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Q02779

- M3K10_HUMAN

UniProt

Q02779 - M3K10_HUMAN

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Protein

Mitogen-activated protein kinase kinase kinase 10

Gene
MAP3K10, MLK2, MST
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Activates the JUN N-terminal pathway.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Homodimerization via the leucine zipper domains is required for autophosphorylation and subsequent activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251ATPPROSITE-ProRule annotations
Active sitei222 – 2221Proton acceptorPROSITE-ProRule annotations

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 1129ATPPROSITE-ProRule annotations

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. bHLH transcription factor binding Source: UniProtKB
  3. JUN kinase kinase kinase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. protein kinase activity Source: ProtInc
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. activation of JNKK activity Source: GOC
  2. activation of JUN kinase activity Source: UniProtKB
  3. apoptotic process Source: ProtInc
  4. JNK cascade Source: ProtInc
  5. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. peptidyl-serine phosphorylation Source: UniProtKB
  8. peptidyl-threonine phosphorylation Source: UniProtKB
  9. positive regulation of apoptotic process Source: Ensembl
  10. positive regulation of JNK cascade Source: UniProtKB
  11. positive regulation of JUN kinase activity Source: UniProtKB
  12. protein autophosphorylation Source: UniProtKB
  13. signal transduction Source: ProtInc
  14. smoothened signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ02779.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase 10 (EC:2.7.11.25)
Alternative name(s):
Mixed lineage kinase 2
Protein kinase MST
Gene namesi
Name:MAP3K10
Synonyms:MLK2, MST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Organism-specific databases

HGNCiHGNC:6849. MAP3K10.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 954954Mitogen-activated protein kinase kinase kinase 10PRO_0000086259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei258 – 2581Phosphothreonine; by autocatalysis
Modified residuei262 – 2621Phosphoserine; by autocatalysis and MAP4K1
Modified residuei498 – 4981Phosphoserine1 Publication
Modified residuei502 – 5021Phosphoserine1 Publication
Modified residuei506 – 5061Phosphoserine1 Publication
Modified residuei558 – 5581Phosphothreonine1 Publication

Post-translational modificationi

Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ02779.
PRIDEiQ02779.

PTM databases

PhosphoSiteiQ02779.

Expressioni

Tissue specificityi

Expressed in brain and skeletal muscle.

Gene expression databases

ArrayExpressiQ02779.
BgeeiQ02779.
CleanExiHS_MAP3K10.
GenevestigatoriQ02779.

Organism-specific databases

HPAiHPA007039.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi110440. 25 interactions.
IntActiQ02779. 3 interactions.
STRINGi9606.ENSP00000253055.

Structurei

Secondary structure

1
954
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 234
Beta strandi42 – 476
Helixi50 – 534
Beta strandi58 – 625
Beta strandi68 – 725
Helixi73 – 753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RF0X-ray2.00A/B/C/D13-78[»]
ProteinModelPortaliQ02779.
SMRiQ02779. Positions 17-78, 92-385.

Miscellaneous databases

EvolutionaryTraceiQ02779.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 8166SH3PROSITE-ProRule annotationsAdd
BLAST
Domaini98 – 360263Protein kinasePROSITE-ProRule annotationsAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni384 – 40522Leucine-zipper 1Add
BLAST
Regioni419 – 44022Leucine-zipper 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 54Poly-Glu
Compositional biasi449 – 46315Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000060081.
HOVERGENiHBG067662.
InParanoidiQ02779.
KOiK04418.
OMAiKGHFKKS.
OrthoDBiEOG7D85VN.
PhylomeDBiQ02779.
TreeFamiTF105118.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR015785. MAP3K10.
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.
[Graphical view]
PANTHERiPTHR23257:SF370. PTHR23257:SF370. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000556. MAPKKK9_11. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00326. SH3. 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]

Sequencei

Sequence statusi: Complete.

Q02779-1 [UniParc]FASTAAdd to Basket

« Hide

MEEEEGAVAK EWGTTPAGPV WTAVFDYEAA GDEELTLRRG DRVQVLSQDC    50
AVSGDEGWWT GQLPSGRVGV FPSNYVAPGA PAAPAGLQLP QEIPFHELQL 100
EEIIGVGGFG KVYRALWRGE EVAVKAARLD PEKDPAVTAE QVCQEARLFG 150
ALQHPNIIAL RGACLNPPHL CLVMEYARGG ALSRVLAGRR VPPHVLVNWA 200
VQVARGMNYL HNDAPVPIIH RDLKSINILI LEAIENHNLA DTVLKITDFG 250
LAREWHKTTK MSAAGTYAWM APEVIRLSLF SKSSDVWSFG VLLWELLTGE 300
VPYREIDALA VAYGVAMNKL TLPIPSTCPE PFARLLEECW DPDPHGRPDF 350
GSILKRLEVI EQSALFQMPL ESFHSLQEDW KLEIQHMFDD LRTKEKELRS 400
REEELLRAAQ EQRFQEEQLR RREQELAERE MDIVERELHL LMCQLSQEKP 450
RVRKRKGNFK RSRLLKLREG GSHISLPSGF EHKITVQASP TLDKRKGSDG 500
ASPPASPSII PRLRAIRLTP VDCGGSSSGS SSGGSGTWSR GGPPKKEELV 550
GGKKKGRTWG PSSTLQKERV GGEERLKGLG EGSKQWSSSA PNLGKSPKHT 600
PIAPGFASLN EMEEFAEAED GGSSVPPSPY STPSYLSVPL PAEPSPGARA 650
PWEPTPSAPP ARWGHGARRR CDLALLGCAT LLGAVGLGAD VAEARAADGE 700
EQRRWLDGLF FPRAGRFPRG LSPPARPHGR REDVGPGLGL APSATLVSLS 750
SVSDCNSTRS LLRSDSDEAA PAAPSPPPSP PAPTPTPSPS TNPLVDLELE 800
SFKKDPRQSL TPTHVTAACA VSRGHRRTPS DGALGQRGPP EPAGHGPGPR 850
DLLDFPRLPD PQALFPARRR PPEFPGRPTT LTFAPRPRPA ASRPRLDPWK 900
LVSFGRTLTI SPPSRPDTPE SPGPPSVQPT LLDMDMEGQN QDSTVPLCGA 950
HGSH 954
Length:954
Mass (Da):103,694
Last modified:April 17, 2007 - v3
Checksum:i59A7596B05751981
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071G → E in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_040702
Natural varianti168 – 1681P → Q.
Corresponds to variant rs36102209 [ dbSNP | Ensembl ].
VAR_051639

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti462 – 4643SRL → AV in CAA88531. 1 Publication
Sequence conflicti465 – 48016LKLRE…LPSGF → AQAAGRRQPHQPALWL1 PublicationAdd
BLAST
Sequence conflicti471 – 4711G → S in CAA88531. 1 Publication
Sequence conflicti807 – 8071R → G in CAA62351. 1 Publication
Sequence conflicti818 – 8181A → V in CAA62351. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X90846 mRNA. Translation: CAA62351.1.
Z48615 mRNA. Translation: CAA88531.1.
CCDSiCCDS12549.1.
PIRiS68178.
RefSeqiNP_002437.2. NM_002446.3.
UniGeneiHs.466743.

Genome annotation databases

EnsembliENST00000253055; ENSP00000253055; ENSG00000130758.
GeneIDi4294.
KEGGihsa:4294.
UCSCiuc002ona.3. human.

Polymorphism databases

DMDMi145559494.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X90846 mRNA. Translation: CAA62351.1 .
Z48615 mRNA. Translation: CAA88531.1 .
CCDSi CCDS12549.1.
PIRi S68178.
RefSeqi NP_002437.2. NM_002446.3.
UniGenei Hs.466743.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RF0 X-ray 2.00 A/B/C/D 13-78 [» ]
ProteinModelPortali Q02779.
SMRi Q02779. Positions 17-78, 92-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110440. 25 interactions.
IntActi Q02779. 3 interactions.
STRINGi 9606.ENSP00000253055.

Chemistry

BindingDBi Q02779.
ChEMBLi CHEMBL2873.
GuidetoPHARMACOLOGYi 2070.

PTM databases

PhosphoSitei Q02779.

Polymorphism databases

DMDMi 145559494.

Proteomic databases

PaxDbi Q02779.
PRIDEi Q02779.

Protocols and materials databases

DNASUi 4294.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253055 ; ENSP00000253055 ; ENSG00000130758 .
GeneIDi 4294.
KEGGi hsa:4294.
UCSCi uc002ona.3. human.

Organism-specific databases

CTDi 4294.
GeneCardsi GC19P040697.
H-InvDB HIX0040140.
HGNCi HGNC:6849. MAP3K10.
HPAi HPA007039.
MIMi 600137. gene.
neXtProti NX_Q02779.
PharmGKBi PA30593.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000060081.
HOVERGENi HBG067662.
InParanoidi Q02779.
KOi K04418.
OMAi KGHFKKS.
OrthoDBi EOG7D85VN.
PhylomeDBi Q02779.
TreeFami TF105118.

Enzyme and pathway databases

SignaLinki Q02779.

Miscellaneous databases

ChiTaRSi MAP3K10. human.
EvolutionaryTracei Q02779.
GeneWikii MAP3K10.
GenomeRNAii 4294.
NextBioi 16901.
PROi Q02779.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q02779.
Bgeei Q02779.
CleanExi HS_MAP3K10.
Genevestigatori Q02779.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR015785. MAP3K10.
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.
[Graphical view ]
PANTHERi PTHR23257:SF370. PTHR23257:SF370. 1 hit.
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PIRSFi PIRSF000556. MAPKKK9_11. 1 hit.
PRINTSi PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence, expression, and chromosomal localisation of human mixed-lineage kinase 2."
    Dorow D.S., Devereux L., Tu G.F., Price G., Nicholl J.K., Sutherland G.R., Simpson R.J.
    Eur. J. Biochem. 234:492-500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Cloning and characterization of MST, a novel (putative) serine/threonine kinase with SH3 domain."
    Katoh M., Hirai M., Sugimura T., Terada M.
    Oncogene 10:1447-1451(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "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 244-480.
    Tissue: Colon epithelium.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; SER-502 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "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: VARIANT [LARGE SCALE ANALYSIS] GLU-107.

Entry informationi

Entry nameiM3K10_HUMAN
AccessioniPrimary (citable) accession number: Q02779
Secondary accession number(s): Q12761, Q14871
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 17, 2007
Last modified: October 1, 2014
This is version 146 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 19
    Human chromosome 19: 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

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