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Q13233 (M3K1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase 1

EC=2.7.11.25
Alternative name(s):
MAPK/ERK kinase kinase 1
Short name=MEK kinase 1
Short name=MEKK 1
Gene names
Name:MAP3K1
Synonyms:MAPKKK1, MEKK, MEKK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a protein kinase signal transduction cascade. Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4. Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Activated by autophosphorylation on Thr-1400 and Thr-1412 following oligomerization.

Subunit structure

Binds both upstream activators and downstream substrates in multimolecular complexes through its N-terminus. Oligomerizes after binding MAP4K2 or TRAF2. Interacts with AXIN1. Interacts (via the kinase catalytic domain) with STK38. Ref.2 Ref.4 Ref.5 Ref.8

Post-translational modification

Autophosphorylated By similarity.

Involvement in disease

46,XY sex reversal 6 (SRXY6) [MIM:613762]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

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

Contains 1 protein kinase domain.

Contains 1 RING-type zinc finger.

Contains 1 SWIM-type zinc finger.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

actin cytoskeleton organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

activation of MAPKK activity

Non-traceable author statement Ref.2. Source: GOC

apoptotic mitochondrial changes

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

epithelial cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

eyelid development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Non-traceable author statement Ref.2. Source: UniProtKB

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

JUN kinase kinase activity

Inferred from electronic annotation. Source: Ensembl

MAP kinase kinase kinase activity

Non-traceable author statement Ref.2. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 15001576. Source: MGI

protein kinase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 15121511Mitogen-activated protein kinase kinase kinase 1
PRO_0000086240

Regions

Domain1243 – 1508266Protein kinase
Zinc finger338 – 36629SWIM-type
Zinc finger443 – 49250RING-type
Nucleotide binding1249 – 12579ATP By similarity
Compositional bias2 – 54Poly-Ala
Compositional bias25 – 295Poly-Gly
Compositional bias36 – 416Poly-Ala
Compositional bias422 – 43110Poly-Ser
Compositional bias842 – 8476Poly-Ser
Compositional bias942 – 9498Poly-Thr
Compositional bias1182 – 11876Poly-Glu
Compositional bias1216 – 12194Poly-Ile

Sites

Active site13691Proton acceptor By similarity
Binding site12721ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue1371Phosphoserine By similarity
Modified residue1541Phosphoserine Ref.7
Modified residue2751Phosphoserine Ref.11
Modified residue2921Phosphoserine Ref.6 Ref.9 Ref.11
Modified residue2971Phosphoserine Ref.9
Modified residue3001Phosphoserine Ref.9
Modified residue5071Phosphoserine Ref.9
Modified residue10181Phosphoserine Ref.9
Modified residue10431Phosphoserine Ref.7
Modified residue14001Phosphothreonine; by autocatalysis By similarity
Modified residue14121Phosphothreonine; by autocatalysis By similarity

Natural variations

Natural variant921S → N. Ref.12
VAR_040680
Natural variant1891L → P in SRXY6; increases phosphorylation of the downstream target MAPK3/MAPK1 compared to wild-type and enhances binding of RHOA to the mutant MAP3K1 complex. Ref.13
VAR_065504
Natural variant1891L → R in SRXY6; increases phosphorylation of the downstream targets MAPK14 and MAPK3/MAPK1 compared to wild-type and enhances binding of RHOA to the mutant MAP3K1 complex. Ref.13
VAR_065505
Natural variant2111V → VIQ in SRXY6.
VAR_065506
Natural variant4431C → S. Ref.12
VAR_040681
Natural variant6161G → R in SRXY6. Ref.13
Corresponds to variant rs143853590 [ dbSNP | Ensembl ].
VAR_065507
Natural variant8061D → N.
Corresponds to variant rs702689 [ dbSNP | Ensembl ].
VAR_051636
Natural variant9061V → I.
Corresponds to variant rs832582 [ dbSNP | Ensembl ].
VAR_051637

Experimental info

Sequence conflict201T → P in AAC97073. Ref.2
Sequence conflict371P → R in AAC97073. Ref.2
Sequence conflict1201G → R in AAC97073. Ref.2
Sequence conflict3511R → H in AAC97073. Ref.2
Sequence conflict8451S → SV in AAC97073. Ref.2
Sequence conflict8591I → Y in AAC97073. Ref.2
Sequence conflict878 – 90225DGQQD…ENSSP → QRQQHNSFCRHLFPTTIWKP QRTVPL in AAC97073. Ref.2
Sequence conflict9331S → R in AAC97073. Ref.2
Sequence conflict10971C → L in AAC97073. Ref.2
Sequence conflict1104 – 11074AVIP → CCYT in AAC97073. Ref.2
Sequence conflict12001D → V in AAC97073. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q13233 [UniParc].

Last modified December 16, 2008. Version 4.
Checksum: 5CB78242295411D9

FASTA1,512164,470
        10         20         30         40         50         60 
MAAAAGNRAS SSGFPGARAT SPEAGGGGGA LKASSAPAAA AGLLREAGSG GRERADWRRR 

        70         80         90        100        110        120 
QLRKVRSVEL DQLPEQPLFL AASPPASSTS PSPEPADAAG SGTGFQPVAV PPPHGAASRG 

       130        140        150        160        170        180 
GAHLTESVAA PDSGASSPAA AEPGEKRAPA AEPSPAAAPA GREMENKETL KGLHKMDDRP 

       190        200        210        220        230        240 
EERMIREKLK ATCMPAWKHE WLERRNRRGP VVVKPIPVKG DGSEMNHLAA ESPGEVQASA 

       250        260        270        280        290        300 
ASPASKGRRS PSPGNSPSGR TVKSESPGVR RKRVSPVPFQ SGRITPPRRA PSPDGFSPYS 

       310        320        330        340        350        360 
PEETNRRVNK VMRARLYLLQ QIGPNSFLIG GDSPDNKYRV FIGPQNCSCA RGTFCIHLLF 

       370        380        390        400        410        420 
VMLRVFQLEP SDPMLWRKTL KNFEVESLFQ KYHSRRSSRI KAPSRNTIQK FVSRMSNSHT 

       430        440        450        460        470        480 
LSSSSTSTSS SENSIKDEEE QMCPICLLGM LDEESLTVCE DGCRNKLHHH CMSIWAEECR 

       490        500        510        520        530        540 
RNREPLICPL CRSKWRSHDF YSHELSSPVD SPSSLRAAQQ QTVQQQPLAG SRRNQESNFN 

       550        560        570        580        590        600 
LTHYGTQQIP PAYKDLAEPW IQVFGMELVG CLFSRNWNVR EMALRRLSHD VSGALLLANG 

       610        620        630        640        650        660 
ESTGNSGGSS GSSPSGGATS GSSQTSISGD VVEACCSVLS MVCADPVYKV YVAALKTLRA 

       670        680        690        700        710        720 
MLVYTPCHSL AERIKLQRLL QPVVDTILVK CADANSRTSQ LSISTLLELC KGQAGELAVG 

       730        740        750        760        770        780 
REILKAGSIG IGGVDYVLNC ILGNQTESNN WQELLGRLCL IDRLLLEFPA EFYPHIVSTD 

       790        800        810        820        830        840 
VSQAEPVEIR YKKLLSLLTF ALQSIDNSHS MVGKLSRRIY LSSARMVTTV PHVFSKLLEM 

       850        860        870        880        890        900 
LSVSSSTHFT RMRRRLMAIA DEVEIAEAIQ LGVEDTLDGQ QDSFLQASVP NNYLETTENS 

       910        920        930        940        950        960 
SPECTVHLEK TGKGLCATKL SASSEDISER LASISVGPSS STTTTTTTTE QPKPMVQTKG 

       970        980        990       1000       1010       1020 
RPHSQCLNSS PLSHHSQLMF PALSTPSSST PSVPAGTATD VSKHRLQGFI PCRIPSASPQ 

      1030       1040       1050       1060       1070       1080 
TQRKFSLQFH RNCPENKDSD KLSPVFTQSR PLPSSNIHRP KPSRPTPGNT SKQGDPSKNS 

      1090       1100       1110       1120       1130       1140 
MTLDLNSSSK CDDSFGCSSN SSNAVIPSDE TVFTPVEEKC RLDVNTELNS SIEDLLEASM 

      1150       1160       1170       1180       1190       1200 
PSSDTTVTFK SEVAVLSPEK AENDDTYKDD VNHNQKCKEK MEAEEEEALA IAMAMSASQD 

      1210       1220       1230       1240       1250       1260 
ALPIVPQLQV ENGEDIIIIQ QDTPETLPGH TKAKQPYRED TEWLKGQQIG LGAFSSCYQA 

      1270       1280       1290       1300       1310       1320 
QDVGTGTLMA VKQVTYVRNT SSEQEEVVEA LREEIRMMSH LNHPNIIRML GATCEKSNYN 

      1330       1340       1350       1360       1370       1380 
LFIEWMAGGS VAHLLSKYGA FKESVVINYT EQLLRGLSYL HENQIIHRDV KGANLLIDST 

      1390       1400       1410       1420       1430       1440 
GQRLRIADFG AAARLASKGT GAGEFQGQLL GTIAFMAPEV LRGQQYGRSC DVWSVGCAII 

      1450       1460       1470       1480       1490       1500 
EMACAKPPWN AEKHSNHLAL IFKIASATTA PSIPSHLSPG LRDVALRCLE LQPQDRPPSR 

      1510 
ELLKHPVFRT TW 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension."
Xia Y., Wu Z., Su B., Murray B., Karin M.
Genes Dev. 12:3369-3381(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-1512, FUNCTION, INTERACTION WITH MAP2K4.
[3]"Mapping of the MEK kinase gene (Mekk) to mouse chromosome 13 and human chromosome 5."
Vinik B.S., Kay E.S., Fiedorek F.T. Jr.
Mamm. Genome 6:782-783(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1238-1274.
Tissue: Leukocyte.
[4]"SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling."
Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.
J. Biol. Chem. 277:42981-42986(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1.
[5]"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.
[6]"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-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-154 AND SER-1043, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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.
[9]"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-292; SER-297; SER-300; SER-507 AND SER-1018, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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-275 AND SER-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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] ASN-92 AND SER-443.
[13]"Mutations in MAP3K1 cause 46,XY disorders of sex development and implicate a common signal transduction pathway in human testis determination."
Pearlman A., Loke J., Le Caignec C., White S., Chin L., Friedman A., Warr N., Willan J., Brauer D., Farmer C., Brooks E., Oddoux C., Riley B., Shajahan S., Camerino G., Homfray T., Crosby A.H., Couper J. expand/collapse author list , David A., Greenfield A., Sinclair A., Ostrer H.
Am. J. Hum. Genet. 87:898-904(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SRXY6 PRO-189; ARG-189; ILE-GLN-211 INS AND ARG-616, CHARACTERIZATION OF VARIANTS SRXY6 PRO-189 AND ARG-189.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC008937 Genomic DNA. No translation available.
AF042838 mRNA. Translation: AAC97073.1.
U29671 Genomic DNA. Translation: AAB05828.1.
PIRG01887.
RefSeqNP_005912.1. NM_005921.1.
UniGeneHs.653654.

3D structure databases

ProteinModelPortalQ13233.
SMRQ13233. Positions 1227-1505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110378. 61 interactions.
DIPDIP-27520N.
IntActQ13233. 31 interactions.
MINTMINT-143285.
STRING9606.ENSP00000382423.

Chemistry

BindingDBQ13233.
ChEMBLCHEMBL3956.
GuidetoPHARMACOLOGY2069.

PTM databases

PhosphoSiteQ13233.

Polymorphism databases

DMDM218512139.

2D gel databases

SWISS-2DPAGEQ13233.

Proteomic databases

PaxDbQ13233.
PRIDEQ13233.

Protocols and materials databases

DNASU4214.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399503; ENSP00000382423; ENSG00000095015.
GeneID4214.
KEGGhsa:4214.
UCSCuc003jqw.4. human.

Organism-specific databases

CTD4214.
GeneCardsGC05P056110.
H-InvDBHIX0024789.
HGNCHGNC:6848. MAP3K1.
HPACAB004500.
HPA046509.
MIM600982. gene.
613762. phenotype.
neXtProtNX_Q13233.
Orphanet242. 46,XY complete gonadal dysgenesis.
251510. 46,XY partial gonadal dysgenesis.
PharmGKBPA30592.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000113437.
HOVERGENHBG006302.
InParanoidQ13233.
KOK04416.
OMASTHFTRM.
OrthoDBEOG7MSMNV.
PhylomeDBQ13233.
TreeFamTF105112.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ13233.

Gene expression databases

BgeeQ13233.
CleanExHS_MAP3K1.
GenevestigatorQ13233.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR007527. Znf_SWIM.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50966. ZF_SWIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMAP3K1.
GenomeRNAi4214.
NextBio16613.
PROQ13233.
SOURCESearch...

Entry information

Entry nameM3K1_HUMAN
AccessionPrimary (citable) accession number: Q13233
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 144 of the entry and version 4 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 5

Human chromosome 5: entries, gene names and cross-references to MIM