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Protein
Submitted name:

Mitogen-activated protein kinase kinase 6

Gene

Map2k6

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase kinase activity Source: RGD

GO - Biological processi

  • apoptotic process Source: RGD
  • cardiac muscle contraction Source: Ensembl
  • cellular response to sorbitol Source: RGD
  • ovulation cycle process Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
  • positive regulation of prostaglandin secretion Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • response to drug Source: RGD
  • response to ischemia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinaseUniRule annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-168638. NOD1/2 Signaling Pathway.
R-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-446652. Interleukin-1 signaling.
R-RNO-450302. activated TAK1 mediates p38 MAPK activation.

Names & Taxonomyi

Protein namesi
Submitted name:
Mitogen-activated protein kinase kinase 6Imported
Submitted name:
Mitogen-activated protein kinase kinase 6, isoform CRA_aImported
Submitted name:
Protein Map2k6Imported
Gene namesi
Name:Map2k6Imported
Synonyms:Mkk6Imported
ORF Names:rCG_34806Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi620666. Map2k6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 314262Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG0984. Eukaryota.
ENOG410XT3F. LUCA.
GeneTreeiENSGT00760000119199.
HOGENOMiHOG000234206.
HOVERGENiHBG108518.
KOiK04433.
OMAiMEVMNTS.
OrthoDBiEOG7J9VPW.
TreeFamiTF350701.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
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.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q925D6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSKGKKRN PGLKIPREAF EQPQTSSTPP RDLDSKACIS IGNQNFEVKA
60 70 80 90 100
DDLEPIVELG RGAYGVVEKM RHVPSGQIMA VKRIRATVNS QEQKRLLMDL
110 120 130 140 150
DVSMRTVDCP FTVTFYGALF REGDVWICME LMDTSLDKFY KQVIDKGQTI
160 170 180 190 200
PEDILGKIAV SIVKALEHLH SKLSVIHRDV KPSNVLINTL GQVKMCDFGI
210 220 230 240 250
SGYLVDSVAK TIDAGCKPYM APERINPELN QKGYSVKSDI WSLGITMIEL
260 270 280 290 300
AILRFPYDSW GTPFQQLKQV VEEPSPQLPA DKFSADFVDF TSQCLKKNSK
310 320 330
ERPTYPELMQ HPFFTVHEAK AADVASFVKL ILGD
Length:334
Mass (Da):37,444
Last modified:December 1, 2001 - v1
Checksum:iC6A4843F82F63D87
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07030670 Genomic DNA. No translation available.
AABR07030671 Genomic DNA. No translation available.
AABR07030672 Genomic DNA. No translation available.
AABR07030673 Genomic DNA. No translation available.
BC087004 mRNA. Translation: AAH87004.1.
AF369384 mRNA. Translation: AAK53428.1.
CH473948 Genomic DNA. Translation: EDM06489.1.
RefSeqiNP_446155.1. NM_053703.3.
UniGeneiRn.17256.

Genome annotation databases

EnsembliENSRNOT00000006217; ENSRNOP00000006217; ENSRNOG00000004437.
GeneIDi114495.
KEGGirno:114495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07030670 Genomic DNA. No translation available.
AABR07030671 Genomic DNA. No translation available.
AABR07030672 Genomic DNA. No translation available.
AABR07030673 Genomic DNA. No translation available.
BC087004 mRNA. Translation: AAH87004.1.
AF369384 mRNA. Translation: AAK53428.1.
CH473948 Genomic DNA. Translation: EDM06489.1.
RefSeqiNP_446155.1. NM_053703.3.
UniGeneiRn.17256.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000006217; ENSRNOP00000006217; ENSRNOG00000004437.
GeneIDi114495.
KEGGirno:114495.

Organism-specific databases

CTDi5608.
RGDi620666. Map2k6.

Phylogenomic databases

eggNOGiKOG0984. Eukaryota.
ENOG410XT3F. LUCA.
GeneTreeiENSGT00760000119199.
HOGENOMiHOG000234206.
HOVERGENiHBG108518.
KOiK04433.
OMAiMEVMNTS.
OrthoDBiEOG7J9VPW.
TreeFamiTF350701.

Enzyme and pathway databases

ReactomeiR-RNO-168638. NOD1/2 Signaling Pathway.
R-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-446652. Interleukin-1 signaling.
R-RNO-450302. activated TAK1 mediates p38 MAPK activation.

Miscellaneous databases

NextBioi618541.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
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.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Glembotski C.C., Smith L.M., Thuerauf D.J., Monia B.P., Craig R.A.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: HeartImported.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ925D6_RAT
AccessioniPrimary (citable) accession number: Q925D6
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.