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Reviewed, UniProtKB/Swiss-Prot Q9NYL2 (MLTK_HUMAN)

Last modified November 3, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase kinase kinase MLT
    EC=2.7.11.25
Alternative name(s):
    MLK-like mitogen-activated protein triple kinase
    Sterile alpha motif- and leucine zipper-containing kinase AZK
    Leucine zipper- and sterile alpha motif-containing kinase
    Mixed lineage kinase-related kinase
      Short name=MLK-related kinase
      Short name=MRK
    Cervical cancer suppressor gene 4 protein
    HCCS-4
Gene names
Name: MLTK
Synonyms: ZAK
ORF Names: HCCS4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length800 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.13 Ref.14 Ref.15

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.12

Subunit structure

Homodimer. Interacts with PKN1 and ZNF33A. Ref.1 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus. Note: Translocates to the nucleus upon ultraviolet B irradiation. Ref.15

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.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processDNA damage checkpoint Ref.4

Inferred from mutant phenotype. Source: UniProtKB

activation of JUN kinase activity Ref.4

Inferred from direct assay. Source: UniProtKB

activation of MAPKK activity Ref.4

Traceable author statement. Source: UniProtKB

cell cycle arrest Ref.4

Inferred from mutant phenotype. Source: UniProtKB

cell death Ref.4

Non-traceable author statement. Source: UniProtKB

cell differentiation Ref.4

Non-traceable author statement. Source: UniProtKB

cell proliferation Ref.4

Non-traceable author statement. Source: UniProtKB

positive regulation of apoptosis Ref.1

Inferred from direct assay. Source: UniProtKB

response to radiation Ref.4

Inferred from direct assay. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding Ref.4

Inferred from direct assay. Source: UniProtKB

MAP kinase kinase kinase activity Ref.4

Inferred from direct assay. Source: UniProtKB

identical protein binding Ref.1

Inferred from physical interaction. Source: IntAct

magnesium ion binding Ref.4

Inferred from direct assay. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-602273,EBI-602273
PKN1Q165121EBI-687346,EBI-602382

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: Phosphorylated on Ser-339, Ser-434 and Ser-454.
Isoform 3 Ref.4 (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
Domain287 – 30822Leucine-zipper UniProtKB P80192
Domain339 – 41072SAM
Nucleotide binding22 – 309ATP By similarity UniProtKB P80192

Sites

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

Amino acid modifications

Modified residue31Phosphoserine Ref.20
Modified residue1611Phosphothreonine; by autocatalysis Ref.14
Modified residue1651Phosphoserine; by autocatalysis Ref.14
Modified residue2681Phosphoserine Ref.20
Modified residue2751Phosphoserine Ref.20
Modified residue3021Phosphoserine Ref.20
Modified residue3281Phosphothreonine Ref.20
Modified residue5911Phosphoserine Ref.19
Modified residue5931Phosphoserine Ref.20 Ref.19
Modified residue5991Phosphoserine Ref.19 Ref.21
Modified residue6281Phosphothreonine Ref.20 Ref.21
Modified residue6331Phosphoserine Ref.20 Ref.21 Ref.18
Modified residue6351Phosphoserine By similarity
Modified residue6371Phosphoserine Ref.20 Ref.18 Ref.16 Ref.17
Modified residue6391Phosphothreonine By similarity
Modified residue6871Phosphoserine Ref.20
Modified residue6911Phosphoserine Ref.20
Modified residue7271Phosphoserine Ref.20 Ref.21
Modified residue7331Phosphoserine Ref.20 Ref.21
Modified residue7811Phosphoserine Ref.20

Natural variations

Alternative sequence285 – 31228CEIEA…LKERE → WVAPTAGHSVWLSKTITRLN EEVNQRSE in isoform 3. Ref.4
VSP_051741
Alternative sequence313 – 800488Missing in isoform 3. Ref.4
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
VAR_040806
Natural variant2811A → T in an ovarian endometrioid sample; somatic mutation. Ref.22
VAR_040807
Natural variant2811A → V
VAR_040808
Natural variant5311L → S: dbSNP rs3769148. Ref.22 Ref.5 Ref.7 Ref.8
VAR_022827
Natural variant5801R → W
VAR_040809
Natural variant7401P → T
VAR_040810
Natural variant7731Y → H
VAR_040811
Natural variant7841K → T
VAR_040812

Experimental info

Mutagenesis451K → M: Loss of kinase activity. Ref.4
Mutagenesis1611T → A: Loss of autophosphorylation activity. Ref.14
Mutagenesis1621T → A: Slight loss of autophosphorylation activity. Ref.14
Mutagenesis1651S → A: Loss of autophosphorylation activity. Ref.14
Sequence conflict3461C → W in AAF63490. Ref.1

Sequences

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

Last modified July 5, 2005. Version 2.
Checksum: B289D836EC52E295

FASTA80091,181
        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 LIQWSRTKPQ 

       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).

Checksum: E87DB84A4D58B752
Show »

FASTA45551,582
Isoform 3 (HCCS-4).

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: 10924358] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, HOMODIMERIZATION.
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: 11042189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION.
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: 11549352] [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: 11836244] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-45.
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), VARIANT SER-531.
Tissue: Lymphoid.
[6]"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).
[7]"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), VARIANTS SER-531 AND THR-784.
[8]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 SER-531.
Tissue: Brain.
[9]"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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORM 2).
Tissue: Colon.
[11]"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: 12535642] [Abstract]
Cited for: INTERACTION WITH ZNF33A.
[12]"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: 12761180] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH PKN1.
[13]"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: 15172994] [Abstract]
Cited for: FUNCTION.
[14]"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: 15342622] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-161 AND SER-165, MUTAGENESIS OF THR-161; THR-162 AND SER-165.
[15]"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: 15684425] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3, SUBCELLULAR LOCATION.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, MASS SPECTROMETRY.
Tissue: Epithelium.
[17]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, MASS SPECTROMETRY.
[18]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-637, MASS SPECTROMETRY.
[19]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591; SER-593 AND SER-599, MASS SPECTROMETRY.
[20]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-268; SER-275; SER-302; THR-328; SER-593; THR-628; SER-633; SER-637; SER-687; SER-691; SER-727; SER-733 AND SER-781, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339; SER-434 AND SER-454 (ISOFORM 2), MASS SPECTROMETRY.
[21]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; THR-628; SER-633; SER-727 AND SER-733, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-454 (ISOFORM 2), MASS SPECTROMETRY.
[22]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-267; THR-281; VAL-281; SER-531; TRP-580; THR-740; HIS-773 AND THR-784.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
AF465843 mRNA. Translation: AAO33376.1.
AF251441 mRNA. Translation: AAF65822.1.
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.
BC001401 mRNA. Translation: AAH01401.1.
IPIIPI00029643.
IPI00329638.
IPI00384771.
RefSeqNP_057737.2.
NP_598407.1.
UniGeneHs.444451

3D structure databases

HSSPHSSP built from PDB template 1BYG based on UniProtKB P41240.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NYL2. 6 interactions.
STRINGQ9NYL2.

PTM databases

PhosphoSiteQ9NYL2.

Proteomic databases

PRIDEQ9NYL2.

Genome annotation databases

EnsemblENST00000338983; ENSP00000340257; ENSG00000091436; Homo sapiens. [Genome view]
ENST00000375213; ENSP00000364361; ENSG00000091436; Homo sapiens. [Genome view]
ENST00000409176; ENSP00000387259; ENSG00000091436; Homo sapiens. [Genome view]
ENST00000422149; ENSP00000411923; ENSG00000091436; Homo sapiens. [Genome view]
ENST00000431503; ENSP00000399787; ENSG00000091436; Homo sapiens. [Genome view]
GeneID51776.
KEGGhsa:51776.
UCSCuc002uhx.2. human.
uc002uhy.1. human.
uc002uhz.1. human.

Organism-specific databases

CTD51776.
GeneCardsGC02P173648.
H-InvDBHIX0002600.
HIX0030332.
HPAHPA017205.
MIM609479. gene.

Phylogenomic databases

HOVERGENQ9NYL2.
OMAHYLHAEA.

Enzyme and pathway databases

BRENDA2.7.11.25. 247.
Pathway_Interaction_DBp38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.

Gene expression databases

ArrayExpressQ9NYL2.
BgeeQ9NYL2.
GenevestigatorQ9NYL2.
GermOnlineENSG00000091436. Homo sapiens.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR011510. SAM_2.
IPR013761. SAM_type.
IPR008271. Ser_thr_pkin_AS.
IPR001245. Tyr_pkinase.
[Graphical view]
Gene3DG3DSA:1.10.150.50. SAM_type. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00454. SAM. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio55903.
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Entry information

Entry nameMLTK_HUMAN
AccessionPrimary (citable) accession number: Q9NYL2
Secondary accession number(s): Q53SX1 expand/collapse secondary AC list , Q580W8, Q59GY5, Q86YW8, Q9HCC4, Q9HCC5, Q9HDD2, Q9NYE9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: November 3, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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