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Protein

Mitogen-activated protein kinase kinase kinase 9

Gene

MAP3K9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

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.3 Publications

Kineticsi

  1. KM=62 µM for ATP1 Publication
  2. KM=7 µM for myelin basic protein (MBP) as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711ATP
Active sitei268 – 2681Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1589ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. JUN kinase kinase kinase activity Source: UniProtKB
  3. MAP kinase kinase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. protein tyrosine kinase activity Source: InterPro

GO - Biological processi

  1. activation of JNKK activity Source: GOC
  2. activation of JUN kinase activity Source: UniProtKB
  3. apoptotic process Source: UniProtKB-KW
  4. positive regulation of apoptotic process Source: Ensembl
  5. protein autophosphorylation Source: UniProtKB
  6. protein phosphorylation Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP80192.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase 9 (EC:2.7.11.25)
Alternative name(s):
Mixed lineage kinase 1
Gene namesi
Name:MAP3K9
Synonyms:MLK1, PRKE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:6861. MAP3K9.

Pathology & Biotechi

Involvement in diseasei

May play a role in esophageal cancer susceptibility and/or development.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711K → A: Loss of kinase activity and threonine phosphorylation. 1 Publication
Mutagenesisi304 – 3041T → A: Reduces threonine phosphorylation. Impairs JNK activation. 1 Publication
Mutagenesisi305 – 3051T → A: Little effect on threonine phosphorylation. Mildly impairs JNK activation. 1 Publication
Mutagenesisi308 – 3081S → A: Impairs JNK activation. 1 Publication
Mutagenesisi312 – 3121T → A: Loss of threonine phosphorylation. Strongly impairs JNK activation. 1 Publication

Organism-specific databases

PharmGKBiPA30607.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11041104Mitogen-activated protein kinase kinase kinase 9PRO_0000086258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041Phosphothreonine; by autocatalysis1 Publication
Modified residuei305 – 3051Phosphothreonine; by autocatalysis1 Publication
Modified residuei308 – 3081Phosphoserine; by autocatalysis1 Publication
Modified residuei312 – 3121Phosphothreonine; by autocatalysis1 Publication

Post-translational modificationi

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-308.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP80192.
PRIDEiP80192.

PTM databases

PhosphoSiteiP80192.

Expressioni

Tissue specificityi

Expressed in epithelial tumor cell lines of colonic, breast and esophageal origin.1 Publication

Gene expression databases

BgeeiP80192.
CleanExiHS_MAP3K9.
ExpressionAtlasiP80192. baseline and differential.
GenevestigatoriP80192.

Organism-specific databases

HPAiHPA000942.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-3951604,EBI-352572

Protein-protein interaction databases

BioGridi110439. 1 interaction.
IntActiP80192. 1 interaction.
STRINGi9606.ENSP00000005198.

Structurei

Secondary structure

1
1104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi143 – 15311Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi166 – 1727Combined sources
Helixi185 – 19713Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi217 – 2215Combined sources
Helixi228 – 2325Combined sources
Helixi239 – 25820Combined sources
Beta strandi259 – 2624Combined sources
Helixi271 – 2733Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi290 – 2923Combined sources
Helixi313 – 3153Combined sources
Helixi318 – 3236Combined sources
Helixi328 – 34417Combined sources
Turni348 – 3514Combined sources
Helixi354 – 3629Combined sources
Helixi376 – 38510Combined sources
Helixi390 – 3923Combined sources
Helixi396 – 4049Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DTCX-ray2.60A136-406[»]
ProteinModelPortaliP80192.
SMRiP80192. Positions 55-113, 126-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80192.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 11665SH3PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 412269Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni430 – 45122Leucine-zipper 1Add
BLAST
Regioni465 – 48622Leucine-zipper 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 4231Ala-richAdd
BLAST
Compositional biasi30 – 389Poly-Glu
Compositional biasi495 – 50915Arg/Lys-rich (basic)Add
BLAST
Compositional biasi863 – 972110Pro-richAdd
BLAST
Compositional biasi1011 – 104131Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000060081.
HOVERGENiHBG067662.
InParanoidiP80192.
KOiK04417.
OMAiHHRRCEV.
OrthoDBiEOG7D85VN.
PhylomeDBiP80192.
TreeFamiTF105118.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR016231. MAPKKK9/10/11.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000556. MAPKKK9_11. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P80192-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEPSRALLGC LASAAAAAPP GEDGAGAGAE EEEEEEEEAA AAVGPGELGC
60 70 80 90 100
DAPLPYWTAV FEYEAAGEDE LTLRLGDVVE VLSKDSQVSG DEGWWTGQLN
110 120 130 140 150
QRVGIFPSNY VTPRSAFSSR CQPGGEDPSC YPPIQLLEID FAELTLEEII
160 170 180 190 200
GIGGFGKVYR AFWIGDEVAV KAARHDPDED ISQTIENVRQ EAKLFAMLKH
210 220 230 240 250
PNIIALRGVC LKEPNLCLVM EFARGGPLNR VLSGKRIPPD ILVNWAVQIA
260 270 280 290 300
RGMNYLHDEA IVPIIHRDLK SSNILILQKV ENGDLSNKIL KITDFGLARE
310 320 330 340 350
WHRTTKMSAA GTYAWMAPEV IRASMFSKGS DVWSYGVLLW ELLTGEVPFR
360 370 380 390 400
GIDGLAVAYG VAMNKLALPI PSTCPEPFAK LMEDCWNPDP HSRPSFTNIL
410 420 430 440 450
DQLTTIEESG FFEMPKDSFH CLQDNWKHEI QEMFDQLRAK EKELRTWEEE
460 470 480 490 500
LTRAALQQKN QEELLRRREQ ELAEREIDIL ERELNIIIHQ LCQEKPRVKK
510 520 530 540 550
RKGKFRKSRL KLKDGNRISL PSDFQHKFTV QASPTMDKRK SLINSRSSPP
560 570 580 590 600
ASPTIIPRLR AIQLTPGESS KTWGRSSVVP KEEGEEEEKR APKKKGRTWG
610 620 630 640 650
PGTLGQKELA SGDEGSPQRR EKANGLSTPS ESPHFHLGLK SLVDGYKQWS
660 670 680 690 700
SSAPNLVKGP RSSPALPGFT SLMEMEDEDS EGPGSGESRL QHSPSQSYLC
710 720 730 740 750
IPFPRGEDGD GPSSDGIHEE PTPVNSATST PQLTPTNSLK RGGAHHRRCE
760 770 780 790 800
VALLGCGAVL AATGLGFDLL EAGKCQLLPL EEPEPPAREE KKRREGLFQR
810 820 830 840 850
SSRPRRSTSP PSRKLFKKEE PMLLLGDPSA SLTLLSLSSI SECNSTRSLL
860 870 880 890 900
RSDSDEIVVY EMPVSPVEAP PLSPCTHNPL VNVRVERFKR DPNQSLTPTH
910 920 930 940 950
VTLTTPSQPS SHRRTPSDGA LKPETLLASR SPSSNGLSPS PGAGMLKTPS
960 970 980 990 1000
PSRDPGEFPR LPDPNVVFPP TPRRWNTQQD STLERPKTLE FLPRPRPSAN
1010 1020 1030 1040 1050
RQRLDPWWFV SPSHARSTSP ANSSSTETPS NLDSCFASSS STVEERPGLP
1060 1070 1080 1090 1100
ALLPFQAGPL PPTERTLLDL DAEGQSQDST VPLCRAELNT HRPAPYEIQQ

EFWS
Length:1,104
Mass (Da):121,895
Last modified:October 17, 2006 - v3
Checksum:i0F059C867FCE7276
GO
Isoform 2 (identifier: P80192-4) [UniParc]FASTAAdd to basket

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

Show »
Length:1,118
Mass (Da):123,373
Checksum:i608E5BDC00DC09B8
GO

Sequence cautioni

The sequence AAI11408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561A → R (PubMed:8477742).Curated
Sequence conflicti433 – 4331M → T in AAQ23054 (PubMed:15610029).Curated
Sequence conflicti511 – 53525KLKDG…QASPT → AQPVLPFPHGHSRCPGGTGS SWGGQ (PubMed:8477742).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti246 – 2461A → V in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_040698
Natural varianti467 – 4671R → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040699
Natural varianti497 – 4971R → Q.1 Publication
Corresponds to variant rs56196343 [ dbSNP | Ensembl ].
VAR_040700
Natural varianti646 – 6461Y → C.1 Publication
Corresponds to variant rs34322726 [ dbSNP | Ensembl ].
VAR_040701

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei675 – 6751M → MALLAASWVVPIDIE in isoform 2. 1 PublicationVSP_013765

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327900 mRNA. Translation: AAQ23054.1.
BC111407 mRNA. Translation: AAI11408.1. Different initiation.
BC133706 mRNA. Translation: AAI33707.1.
AF251442 mRNA. Translation: AAG44591.1.
CCDSiCCDS32112.1. [P80192-4]
CCDS61488.1. [P80192-1]
PIRiS32467. JU0229.
RefSeqiNP_001271159.1. NM_001284230.1. [P80192-1]
NP_149132.2. NM_033141.3. [P80192-4]
UniGeneiHs.445496.
Hs.593542.

Genome annotation databases

EnsembliENST00000554752; ENSP00000451612; ENSG00000006432. [P80192-1]
ENST00000555993; ENSP00000451263; ENSG00000006432. [P80192-4]
GeneIDi4293.
KEGGihsa:4293.
UCSCiuc001xml.3. human. [P80192-4]
uc001xmm.3. human. [P80192-1]

Polymorphism databases

DMDMi116242625.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327900 mRNA. Translation: AAQ23054.1.
BC111407 mRNA. Translation: AAI11408.1. Different initiation.
BC133706 mRNA. Translation: AAI33707.1.
AF251442 mRNA. Translation: AAG44591.1.
CCDSiCCDS32112.1. [P80192-4]
CCDS61488.1. [P80192-1]
PIRiS32467. JU0229.
RefSeqiNP_001271159.1. NM_001284230.1. [P80192-1]
NP_149132.2. NM_033141.3. [P80192-4]
UniGeneiHs.445496.
Hs.593542.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DTCX-ray2.60A136-406[»]
ProteinModelPortaliP80192.
SMRiP80192. Positions 55-113, 126-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110439. 1 interaction.
IntActiP80192. 1 interaction.
STRINGi9606.ENSP00000005198.

Chemistry

BindingDBiP80192.
ChEMBLiCHEMBL2872.
GuidetoPHARMACOLOGYi2084.

PTM databases

PhosphoSiteiP80192.

Polymorphism databases

DMDMi116242625.

Proteomic databases

PaxDbiP80192.
PRIDEiP80192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000554752; ENSP00000451612; ENSG00000006432. [P80192-1]
ENST00000555993; ENSP00000451263; ENSG00000006432. [P80192-4]
GeneIDi4293.
KEGGihsa:4293.
UCSCiuc001xml.3. human. [P80192-4]
uc001xmm.3. human. [P80192-1]

Organism-specific databases

CTDi4293.
GeneCardsiGC14M071189.
H-InvDBHIX0011779.
HGNCiHGNC:6861. MAP3K9.
HPAiHPA000942.
MIMi600136. gene.
neXtProtiNX_P80192.
PharmGKBiPA30607.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000060081.
HOVERGENiHBG067662.
InParanoidiP80192.
KOiK04417.
OMAiHHRRCEV.
OrthoDBiEOG7D85VN.
PhylomeDBiP80192.
TreeFamiTF105118.

Enzyme and pathway databases

SignaLinkiP80192.

Miscellaneous databases

ChiTaRSiMAP3K9. human.
EvolutionaryTraceiP80192.
GeneWikiiMAP3K9.
GenomeRNAii4293.
NextBioi16897.
PROiP80192.
SOURCEiSearch...

Gene expression databases

BgeeiP80192.
CleanExiHS_MAP3K9.
ExpressionAtlasiP80192. baseline and differential.
GenevestigatoriP80192.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR016231. MAPKKK9/10/11.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000556. MAPKKK9_11. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiM3K9_HUMAN
AccessioniPrimary (citable) accession number: P80192
Secondary accession number(s): A3KN85
, Q0D2G7, Q6EH31, Q9H2N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 17, 2006
Last modified: January 7, 2015
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.