Q9Y2U5 (M3K2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MAP3K2
Synonyms:	MAPKKK2, MEKK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	619 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of JUN kinase activity Traceable author statement PubMed 8621389. Source: ProtInc activation of MAPKK activity Inferred from electronic annotation. Source: GOC cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 14515274. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Traceable author statement PubMed 8621389. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 619

619

Mitogen-activated protein kinase kinase kinase 2

PRO_0000086243

Regions

Domain

43 – 122

80

OPR

Domain

357 – 617

261

Protein kinase

Nucleotide binding

362 – 371

10

ATP By similarity

Sites

Active site

483

1

Proton acceptor By similarity

Binding site

385

1

ATP By similarity

Amino acid modifications

Modified residue

26

1

Phosphoserine Ref.18

Modified residue

153

1

Phosphoserine Ref.15 Ref.17 Ref.18 Ref.20

Modified residue

159

1

Phosphoserine Ref.17

Modified residue

164

1

Phosphoserine Ref.17

Modified residue

239

1

Phosphoserine Ref.19

Modified residue

297

1

Phosphoserine Ref.13

Modified residue

304

1

Phosphothreonine By similarity

Modified residue

331

1

Phosphoserine Ref.15 Ref.18 Ref.19

Modified residue

344

1

Phosphoserine Ref.15 Ref.18 Ref.19

Natural variations

Natural variant

110

1

I → V. Ref.23
Corresponds to variant rs55767983 [ dbSNP | Ensembl ].

VAR_040682

Natural variant

112

1

M → I in a lung large cell carcinoma sample; somatic mutation. Ref.23

VAR_040683

Natural variant

140

1

D → G. Ref.23
Corresponds to variant rs56307783 [ dbSNP | Ensembl ].

VAR_040684

Experimental info

Sequence conflict

1

1

M → GTR in BAD92200. Ref.3

Sequence conflict

103

1

V → L in AAD28547. Ref.1

Sequence conflict

103

1

V → L in AAF63496. Ref.2

Sequence conflict

198

1

D → E in AAD28547. Ref.1

Sequence conflict

198

1

D → E in AAF63496. Ref.2

Sequence conflict

225

1

D → G in AAD28547. Ref.1

Sequence conflict

275 – 277

3

QEY → KD in AAD28547. Ref.1

Sequence conflict

293 – 296

4

TSLR → NQLT in AAD28547. Ref.1

Sequence conflict

293 – 296

4

TSLR → NQLT in AAF63496. Ref.2

Sequence conflict

413

1

L → F in AAD28547. Ref.1

Sequence conflict

459

1

V → G in AAD28547. Ref.1

Sequence conflict

480

1

V → L in AAD28547. Ref.1

Sequence conflict

536

1

E → Q in AAD28547. Ref.1

Sequence conflict

536

1

E → Q in AAF63496. Ref.2

Sequence conflict

579

1

N → S in BAC11348. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

619

Helix Strand Turn

Details...

Beta strand

44 – 50

7

Beta strand

53 – 59

7

Helix

65 – 76

12

Beta strand

80 – 86

7

Beta strand

89 – 92

4

Helix

96 – 108

13

Beta strand

114 – 121

8

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2U5 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: E034580D349F097F	FASTA	619	69,741
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
+	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.

IPI

IPI00513803.

RefSeq

NP_006600.3. NM_006609.4.

UniGene

Hs.740551.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CU1	NMR	-	A	43-132	[»]
2NPT	X-ray	1.75	B/D	26-123	[»]

ProteinModelPortal

Q9Y2U5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y2U5. 3 interactions.

MINT

MINT-272127.

STRING

9606.ENSP00000343463.

PTM databases

PhosphoSite

Q9Y2U5.

Polymorphism databases

DMDM

97536681.

Proteomic databases

PaxDb

Q9Y2U5.

PRIDE

Q9Y2U5.

Protocols and materials databases

DNASU

10746.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344908; ENSP00000343463; ENSG00000169967.
ENST00000409947; ENSP00000387246; ENSG00000169967.

GeneID

10746.

KEGG

hsa:10746.

UCSC

uc002toj.2. human.

Organism-specific databases

CTD

10746.

GeneCards

GC02M128057.

H-InvDB

HIX0002433.

HGNC

HGNC:6854. MAP3K2.

MIM

609487. gene.

neXtProt

NX_Q9Y2U5.

PharmGKB

PA30598.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG006303.

InParanoid

Q9Y2U5.

KO

K04420.

OMA

RSVHMKS.

OrthoDB

EOG4R7V9F.

PhylomeDB

Q9Y2U5.

Enzyme and pathway databases

BRENDA

2.7.12.2. 2681.

Pathway_Interaction_DB

mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.

Gene expression databases

ArrayExpress

Q9Y2U5.

Bgee

Q9Y2U5.

CleanEx

HS_MAP3K2.

Genevestigator

Q9Y2U5.

GermOnline

ENSG00000169967. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]

Pfam

PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00666. PB1. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9Y2U5.

ChEMBL

CHEMBL5914.

EvolutionaryTrace

Q9Y2U5.

GenomeRNAi

10746.

NextBio

40805.

SOURCE

Search...

Entry information

Entry name

M3K2_HUMAN

Accession

Primary (citable) accession number: Q9Y2U5
Secondary accession number(s): B9EG87 , Q53QL9, Q53S75, Q59GZ6, Q8NC32, Q9NYK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 16, 2006
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.