P80192 (M3K9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase kinase kinase 9
EC=2.7.11.25

Alternative name(s):
Mixed lineage kinase 1

Gene names

Name:	MAP3K9
Synonyms:	MLK1, PRKE1

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	1104 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Ref.1 Ref.6 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Homodimerization via the leucine zipper domains is required for autophosphorylation of multiple sites in the activation loop and subsequent activation. Autophosphorylation at Thr-312 is the key step in activation of MAP3K9/MLK1 and is required for full phosphorylation. Autophosphorylation at Thr-304 and Ser-308 have been shown to be of secondary importance in the activation of MAP3K9/MLK1. CEP-1347 and many indolocarbazole analogs have been shown to act as inhibitors of MAP3K9/MLK1 activity. Ref.1 Ref.5 Ref.7
Subunit structure	Homodimer By similarity.
Tissue specificity	Expressed in epithelial tumor cell lines of colonic, breast and esophageal origin. Ref.4
Post-translational modification	Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-312 is likely to be the main autophosphorylation site. Autophosphorylation also occurs on Thr-304 and Ser-308.
Involvement in disease	May play a role in esophageal cancer susceptibility and/or development.
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 SH3 domain.
Biophysicochemical properties	Kinetic parameters: KM=62 µM for ATP Ref.5 KM=7 µM for myelin basic protein (MBP) as substrate
Sequence caution	The sequence AAI11408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Apoptosis Stress response Transcription Transcription regulation
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain
Ligand	ATP-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	activation of JUN kinase activity Inferred from sequence or structural similarity PubMed 8195146. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW protein autophosphorylation Inferred from direct assay Ref.1. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Non-traceable author statement. Source: UniProtKB JUN kinase kinase kinase activity Inferred from sequence or structural similarity. Source: UniProtKB MAP kinase kinase activity Non-traceable author statement Ref.4. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity PubMed 8195146. Source: UniProtKB protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-3951604,EBI-352572

Alternative products

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

Isoform 1 (identifier: P80192-1)

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: P80192-4)

The sequence of this isoform differs from the canonical sequence as follows:
     675-675: M → MALLAASWVVPIDIE

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1104

1104

Mitogen-activated protein kinase kinase kinase 9

PRO_0000086258

Regions

Domain

52 – 116

65

SH3

Domain

144 – 412

269

Protein kinase

Nucleotide binding

150 – 158

9

ATP By similarity

Region

430 – 451

22

Leucine-zipper 1

Region

465 – 486

22

Leucine-zipper 2

Compositional bias

12 – 42

31

Ala-rich

Compositional bias

30 – 38

9

Poly-Glu

Compositional bias

495 – 509

15

Arg/Lys-rich (basic)

Compositional bias

863 – 972

110

Pro-rich

Compositional bias

1011 – 1041

31

Ser-rich

Sites

Active site

268

1

Proton acceptor By similarity

Binding site

171

1

ATP

Amino acid modifications

Modified residue

304

1

Phosphothreonine; by autocatalysis Ref.1

Modified residue

305

1

Phosphothreonine; by autocatalysis Ref.1

Modified residue

308

1

Phosphoserine; by autocatalysis Ref.1

Modified residue

312

1

Phosphothreonine; by autocatalysis Ref.1

Natural variations

Alternative sequence

675

1

M → MALLAASWVVPIDIE in isoform 2.

VSP_013765

Natural variant

246

1

A → V in a metastatic melanoma sample; somatic mutation. Ref.11

VAR_040698

Natural variant

467

1

R → C in a gastric adenocarcinoma sample; somatic mutation. Ref.11

VAR_040699

Natural variant

497

1

R → Q. Ref.11
Corresponds to variant rs56196343 [ dbSNP | Ensembl ].

VAR_040700

Natural variant

646

1

Y → C. Ref.11
Corresponds to variant rs34322726 [ dbSNP | Ensembl ].

VAR_040701

Experimental info

Mutagenesis

171

1

K → A: Loss of kinase activity and threonine phosphorylation. Ref.1

Mutagenesis

304

1

T → A: Reduces threonine phosphorylation. Impairs JNK activation. Ref.1

Mutagenesis

305

1

T → A: Little effect on threonine phosphorylation. Mildly impairs JNK activation. Ref.1

Mutagenesis

308

1

S → A: Impairs JNK activation. Ref.1

Mutagenesis

312

1

T → A: Loss of threonine phosphorylation. Strongly impairs JNK activation. Ref.1

Sequence conflict

356

1

A → R Ref.4

Sequence conflict

433

1

M → T in AAQ23054. Ref.1

Sequence conflict

511 – 535

25

KLKDG…QASPT → AQPVLPFPHGHSRCPGGTGS SWGGQ Ref.4

Secondary structure

1

.

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1104

Helix Strand Turn

Details...

Beta strand

143 – 153

11

Beta strand

156 – 163

8

Beta strand

166 – 172

7

Helix

185 – 197

13

Beta strand

206 – 210

5

Beta strand

217 – 221

5

Helix

228 – 232

5

Helix

239 – 258

20

Beta strand

259 – 262

4

Helix

271 – 273

3

Beta strand

274 – 278

5

Beta strand

281 – 283

3

Beta strand

290 – 292

3

Helix

313 – 315

3

Helix

318 – 323

6

Helix

328 – 344

17

Turn

348 – 351

4

Helix

354 – 362

9

Helix

376 – 385

10

Helix

390 – 392

3

Helix

396 – 404

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 0F059C867FCE7276	FASTA	1,104	121,895
	10 20 30 40 50 60 MEPSRALLGC LASAAAAAPP GEDGAGAGAE EEEEEEEEAA AAVGPGELGC DAPLPYWTAV 70 80 90 100 110 120 FEYEAAGEDE LTLRLGDVVE VLSKDSQVSG DEGWWTGQLN QRVGIFPSNY VTPRSAFSSR 130 140 150 160 170 180 CQPGGEDPSC YPPIQLLEID FAELTLEEII GIGGFGKVYR AFWIGDEVAV KAARHDPDED 190 200 210 220 230 240 ISQTIENVRQ EAKLFAMLKH PNIIALRGVC LKEPNLCLVM EFARGGPLNR VLSGKRIPPD 250 260 270 280 290 300 ILVNWAVQIA RGMNYLHDEA IVPIIHRDLK SSNILILQKV ENGDLSNKIL KITDFGLARE 310 320 330 340 350 360 WHRTTKMSAA GTYAWMAPEV IRASMFSKGS DVWSYGVLLW ELLTGEVPFR GIDGLAVAYG 370 380 390 400 410 420 VAMNKLALPI PSTCPEPFAK LMEDCWNPDP HSRPSFTNIL DQLTTIEESG FFEMPKDSFH 430 440 450 460 470 480 CLQDNWKHEI QEMFDQLRAK EKELRTWEEE LTRAALQQKN QEELLRRREQ ELAEREIDIL 490 500 510 520 530 540 ERELNIIIHQ LCQEKPRVKK RKGKFRKSRL KLKDGNRISL PSDFQHKFTV QASPTMDKRK 550 560 570 580 590 600 SLINSRSSPP ASPTIIPRLR AIQLTPGESS KTWGRSSVVP KEEGEEEEKR APKKKGRTWG 610 620 630 640 650 660 PGTLGQKELA SGDEGSPQRR EKANGLSTPS ESPHFHLGLK SLVDGYKQWS SSAPNLVKGP 670 680 690 700 710 720 RSSPALPGFT SLMEMEDEDS EGPGSGESRL QHSPSQSYLC IPFPRGEDGD GPSSDGIHEE 730 740 750 760 770 780 PTPVNSATST PQLTPTNSLK RGGAHHRRCE VALLGCGAVL AATGLGFDLL EAGKCQLLPL 790 800 810 820 830 840 EEPEPPAREE KKRREGLFQR SSRPRRSTSP PSRKLFKKEE PMLLLGDPSA SLTLLSLSSI 850 860 870 880 890 900 SECNSTRSLL RSDSDEIVVY EMPVSPVEAP PLSPCTHNPL VNVRVERFKR DPNQSLTPTH 910 920 930 940 950 960 VTLTTPSQPS SHRRTPSDGA LKPETLLASR SPSSNGLSPS PGAGMLKTPS PSRDPGEFPR 970 980 990 1000 1010 1020 LPDPNVVFPP TPRRWNTQQD STLERPKTLE FLPRPRPSAN RQRLDPWWFV SPSHARSTSP 1030 1040 1050 1060 1070 1080 ANSSSTETPS NLDSCFASSS STVEERPGLP ALLPFQAGPL PPTERTLLDL DAEGQSQDST 1090 1100 VPLCRAELNT HRPAPYEIQQ EFWS
	Isoform 2 [UniParc]. Checksum: 608E5BDC00DC09B8	FASTA	1,118	123,373
	10 20 30 40 50 60 MEPSRALLGC LASAAAAAPP GEDGAGAGAE EEEEEEEEAA AAVGPGELGC DAPLPYWTAV 70 80 90 100 110 120 FEYEAAGEDE LTLRLGDVVE VLSKDSQVSG DEGWWTGQLN QRVGIFPSNY VTPRSAFSSR 130 140 150 160 170 180 CQPGGEDPSC YPPIQLLEID FAELTLEEII GIGGFGKVYR AFWIGDEVAV KAARHDPDED 190 200 210 220 230 240 ISQTIENVRQ EAKLFAMLKH PNIIALRGVC LKEPNLCLVM EFARGGPLNR VLSGKRIPPD 250 260 270 280 290 300 ILVNWAVQIA RGMNYLHDEA IVPIIHRDLK SSNILILQKV ENGDLSNKIL KITDFGLARE 310 320 330 340 350 360 WHRTTKMSAA GTYAWMAPEV IRASMFSKGS DVWSYGVLLW ELLTGEVPFR GIDGLAVAYG 370 380 390 400 410 420 VAMNKLALPI PSTCPEPFAK LMEDCWNPDP HSRPSFTNIL DQLTTIEESG FFEMPKDSFH 430 440 450 460 470 480 CLQDNWKHEI QEMFDQLRAK EKELRTWEEE LTRAALQQKN QEELLRRREQ ELAEREIDIL 490 500 510 520 530 540 ERELNIIIHQ LCQEKPRVKK RKGKFRKSRL KLKDGNRISL PSDFQHKFTV QASPTMDKRK 550 560 570 580 590 600 SLINSRSSPP ASPTIIPRLR AIQLTPGESS KTWGRSSVVP KEEGEEEEKR APKKKGRTWG 610 620 630 640 650 660 PGTLGQKELA SGDEGSPQRR EKANGLSTPS ESPHFHLGLK SLVDGYKQWS SSAPNLVKGP 670 680 690 700 710 720 RSSPALPGFT SLMEMALLAA SWVVPIDIEE DEDSEGPGSG ESRLQHSPSQ SYLCIPFPRG 730 740 750 760 770 780 EDGDGPSSDG IHEEPTPVNS ATSTPQLTPT NSLKRGGAHH RRCEVALLGC GAVLAATGLG 790 800 810 820 830 840 FDLLEAGKCQ LLPLEEPEPP AREEKKRREG LFQRSSRPRR STSPPSRKLF KKEEPMLLLG 850 860 870 880 890 900 DPSASLTLLS LSSISECNST RSLLRSDSDE IVVYEMPVSP VEAPPLSPCT HNPLVNVRVE 910 920 930 940 950 960 RFKRDPNQSL TPTHVTLTTP SQPSSHRRTP SDGALKPETL LASRSPSSNG LSPSPGAGML 970 980 990 1000 1010 1020 KTPSPSRDPG EFPRLPDPNV VFPPTPRRWN TQQDSTLERP KTLEFLPRPR PSANRQRLDP 1030 1040 1050 1060 1070 1080 WWFVSPSHAR STSPANSSST ETPSNLDSCF ASSSSTVEER PGLPALLPFQ AGPLPPTERT 1090 1100 1110 LLDLDAEGQS QDSTVPLCRA ELNTHRPAPY EIQQEFWS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phosphoregulation of mixed-lineage kinase 1 activity by multiple phosphorylation in the activation loop." Durkin J.T., Holskin B.P., Kopec K.K., Reed M.S., Spais C.M., Steffy B.M., Gessner G., Angeles T.S., Pohl J., Ator M.A., Meyer S.L. Biochemistry 43:16348-16355(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-304; THR-305; SER-308 AND THR-312, MUTAGENESIS OF LYS-171; THR-304; THR-305; SER-308 AND THR-312.
[2]	"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] (ISOFORM 1).
[3]	"cDNA sequence and gene organisation of mixed lineage kinase 1." McNee J.J., Dower S.K., Guesdon F. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-1104 (ISOFORM 2).
[4]	"Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains." Dorow D.S., Devereux L., Dietzsch E., de Kretser T. Eur. J. Biochem. 213:701-710(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-535, TISSUE SPECIFICITY. Tissue: Colon epithelium.
[5]	"Cep-1347 (KT7515), a semisynthetic inhibitor of the mixed lineage kinase family." Maroney A.C., Finn J.P., Connors T.J., Durkin J.T., Angeles T., Gessner G., Xu Z., Meyer S.L., Savage M.J., Greene L.A., Scott R.W., Vaught J.L. J. Biol. Chem. 276:25302-25308(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION OF MAP2K4/MKK4.
[6]	"The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis." Xu Z., Maroney A.C., Dobrzanski P., Kukekov N.V., Greene L.A. Mol. Cell. Biol. 21:4713-4724(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE APOPTOSIS PATHWAY.
[7]	"Mixed lineage kinase activity of indolocarbazole analogues." Murakata C., Kaneko M., Gessner G., Angeles T.S., Ator M.A., O'Kane T.M., McKenna B.A., Thomas B.A., Mathiasen J.R., Saporito M.S., Bozyczko-Coyne D., Hudkins R.L. Bioorg. Med. Chem. Lett. 12:147-150(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Genomic profiling of 766 cancer-related genes in archived esophageal normal and carcinoma tissues." Chen J., Guo L., Peiffer D.A., Zhou L., Chan O.T., Bibikova M., Wickham-Garcia E., Lu S.H., Zhan Q., Wang-Rodriguez J., Jiang W., Fan J.B. Int. J. Cancer 122:2249-2254(2008) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE ROLE IN ESOPHAGEAL CANCER.
[9]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Mixed-lineage kinase 1 and mixed-lineage kinase 3 subtype-selective dihydronaphthyl[3,4-a]pyrrolo[3,4-c]carbazole-5-ones: optimization, mixed-lineage kinase 1 crystallography, and oral in vivo activity in 1-methyl-4-phenyltetrahydropyridine models." Hudkins R.L., Diebold J.L., Tao M., Josef K.A., Park C.H., Angeles T.S., Aimone L.D., Husten J., Ator M.A., Meyer S.L., Holskin B.P., Durkin J.T., Fedorov A.A., Fedorov E.V., Almo S.C., Mathiasen J.R., Bozyczko-Coyne D., Saporito M.S., Scott R.W., Mallamo J.P. J. Med. Chem. 51:5680-5689(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 136-406.
[11]	"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-246; CYS-467; GLN-497 AND CYS-646.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY327900 mRNA. Translation: AAQ23054.1.
BC111407 mRNA. Translation: AAI11408.1. Different initiation.
BC133706 mRNA. Translation: AAI33707.1.
AF251442 mRNA. Translation: AAG44591.1.

IPI

IPI00008115.
IPI00179189.

PIR

JU0229. S32467.

RefSeq

NP_149132.2. NM_033141.2.

UniGene

Hs.445496.
Hs.593542.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DTC	X-ray	2.60	A	136-406	[»]

ProteinModelPortal

P80192.

ModBase

Search...

Protein-protein interaction databases

IntAct

P80192. 1 interaction.

STRING

9606.ENSP00000005198.

PTM databases

PhosphoSite

P80192.

Polymorphism databases

DMDM

116242625.

Proteomic databases

PaxDb

P80192.

PRIDE

P80192.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000554752; ENSP00000451612; ENSG00000006432.
ENST00000555993; ENSP00000451263; ENSG00000006432.

GeneID

4293.

KEGG

hsa:4293.

UCSC

uc001xml.3. human.
uc001xmm.3. human.

Organism-specific databases

CTD

4293.

GeneCards

GC14M071189.

H-InvDB

HIX0011779.

HGNC

HGNC:6861. MAP3K9.

HPA

HPA000942.

MIM

600136. gene.

neXtProt

NX_P80192.

PharmGKB

PA30607.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000060081.

HOVERGEN

HBG067662.

KO

K04417.

OMA

PGAGMLK.

Gene expression databases

ArrayExpress

P80192.

Bgee

P80192.

CleanEx

HS_MAP3K9.

Genevestigator

P80192.

GermOnline

ENSG00000006432. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR016231. MAPKKK9/10/11.
IPR015785. MAPKKK9/10/11-like.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

PANTHER

PTHR23257:SF87. PTHR23257:SF87. 1 hit.

Pfam

PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000556. MAPKKK9_11. 1 hit.

PRINTS

PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P80192.

ChEMBL

CHEMBL2872.

EvolutionaryTrace

P80192.

GenomeRNAi

4293.

NextBio

16897.

SOURCE

Search...

Entry information

Entry name

M3K9_HUMAN

Accession

Primary (citable) accession number: P80192
Secondary accession number(s): A3KN85 , Q0D2G7, Q6EH31, Q9H2N5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 132 of the entry and version 3 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.