Q99759 (M3K3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase kinase kinase 3
EC=2.7.11.25

Alternative name(s):
MAPK/ERK kinase kinase 3
Short name=MEK kinase 3
Short name=MEKK 3

Gene names

Name:	MAP3K3
Synonyms:	MAPKKK3, MEKK3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. Ref.1 Ref.8 Ref.9 Ref.10
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by phosphorylation on Thr-530 By similarity.
Subunit structure	Binds both upstream activators and downstream substrates in multimolecular complexes. Part of a complex with MAP2K3, RAC1 and CCM2. Interacts with MAP2K5 and SPAG9. Ref.8 Ref.9 Ref.10
Post-translational modification	Phosphorylation at Ser-166 and Ser-337 by SGK1 inhibits its activity.
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.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	MAPKKK cascade Traceable author statement. Source: ProtInc positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern. Source: UniProtKB protein autophosphorylation Inferred from direct assay. Source: MGI
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRAF7	Q6Q0C0	3	EBI-307281,EBI-307556

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99759-1)

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: Q99759-2)

The sequence of this isoform differs from the canonical sequence as follows:
     42-42: Q → QKKHNSSSSALLNSPTVTTSSCAGASEKKKFL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 626

626

Mitogen-activated protein kinase kinase kinase 3

PRO_0000086245

Regions

Domain

44 – 123

80

OPR

Domain

362 – 622

261

Protein kinase

Nucleotide binding

368 – 376

9

ATP By similarity

Sites

Active site

489

1

Proton acceptor By similarity

Binding site

391

1

ATP By similarity

Amino acid modifications

Modified residue

129

1

Phosphoserine Ref.15

Modified residue

130

1

Phosphoserine Ref.15

Modified residue

131

1

Phosphoserine Ref.13

Modified residue

145

1

Phosphoserine Ref.15

Modified residue

147

1

Phosphoserine Ref.15

Modified residue

166

1

Phosphoserine; by SGK1 Ref.7 Ref.12 Ref.13 Ref.15

Modified residue

168

1

Phosphoserine Ref.15

Modified residue

175

1

Phosphoserine Ref.15

Modified residue

176

1

Phosphoserine Ref.15

Modified residue

234

1

Phosphoserine Ref.13

Modified residue

237

1

Phosphoserine Ref.13 Ref.15

Modified residue

250

1

Phosphoserine Ref.13 Ref.15

Modified residue

288

1

Phosphotyrosine Ref.11

Modified residue

289

1

Phosphoserine Ref.11

Modified residue

294

1

Phosphothreonine Ref.11

Modified residue

311

1

Phosphoserine Ref.15

Modified residue

314

1

Phosphoserine Ref.15

Modified residue

316

1

Phosphoserine Ref.15

Modified residue

317

1

Phosphothreonine Ref.15

Modified residue

337

1

Phosphoserine; by SGK1 Ref.7 Ref.13 Ref.15 Ref.16

Modified residue

340

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16

Modified residue

353

1

Phosphothreonine Ref.15

Modified residue

355

1

Phosphoserine Ref.13 Ref.15

Modified residue

464

1

Phosphoserine Ref.15

Modified residue

526

1

Phosphoserine Ref.15

Modified residue

530

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

42

1

Q → QKKHNSSSSALLNSPTVTTS SCAGASEKKKFL in isoform 2.

VSP_035967

Natural variant

281

1

V → M. Ref.17
Corresponds to variant rs36109904 [ dbSNP | Ensembl ].

VAR_040685

Natural variant

325

1

A → G.
Corresponds to variant rs34042309 [ dbSNP | Ensembl ].

VAR_037275

Natural variant

435

1

A → G.
Corresponds to variant rs9910858 [ dbSNP | Ensembl ].

VAR_037276

Experimental info

Sequence conflict

135

1

G → E in AAB41729. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

626

Helix Strand Turn

Details...

Beta strand

45 – 51

7

Beta strand

54 – 60

7

Helix

66 – 77

12

Beta strand

82 – 86

5

Beta strand

91 – 93

3

Helix

97 – 109

13

Beta strand

115 – 121

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 28129168A57571DD	FASTA	626	70,898
	10 20 30 40 50 60 MDEQEALNSI MNDLVALQMN RRHRMPGYET MKNKDTGHSN RQSDVRIKFE HNGERRIIAF 70 80 90 100 110 120 SRPVKYEDVE HKVTTVFGQP LDLHYMNNEL SILLKNQDDL DKAIDILDRS SSMKSLRILL 130 140 150 160 170 180 LSQDRNHNSS SPHSGVSRQV RIKASQSAGD INTIYQPPEP RSRHLSVSSQ NPGRSSPPPG 190 200 210 220 230 240 YVPERQQHIA RQGSYTSINS EGEFIPETSE QCMLDPLSSA ENSLSGSCQS LDRSADSPSF 250 260 270 280 290 300 RKSRMSRAQS FPDNRQEYSD RETQLYDKGV KGGTYPRRYH VSVHHKDYSD GRRTFPRIRR 310 320 330 340 350 360 HQGNLFTLVP SSRSLSTNGE NMGLAVQYLD PRGRLRSADS ENALSVQERN VPTKSPSAPI 370 380 390 400 410 420 NWRRGKLLGQ GAFGRVYLCY DVDTGRELAS KQVQFDPDSP ETSKEVSALE CEIQLLKNLQ 430 440 450 460 470 480 HERIVQYYGC LRDRAEKTLT IFMEYMPGGS VKDQLKAYGA LTESVTRKYT RQILEGMSYL 490 500 510 520 530 540 HSNMIVHRDI KGANILRDSA GNVKLGDFGA SKRLQTICMS GTGMRSVTGT PYWMSPEVIS 550 560 570 580 590 600 GEGYGRKADV WSLGCTVVEM LTEKPPWAEY EAMAAIFKIA TQPTNPQLPS HISEHGRDFL 610 620 RRIFVEARQR PSAEELLTHH FAQLMY
	Isoform 2 [UniParc]. Checksum: DF37E5E568FE937E	FASTA	657	74,089
	10 20 30 40 50 60 MDEQEALNSI MNDLVALQMN RRHRMPGYET MKNKDTGHSN RQKKHNSSSS ALLNSPTVTT 70 80 90 100 110 120 SSCAGASEKK KFLSDVRIKF EHNGERRIIA FSRPVKYEDV EHKVTTVFGQ PLDLHYMNNE 130 140 150 160 170 180 LSILLKNQDD LDKAIDILDR SSSMKSLRIL LLSQDRNHNS SSPHSGVSRQ VRIKASQSAG 190 200 210 220 230 240 DINTIYQPPE PRSRHLSVSS QNPGRSSPPP GYVPERQQHI ARQGSYTSIN SEGEFIPETS 250 260 270 280 290 300 EQCMLDPLSS AENSLSGSCQ SLDRSADSPS FRKSRMSRAQ SFPDNRQEYS DRETQLYDKG 310 320 330 340 350 360 VKGGTYPRRY HVSVHHKDYS DGRRTFPRIR RHQGNLFTLV PSSRSLSTNG ENMGLAVQYL 370 380 390 400 410 420 DPRGRLRSAD SENALSVQER NVPTKSPSAP INWRRGKLLG QGAFGRVYLC YDVDTGRELA 430 440 450 460 470 480 SKQVQFDPDS PETSKEVSAL ECEIQLLKNL QHERIVQYYG CLRDRAEKTL TIFMEYMPGG 490 500 510 520 530 540 SVKDQLKAYG ALTESVTRKY TRQILEGMSY LHSNMIVHRD IKGANILRDS AGNVKLGDFG 550 560 570 580 590 600 ASKRLQTICM SGTGMRSVTG TPYWMSPEVI SGEGYGRKAD VWSLGCTVVE MLTEKPPWAE 610 620 630 640 650 YEAMAAIFKI ATQPTNPQLP SHISEHGRDF LRRIFVEARQ RPSAEELLTH HFAQLMY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Direct activation of the stress-activated protein kinase (SAPK) and extracellular signal-regulated protein kinase (ERK) pathways by an inducible mitogen-activated protein kinase/ERK kinase kinase 3 (MEKK) derivative." Ellinger-Ziegelbauer H.C., Brown K., Kelly K., Siebenlist U. J. Biol. Chem. 272:2668-2674(1997) [PubMed: 9006902] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Melanoma.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [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 (SEP-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and PNS.
[7]	"Inhibition of mitogen-activated kinase kinase kinase 3 activity through phosphorylation by the serum- and glucocorticoid-induced kinase 1." Chun J., Kwon T., Kim D.J., Park I., Chung G., Lee E.J., Hong S.K., Chang S.I., Kim H.Y., Kang S.S. J. Biochem. 133:103-108(2003) [PubMed: 12761204] [Abstract] Cited for: PHOSPHORYLATION AT SER-166 AND SER-337 BY SGK1.
[8]	"PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway." Nakamura K., Johnson G.L. J. Biol. Chem. 278:36989-36992(2003) [PubMed: 12912994] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAP2K5.
[9]	"Differential regulation of interleukin 1 receptor and Toll-like receptor signaling by MEKK3." Huang Q., Yang J., Lin Y., Walker C., Cheng J., Liu Z.G., Su B. Nat. Immunol. 5:98-103(2004) [PubMed: 14661019] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRAF6.
[10]	"A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway." Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G., Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S., Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J., Schwab M., Stein M.A. , Bauer A., Casari G., Drewes G., Gavin A.-C., Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B., Superti-Furga G. Nat. Cell Biol. 6:97-105(2004) [PubMed: 14743216] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRAF7.
[11]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-288; SER-289 AND THR-294, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-166; SER-234; SER-237; SER-250; SER-337; SER-340 AND SER-355, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-130; SER-145; SER-147; SER-166; SER-168; SER-175; SER-176; SER-237; SER-250; SER-311; SER-314; SER-316; THR-317; SER-337; SER-340; THR-353; SER-355; SER-464 AND SER-526, MASS SPECTROMETRY.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-340, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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: 17344846] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-281.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U78876 mRNA. Translation: AAB41729.1.
AK315305 mRNA. Translation: BAG37709.1.
AL834303 mRNA. Translation: CAD38973.1.
AC046185 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94297.1.
CH471109 Genomic DNA. Translation: EAW94298.1.
CH471109 Genomic DNA. Translation: EAW94299.1.
BC090859 mRNA. Translation: AAH90859.1.
BC093672 mRNA. Translation: AAH93672.1.
BC093674 mRNA. Translation: AAH93674.1.

IPI

IPI00017801.
IPI00181703.

RefSeq

NP_002392.2. NM_002401.3.
NP_976226.1. NM_203351.1.

UniGene

Hs.29282.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C60	X-ray	1.25	A	37-124	[»]
2JRH	NMR	-	A	42-126	[»]
2O2V	X-ray	1.83	B	37-124	[»]
2PPH	NMR	-	A	42-126	[»]

ProteinModelPortal

Q99759.

SMR

Q99759. Positions 43-122, 359-624.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27521N.

IntAct

Q99759. 5 interactions.

MINT

MINT-272157.

STRING

Q99759.

PTM databases

PhosphoSite

Q99759.

Polymorphism databases

DMDM

160332306.

Proteomic databases

PRIDE

Q99759.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361733; ENSP00000354485; ENSG00000198909.

GeneID

4215.

KEGG

hsa:4215.

NMPDR

fig|9606.3.peg.14206.

UCSC

uc002jbg.1. human.

Organism-specific databases

CTD

4215.

GeneCards

GC17P061699.

HGNC

HGNC:6855. MAP3K3.

HPA

CAB007764.

MIM

602539. gene.

neXtProt

NX_Q99759.

PharmGKB

PA30599.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06004.

GeneTree

ENSGT00600000084293.

HOVERGEN

HBG006303.

OMA

SGYETMK.

PhylomeDB

Q99759.

Enzyme and pathway databases

BRENDA

2.7.12.2. 2681.

Pathway_Interaction_DB

il1pathway. IL1-mediated signaling events.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q99759.

Bgee

Q99759.

CleanEx

HS_MAP3K3.

Genevestigator

Q99759.

GermOnline

ENSG00000198909. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_kinase-like_dom.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K04421.

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

ProtoNet

Search...

Other

NextBio

16621.

SOURCE

Search...

Entry information

Entry name

M3K3_HUMAN

Accession

Primary (citable) accession number: Q99759
Secondary accession number(s): B2RCW2 , D3DU15, Q5BKZ6, Q8N3I9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 128 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.