Q13233 (M3K1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.9
Post-translational modification	Autophosphorylated By similarity. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12
Involvement in disease	Defects in MAP3K1 are the cause of 46,XY sex reversal type 6 (SRXY6) [MIM:613762]. SRXY6 is a disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. Ref.14
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 diversity	Polymorphism
Domain	Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome cellular response to mechanical stimulus Inferred from expression pattern. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome toll-like receptor 1 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
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Non-traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAP2K4	P45985	3	EBI-49776,EBI-447868
MAP4K2	Q12851	2	EBI-49776,EBI-49783

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 1512	1511	Mitogen-activated protein kinase kinase kinase 1		PRO_0000086240
Regions
	Domain	1243 – 1508	266	Protein kinase
	Zinc finger	338 – 366	29	SWIM-type
	Zinc finger	443 – 492	50	RING-type
	Nucleotide binding	1249 – 1257	9	ATP By similarity
	Compositional bias	2 – 5	4	Poly-Ala
	Compositional bias	25 – 29	5	Poly-Gly
	Compositional bias	36 – 41	6	Poly-Ala
	Compositional bias	422 – 431	10	Poly-Ser
	Compositional bias	842 – 847	6	Poly-Ser
	Compositional bias	942 – 949	8	Poly-Thr
	Compositional bias	1182 – 1187	6	Poly-Glu
	Compositional bias	1216 – 1219	4	Poly-Ile
Sites
	Active site	1369	1	Proton acceptor By similarity
	Binding site	1272	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.11
	Modified residue	20	1	Phosphothreonine Ref.12
	Modified residue	21	1	Phosphoserine Ref.8 Ref.11 Ref.12
	Modified residue	35	1	Phosphoserine Ref.8 Ref.12
	Modified residue	133	1	Phosphoserine Ref.12
	Modified residue	136	1	Phosphoserine Ref.12
	Modified residue	154	1	Phosphoserine Ref.8
	Modified residue	232	1	Phosphoserine Ref.8
	Modified residue	242	1	Phosphoserine Ref.8
	Modified residue	252	1	Phosphoserine Ref.12
	Modified residue	275	1	Phosphoserine Ref.12
	Modified residue	292	1	Phosphoserine Ref.7 Ref.8 Ref.10 Ref.12
	Modified residue	297	1	Phosphoserine Ref.8 Ref.10
	Modified residue	300	1	Phosphoserine Ref.8 Ref.10
	Modified residue	507	1	Phosphoserine Ref.8 Ref.10 Ref.12
	Modified residue	511	1	Phosphoserine Ref.8 Ref.10
	Modified residue	657	1	Phosphothreonine Ref.6
	Modified residue	665	1	Phosphothreonine Ref.6
	Modified residue	923	1	Phosphoserine Ref.8 Ref.11 Ref.12
	Modified residue	1016	1	Phosphoserine Ref.12
	Modified residue	1018	1	Phosphoserine Ref.8 Ref.10 Ref.12
	Modified residue	1043	1	Phosphoserine Ref.8
	Modified residue	1157	1	Phosphoserine Ref.8 Ref.12
	Modified residue	1400	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	1412	1	Phosphothreonine; by autocatalysis By similarity
Natural variations
	Natural variant	92	1	S → N. Ref.13		VAR_040680
	Natural variant	189	1	L → 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.14		VAR_065504
	Natural variant	189	1	L → 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.14		VAR_065505
	Natural variant	211	1	V → VIQ in SRXY6.		VAR_065506
	Natural variant	443	1	C → S. Ref.13		VAR_040681
	Natural variant	616	1	G → R in SRXY6. Ref.14		VAR_065507
	Natural variant	806	1	D → N. Corresponds to variant rs702689 [ dbSNP | Ensembl ].		VAR_051636
	Natural variant	906	1	V → I. Corresponds to variant rs832582 [ dbSNP | Ensembl ].		VAR_051637
Experimental info
	Sequence conflict	20	1	T → P in AAC97073. Ref.2
	Sequence conflict	37	1	P → R in AAC97073. Ref.2
	Sequence conflict	120	1	G → R in AAC97073. Ref.2
	Sequence conflict	351	1	R → H in AAC97073. Ref.2
	Sequence conflict	845	1	S → SV in AAC97073. Ref.2
	Sequence conflict	859	1	I → Y in AAC97073. Ref.2
	Sequence conflict	878 – 902	25	DGQQD…ENSSP → QRQQHNSFCRHLFPTTIWKP QRTVPL in AAC97073. Ref.2
	Sequence conflict	933	1	S → R in AAC97073. Ref.2
	Sequence conflict	1097	1	C → L in AAC97073. Ref.2
	Sequence conflict	1104 – 1107	4	AVIP → CCYT in AAC97073. Ref.2
	Sequence conflict	1200	1	D → V in AAC97073. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q13233 [UniParc]. Last modified December 16, 2008. Version 4. Checksum: 5CB78242295411D9	FASTA	1,512	164,470
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 15372022] [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: 9808624] [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: 8597633] [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: 12223491] [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: 15262978] [Abstract] Cited for: INTERACTION WITH AXIN1.
[6]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-657 AND THR-665, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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-292, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-21; SER-35; SER-154; SER-232; SER-242; SER-292; SER-297; SER-300; SER-507; SER-511; SER-923; SER-1018; SER-1043 AND SER-1157, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 17906693] [Abstract] Cited for: INTERACTION WITH STK38.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-297; SER-300; SER-507; SER-511 AND SER-1018, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-923, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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 THR-20; SER-21; SER-35; SER-133; SER-136; SER-252; SER-275; SER-292; SER-507; SER-923; SER-1016; SER-1018 AND SER-1157, MASS SPECTROMETRY.
[13]	"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: VARIANTS [LARGE SCALE ANALYSIS] ASN-92 AND SER-443.
[14]	"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. , David A., Greenfield A., Sinclair A., Ostrer H. Am. J. Hum. Genet. 87:898-904(2010) [PubMed: 21129722] [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.
IPI	IPI00855985.
PIR	G01887.
RefSeq	NP_005912.1. NM_005921.1.
UniGene	Hs.653654.
3D structure databases
ProteinModelPortal	Q13233.
SMR	Q13233. Positions 429-497, 1243-1509.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27520N.
IntAct	Q13233. 15 interactions.
MINT	MINT-143285.
STRING	Q13233.
PTM databases
PhosphoSite	Q13233.
Polymorphism databases
DMDM	218512139.
2D gel databases
SWISS-2DPAGE	Q13233.
Proteomic databases
PRIDE	Q13233.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000399503; ENSP00000382423; ENSG00000095015.
GeneID	4214.
KEGG	hsa:4214.
Organism-specific databases
CTD	4214.
GeneCards	GC05P056146.
H-InvDB	HIX0024789.
HGNC	HGNC:6848. MAP3K1.
HPA	CAB004500.
MIM	600982. gene. 613762. phenotype.
neXtProt	NX_Q13233.
Orphanet	242. 46,XY complete gonadal dysgenesis.
PharmGKB	PA30592.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09698.
GeneTree	ENSGT00600000084224.
HOGENOM	HBG282047.
HOVERGEN	HBG006302.
InParanoid	Q13233.
OMA	QGFVPCK.
OrthoDB	EOG4F1X27.
PhylomeDB	Q13233.
Enzyme and pathway databases
Pathway_Interaction_DB	bcr_5pathway. BCR signaling pathway. caspase_pathway. Caspase cascade in apoptosis. ceramidepathway. Ceramide signaling pathway. faspathway. FAS signaling pathway (CD95). fcer1pathway. Fc-epsilon receptor I signaling in mast cells. ifngpathway. IFN-gamma pathway. tcrjnkpathway. JNK signaling in the CD4+ TCR pathway. avb3_opn_pathway. Osteopontin-mediated events. p38_mkk3_6pathway. p38 MAPK signaling pathway. smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling. nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes. tnfpathway. TNF receptor signaling pathway. trail_pathway. TRAIL signaling pathway.
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q13233.
Bgee	Q13233.
CleanEx	HS_MAP3K1.
Genevestigator	Q13233.
GermOnline	ENSG00000095015. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR007527. Znf_SWIM. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KO	K04416.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00184. RING. 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. 1 hit. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. PS50966. ZF_SWIM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	16613.
SOURCE	Search...

Entry information

Entry name

M3K1_HUMAN

Accession

Primary (citable) accession number: Q13233

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 16, 2008
Last modified:	January 25, 2012
This is version 120 of the entry and version 4 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.