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Q7T2V3 (M3K10_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase kinase kinase 10

EC=2.7.11.25
Alternative name(s):
Mixed lineage kinase 2
Short name=xMLK2
Gene names
Name:map3k10
Synonyms:mlk2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length1005 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates the JUN N-terminal pathway. Essential for pronephros and cement gland development. Ref.1 Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

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

Subunit structure

Homodimer. Binds to the GTPase rac1 but not cdc42 or rhoA. Interacts (via kinase domain) with pak1 (via kinase domain). Interacts with the ubiquitin-conjugating enzyme ube2d4. Ref.1 Ref.2 Ref.3

Tissue specificity

In adults, strongly expressed in the brain and spleen with lower levels in pancreas, heart, muscle and kidney (at protein level). In the developing embryo, expressed at stage 22 in the cement gland. Weakly expressed in the pronephros from stage 24 or 25, with expression increasing in strength by stage 30 and continuing at least until stage 37. Expression in the developing pronephros correlates with epithelialization of the proximal pronephric tubules. Ref.1

Developmental stage

Expressed zygotically from stages 12 to 14 (late gastrula to early neurula), increasing in concentration up to stages 40 to 45 (late tadpole). Expression continues through to adults. Ref.1

Post-translational modification

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

Mono- and poly-ubiquitinated.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10051005Mitogen-activated protein kinase kinase kinase 10
PRO_0000277827

Regions

Domain32 – 9665SH3
Domain118 – 380263Protein kinase
Nucleotide binding124 – 1329ATP By similarity
Region404 – 42522Leucine-zipper 1
Region439 – 46022Leucine-zipper 2
Compositional bias724 – 76542Ser-rich

Sites

Active site2421Proton acceptor By similarity
Binding site1451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7T2V3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B406102A77244309

FASTA1,005111,875
        10         20         30         40         50         60 
MDGLPKDEAF LWQSSKDNKE NGVWSDVQSY GVSNPLWMAV FDYEPTAEEE LTLRRGDLVE 

        70         80         90        100        110        120 
ILSKDSTVSG DEGWWTGKIK DKVGIFPSNY VVSDDKYTTL TGAPKQCPLP LEIEFDELNL 

       130        140        150        160        170        180 
DEIIGVGGFG KVYKGLWRDE EVAVKAVRHD PDEDINVTAE NVRQEAKIFC MLCHPNIIAL 

       190        200        210        220        230        240 
TGVCLKPPHL CLVMEYARGG PLHRALAGKK VPAHVLVNWA VQIAKGMTYL HNEAIVPIIH 

       250        260        270        280        290        300 
RDLGSSNILI LEKAENDDLF NKTLNITDFG LAREWQKTTK MSAAGTYAWM APEVIRLSLF 

       310        320        330        340        350        360 
SKSSDVWSFG VLLWELLTGE VPYREIDALA VAYGVAMNKL TLPIPSTCPE PFVRILEACW 

       370        380        390        400        410        420 
DPDPHSRPTF SCILEQLTTI EQSAMFQMPL ESFHSLQEDW RLEIQQMFDE LRTKEKELRS 

       430        440        450        460        470        480 
REEELVRAAE EQRILEDLLK RREQELAERE IDIVERELNI IMYQMYQEKP KVKKRKGNFK 

       490        500        510        520        530        540 
KSRLKLKDGN RISLPSGFEH KITVQASPML DKCKGQGTSS YSPPGSPLII PRLRAIRLTP 

       550        560        570        580        590        600 
VDGSKTWGRS SVLKKEEVTT SNKKKGRTWG PSSTQQKERV GGEERLKTLG EGNKQWSSSA 

       610        620        630        640        650        660 
PNLGKSPKHT PISVGFASLT EMEEYADSDG SVPQSPYSQS YLTLPVQSDH RSHPEDTAHA 

       670        680        690        700        710        720 
GAPSSDSPKR GSQSRRKSEL VLLGCASLLA AVALGSDLSE LVPQEEKRKG IFQWAGRGPR 

       730        740        750        760        770        780 
RRASSPSRSM SYGEDSVIPS SSVTLISLSS ISDCNSTRSL IRSDSDDIGL DHDNVSSGRG 

       790        800        810        820        830        840 
VKEDRGQQPN VGSNPLVDYK VESFKRDPKQ SLTPTHVTVG RNNTTETRGH RRTPSDGAIR 

       850        860        870        880        890        900 
QVTQGHKRSP SDGSTPYQCE PEPSPFPRLP DPHFVFPPPV RRKDTGVERP TSLEFAPRPR 

       910        920        930        940        950        960 
PSSNRPRMDP WKFVSLSQTH SSSPSSGGGD ACSSGSAEGA QVADVEETLL DMEVEGQRLD 

       970        980        990       1000 
STVPLCGLGL RPTTDPFFKY GNRRVLMKEL SISLLQYKVE SGVLL 

« Hide

References

[1]"A tissue restricted role for the Xenopus Jun N-terminal kinase kinase kinase MLK2 in cement gland and pronephric tubule differentiation."
Poitras L., Bisson N., Islam N., Moss T.
Dev. Biol. 254:200-214(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAC1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Tail bud.
[2]"PAK interacts with NCK and MLK2 to regulate the activation of jun N-terminal kinase."
Poitras L., Jean S., Islam N., Moss T.
FEBS Lett. 543:129-135(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAK1.
[3]"A ubiquitin-conjugating enzyme, ube2d3.2, regulates xMLK2 and pronephros formation in Xenopus."
Jean S., Moss T.
Differentiation 76:431-441(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE2D4, HOMODIMERIZATION, UBIQUITINATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF510499 mRNA. Translation: AAP46399.1.
RefSeqNP_001082629.1. NM_001089160.1.
UniGeneXl.26500.

3D structure databases

ProteinModelPortalQ7T2V3.
SMRQ7T2V3. Positions 33-91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid99942. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398612.
KEGGxla:398612.

Organism-specific databases

CTD4294.
XenbaseXB-GENE-920952. map3k10.

Phylogenomic databases

HOVERGENHBG067662.
KOK04418.

Family and domain databases

InterProIPR011009. 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.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR23257:SF370. PTHR23257:SF370. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFPIRSF000556. MAPKKK9_11. 1 hit.
PRINTSPR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameM3K10_XENLA
AccessionPrimary (citable) accession number: Q7T2V3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families