Mitogen-activated protein kinase kinase kinase 11

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q80XI6 (M3K11_MOUSE)

Last modified November 3, 2009. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase kinase kinase 11
    EC=2.7.11.25
Alternative name(s):
    Mixed lineage kinase 3

Gene names

Name:	Map3k11
Synonyms:	Mlk3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length	850 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1). Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle By similarity.
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; undergoes dimerization during activation By similarity.
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Note: Location is cell cycle dependent By similarity.
Post-translational modification	Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-278 is likely to be the main autophosphorylation site. Phosphorylation of Ser-556 and Ser-557 is induced by CDC42 By similarity.
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.

Hide | Top

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of JNK cascade Inferred from direct assay. Source: MGI
Cellular component	centrosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 850

850

Mitogen-activated protein kinase kinase kinase 11

PRO_0000277828

Regions

Domain

42 – 106

SH3

Domain

118 – 380

263

Protein kinase

Domain

404 – 425

Leucine-zipper 1 By similarity

Domain

439 – 460

Leucine-zipper 2 By similarity

Nucleotide binding

124 – 132

ATP By similarity

Compositional bias

18 – 29

Poly-Gly

Compositional bias

473 – 476

Poly-Arg

Compositional bias

600 – 823

224

Pro-rich

Sites

Active site

242

Proton acceptor By similarity

Binding site

145

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

278

Phosphothreonine; by autocatalysis By similarity

Modified residue

282

Phosphoserine; by autocatalysis and MAP4K1 By similarity

Modified residue

494

Phosphoserine By similarity

Modified residue

508

Phosphoserine By similarity

Modified residue

525

Phosphoserine By similarity

Modified residue

549

Phosphoserine By similarity

Modified residue

556

Phosphoserine By similarity

Modified residue

557

Phosphoserine By similarity

Modified residue

655

Phosphoserine By similarity

Modified residue

709

Phosphoserine By similarity

Modified residue

712

Phosphothreonine By similarity

Modified residue

728

Phosphoserine By similarity

Modified residue

731

Phosphoserine By similarity

Modified residue

741

Phosphothreonine By similarity

Modified residue

743

Phosphoserine Ref.3

Modified residue

749

Phosphoserine By similarity

Modified residue

751

Phosphoserine By similarity

Modified residue

755

Phosphothreonine By similarity

Modified residue

758

Phosphothreonine By similarity

Modified residue

761

Phosphoserine By similarity

Modified residue

773

Phosphoserine By similarity

Modified residue

792

Phosphoserine By similarity

Modified residue

796

Phosphoserine By similarity

Modified residue

818

Phosphoserine By similarity

Experimental info

Sequence conflict

457 – 458

EL → DV in AAF73281. Ref.1

Sequence conflict

840 – 841

AQ → CP in AAF73281. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q80XI6-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 96DE238A1A0E2564
Show »

FASTA

850

93,226

        10         20         30         40         50         60 
MEPLKNLFLK SPLGSWNGSG SGGGGGTGGV RPEGSPKATA AYANPVWTAL FDYEPNGQDE 

        70         80         90        100        110        120 
LALRKGDRVE VLSRDAAISG DEGWWAGQVG GQVGIFPSNY VSRGGGPPPC EVASFQELRL 

       130        140        150        160        170        180 
EEVIGIGGFG KVYRGSWRGE LVAVKAARQD PDEDISVTAE SVRQEARLFA MLAHPNIIAL 

       190        200        210        220        230        240 
KAVCLEEPNL CLVMEYAAGG PLSRALAGRR VPPHVLVNWA VQIARGMHYL HCEALVPVIH 

       250        260        270        280        290        300 
RDLKSNNILL LQPIEGDDME HKTLKITDFG LAREWHKTTQ MSAAGTYAWM APEVIKASTF 

       310        320        330        340        350        360 
SKGSDVWSFG VLLWELLTGE VPYRGIDCLA VAYGVAVNKL TLPIPSTCPE PFAQLMADCW 

       370        380        390        400        410        420 
AQDPHRRPDF ASILQQLEAL EAQVLREMPR DSFHSMQEGW KREIQGLFDE LRAKEKELLS 

       430        440        450        460        470        480 
REEELTRAAR EQRSQAEQLR RREHLLAQWE LEVFERELTL LLQQVDRERP HVRRRRGTFK 

       490        500        510        520        530        540 
RSKLRARDGG ERISMPLDFK HRITVQASPG LDRRRNVFEV GAGDSPTFPR FRAIQLEPTE 

       550        560        570        580        590        600 
SGQTWGRQSP RRLEDSSNGE RRACWAWGPS SPKPGEAQNG RRRSRMDEAT WYLDSDDSSP 

       610        620        630        640        650        660 
LGSPSTPPAL NGNPPRPSPE PEEPRRAGPT ERGNSSGTPK LIQRALLRGT ALLASLGLGR 

       670        680        690        700        710        720 
DLQPPGGLSR ERGESPTAPP PAQMPSPCPP ELPSTPLIRL SQTTPDAHSS PTPGPLLLDL 

       730        740        750        760        770        780 
GVPSGQPSAK SPRREETRGR TVSPPPGISR SAPGTPGTPR SPPLGLISRP RPSPLRSRID 

       790        800        810        820        830        840 
PWSFVSAGPR PSPLPSPQPA PRRAPWTLFP DSDPFWDSPP ANPFRGGSQD CRTQTKDMGA 

       850 
QAPWAPEAGP

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequencing reveals the structure of the Kcnk6 and map3k11 genes and their close vicinity to the sipa1 gene on mouse chromosome 19." Saridaki A., Ferraz C., Demaille J., Scherer G., Roux A.-F. Cytogenet. Cell Genet. 89:85-88(2000) [PubMed: 10894943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Ola.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon, Eye and Salivary gland.
[3]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, MASS SPECTROMETRY. Tissue: Macrophage.

Hide | Top

Cross-references

Sequence databases
	AF155142 Genomic DNA. Translation: AAF73281.1. BC030928 mRNA. Translation: AAH30928.1. BC047152 mRNA. Translation: AAH47152.1. BC095963 mRNA. Translation: AAH95963.1.
IPI	IPI00330731.
RefSeq	NP_071295.2.
UniGene	Mm.185026
3D structure databases
HSSP	HSSP built from PDB template 1R1W based on UniProtKB P08581.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q80XI6. 2 interactions.
STRING	Q80XI6.
PTM databases
PhosphoSite	Q80XI6.
Proteomic databases
PRIDE	Q80XI6.
Genome annotation databases
Ensembl	ENSMUST00000004156; ENSMUSP00000004156; ENSMUSG00000004054; Mus musculus. [Genome view]
GeneID	26403.
KEGG	mmu:26403.
UCSC	uc008get.1. mouse.
Organism-specific databases
CTD	26403.
MGI	MGI:1346880. Map3k11.
Phylogenomic databases
HOVERGEN	Q80XI6.
OMA	QVGIFPS.
Enzyme and pathway databases
BRENDA	2.7.11.25. 244.
Gene expression databases
ArrayExpress	Q80XI6.
Bgee	Q80XI6.
CleanEx	MM_MAP3K11.
Genevestigator	Q80XI6.
Family and domain databases
InterPro	IPR015785. MAPKKK-like. IPR016231. MAPKKK9/10/11. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR001452. SH3_domain. IPR020473. SH3_region. IPR001245. Tyr_pkinase. [Graphical view]
PANTHER	PTHR23257:SF87. MAPKKK-like. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PIRSF	PIRSF000556. MAPKKK9_11. 1 hit.
PRINTS	PR00452. SH3DOMAIN. PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
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 Resources
NextBio	304369.
SOURCE	Search...

Hide | Top

Entry information

Entry name

M3K11_MOUSE

Accession

Primary (citable) accession number: Q80XI6
Secondary accession number(s): Q8K0M8, Q9JJ15

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents