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Q9NYL2 (MLTK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ZAK
Synonyms:MLTK
ORF Names:HCCS4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length800 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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'. Ref.1 Ref.2 Ref.4 Ref.15 Ref.16 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.4

Cofactor

Magnesium. Ref.4

Enzyme regulation

Activated by phosphorylation by PKN1 and autophosphorylation on Thr-161 and Ser-165. Ref.2 Ref.14 Ref.16

Subunit structure

Homodimer. Interacts with PKN1 and ZNF33A. Ref.1 Ref.13 Ref.14

Subcellular location

Cytoplasm. Nucleus. Note: Translocates to the nucleus upon ultraviolet B irradiation. Ref.17

Tissue specificity

Ubiquitously expressed. Isoform 2 is the predominant form in all tissues examined, except for liver, in which isoform 1 is more highly expressed. Ref.1 Ref.4

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 SAM (sterile alpha motif) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from mutant phenotype Ref.4. Source: UniProtKB

activation of JUN kinase activity

Inferred from direct assay Ref.4. Source: UniProtKB

cell cycle arrest

Inferred from mutant phenotype Ref.4. Source: UniProtKB

cell death

Non-traceable author statement Ref.4. Source: UniProtKB

cell differentiation

Non-traceable author statement Ref.4. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.4. Source: UniProtKB

cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay Ref.1. Source: UniProtKB

response to radiation

Inferred from direct assay Ref.4. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.4. Source: UniProtKB

MAP kinase kinase kinase activity

Inferred from direct assay Ref.4. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.2 (identifier: Q9NYL2-1)

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.
Isoform 2 Ref.2 (identifier: Q9NYL2-2)

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.
Isoform 3 Ref.6 (identifier: Q9NYL2-3)

Also known as: HCCS-4;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 800800Mitogen-activated protein kinase kinase kinase MLT
PRO_0000086338

Regions

Domain16 – 277262Protein kinase
Domain339 – 41072SAM
Nucleotide binding22 – 309ATP By similarity UniProtKB P80192
Region287 – 30822Leucine-zipper

Sites

Active site1331Proton acceptor By similarity UniProtKB P80192
Binding site451ATP Ref.4

Amino acid modifications

Modified residue21Phosphoserine
Modified residue31Phosphoserine
Modified residue1551Phosphoserine
Modified residue1611Phosphothreonine; by autocatalysis Ref.16
Modified residue1651Phosphoserine; by autocatalysis Ref.16
Modified residue2641Phosphoserine
Modified residue2681Phosphoserine
Modified residue2751Phosphoserine
Modified residue3021Phosphoserine
Modified residue3261Phosphoserine
Modified residue3281Phosphothreonine
Modified residue5571Phosphoserine
Modified residue5651Phosphoserine
Modified residue5681Phosphoserine
Modified residue5841Phosphoserine
Modified residue5861Phosphothreonine
Modified residue5911Phosphoserine
Modified residue5931Phosphoserine
Modified residue5991Phosphoserine Ref.19
Modified residue6281Phosphothreonine Ref.18 Ref.19 Ref.21
Modified residue6331Phosphoserine Ref.19 Ref.21 Ref.22
Modified residue6351Phosphoserine
Modified residue6361Phosphoserine
Modified residue6371Phosphoserine
Modified residue6391Phosphothreonine
Modified residue6481Phosphoserine
Modified residue6601Phosphoserine
Modified residue6661Phosphothreonine
Modified residue6671Phosphoserine
Modified residue6681Phosphoserine
Modified residue6871Phosphoserine
Modified residue6901Phosphoserine
Modified residue6911Phosphoserine
Modified residue7181Phosphoserine
Modified residue7271Phosphoserine Ref.18 Ref.19 Ref.21 Ref.23
Modified residue7331Phosphoserine Ref.18 Ref.19
Modified residue7541Phosphoserine
Modified residue7811Phosphoserine

Natural variations

Alternative sequence285 – 31228CEIEA…LKERE → WVAPTAGHSVWLSKTITRLN EEVNQRSE in isoform 3. Ref.6
VSP_051741
Alternative sequence313 – 800488Missing in isoform 3. Ref.6
VSP_051742
Alternative sequence332 – 455124PSFEI…GPQDC → LPLAARMSEESYFESKTEES NSAEMSCQITATSNGEGHGM NPSLQAMMLMGFGDIFSMNK AGAVMHSGMQINMQAKQNSS KTTSKRRGKKVNMALGFSDF DLSEGDDDDDDDGEEEDNDM DNSE in isoform 2. Ref.2
VSP_051743
Alternative sequence456 – 800345Missing in isoform 2. Ref.2
VSP_051744
Natural variant2671T → M. Ref.25
Corresponds to variant rs6758025 [ dbSNP | Ensembl ].
VAR_040806
Natural variant2811A → T in an ovarian endometrioid sample; somatic mutation. Ref.25
VAR_040807
Natural variant2811A → V. Ref.25
Corresponds to variant rs34683477 [ dbSNP | Ensembl ].
VAR_040808
Natural variant5311S → L. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.25
Corresponds to variant rs3769148 [ dbSNP | Ensembl ].
VAR_022827
Natural variant5801R → W. Ref.25
Corresponds to variant rs7593622 [ dbSNP | Ensembl ].
VAR_040809
Natural variant7401P → T. Ref.25
Corresponds to variant rs56202258 [ dbSNP | Ensembl ].
VAR_040810
Natural variant7731Y → H. Ref.25
Corresponds to variant rs35608243 [ dbSNP | Ensembl ].
VAR_040811
Natural variant7841K → T. Ref.9 Ref.25
Corresponds to variant rs55830025 [ dbSNP | Ensembl ].
VAR_040812

Experimental info

Mutagenesis451K → M: Loss of kinase activity. Ref.4
Mutagenesis1611T → A: Loss of autophosphorylation activity. Ref.16
Mutagenesis1621T → A: Slight loss of autophosphorylation activity. Ref.16
Mutagenesis1651S → A: Loss of autophosphorylation activity. Ref.16
Sequence conflict3461C → W in AAF63490. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: B2814509EC54B07A

FASTA80091,155
        10         20         30         40         50         60 
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI EKEAEILSVL 

        70         80         90        100        110        120 
SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE EMDMDHIMTW ATDVAKGMHY 

       130        140        150        160        170        180 
LHMEAPVKVI HRDLKSRNVV IAADGVLKIC DFGASRFHNH TTHMSLVGTF PWMAPEVIQS 

       190        200        210        220        230        240 
LPVSETCDTY SYGVVLWEML TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH 

       250        260        270        280        290        300 
QCWEADAKKR PSFKQIISIL ESMSNDTSLP DKCNSFLHNK AEWRCEIEAT LERLKKLERD 

       310        320        330        340        350        360 
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYCWVQQ LVRKGDSSAE 

       370        380        390        400        410        420 
MSVYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF KSAIEKLTHD YINLFHFPPL 

       430        440        450        460        470        480 
IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT GPQDCKWKMY MEMDGDEIAI TYIKDVTFNT 

       490        500        510        520        530        540 
NLPDAEILKM TKPPFVMEKW IVGIAKSQTV ECTVTYESDV RTPKSTKHVH SIQWSRTKPQ 

       550        560        570        580        590        600 
DEVKAVQLAI QTLFTNSDGN PGSRSDSSAD CQWLDTLRMR QIASNTSLQR SQSNPILGSP 

       610        620        630        640        650        660 
FFSHFDGQDS YAAAVRRPQV PIKYQQITPV NQSRSSSPTQ YGLTKNFSSL HLNSRDSGFS 

       670        680        690        700        710        720 
SGNTDTSSER GRYSDRSRNK YGRGSISLNS SPRGRYSGKS QHSTPSRGRY PGKFYRVSQS 

       730        740        750        760        770        780 
ALNPHQSPDF KRSPRDLHQP NTIPGMPLHP ETDSRASEED SKVSEGGWTK VEYRKKPHRP 

       790        800 
SPAKTNKERA RGDHRGWRNF 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: E87DB84A4D58B752
Show »

FASTA45551,582
Isoform 3 (HCCS-4) [UniParc].

Checksum: B655E873246339FB
Show »

FASTA31235,468

References

« Hide 'large scale' references
[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: Placenta.
[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 brain.
[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: Heart.
[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-cell.
[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. expand/collapse author list , 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: Brain.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: Colon.
[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, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; THR-628; SER-633; SER-727 AND SER-733, MASS SPECTROMETRY, 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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628; SER-633 AND SER-727, MASS SPECTROMETRY, 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, MASS SPECTROMETRY, 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, MASS SPECTROMETRY, 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_057737.2. NM_016653.2.
NP_598407.1. NM_133646.2.
XP_005246697.1. XM_005246640.1.
UniGeneHs.444451.

3D structure databases

ProteinModelPortalQ9NYL2.
SMRQ9NYL2. Positions 9-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119725. 29 interactions.
IntActQ9NYL2. 23 interactions.
MINTMINT-1465549.

Chemistry

BindingDBQ9NYL2.
ChEMBLCHEMBL3886.
GuidetoPHARMACOLOGY2289.

PTM databases

PhosphoSiteQ9NYL2.

Polymorphism databases

DMDM68565548.

Proteomic databases

PaxDbQ9NYL2.
PRIDEQ9NYL2.

Protocols and materials databases

DNASU51776.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID51776.
KEGGhsa:51776.
UCSCuc002uhx.3. human. [Q9NYL2-3]
uc002uhz.3. human. [Q9NYL2-1]

Organism-specific databases

CTD51776.
GeneCardsGC02P173940.
H-InvDBHIX0030332.
HPAHPA017205.
MIM609479. gene.
neXtProtNX_Q9NYL2.

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG080445.
KOK04424.
OMALHSGMQI.

Enzyme and pathway databases

SignaLinkQ9NYL2.

Gene expression databases

ArrayExpressQ9NYL2.
BgeeQ9NYL2.
GenevestigatorQ9NYL2.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR028429. MLTK.
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]
PANTHERPTHR23257:SF67. PTHR23257:SF67. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZAK. human.
GeneWikiZAK.
GenomeRNAi51776.
NextBio55903.
PROQ9NYL2.
SOURCESearch...

Entry information

Entry nameMLTK_HUMAN
AccessionPrimary (citable) accession number: Q9NYL2
Secondary accession number(s): B3KPG2 expand/collapse secondary AC list , Q53SX1, Q580W8, Q59GY5, Q86YW8, Q9HCC4, Q9HCC5, Q9HDD2, Q9NYE9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 30, 2010
Last modified: March 19, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM