Reviewed, UniProtKB/Swiss-Prot Q9NYL2 (MLTK_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	800 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Cell cycle
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Proto-oncogene
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA 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 component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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
itself		1	EBI-602273,EBI-602273
PKN1	Q16512	1	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 800	800	Mitogen-activated protein kinase kinase kinase MLT		PRO_0000086338
Regions
	Domain	16 – 277	262	Protein kinase
	Domain	287 – 308	22	Leucine-zipper UniProtKB P80192
	Domain	339 – 410	72	SAM
	Nucleotide binding	22 – 30	9	ATP By similarity UniProtKB P80192
Sites
	Active site	133	1	Proton acceptor By similarity UniProtKB P80192
	Binding site	45	1	ATP Ref.4
Amino acid modifications
	Modified residue	3	1	Phosphoserine Ref.20
	Modified residue	161	1	Phosphothreonine; by autocatalysis Ref.14
	Modified residue	165	1	Phosphoserine; by autocatalysis Ref.14
	Modified residue	268	1	Phosphoserine Ref.20
	Modified residue	275	1	Phosphoserine Ref.20
	Modified residue	302	1	Phosphoserine Ref.20
	Modified residue	328	1	Phosphothreonine Ref.20
	Modified residue	591	1	Phosphoserine Ref.19
	Modified residue	593	1	Phosphoserine Ref.20 Ref.19
	Modified residue	599	1	Phosphoserine Ref.19 Ref.21
	Modified residue	628	1	Phosphothreonine Ref.20 Ref.21
	Modified residue	633	1	Phosphoserine Ref.20 Ref.21 Ref.18
	Modified residue	635	1	Phosphoserine By similarity
	Modified residue	637	1	Phosphoserine Ref.20 Ref.18 Ref.16 Ref.17
	Modified residue	639	1	Phosphothreonine By similarity
	Modified residue	687	1	Phosphoserine Ref.20
	Modified residue	691	1	Phosphoserine Ref.20
	Modified residue	727	1	Phosphoserine Ref.20 Ref.21
	Modified residue	733	1	Phosphoserine Ref.20 Ref.21
	Modified residue	781	1	Phosphoserine Ref.20
Natural variations
	Alternative sequence	285 – 312	28	CEIEA…LKERE → WVAPTAGHSVWLSKTITRLN EEVNQRSE in isoform 3. Ref.4		VSP_051741
	Alternative sequence	313 – 800	488	Missing in isoform 3. Ref.4		VSP_051742
	Alternative sequence	332 – 455	124	PSFEI…GPQDC → LPLAARMSEESYFESKTEES NSAEMSCQITATSNGEGHGM NPSLQAMMLMGFGDIFSMNK AGAVMHSGMQINMQAKQNSS KTTSKRRGKKVNMALGFSDF DLSEGDDDDDDDGEEEDNDM DNSE in isoform 2. Ref.2		VSP_051743
	Alternative sequence	456 – 800	345	Missing in isoform 2. Ref.2		VSP_051744
	Natural variant	267	1	T → M		VAR_040806
	Natural variant	281	1	A → T in an ovarian endometrioid sample; somatic mutation. Ref.22		VAR_040807
	Natural variant	281	1	A → V		VAR_040808
	Natural variant	531	1	L → S: dbSNP rs3769148. Ref.22 Ref.5 Ref.7 Ref.8		VAR_022827
	Natural variant	580	1	R → W		VAR_040809
	Natural variant	740	1	P → T		VAR_040810
	Natural variant	773	1	Y → H		VAR_040811
	Natural variant	784	1	K → T		VAR_040812
Experimental info
	Mutagenesis	45	1	K → M: Loss of kinase activity. Ref.4
	Mutagenesis	161	1	T → A: Loss of autophosphorylation activity. Ref.14
	Mutagenesis	162	1	T → A: Slight loss of autophosphorylation activity. Ref.14
	Mutagenesis	165	1	S → A: Loss of autophosphorylation activity. Ref.14
	Sequence conflict	346	1	C → W in AAF63490. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified July 5, 2005. Version 2. Checksum: B289D836EC52E295	FASTA	800	91,181
	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
	Isoform 2 (Beta). Checksum: E87DB84A4D58B752	FASTA	455	51,582
	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 LLPLAARMSE ESYFESKTEE SNSAEMSCQI 370 380 390 400 410 420 TATSNGEGHG MNPSLQAMML MGFGDIFSMN KAGAVMHSGM QINMQAKQNS SKTTSKRRGK 430 440 450 KVNMALGFSD FDLSEGDDDD DDDGEEEDND MDNSE
	Isoform 3 (HCCS-4). Checksum: B655E873246339FB	FASTA	312	35,468
	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 AEWRWVAPTA GHSVWLSKTI 310 TRLNEEVNQR SE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00029643. IPI00329638. IPI00384771.
RefSeq	NP_057737.2. NP_598407.1.
UniGene	Hs.444451
3D structure databases
HSSP	HSSP built from PDB template 1BYG based on UniProtKB P41240.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NYL2. 6 interactions.
STRING	Q9NYL2.
PTM databases
PhosphoSite	Q9NYL2.
Proteomic databases
PRIDE	Q9NYL2.
Genome annotation databases
Ensembl	ENST00000338983; 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]
GeneID	51776.
KEGG	hsa:51776.
UCSC	uc002uhx.2. human. uc002uhy.1. human. uc002uhz.1. human.
Organism-specific databases
CTD	51776.
GeneCards	GC02P173648.
H-InvDB	HIX0002600. HIX0030332.
HPA	HPA017205.
MIM	609479. gene.
Phylogenomic databases
HOVERGEN	Q9NYL2.
OMA	HYLHAEA.
Enzyme and pathway databases
BRENDA	2.7.11.25. 247.
Pathway_Interaction_DB	p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.
Gene expression databases
ArrayExpress	Q9NYL2.
Bgee	Q9NYL2.
Genevestigator	Q9NYL2.
GermOnline	ENSG00000091436. Homo sapiens.
Family and domain databases
InterPro	IPR000719. 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]
Gene3D	G3DSA:1.10.150.50. SAM_type. 1 hit.
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF07647. SAM_2. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00454. SAM. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50105. SAM_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	55903.
SOURCE	Search...

Entry information

Entry name

MLTK_HUMAN

Accession

Primary (citable) accession number: Q9NYL2
Secondary accession number(s): Q53SX1 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.