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Q9NYL2

- MLTK_HUMAN

UniProt

Q9NYL2 - MLTK_HUMAN

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Protein

Mitogen-activated protein kinase kinase kinase MLT

Gene

ZAK

Organism
Homo sapiens (Human)
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, causes cell shrinkage and disruption of actin stress fibers. Isoform 1 may have role in neoplastic cell transformation and cancer development. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'.6 Publications

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-165.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATP1 PublicationPROSITE-ProRule annotation
Active sitei133 – 1331Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. MAP kinase kinase kinase activity Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of JUN kinase activity Source: UniProtKB
  2. activation of MAPKK activity Source: UniProtKB
  3. cell cycle arrest Source: UniProtKB
  4. cell cycle checkpoint Source: UniProtKB
  5. cell death Source: UniProtKB
  6. cell differentiation Source: UniProtKB
  7. cell proliferation Source: UniProtKB
  8. cytoskeleton organization Source: Ensembl
  9. DNA damage checkpoint Source: UniProtKB
  10. intracellular signal transduction Source: UniProtKB
  11. positive regulation of apoptotic process Source: UniProtKB
  12. protein phosphorylation Source: UniProtKB
  13. response to radiation Source: UniProtKB
  14. response to stress Source: UniProtKB
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

Enzyme and pathway databases

SignaLinkiQ9NYL2.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase kinase kinase MLT (EC:2.7.11.25)
Alternative name(s):
Human cervical cancer suppressor gene 4 protein
Short name:
HCCS-4
Leucine zipper- and sterile alpha motif-containing kinase
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
ORF Names:HCCS4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Translocates to the nucleus upon ultraviolet B irradiation.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
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
Mutagenesisi161 – 1611T → A: Loss of autophosphorylation activity. 1 Publication
Mutagenesisi162 – 1621T → A: Slight loss of autophosphorylation activity. 1 Publication
Mutagenesisi165 – 1651S → A: Loss of autophosphorylation activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 800800Mitogen-activated protein kinase kinase kinase MLTPRO_0000086338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Phosphoserine
Modified residuei3 – 31Phosphoserine
Modified residuei155 – 1551Phosphoserine
Modified residuei161 – 1611Phosphothreonine; by autocatalysis1 Publication
Modified residuei165 – 1651Phosphoserine; by autocatalysis1 Publication
Modified residuei264 – 2641Phosphoserine
Modified residuei268 – 2681Phosphoserine
Modified residuei275 – 2751Phosphoserine
Modified residuei302 – 3021Phosphoserine
Modified residuei326 – 3261Phosphoserine
Modified residuei328 – 3281Phosphothreonine
Modified residuei557 – 5571Phosphoserine
Modified residuei565 – 5651Phosphoserine
Modified residuei568 – 5681Phosphoserine
Modified residuei584 – 5841Phosphoserine
Modified residuei586 – 5861Phosphothreonine
Modified residuei591 – 5911Phosphoserine
Modified residuei593 – 5931Phosphoserine
Modified residuei599 – 5991Phosphoserine1 Publication
Modified residuei628 – 6281Phosphothreonine3 Publications
Modified residuei633 – 6331Phosphoserine3 Publications
Modified residuei635 – 6351Phosphoserine
Modified residuei636 – 6361Phosphoserine
Modified residuei637 – 6371Phosphoserine
Modified residuei639 – 6391Phosphothreonine
Modified residuei648 – 6481Phosphoserine
Modified residuei660 – 6601Phosphoserine
Modified residuei666 – 6661Phosphothreonine
Modified residuei667 – 6671Phosphoserine
Modified residuei668 – 6681Phosphoserine
Modified residuei687 – 6871Phosphoserine
Modified residuei690 – 6901Phosphoserine
Modified residuei691 – 6911Phosphoserine
Modified residuei718 – 7181Phosphoserine
Modified residuei727 – 7271Phosphoserine4 Publications
Modified residuei733 – 7331Phosphoserine2 Publications
Modified residuei754 – 7541Phosphoserine
Modified residuei781 – 7811Phosphoserine

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NYL2.
PaxDbiQ9NYL2.
PRIDEiQ9NYL2.

PTM databases

PhosphoSiteiQ9NYL2.

Expressioni

Tissue specificityi

Ubiquitously expressed. Isoform 2 is the predominant form in all tissues examined, except for liver, in which isoform 1 is more highly expressed.2 Publications

Gene expression databases

BgeeiQ9NYL2.
ExpressionAtlasiQ9NYL2. baseline and differential.
GenevestigatoriQ9NYL2.

Organism-specific databases

HPAiHPA017205.

Interactioni

Subunit structurei

Homodimer. Interacts with PKN1 and ZNF33A.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PKN1Q165122EBI-687346,EBI-602382
RPS6KA5O755824EBI-602273,EBI-73869
YWHAZP631044EBI-602273,EBI-347088

Protein-protein interaction databases

BioGridi119725. 29 interactions.
IntActiQ9NYL2. 23 interactions.
MINTiMINT-1465549.

Structurei

3D structure databases

ProteinModelPortaliQ9NYL2.
SMRiQ9NYL2. Positions 9-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 277262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini339 – 41072SAMPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOVERGENiHBG080445.
InParanoidiQ9NYL2.
KOiK04424.
OMAiLHSGMQI.
PhylomeDBiQ9NYL2.

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: Q9NYL2-1) [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

        10         20         30         40         50
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI
60 70 80 90 100
EKEAEILSVL SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE
110 120 130 140 150
EMDMDHIMTW ATDVAKGMHY LHMEAPVKVI HRDLKSRNVV IAADGVLKIC
160 170 180 190 200
DFGASRFHNH TTHMSLVGTF PWMAPEVIQS LPVSETCDTY SYGVVLWEML
210 220 230 240 250
TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH QCWEADAKKR
260 270 280 290 300
PSFKQIISIL ESMSNDTSLP DKCNSFLHNK AEWRCEIEAT LERLKKLERD
310 320 330 340 350
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYCWVQQ
360 370 380 390 400
LVRKGDSSAE MSVYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF
410 420 430 440 450
KSAIEKLTHD YINLFHFPPL IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT
460 470 480 490 500
GPQDCKWKMY MEMDGDEIAI TYIKDVTFNT NLPDAEILKM TKPPFVMEKW
510 520 530 540 550
IVGIAKSQTV ECTVTYESDV RTPKSTKHVH SIQWSRTKPQ DEVKAVQLAI
560 570 580 590 600
QTLFTNSDGN PGSRSDSSAD CQWLDTLRMR QIASNTSLQR SQSNPILGSP
610 620 630 640 650
FFSHFDGQDS YAAAVRRPQV PIKYQQITPV NQSRSSSPTQ YGLTKNFSSL
660 670 680 690 700
HLNSRDSGFS SGNTDTSSER GRYSDRSRNK YGRGSISLNS SPRGRYSGKS
710 720 730 740 750
QHSTPSRGRY PGKFYRVSQS ALNPHQSPDF KRSPRDLHQP NTIPGMPLHP
760 770 780 790 800
ETDSRASEED SKVSEGGWTK VEYRKKPHRP SPAKTNKERA RGDHRGWRNF
Length:800
Mass (Da):91,155
Last modified:November 30, 2010 - v3
Checksum:iB2814509EC54B07A
GO
Isoform 21 Publication (identifier: Q9NYL2-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     332-455: PSFEIGAWTE...LKPGTGPQDC → LPLAARMSEE...EEDNDMDNSE
     456-800: Missing.

Note: Contains a phosphoserine at position 339. Contains a phosphoserine at position 429. Contains a phosphoserine at position 434. Contains a phosphoserine at position 454.

Show »
Length:455
Mass (Da):51,582
Checksum:iE87DB84A4D58B752
GO
Isoform 3 (identifier: Q9NYL2-3) [UniParc]FASTAAdd to Basket

Also known as: HCCS-4

The sequence of this isoform differs from the canonical sequence as follows:
     285-312: CEIEATLERLKKLERDLSFKEQELKERE → WVAPTAGHSVWLSKTITRLNEEVNQRSE
     313-800: Missing.

Show »
Length:312
Mass (Da):35,468
Checksum:iB655E873246339FB
GO

Sequence cautioni

The sequence BAD92211.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461C → W in AAF63490. (PubMed:10924358)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti267 – 2671T → M.1 Publication
Corresponds to variant rs6758025 [ dbSNP | Ensembl ].
VAR_040806
Natural varianti281 – 2811A → T in an ovarian endometrioid sample; somatic mutation. 1 Publication
VAR_040807
Natural varianti281 – 2811A → V.1 Publication
Corresponds to variant rs34683477 [ dbSNP | Ensembl ].
VAR_040808
Natural varianti531 – 5311S → L.5 Publications
Corresponds to variant rs3769148 [ dbSNP | Ensembl ].
VAR_022827
Natural varianti580 – 5801R → W.1 Publication
Corresponds to variant rs7593622 [ dbSNP | Ensembl ].
VAR_040809
Natural varianti740 – 7401P → T.1 Publication
Corresponds to variant rs56202258 [ dbSNP | Ensembl ].
VAR_040810
Natural varianti773 – 7731Y → H.1 Publication
Corresponds to variant rs35608243 [ dbSNP | Ensembl ].
VAR_040811
Natural varianti784 – 7841K → T.2 Publications
Corresponds to variant rs55830025 [ dbSNP | Ensembl ].
VAR_040812

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei285 – 31228CEIEA…LKERE → WVAPTAGHSVWLSKTITRLN EEVNQRSE in isoform 3. 1 PublicationVSP_051741Add
BLAST
Alternative sequencei313 – 800488Missing in isoform 3. 1 PublicationVSP_051742Add
BLAST
Alternative sequencei332 – 455124PSFEI…GPQDC → LPLAARMSEESYFESKTEES NSAEMSCQITATSNGEGHGM NPSLQAMMLMGFGDIFSMNK AGAVMHSGMQINMQAKQNSS KTTSKRRGKKVNMALGFSDF DLSEGDDDDDDDGEEEDNDM DNSE in isoform 2. 5 PublicationsVSP_051743Add
BLAST
Alternative sequencei456 – 800345Missing in isoform 2. 5 PublicationsVSP_051744Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF238255 mRNA. Translation: AAF63490.1.
AB049733 mRNA. Translation: BAB16444.1.
AB049734 mRNA. Translation: BAB16445.1.
AF325454 mRNA. Translation: AAK11615.1.
AF480461 mRNA. Translation: AAL85891.1.
AF480462 mRNA. Translation: AAL85892.1.
AB030034 mRNA. Translation: BAB12040.1.
AF251441 mRNA. Translation: AAF65822.1.
AF465843 mRNA. Translation: AAO33376.1.
AK056310 mRNA. Translation: BAG51674.1.
AB208974 mRNA. Translation: BAD92211.1. Different initiation.
AC092573 Genomic DNA. Translation: AAX82002.1.
AC013461 Genomic DNA. Translation: AAX93067.1.
AC019046 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11164.1.
BC001401 mRNA. Translation: AAH01401.1.
CCDSiCCDS2251.1. [Q9NYL2-2]
CCDS42777.1. [Q9NYL2-1]
RefSeqiNP_057737.2. NM_016653.2. [Q9NYL2-1]
NP_598407.1. NM_133646.2. [Q9NYL2-2]
XP_005246697.1. XM_005246640.1. [Q9NYL2-1]
UniGeneiHs.444451.

Genome annotation databases

GeneIDi51776.
KEGGihsa:51776.
UCSCiuc002uhx.3. human. [Q9NYL2-3]
uc002uhz.3. human. [Q9NYL2-1]

Polymorphism databases

DMDMi313104215.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF238255 mRNA. Translation: AAF63490.1 .
AB049733 mRNA. Translation: BAB16444.1 .
AB049734 mRNA. Translation: BAB16445.1 .
AF325454 mRNA. Translation: AAK11615.1 .
AF480461 mRNA. Translation: AAL85891.1 .
AF480462 mRNA. Translation: AAL85892.1 .
AB030034 mRNA. Translation: BAB12040.1 .
AF251441 mRNA. Translation: AAF65822.1 .
AF465843 mRNA. Translation: AAO33376.1 .
AK056310 mRNA. Translation: BAG51674.1 .
AB208974 mRNA. Translation: BAD92211.1 . Different initiation.
AC092573 Genomic DNA. Translation: AAX82002.1 .
AC013461 Genomic DNA. Translation: AAX93067.1 .
AC019046 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11164.1 .
BC001401 mRNA. Translation: AAH01401.1 .
CCDSi CCDS2251.1. [Q9NYL2-2 ]
CCDS42777.1. [Q9NYL2-1 ]
RefSeqi NP_057737.2. NM_016653.2. [Q9NYL2-1 ]
NP_598407.1. NM_133646.2. [Q9NYL2-2 ]
XP_005246697.1. XM_005246640.1. [Q9NYL2-1 ]
UniGenei Hs.444451.

3D structure databases

ProteinModelPortali Q9NYL2.
SMRi Q9NYL2. Positions 9-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119725. 29 interactions.
IntActi Q9NYL2. 23 interactions.
MINTi MINT-1465549.

Chemistry

BindingDBi Q9NYL2.
ChEMBLi CHEMBL3886.
GuidetoPHARMACOLOGYi 2289.

PTM databases

PhosphoSitei Q9NYL2.

Polymorphism databases

DMDMi 313104215.

Proteomic databases

MaxQBi Q9NYL2.
PaxDbi Q9NYL2.
PRIDEi Q9NYL2.

Protocols and materials databases

DNASUi 51776.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 51776.
KEGGi hsa:51776.
UCSCi uc002uhx.3. human. [Q9NYL2-3 ]
uc002uhz.3. human. [Q9NYL2-1 ]

Organism-specific databases

CTDi 51776.
GeneCardsi GC02P173940.
H-InvDB HIX0030332.
HPAi HPA017205.
MIMi 609479. gene.
neXtProti NX_Q9NYL2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118807.
HOVERGENi HBG080445.
InParanoidi Q9NYL2.
KOi K04424.
OMAi LHSGMQI.
PhylomeDBi Q9NYL2.

Enzyme and pathway databases

SignaLinki Q9NYL2.

Miscellaneous databases

ChiTaRSi ZAK. human.
GeneWikii ZAK.
GenomeRNAii 51776.
NextBioi 55903.
PROi Q9NYL2.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYL2.
ExpressionAtlasi Q9NYL2. baseline and differential.
Genevestigatori Q9NYL2.

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. "Cloning and expression of ZAK, a mixed lineage kinase-like protein containing a leucine-zipper and a sterile-alpha motif."
    Liu T.-C., Huang C.-J., Chu Y.-C., Wei C.-C., Chou C.-C., Chou M.-Y., Chou C.-K., Yang J.-J.
    Biochem. Biophys. Res. Commun. 274:811-816(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, HOMODIMERIZATION, VARIANT LEU-531.
    Tissue: Placenta1 Publication.
  2. "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, PHOSPHORYLATION, VARIANT LEU-531.
    Tissue: Fetal brain1 Publication.
  3. "Tissue distribution and functional expression of a cDNA encoding a novel mixed lineage kinase."
    Bloem L.J., Pickard T.R., Acton S., Donoghue M., Beavis R.C., Knierman M.D., Wang X.
    J. Mol. Cell. Cardiol. 33:1739-1750(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Heart1 Publication.
  4. "MRK, a mixed lineage kinase-related molecule that plays a role in gamma-radiation-induced cell cycle arrest."
    Gross E.A., Callow M.G., Waldbaum L., Thomas S., Ruggieri R.
    J. Biol. Chem. 277:13873-13882(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-45, VARIANT LEU-531.
    Tissue: T-cell1 Publication.
  5. "Placible mixed-lineage kinase derived from LAK cell."
    Abe Y., Ueda N.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphoid tissue.
  6. "Cloning and characterisation of AZK, a mixed lineage kinase containing a sterile-alpha motif."
    McNee J.J., Frima N., Diamond T.E., Dower S.K., Guesdon F.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-531.
  7. "Identification of a new tumor suppressor in human cancers."
    Kim J.W.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-784.
    Tissue: BrainImported.
  10. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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 2).
    Tissue: ColonImported.
  13. "A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle."
    Yang J.-J.
    Biochem. Biophys. Res. Commun. 301:71-77(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF33A.
  14. "Regulation of a mitogen-activated protein kinase kinase kinase, MLTK by PKN."
    Takahashi M., Gotoh Y., Isagawa T., Nishimura T., Goyama E., Kim H.-S., Mukai H., Ono Y.
    J. Biochem. 133:181-187(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH PKN1.
  15. "A novel role for mixed-lineage kinase-like mitogen-activated protein triple kinase alpha in neoplastic cell transformation and tumor development."
    Cho Y.-Y., Bode A.M., Mizuno H., Choi B.Y., Choi H.S., Dong Z.
    Cancer Res. 64:3855-3864(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway."
    Tosti E., Waldbaum L., Warshaw G., Gross E.A., Ruggieri R.
    J. Biol. Chem. 279:47652-47660(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA DAMAGE CHECKPOINTS, FUNCTION IN PHOSPHORYLATION OF CHEK2, ENZYME REGULATION, PHOSPHORYLATION AT THR-161 AND SER-165, MUTAGENESIS OF THR-161; THR-162 AND SER-165.
  17. "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
    Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
    J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3, SUBCELLULAR LOCATION.
  18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628; SER-727 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; THR-628; SER-633; SER-727 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628; SER-633 AND SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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] MET-267; THR-281; VAL-281; LEU-531; TRP-580; THR-740; HIS-773 AND THR-784.

Entry informationi

Entry nameiMLTK_HUMAN
AccessioniPrimary (citable) accession number: Q9NYL2
Secondary accession number(s): B3KPG2
, Q53SX1, Q580W8, Q59GY5, Q86YW8, Q9HCC4, Q9HCC5, Q9HDD2, Q9NYE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3