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Q9Y2U5 (M3K2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase 2

EC=2.7.11.25
Alternative name(s):
MAPK/ERK kinase kinase 2
Short name=MEK kinase 2
Short name=MEKK 2
Gene names
Name:MAP3K2
Synonyms:MAPKKK2, MEKK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 By similarity. Plays a role in caveolae kiss-and-run dynamics. Ref.8 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Activated by phosphorylation on Thr-524 By similarity.

Subunit structure

Interacts with PKN2; the interaction activates PKN2 kinase activity in a MAP3K2-independent kinase activity By similarity. Self-associates. Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts (via the kinase catalytic domain) with STK38. Interacts with XIAP/BIRC4. Ref.8 Ref.12 Ref.16

Subcellular location

Cytoplasm. Nucleus. Note: Upon EGF stimulation, translocates into the nucleus. Ref.9

Post-translational modification

Autophosphorylated By similarity.

Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation.

Sequence similarities

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

Contains 1 OPR domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAC11348.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Traceable author statement PubMed 8621389. Source: ProtInc

activation of MAPK activity

Traceable author statement PubMed 8621389. Source: ProtInc

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14515274. Source: UniProtKB

protein phosphorylation

Traceable author statement PubMed 8621389. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from direct assay PubMed 15001576. Source: MGI

protein kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

protein serine/threonine kinase activity

Traceable author statement PubMed 8621389. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STUB1Q9UNE79EBI-357393,EBI-357085

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Mitogen-activated protein kinase kinase kinase 2
PRO_0000086243

Regions

Domain43 – 12280OPR
Domain357 – 617261Protein kinase
Nucleotide binding362 – 37110ATP By similarity

Sites

Active site4831Proton acceptor By similarity
Binding site3851ATP By similarity

Amino acid modifications

Modified residue261Phosphoserine Ref.18
Modified residue1531Phosphoserine Ref.15 Ref.17 Ref.18 Ref.20
Modified residue1591Phosphoserine Ref.17
Modified residue1641Phosphoserine Ref.17
Modified residue2391Phosphoserine Ref.19
Modified residue2971Phosphoserine Ref.13
Modified residue3311Phosphoserine Ref.15 Ref.18 Ref.19
Modified residue3441Phosphoserine Ref.15 Ref.18 Ref.19

Natural variations

Natural variant1101I → V. Ref.23
Corresponds to variant rs55767983 [ dbSNP | Ensembl ].
VAR_040682
Natural variant1121M → I in a lung large cell carcinoma sample; somatic mutation. Ref.23
VAR_040683
Natural variant1401D → G. Ref.23
Corresponds to variant rs56307783 [ dbSNP | Ensembl ].
VAR_040684

Experimental info

Sequence conflict11M → GTR in BAD92200. Ref.3
Sequence conflict1031V → L in AAD28547. Ref.1
Sequence conflict1031V → L in AAF63496. Ref.2
Sequence conflict1981D → E in AAD28547. Ref.1
Sequence conflict1981D → E in AAF63496. Ref.2
Sequence conflict2251D → G in AAD28547. Ref.1
Sequence conflict275 – 2773QEY → KD in AAD28547. Ref.1
Sequence conflict293 – 2964TSLR → NQLT in AAD28547. Ref.1
Sequence conflict293 – 2964TSLR → NQLT in AAF63496. Ref.2
Sequence conflict4131L → F in AAD28547. Ref.1
Sequence conflict4591V → G in AAD28547. Ref.1
Sequence conflict4801V → L in AAD28547. Ref.1
Sequence conflict5361E → Q in AAD28547. Ref.1
Sequence conflict5361E → Q in AAF63496. Ref.2
Sequence conflict5791N → S in BAC11348. Ref.7

Secondary structure

............... 619
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y2U5 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: E034580D349F097F

FASTA61969,741
        10         20         30         40         50         60 
MDDQQALNSI MQDLAVLHKA SRPALSLQET RKAKSSSPKK QNDVRVKFEH RGEKRILQFP 

        70         80         90        100        110        120 
RPVKLEDLRS KAKIAFGQSM DLHYTNNELV IPLTTQDDLD KAVELLDRSI HMKSLKILLV 

       130        140        150        160        170        180 
INGSTQATNL EPLPSLEDLD NTVFGAERKK RLSIIGPTSR DRSSPPPGYI PDELHQVARN 

       190        200        210        220        230        240 
GSFTSINSEG EFIPESMDQM LDPLSLSSPE NSGSGSCPSL DSPLDGESYP KSRMPRAQSY 

       250        260        270        280        290        300 
PDNHQEFSDY DNPIFEKFGK GGTYPRRYHV SYHHQEYNDG RKTFPRARRT QGTSLRSPVS 

       310        320        330        340        350        360 
FSPTDHSLST SSGSSIFTPE YDDSRIRRRG SDIDNPTLTV MDISPPSRSP RAPTNWRLGK 

       370        380        390        400        410        420 
LLGQGAFGRV YLCYDVDTGR ELAVKQVQFD PDSPETSKEV NALECEIQLL KNLLHERIVQ 

       430        440        450        460        470        480 
YYGCLRDPQE KTLSIFMEYM PGGSIKDQLK AYGALTENVT RKYTRQILEG VHYLHSNMIV 

       490        500        510        520        530        540 
HRDIKGANIL RDSTGNVKLG DFGASKRLQT ICLSGTGMKS VTGTPYWMSP EVISGEGYGR 

       550        560        570        580        590        600 
KADIWSVACT VVEMLTEKPP WAEFEAMAAI FKIATQPTNP KLPPHVSDYT RDFLKRIFVE 

       610 
AKLRPSADEL LRHMFVHYH 

« Hide

References

« Hide 'large scale' references
[1]"MEKK2 is involved in transducing T-cell co-stimulatory signals to the JNK cascade."
Su B., Yang J.H., Xia Y., Karin M.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human MEKK2b cDNA."
Wang C., Lo H.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: T-cell.
[3]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].
Tissue: Brain.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Testis.
[7]"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] OF 180-619.
Tissue: Teratocarcinoma.
[8]"Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation."
Cheng J., Yang J., Xia Y., Karin M., Su B.
Mol. Cell. Biol. 20:2334-2342(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP2K7 AND MAPK8.
[9]"MEK5 and ERK5 are localized in the nuclei of resting as well as stimulated cells, while MEKK2 translocates from the cytosol to the nucleus upon stimulation."
Raviv Z., Kalie E., Seger R.
J. Cell Sci. 117:1773-1784(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae."
Pelkmans L., Zerial M.
Nature 436:128-133(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2."
Winsauer G., Resch U., Hofer-Warbinek R., Schichl Y.M., de Martin R.
Cell. Signal. 20:2107-2112(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY XIAP/BIRC4, INTERACTION WITH XIAP/BIRC4.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38)."
Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N., Hosoi Y., Miyagawa K.
Oncogene 27:1930-1938(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STK38, SELF-ASSOCIATION.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-159 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-153; SER-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Solution structure of the PB1 domain of human protein kinase MEKK2B."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 43-132.
[23]"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] VAL-110; ILE-112 AND GLY-140.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF111105 mRNA. Translation: AAD28547.1.
AF239798 mRNA. Translation: AAF63496.1.
AB208963 mRNA. Translation: BAD92200.1.
AC068282 Genomic DNA. Translation: AAY15043.1.
AC110926 Genomic DNA. Translation: AAY15070.1.
CH471103 Genomic DNA. Translation: EAW95315.1.
BC136293 mRNA. Translation: AAI36294.1.
AK075004 mRNA. Translation: BAC11348.1. Different initiation.
RefSeqNP_006600.3. NM_006609.4.
UniGeneHs.145605.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU1NMR-A43-132[»]
2NPTX-ray1.75B/D26-123[»]
ProteinModelPortalQ9Y2U5.
SMRQ9Y2U5. Positions 35-122, 328-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115969. 23 interactions.
IntActQ9Y2U5. 8 interactions.
MINTMINT-272127.
STRING9606.ENSP00000343463.

Chemistry

BindingDBQ9Y2U5.
ChEMBLCHEMBL5914.
GuidetoPHARMACOLOGY2077.

PTM databases

PhosphoSiteQ9Y2U5.

Polymorphism databases

DMDM97536681.

Proteomic databases

PaxDbQ9Y2U5.
PRIDEQ9Y2U5.

Protocols and materials databases

DNASU10746.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344908; ENSP00000343463; ENSG00000169967.
ENST00000409947; ENSP00000387246; ENSG00000169967.
GeneID10746.
KEGGhsa:10746.
UCSCuc002toj.2. human.

Organism-specific databases

CTD10746.
GeneCardsGC02M128057.
H-InvDBHIX0002433.
HGNCHGNC:6854. MAP3K2.
HPAHPA021540.
MIM609487. gene.
neXtProtNX_Q9Y2U5.
PharmGKBPA30598.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG006303.
InParanoidQ9Y2U5.
KOK04420.
OMARSVHMKS.
OrthoDBEOG747PHJ.
PhylomeDBQ9Y2U5.
TreeFamTF105113.

Enzyme and pathway databases

BRENDA2.7.12.2. 2681.
SignaLinkQ9Y2U5.

Gene expression databases

ArrayExpressQ9Y2U5.
BgeeQ9Y2U5.
CleanExHS_MAP3K2.
GenevestigatorQ9Y2U5.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y2U5.
GeneWikiMAP3K2.
GenomeRNAi10746.
NextBio40805.
PROQ9Y2U5.
SOURCESearch...

Entry information

Entry nameM3K2_HUMAN
AccessionPrimary (citable) accession number: Q9Y2U5
Secondary accession number(s): B9EG87 expand/collapse secondary AC list , Q53QL9, Q53S75, Q59GZ6, Q8NC32, Q9NYK3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 149 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 2

Human chromosome 2: entries, gene names and cross-references to MIM