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 419418Dual specificity mitogen-activated protein kinase kinase 7
PRO_0000086388

Regions

Domain120 – 380261Protein kinase
Nucleotide binding126 – 1349ATP By similarity
Region37 – 5721D domain By similarity
Region377 – 40024DVD domain
Coiled coil2 – 3029 Potential

Sites

Active site2431Proton acceptor By similarity
Binding site1491ATP By similarity
Site44 – 452Cleavage; by anthrax lethal factor
Site76 – 772Cleavage; by anthrax lethal factor

Amino acid modifications

Modified residue21N-acetylalanine Ref.16 Ref.20
Modified residue2711Phosphoserine; by MAP3K By similarity
Modified residue2751Phosphothreonine; by MAP3K By similarity

Natural variations

Alternative sequence421T → IIVITLSPAPAPSQRAA in isoform 3.
VSP_022309
Alternative sequence1111Q → QVPPSLWRGEGGGPARLDPS WERQWGAGGGGRAPGTLQPS LSSQ in isoform 2.
VSP_004883
Alternative sequence3121L → LPCPSPSQ in isoform 4.
VSP_022310
Natural variant1181N → S. Ref.22
Corresponds to variant rs56316660 [ dbSNP | Ensembl ].
VAR_040825
Natural variant1381R → C. Ref.22
Corresponds to variant rs56106612 [ dbSNP | Ensembl ].
VAR_040826
Natural variant1621R → C in a colorectal adenocarcinoma sample; somatic mutation. Ref.22
VAR_040827
Natural variant1621R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.22
VAR_040828
Natural variant1951A → T. Ref.22
Corresponds to variant rs55800262 [ dbSNP | Ensembl ].
VAR_040829
Natural variant2591L → F. Ref.3
Corresponds to variant rs1053566 [ dbSNP | Ensembl ].
VAR_029890

Experimental info

Sequence conflict941Q → H in AAB97813. Ref.2
Sequence conflict1061L → P in ABE03013. Ref.4
Sequence conflict1331Q → P in AAB97813. Ref.2
Sequence conflict1421T → N in AAB88048. Ref.1
Sequence conflict4071S → N in AAB97813. Ref.2
Sequence conflict4151L → LG in AAB97813. Ref.2

Secondary structure

................................................ 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: F1B22E050F54299A

FASTA41947,485
        10         20         30         40         50         60 
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND GGSRSPSSES 

        70         80         90        100        110        120 
SPQHPTPPAR PRHMLGLPST LFTPRSMESI EIDQKLQEIM KQTGYLTIGG QRYQAEINDL 

       130        140        150        160        170        180 
ENLGEMGSGT CGQVWKMRFR KTGHVIAVKQ MRRSGNKEEN KRILMDLDVV LKSHDCPYIV 

       190        200        210        220        230        240 
QCFGTFITNT DVFIAMELMG TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI 

       250        260        270        280        290        300 
HRDVKPSNIL LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD 

       310        320        330        340        350        360 
IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS GDFQSFVKDC 

       370        380        390        400        410 
LTKDHRKRPK YNKLLEHSFI KRYETLEVDV ASWFKDVMAK TESPRTSGVL SQPHLPFFR 

« Hide

Isoform 2 (B) [UniParc].

Checksum: DF3496066961B0C7
Show »

FASTA46251,881
Isoform 3 (gamma1) [UniParc].

Checksum: 8812A87DB28F2C22
Show »

FASTA43549,071
Isoform 4 [UniParc].

Checksum: 7934E29217D8A137
Show »

FASTA42648,182

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of human JNKK2, a novel jun NH2-terminal kinase-specific kinase."
Wu Z., Wu J., Jacinto E., Karin M.
Mol. Cell. Biol. 17:7407-7416(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Heart and Skeletal muscle.
[2]"Identification of c-Jun NH2-terminal protein kinase (JNK)-activating kinase 2 as an activator of JNK but not p38."
Lu X., Nemoto S., Lin A.
J. Biol. Chem. 272:24751-24754(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION.
[3]"Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli."
Foltz I.N., Gerl R.E., Wieler J.S., Luckach M., Salmon R.A., Schrader J.W.
J. Biol. Chem. 273:9344-9351(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANT PHE-259.
Tissue: Fetal kidney.
[4]"Cloning and expression of human mitogen-activated protein kinase kinase 7gamma1."
Michael L., Swantek J., Robinson M.J.
Biochem. Biophys. Res. Commun. 341:679-683(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ENZYME REGULATION, TISSUE SPECIFICITY.
[5]"Molecular cloning of human JNKK2 reveals a novel kinase module for c-Jun N-terminal kinase activation."
Yang J., New L., Yong J., Han J., Su B.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF MAPK8/JNK1 AND MAPK9/JNK2.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 4).
Tissue: Testis.
[9]"Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase."
Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.
Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-260 (ISOFORMS 1/4).
[10]"The JIP group of mitogen-activated protein kinase scaffold proteins."
Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.
Mol. Cell. Biol. 19:7245-7254(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPK8IP1/JIP1 AND MAPK8IP2/JIP2.
[11]"Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
[12]"Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade."
Matsuura H., Nishitoh H., Takeda K., Matsuzawa A., Amagasa T., Ito M., Yoshioka K., Ichijo H.
J. Biol. Chem. 277:40703-40709(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPK8IP3/JIP3.
[13]"Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases."
Takekawa M., Tatebayashi K., Saito H.
Mol. Cell 18:295-306(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[14]"Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VRK2.
[15]"Differential regulation and properties of MAPKs."
Raman M., Chen W., Cobb M.H.
Oncogene 26:3100-3112(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ENZYME REGULATION.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"Diverse physiological functions of MKK4 and MKK7 during early embryogenesis."
Asaoka Y., Nishina H.
J. Biochem. 148:393-401(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[18]"RASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting the activity of phosphorylated-MKK7."
Takahashi S., Ebihara A., Kajiho H., Kontani K., Nishina H., Katada T.
Cell Death Differ. 18:645-655(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASSF7.
[19]"The bottleneck of JNK signaling: molecular and functional characteristics of MKK4 and MKK7."
Haeusgen W., Herdegen T., Waetzig V.
Eur. J. Cell Biol. 90:536-544(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON REGULATION, REVIEW ON FUNCTION.
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystal structure of human mitogen-activated protein kinase kinase 7 activated mutant (s287d, t291d)."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 101-405.
[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. expand/collapse author list , 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] SER-118; CYS-138; CYS-162; HIS-162 AND THR-195.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF014401 mRNA. Translation: AAB88048.1.
AF006689 mRNA. Translation: AAB97813.1. Sequence problems.
AF013588 mRNA. Translation: AAC16272.1.
AF013589 mRNA. Translation: AAC16273.1.
DQ445915 mRNA. Translation: ABE03013.1.
AF022805 mRNA. Translation: AAC26142.1.
AK313899 mRNA. Translation: BAG36622.1.
CH471139 Genomic DNA. Translation: EAW68964.1.
CH471139 Genomic DNA. Translation: EAW68968.1.
BC038295 mRNA. Translation: AAH38295.1.
AF003199 mRNA. Translation: AAB63374.1.
RefSeqNP_660186.1. NM_145185.2.
XP_005272546.1. XM_005272489.1.
XP_005272547.1. XM_005272490.1.
UniGeneHs.531754.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DYLX-ray2.45A101-405[»]
ProteinModelPortalO14733.
SMRO14733. Positions 53-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111595. 34 interactions.
IntActO14733. 18 interactions.
MINTMINT-1378223.
STRING9606.ENSP00000381066.

Chemistry

BindingDBO14733.
ChEMBLCHEMBL3530.
DrugBankDB00773. Etoposide.
GuidetoPHARMACOLOGY2068.

PTM databases

PhosphoSiteO14733.

Proteomic databases

PaxDbO14733.
PRIDEO14733.

Protocols and materials databases

DNASU5609.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397979; ENSP00000381066; ENSG00000076984. [O14733-1]
ENST00000397981; ENSP00000381068; ENSG00000076984. [O14733-4]
ENST00000397983; ENSP00000381070; ENSG00000076984. [O14733-3]
GeneID5609.
KEGGhsa:5609.
UCSCuc002mit.3. human. [O14733-1]
uc002miv.2. human. [O14733-4]

Organism-specific databases

CTD5609.
GeneCardsGC19P007968.
HGNCHGNC:6847. MAP2K7.
HPACAB004262.
HPA001633.
MIM603014. gene.
neXtProtNX_O14733.
PharmGKBPA284.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108518.
KOK04431.
OrthoDBEOG7J9VPW.
PhylomeDBO14733.
TreeFamTF350701.

Enzyme and pathway databases

BRENDA2.7.12.2. 2681.
ReactomeREACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkO14733.

Gene expression databases

ArrayExpressO14733.
BgeeO14733.
CleanExHS_MAP2K7.
GenevestigatorO14733.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO14733.
GeneWikiMAP2K7.
GenomeRNAi5609.
NextBio21802.
PMAP-CutDBO14733.
PROO14733.
SOURCESearch...

Entry information

Entry nameMP2K7_HUMAN
AccessionPrimary (citable) accession number: O14733
Secondary accession number(s): B2R9S5 expand/collapse secondary AC list , D6W659, O14648, O14816, O60452, O60453, Q1PG43, Q8IY10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM