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Q9ESL4

- MLTK_MOUSE

UniProt

Q9ESL4 - MLTK_MOUSE

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Protein

Mitogen-activated protein kinase kinase kinase MLT

Gene
Zak, Mltk
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication

Enzyme regulationi

Activated by phosphorylation by PKN1 and autophosphorylation on Thr-161 and Ser-165 By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATP By similarityBy similarity
Active sitei133 – 1331Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. MAP kinase kinase kinase activity Source: MGI
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of JUN kinase activity Source: Ensembl
  2. activation of MAPKK activity Source: GOC
  3. cell cycle arrest Source: Ensembl
  4. cell cycle checkpoint Source: UniProtKB
  5. cytoskeleton organization Source: MGI
  6. DNA damage checkpoint Source: Ensembl
  7. intracellular signal transduction Source: UniProtKB
  8. positive regulation of apoptotic process Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. response to radiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase MLT (EC:2.7.11.25)
Alternative name(s):
Leucine zipper- and sterile alpha motif kinase ZAK
MLK-like mitogen-activated protein triple kinase
Mixed lineage kinase-related kinase
Short name:
MLK-related kinase
Short name:
MRK
Sterile alpha motif- and leucine zipper-containing kinase AZK
Gene namesi
Name:Zak
Synonyms:Mltk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2443258. Zak.

Subcellular locationi

Cytoplasm. Nucleus
Note: Appears to shuttle between nucleus and cytoplasm.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451K → M: Loss of kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802Mitogen-activated protein kinase kinase kinase MLTPRO_0000086339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei3 – 31Phosphoserine By similarity
Modified residuei155 – 1551Phosphoserine By similarity
Modified residuei161 – 1611Phosphothreonine; by autocatalysis By similarityBy similarity
Modified residuei165 – 1651Phosphoserine; by autocatalysis By similarityBy similarity
Modified residuei264 – 2641Phosphoserine By similarity
Modified residuei275 – 2751Phosphoserine By similarity
Modified residuei302 – 3021Phosphoserine By similarity
Modified residuei326 – 3261Phosphoserine By similarity
Modified residuei328 – 3281Phosphothreonine By similarity
Modified residuei557 – 5571Phosphoserine By similarity
Modified residuei565 – 5651Phosphoserine By similarity
Modified residuei568 – 5681Phosphoserine By similarity
Modified residuei584 – 5841Phosphoserine By similarity
Modified residuei586 – 5861Phosphothreonine By similarity
Modified residuei591 – 5911Phosphoserine By similarity
Modified residuei593 – 5931Phosphoserine By similarity
Modified residuei599 – 5991Phosphoserine By similarity
Modified residuei628 – 6281Phosphothreonine By similarity
Modified residuei634 – 6341Phosphoserine By similarity
Modified residuei636 – 6361Phosphoserine By similarity
Modified residuei637 – 6371Phosphoserine By similarity
Modified residuei638 – 6381Phosphoserine By similarity
Modified residuei640 – 6401Phosphothreonine By similarity
Modified residuei649 – 6491Phosphoserine By similarity
Modified residuei661 – 6611Phosphoserine By similarity
Modified residuei667 – 6671Phosphoserine By similarity
Modified residuei668 – 6681Phosphoserine By similarity
Modified residuei687 – 6871Phosphoserine By similarity
Modified residuei690 – 6901Phosphoserine By similarity
Modified residuei691 – 6911Phosphoserine By similarity
Modified residuei727 – 7271Phosphoserine By similarity
Modified residuei733 – 7331Phosphoserine By similarity
Modified residuei756 – 7561Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ESL4.
PaxDbiQ9ESL4.
PRIDEiQ9ESL4.

PTM databases

PhosphoSiteiQ9ESL4.

Expressioni

Gene expression databases

ArrayExpressiQ9ESL4.
BgeeiQ9ESL4.
CleanExiMM_B230120H23RIK.
GenevestigatoriQ9ESL4.

Interactioni

Subunit structurei

Homodimer. Interacts with PKN1 and ZNF33A By similarity.1 Publication

Protein-protein interaction databases

IntActiQ9ESL4. 1 interaction.
MINTiMINT-4129310.
STRINGi10090.ENSMUSP00000088334.

Structurei

3D structure databases

ProteinModelPortaliQ9ESL4.
SMRiQ9ESL4. Positions 9-325.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 277262Protein kinaseAdd
BLAST
Domaini339 – 41072SAMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 30822Leucine-zipperAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117425.
HOGENOMiHOG000231813.
HOVERGENiHBG080445.
InParanoidiQ9ESL4.
KOiK04424.
OMAiHRDSHET.
OrthoDBiEOG7D85VN.
PhylomeDBiQ9ESL4.
TreeFamiTF106505.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9ESL4-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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

MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI    50
EKEAEILSVL SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE 100
EMDMEHIMTW ATDVAKGMHY LHMEAPVKVI HRDLKSRNVV IAADGVLKIC 150
DFGASRFHNH TTHMSLVGTF PWMAPEVIQS LPVSETCDTY SYGVVLWEML 200
TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH QCWEADAKKR 250
PSFKQIISIL ESMSNDTNLP DQCNSFLHNK AEWRCEIEAT LERLKKLERD 300
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYFWVQQ 350
LVRKGESSVE MSGYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF 400
KSAIEKLTHD YLNLFHFPPL IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT 450
GPQDCKWKMY MEMDGDEVAI TYIKDVTFNT SLPDAEILKM TKPPFVMEKW 500
IVGIAEDQTV ECTVTYENDV RTPKLTKHVH SIQWDRTKPQ DEVKAVQLAI 550
QTLFSSSEGN PGSRSDSSAD CQWLDTLRMR QIASHTSLQR SQSNPILGSP 600
FFPYFANQDS YAAAVRRTQT PVKYQQITPS INPSRSSSPT QYGLSRNFSS 650
LNLSSRDSGF SSLNDSSSER GRYSDRSRNK YYRGSVSLNS SPKGRYGGKS 700
QHSTPSRERY SGKFYRLPQS ALNTHQSPDF KRSPNDHDRR VPRTIPGMPL 750
HPETASKAGE EESRVSEGGW TKVEYRKKTH RQLSAKTSKE RTRGNYRGRR 800
NF 802
Length:802
Mass (Da):91,720
Last modified:March 1, 2001 - v1
Checksum:iD431DF8F312A43CC
GO
Isoform 21 Publication (identifier: Q9ESL4-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     332-454: PSFEIGAWTE...HLKPGTGPQD → LPLSARMSEE...DAENDVDNSE
     455-802: Missing.

Note: Contains a phosphoserine at position 434 (By similarity). Contains a phosphoserine at position 453 (By similarity).

Show »
Length:454
Mass (Da):51,366
Checksum:i35C2FC0D729D9395
GO
Isoform 3 (identifier: Q9ESL4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     285-289: CEIEA → WVAPA
     290-802: Missing.

Note: No experimental confirmation available.

Show »
Length:289
Mass (Da):32,842
Checksum:i440E5651076A04A4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei285 – 2895CEIEA → WVAPA in isoform 3. VSP_051747
Alternative sequencei290 – 802513Missing in isoform 3. VSP_051748Add
BLAST
Alternative sequencei332 – 454123PSFEI…TGPQD → LPLSARMSEESYFESKTEES NSAEMSCQITAASNGEGHGM NPGLQAMMLMGFGDVFSMNK AGAVLHSGMQINMQAKQNSS KTTCKRRGKKVNMALGFSDF DLSEGDDDDHDGDDAENDVD NSE in isoform 2. 1 PublicationVSP_051745Add
BLAST
Alternative sequencei455 – 802348Missing in isoform 2. 1 PublicationVSP_051746Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711P → Q in BAC32371. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB049731 mRNA. Translation: BAB16442.1.
AB049732 mRNA. Translation: BAB16443.1.
AK045444 mRNA. Translation: BAC32371.1.
AK132186 mRNA. Translation: BAE21021.1.
BC023718 mRNA. Translation: AAH23718.1.
CCDSiCCDS38143.1. [Q9ESL4-1]
CCDS50605.1. [Q9ESL4-2]
RefSeqiNP_001158263.1. NM_001164791.1. [Q9ESL4-2]
NP_075544.1. NM_023057.5. [Q9ESL4-1]
NP_835185.2. NM_178084.4. [Q9ESL4-3]
XP_006500060.1. XM_006499997.1. [Q9ESL4-1]
UniGeneiMm.304143.
Mm.314618.

Genome annotation databases

EnsembliENSMUST00000090824; ENSMUSP00000088334; ENSMUSG00000004085. [Q9ESL4-1]
ENSMUST00000135469; ENSMUSP00000118983; ENSMUSG00000004085. [Q9ESL4-2]
GeneIDi65964.
KEGGimmu:65964.
UCSCiuc008kbs.2. mouse. [Q9ESL4-3]
uc008kbv.2. mouse. [Q9ESL4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB049731 mRNA. Translation: BAB16442.1 .
AB049732 mRNA. Translation: BAB16443.1 .
AK045444 mRNA. Translation: BAC32371.1 .
AK132186 mRNA. Translation: BAE21021.1 .
BC023718 mRNA. Translation: AAH23718.1 .
CCDSi CCDS38143.1. [Q9ESL4-1 ]
CCDS50605.1. [Q9ESL4-2 ]
RefSeqi NP_001158263.1. NM_001164791.1. [Q9ESL4-2 ]
NP_075544.1. NM_023057.5. [Q9ESL4-1 ]
NP_835185.2. NM_178084.4. [Q9ESL4-3 ]
XP_006500060.1. XM_006499997.1. [Q9ESL4-1 ]
UniGenei Mm.304143.
Mm.314618.

3D structure databases

ProteinModelPortali Q9ESL4.
SMRi Q9ESL4. Positions 9-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9ESL4. 1 interaction.
MINTi MINT-4129310.
STRINGi 10090.ENSMUSP00000088334.

PTM databases

PhosphoSitei Q9ESL4.

Proteomic databases

MaxQBi Q9ESL4.
PaxDbi Q9ESL4.
PRIDEi Q9ESL4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000090824 ; ENSMUSP00000088334 ; ENSMUSG00000004085 . [Q9ESL4-1 ]
ENSMUST00000135469 ; ENSMUSP00000118983 ; ENSMUSG00000004085 . [Q9ESL4-2 ]
GeneIDi 65964.
KEGGi mmu:65964.
UCSCi uc008kbs.2. mouse. [Q9ESL4-3 ]
uc008kbv.2. mouse. [Q9ESL4-1 ]

Organism-specific databases

CTDi 51776.
MGIi MGI:2443258. Zak.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117425.
HOGENOMi HOG000231813.
HOVERGENi HBG080445.
InParanoidi Q9ESL4.
KOi K04424.
OMAi HRDSHET.
OrthoDBi EOG7D85VN.
PhylomeDBi Q9ESL4.
TreeFami TF106505.

Miscellaneous databases

NextBioi 320398.
PROi Q9ESL4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ESL4.
Bgeei Q9ESL4.
CleanExi MM_B230120H23RIK.
Genevestigatori Q9ESL4.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel MAP kinase kinase kinase, MLTK."
    Gotoh I., Adachi M., Nishida E.
    J. Biol. Chem. 276:4276-4286(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-45.
    Tissue: Heart.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Head.
  3. "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).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 225-233, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMLTK_MOUSE
AccessioniPrimary (citable) accession number: Q9ESL4
Secondary accession number(s): Q3V1X8, Q8BR73, Q9ESL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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