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Q9Y6R4 (M3K4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase 4

EC=2.7.11.25
Alternative name(s):
MAP three kinase 1
MAPK/ERK kinase kinase 4
Short name=MEK kinase 4
Short name=MEKK 4
Gene names
Name:MAP3K4
Synonyms:KIAA0213, MAPKKK4, MEKK4, MTK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1608 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. Ref.1 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

N-terminal autoinhibitory domain interacts with the C-terminal kinase domain, inhibiting kinase activity, and preventing interaction with its substrate, MAP2K6. The GADD45 proteins activate the kinase by binding to the N-terminal domain. Activated by phosphorylation on Thr-1505. Ref.7

Subunit structure

Monomer and homodimer. Homodimerization enhances kinase activity. Interacts with TRAF4; this promotes homodimerization By similarity. Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with AXIN1 and DIXDC1; interaction with DIXDC1 prevents interaction with AXIN1. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasmperinuclear region By similarity. Note: Localized in perinuclear vesicular-like structures, probably Golgi-associated vesicles By similarity.

Tissue specificity

Expressed at high levels in heart, placenta, skeletal muscle and pancreas, and at lower levels in other tissues. Ref.1

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence BAA13204.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAC12766.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH70639.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH70640.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20815.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20816.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI21477.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41309.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41310.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.1PubMed 9827804. Source: GOC

activation of MAPKK activity

Inferred from direct assay Ref.1PubMed 9827804. Source: UniProtKB

chorionic trophoblast cell differentiation

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

male germ-line sex determination

Inferred from electronic annotation. Source: Ensembl

placenta development

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of p38MAPK cascade

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

response to UV-C

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 9827804. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from direct assay Ref.1PubMed 9827804. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6R4-1)

Also known as: A;

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: Q9Y6R4-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1175-1224: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16081608Mitogen-activated protein kinase kinase kinase 4
PRO_0000086247

Regions

Domain1343 – 1601259Protein kinase
Nucleotide binding1349 – 13579ATP By similarity
Compositional bias4 – 74Poly-Ala
Compositional bias25 – 3814Poly-Pro
Compositional bias1190 – 120213Poly-Ala

Sites

Active site14631Proton acceptor By similarity
Binding site13721ATP By similarity

Amino acid modifications

Modified residue4561Phosphoserine Ref.14
Modified residue4571Phosphoserine Ref.14
Modified residue4581Phosphothreonine Ref.14
Modified residue4611Phosphoserine Ref.14
Modified residue4991Phosphoserine Ref.11

Natural variations

Alternative sequence1175 – 122450Missing in isoform 2.
VSP_004884
Natural variant1571R → H. Ref.6
Corresponds to variant rs4559074 [ dbSNP | Ensembl ].
VAR_059767
Natural variant2941I → T. Ref.15
Corresponds to variant rs35842248 [ dbSNP | Ensembl ].
VAR_040686
Natural variant3351V → I. Ref.15
Corresponds to variant rs35730939 [ dbSNP | Ensembl ].
VAR_040687
Natural variant5661R → H. Ref.15
Corresponds to variant rs55765351 [ dbSNP | Ensembl ].
VAR_040688
Natural variant5841Q → H. Ref.15
Corresponds to variant rs34018542 [ dbSNP | Ensembl ].
VAR_040689
Natural variant9061H → P. Ref.15
Corresponds to variant rs35533223 [ dbSNP | Ensembl ].
VAR_040690
Natural variant14131E → Q in an ovarian serous carcinoma sample; somatic mutation. Ref.15
VAR_040691
Natural variant14921A → V. Ref.15
Corresponds to variant rs41267837 [ dbSNP | Ensembl ].
VAR_040692

Experimental info

Mutagenesis13721K → R: Loss of activity. Ref.1 Ref.7
Sequence conflict351P → PP in AAI36277. Ref.6
Sequence conflict5001E → D in AAI46771. Ref.6
Sequence conflict7911R → I in AAB68804. Ref.1
Sequence conflict11901Missing in EAW47587. Ref.5
Sequence conflict11901Missing in AAI43736. Ref.6
Sequence conflict11901Missing in AAI36277. Ref.6
Sequence conflict11991Missing in AAB68804. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: C22294914945EA91

FASTA1,608181,685
        10         20         30         40         50         60 
MREAAAALVP PPAFAVTPAA AMEEPPPPPP PPPPPPEPET ESEPECCLAA RQEGTLGDSA 

        70         80         90        100        110        120 
CKSPESDLED FSDETNTENL YGTSPPSTPR QMKRMSTKHQ RNNVGRPASR SNLKEKMNAP 

       130        140        150        160        170        180 
NQPPHKDTGK TVENVEEYSY KQEKKIRAAL RTTERDRKKN VQCSFMLDSV GGSLPKKSIP 

       190        200        210        220        230        240 
DVDLNKPYLS LGCSNAKLPV SVPMPIARPA RQTSRTDCPA DRLKFFETLR LLLKLTSVSK 

       250        260        270        280        290        300 
KKDREQRGQE NTSGFWLNRS NELIWLELQA WHAGRTINDQ DFFLYTARQA IPDIINEILT 

       310        320        330        340        350        360 
FKVDYGSFAF VRDRAGFNGT SVEGQCKATP GTKIVGYSTH HEHLQRQRVS FEQVKRIMEL 

       370        380        390        400        410        420 
LEYIEALYPS LQALQKDYEK YAAKDFQDRV QALCLWLNIT KDLNQKLRIM GTVLGIKNLS 

       430        440        450        460        470        480 
DIGWPVFEIP SPRPSKGNEP EYEGDDTEGE LKELESSTDE SEEEQISDPR VPEIRQPIDN 

       490        500        510        520        530        540 
SFDIQSRDCI SKKLERLESE DDSLGWGAPD WSTEAGFSRH CLTSIYRPFV DKALKQMGLR 

       550        560        570        580        590        600 
KLILRLHKLM DGSLQRARIA LVKNDRPVEF SEFPDPMWGS DYVQLSRTPP SSEEKCSAVS 

       610        620        630        640        650        660 
WEELKAMDLP SFEPAFLVLC RVLLNVIHEC LKLRLEQRPA GEPSLLSIKQ LVRECKEVLK 

       670        680        690        700        710        720 
GGLLMKQYYQ FMLQEVLEDL EKPDCNIDAF EEDLHKMLMV YFDYMRSWIQ MLQQLPQASH 

       730        740        750        760        770        780 
SLKNLLEEEW NFTKEITHYI RGGEAQAGKL FCDIAGMLLK STGSFLEFGL QESCAEFWTS 

       790        800        810        820        830        840 
ADDSSASDEI RRSVIEISRA LKELFHEARE RASKALGFAK MLRKDLEIAA EFRLSAPVRD 

       850        860        870        880        890        900 
LLDVLKSKQY VKVQIPGLEN LQMFVPDTLA EEKSIILQLL NAAAGKDCSK DSDDVLIDAY 

       910        920        930        940        950        960 
LLLTKHGDRA RDSEDSWGTW EAQPVKVVPQ VETVDTLRSM QVDNLLLVVM QSAHLTIQRK 

       970        980        990       1000       1010       1020 
AFQQSIEGLM TLCQEQTSSQ PVIAKALQQL KNDALELCNR ISNAIDRVDH MFTSEFDAEV 

      1030       1040       1050       1060       1070       1080 
DESESVTLQQ YYREAMIQGY NFGFEYHKEV VRLMSGEFRQ KIGDKYISFA RKWMNYVLTK 

      1090       1100       1110       1120       1130       1140 
CESGRGTRPR WATQGFDFLQ AIEPAFISAL PEDDFLSLQA LMNECIGHVI GKPHSPVTGL 

      1150       1160       1170       1180       1190       1200 
YLAIHRNSPR PMKVPRCHSD PPNPHLIIPT PEGFSTRSMP SDARSHGSPA AAAAAAAAAV 

      1210       1220       1230       1240       1250       1260 
AASRPSPSGG DSVLPKSISS AHDTRGSSVP ENDRLASIAA ELQFRSLSRH SSPTEERDEP 

      1270       1280       1290       1300       1310       1320 
AYPRGDSSGS TRRSWELRTL ISQSKDTASK LGPIEAIQKS VRLFEEKRYR EMRRKNIIGQ 

      1330       1340       1350       1360       1370       1380 
VCDTPKSYDN VMHVGLRKVT FKWQRGNKIG EGQYGKVYTC ISVDTGELMA MKEIRFQPND 

      1390       1400       1410       1420       1430       1440 
HKTIKETADE LKIFEGIKHP NLVRYFGVEL HREEMYIFME YCDEGTLEEV SRLGLQEHVI 

      1450       1460       1470       1480       1490       1500 
RLYSKQITIA INVLHEHGIV HRDIKGANIF LTSSGLIKLG DFGCSVKLKN NAQTMPGEVN 

      1510       1520       1530       1540       1550       1560 
STLGTAAYMA PEVITRAKGE GHGRAADIWS LGCVVIEMVT GKRPWHEYEH NFQIMYKVGM 

      1570       1580       1590       1600 
GHKPPIPERL SPEGKDFLSH CLESDPKMRW TASQLLDHSF VKVCTDEE 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 4F94E9CF82E88354
Show »

FASTA1,558177,014

References

« Hide 'large scale' references
[1]"A human homolog of the yeast Ssk2/Ssk22 MAP kinase kinase kinases, MTK1, mediates stress-induced activation of the p38 and JNK pathways."
Takekawa M., Posas F., Saito H.
EMBO J. 16:4973-4982(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, MUTAGENESIS OF LYS-1372.
Tissue: Fetal liver and Skeletal muscle.
[2]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Bone marrow.
[3]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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 (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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT HIS-157.
Tissue: Cerebellum.
[7]"Regulation of MTK1/MEKK4 kinase activity by its N-terminal autoinhibitory domain and GADD45 binding."
Mita H., Tsutsui J., Takekawa M., Witten E.A., Saito H.
Mol. Cell. Biol. 22:4544-4555(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH GADD45 AND MAP2K6, MUTAGENESIS OF LYS-1372.
[8]"The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms."
Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.
J. Biol. Chem. 279:39366-39373(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1 AND DIXDC1.
[9]"MEKK4 is an effector of the embryonic TRAF4 for JNK activation."
Abell A.N., Johnson G.L.
J. Biol. Chem. 280:35793-35796(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF4.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-457; THR-458 AND SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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] THR-294; ILE-335; HIS-566; HIS-584; PRO-906; GLN-1413 AND VAL-1492.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF002715 mRNA. Translation: AAB68804.1.
D86968 mRNA. Translation: BAA13204.2. Different initiation.
AL109942 expand/collapse EMBL AC list , AL139393, AL591045, AL596452 Genomic DNA. Translation: CAC12766.2. Sequence problems.
AL109942 expand/collapse EMBL AC list , AL139393, AL591045, AL596452 Genomic DNA. Translation: CAI21477.1. Sequence problems.
AL139393 expand/collapse EMBL AC list , AL109942, AL591045, AL596452 Genomic DNA. Translation: CAI20815.1. Sequence problems.
AL139393 expand/collapse EMBL AC list , AL109942, AL591045, AL596452 Genomic DNA. Translation: CAI20816.1. Sequence problems.
AL591045 expand/collapse EMBL AC list , AL109942, AL139393, AL596452 Genomic DNA. Translation: CAH70639.1. Sequence problems.
AL591045 expand/collapse EMBL AC list , AL109942, AL139393, AL596452 Genomic DNA. Translation: CAH70640.1. Sequence problems.
AL596452 expand/collapse EMBL AC list , AL109942, AL139393, AL591045 Genomic DNA. Translation: CAI41309.1. Sequence problems.
AL596452 expand/collapse EMBL AC list , AL109942, AL139393, AL591045 Genomic DNA. Translation: CAI41310.1. Sequence problems.
CH471051 Genomic DNA. Translation: EAW47587.1.
BC136276 mRNA. Translation: AAI36277.1.
BC143735 mRNA. Translation: AAI43736.1.
BC146770 mRNA. Translation: AAI46771.1.
PIRT03022.
RefSeqNP_005913.2. NM_005922.2.
NP_006715.2. NM_006724.2.
UniGeneHs.390428.

3D structure databases

ProteinModelPortalQ9Y6R4.
SMRQ9Y6R4. Positions 1301-1603.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110380. 22 interactions.
IntActQ9Y6R4. 10 interactions.
MINTMINT-1213156.
STRING9606.ENSP00000375986.

Chemistry

ChEMBLCHEMBL4853.
GuidetoPHARMACOLOGY2079.

PTM databases

PhosphoSiteQ9Y6R4.

Polymorphism databases

DMDM296434576.

Proteomic databases

PaxDbQ9Y6R4.
PRIDEQ9Y6R4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366919; ENSP00000355886; ENSG00000085511. [Q9Y6R4-2]
ENST00000392142; ENSP00000375986; ENSG00000085511. [Q9Y6R4-1]
GeneID4216.
KEGGhsa:4216.
UCSCuc003qtn.3. human. [Q9Y6R4-1]
uc003qto.3. human. [Q9Y6R4-2]

Organism-specific databases

CTD4216.
GeneCardsGC06P161412.
H-InvDBHIX0151295.
HGNCHGNC:6856. MAP3K4.
HPAHPA007625.
MIM602425. gene.
neXtProtNX_Q9Y6R4.
PharmGKBPA30600.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG006304.
InParanoidQ9Y6R4.
KOK04428.
OMAFVKVCTD.
OrthoDBEOG7P5T02.
PhylomeDBQ9Y6R4.
TreeFamTF105114.

Enzyme and pathway databases

BRENDA2.7.12.2. 2681.
SignaLinkQ9Y6R4.

Gene expression databases

ArrayExpressQ9Y6R4.
BgeeQ9Y6R4.
CleanExHS_MAP3K4.
GenevestigatorQ9Y6R4.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP3K4. human.
GeneWikiMAP3K4.
GenomeRNAi4216.
NextBio16627.
PROQ9Y6R4.
SOURCESearch...

Entry information

Entry nameM3K4_HUMAN
AccessionPrimary (citable) accession number: Q9Y6R4
Secondary accession number(s): A6H8W0 expand/collapse secondary AC list , B7ZLD3, B9EG75, Q5VTT8, Q5VTT9, Q92612, Q9H408
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 137 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM