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Q9Y2U5

- M3K2_HUMAN

UniProt

Q9Y2U5 - M3K2_HUMAN

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Protein

Mitogen-activated protein kinase kinase kinase 2

Gene
MAP3K2, MAPKKK2, MEKK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Activated by phosphorylation on Thr-524 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei385 – 3851ATP By similarity
Active sitei483 – 4831Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi362 – 37110ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase kinase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: IntAct
  5. protein kinase activity Source: MGI
  6. protein kinase binding Source: UniProtKB
  7. protein serine/threonine kinase activity Source: ProtInc

GO - Biological processi

  1. activation of JUN kinase activity Source: ProtInc
  2. activation of MAPK activity Source: ProtInc
  3. cellular response to mechanical stimulus Source: UniProtKB
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. protein phosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
SignaLinkiQ9Y2U5.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MAP3K2
Synonyms:MAPKKK2, MEKK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6854. MAP3K2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Upon EGF stimulation, translocates into the nucleus.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Ensembl
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Mitogen-activated protein kinase kinase kinase 2PRO_0000086243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphoserine1 Publication
Modified residuei153 – 1531Phosphoserine4 Publications
Modified residuei159 – 1591Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine1 Publication
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei297 – 2971Phosphoserine1 Publication
Modified residuei331 – 3311Phosphoserine3 Publications
Modified residuei344 – 3441Phosphoserine3 Publications

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y2U5.
PaxDbiQ9Y2U5.
PRIDEiQ9Y2U5.

PTM databases

PhosphoSiteiQ9Y2U5.

Expressioni

Gene expression databases

ArrayExpressiQ9Y2U5.
BgeeiQ9Y2U5.
CleanExiHS_MAP3K2.
GenevestigatoriQ9Y2U5.

Organism-specific databases

HPAiHPA021540.

Interactioni

Subunit structurei

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/BIRC4.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STUB1Q9UNE79EBI-357393,EBI-357085

Protein-protein interaction databases

BioGridi115969. 23 interactions.
IntActiQ9Y2U5. 8 interactions.
MINTiMINT-272127.
STRINGi9606.ENSP00000343463.

Structurei

Secondary structure

1
619
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 507
Beta strandi53 – 597
Helixi65 – 7612
Beta strandi80 – 867
Beta strandi89 – 924
Helixi96 – 10813
Beta strandi114 – 1218

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU1NMR-A43-132[»]
2NPTX-ray1.75B/D26-123[»]
ProteinModelPortaliQ9Y2U5.
SMRiQ9Y2U5. Positions 35-122, 328-616.

Miscellaneous databases

EvolutionaryTraceiQ9Y2U5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 12280OPRAdd
BLAST
Domaini357 – 617261Protein kinaseAdd
BLAST

Sequence similaritiesi

Contains 1 OPR domain.

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG006303.
InParanoidiQ9Y2U5.
KOiK04420.
OMAiRSVHMKS.
OrthoDBiEOG747PHJ.
PhylomeDBiQ9Y2U5.
TreeFamiTF105113.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamiPF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y2U5-1 [UniParc]FASTAAdd to Basket

« Hide

MDDQQALNSI MQDLAVLHKA SRPALSLQET RKAKSSSPKK QNDVRVKFEH    50
RGEKRILQFP RPVKLEDLRS KAKIAFGQSM DLHYTNNELV IPLTTQDDLD 100
KAVELLDRSI HMKSLKILLV INGSTQATNL EPLPSLEDLD NTVFGAERKK 150
RLSIIGPTSR DRSSPPPGYI PDELHQVARN GSFTSINSEG EFIPESMDQM 200
LDPLSLSSPE NSGSGSCPSL DSPLDGESYP KSRMPRAQSY PDNHQEFSDY 250
DNPIFEKFGK GGTYPRRYHV SYHHQEYNDG RKTFPRARRT QGTSLRSPVS 300
FSPTDHSLST SSGSSIFTPE YDDSRIRRRG SDIDNPTLTV MDISPPSRSP 350
RAPTNWRLGK LLGQGAFGRV YLCYDVDTGR ELAVKQVQFD PDSPETSKEV 400
NALECEIQLL KNLLHERIVQ YYGCLRDPQE KTLSIFMEYM PGGSIKDQLK 450
AYGALTENVT RKYTRQILEG VHYLHSNMIV HRDIKGANIL RDSTGNVKLG 500
DFGASKRLQT ICLSGTGMKS VTGTPYWMSP EVISGEGYGR KADIWSVACT 550
VVEMLTEKPP WAEFEAMAAI FKIATQPTNP KLPPHVSDYT RDFLKRIFVE 600
AKLRPSADEL LRHMFVHYH 619
Length:619
Mass (Da):69,741
Last modified:May 16, 2006 - v2
Checksum:iE034580D349F097F
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101I → V.1 Publication
Corresponds to variant rs55767983 [ dbSNP | Ensembl ].
VAR_040682
Natural varianti112 – 1121M → I in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_040683
Natural varianti140 – 1401D → G.1 Publication
Corresponds to variant rs56307783 [ dbSNP | Ensembl ].
VAR_040684

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → GTR in BAD92200. 1 Publication
Sequence conflicti103 – 1031V → L in AAD28547. 1 Publication
Sequence conflicti103 – 1031V → L in AAF63496. 1 Publication
Sequence conflicti198 – 1981D → E in AAD28547. 1 Publication
Sequence conflicti198 – 1981D → E in AAF63496. 1 Publication
Sequence conflicti225 – 2251D → G in AAD28547. 1 Publication
Sequence conflicti275 – 2773QEY → KD in AAD28547. 1 Publication
Sequence conflicti293 – 2964TSLR → NQLT in AAD28547. 1 Publication
Sequence conflicti293 – 2964TSLR → NQLT in AAF63496. 1 Publication
Sequence conflicti413 – 4131L → F in AAD28547. 1 Publication
Sequence conflicti459 – 4591V → G in AAD28547. 1 Publication
Sequence conflicti480 – 4801V → L in AAD28547. 1 Publication
Sequence conflicti536 – 5361E → Q in AAD28547. 1 Publication
Sequence conflicti536 – 5361E → Q in AAF63496. 1 Publication
Sequence conflicti579 – 5791N → S in BAC11348. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS46404.1.
RefSeqiNP_006600.3. NM_006609.4.
UniGeneiHs.145605.

Genome annotation databases

EnsembliENST00000344908; ENSP00000343463; ENSG00000169967.
ENST00000409947; ENSP00000387246; ENSG00000169967.
GeneIDi10746.
KEGGihsa:10746.
UCSCiuc002toj.2. human.

Polymorphism databases

DMDMi97536681.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS46404.1.
RefSeqi NP_006600.3. NM_006609.4.
UniGenei Hs.145605.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CU1 NMR - A 43-132 [» ]
2NPT X-ray 1.75 B/D 26-123 [» ]
ProteinModelPortali Q9Y2U5.
SMRi Q9Y2U5. Positions 35-122, 328-616.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115969. 23 interactions.
IntActi Q9Y2U5. 8 interactions.
MINTi MINT-272127.
STRINGi 9606.ENSP00000343463.

Chemistry

BindingDBi Q9Y2U5.
ChEMBLi CHEMBL5914.
GuidetoPHARMACOLOGYi 2077.

PTM databases

PhosphoSitei Q9Y2U5.

Polymorphism databases

DMDMi 97536681.

Proteomic databases

MaxQBi Q9Y2U5.
PaxDbi Q9Y2U5.
PRIDEi Q9Y2U5.

Protocols and materials databases

DNASUi 10746.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344908 ; ENSP00000343463 ; ENSG00000169967 .
ENST00000409947 ; ENSP00000387246 ; ENSG00000169967 .
GeneIDi 10746.
KEGGi hsa:10746.
UCSCi uc002toj.2. human.

Organism-specific databases

CTDi 10746.
GeneCardsi GC02M128057.
H-InvDB HIX0002433.
HGNCi HGNC:6854. MAP3K2.
HPAi HPA021540.
MIMi 609487. gene.
neXtProti NX_Q9Y2U5.
PharmGKBi PA30598.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG006303.
InParanoidi Q9Y2U5.
KOi K04420.
OMAi RSVHMKS.
OrthoDBi EOG747PHJ.
PhylomeDBi Q9Y2U5.
TreeFami TF105113.

Enzyme and pathway databases

BRENDAi 2.7.12.2. 2681.
SignaLinki Q9Y2U5.

Miscellaneous databases

EvolutionaryTracei Q9Y2U5.
GeneWikii MAP3K2.
GenomeRNAii 10746.
NextBioi 40805.
PROi Q9Y2U5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y2U5.
Bgeei Q9Y2U5.
CleanExi HS_MAP3K2.
Genevestigatori Q9Y2U5.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view ]
Pfami PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. 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.
    , 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.

Entry informationi

Entry nameiM3K2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2U5
Secondary accession number(s): B9EG87
, Q53QL9, Q53S75, Q59GZ6, Q8NC32, Q9NYK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 16, 2006
Last modified: July 9, 2014
This is version 152 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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