P42679 (MATK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Megakaryocyte-associated tyrosine-protein kinase
EC=2.7.10.2

Alternative name(s):
CSK homologous kinase
Short name=CHK
Hematopoietic consensus tyrosine-lacking kinase
Protein kinase HYL
Tyrosine-protein kinase CTK

Gene names

Name:	MATK
Synonyms:	CTK, HYL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC-family members in brain by specifically phosphorylating their C-terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T-cell proliferation. Ref.10
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with KIT. Ref.11
Subcellular location	Cytoplasm. Membrane. Note: In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation. Ref.10
Tissue specificity	Expressed in various myeloid cell lines, detected in brain and lung.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement Ref.2. Source: ProtInc mesoderm development Traceable author statement Ref.2. Source: ProtInc positive regulation of cell proliferation Traceable author statement PubMed 8999872. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-751664,EBI-352572

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P42679-1)

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 (identifier: P42679-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MAGRGSLVSWRAFHGCDSAEELPR → MQGHFPAERREGRPRRGTRGQQQLL

Note: No experimental confirmation available.

Isoform 3 (identifier: P42679-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 507

507

Megakaryocyte-associated tyrosine-protein kinase

PRO_0000088073

Regions

Domain

58 – 110

53

SH3

Domain

122 – 211

90

SH2

Domain

235 – 482

248

Protein kinase

Nucleotide binding

241 – 249

9

ATP By similarity

Sites

Active site

352

1

Proton acceptor By similarity

Binding site

262

1

ATP By similarity

Amino acid modifications

Modified residue

501

1

Phosphoserine Ref.14

Natural variations

Alternative sequence

1 – 41

41

Missing in isoform 3.

VSP_044277

Alternative sequence

1 – 24

24

MAGRG…EELPR → MQGHFPAERREGRPRRGTRG QQQLL in isoform 2.

VSP_043123

Natural variant

354

1

A → T in an ovarian mucinous carcinoma sample; somatic mutation. Ref.18

VAR_041679

Natural variant

496

1

A → T. Ref.18
Corresponds to variant rs35351680 [ dbSNP | Ensembl ].

VAR_041680

Natural variant

503

1

R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.18

VAR_041681

Experimental info

Sequence conflict

107 – 108

2

ER → DG in AAA16703. Ref.1

Sequence conflict

400

1

Missing in AAA16703. Ref.1

Sequence conflict

466 – 507

42

ARRPP…RSQEP → PAGHPSANWPRSWPGSYAVQ VPQPPSQGRTPTVHLAPKPG ALTPPGGPWPQRTERVESAA WGH in AAA16703. Ref.1

Secondary structure

1

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507

Helix Strand Turn

Details...

Beta strand

52 – 57

6

Beta strand

59 – 61

3

Beta strand

74 – 79

6

Beta strand

83 – 91

9

Turn

92 – 94

3

Beta strand

97 – 101

5

Helix

102 – 104

3

Beta strand

105 – 107

3

Beta strand

123 – 126

4

Helix

129 – 135

7

Beta strand

144 – 148

5

Beta strand

150 – 152

3

Beta strand

156 – 162

7

Beta strand

165 – 174

10

Beta strand

177 – 188

12

Helix

189 – 198

10

Beta strand

203 – 205

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 85721C6E024575EF	FASTA	507	56,469
	10 20 30 40 50 60 MAGRGSLVSW RAFHGCDSAE ELPRVSPRFL RAWHPPPVSA RMPTRRWAPG TQCITKCEHT 70 80 90 100 110 120 RPKPGELAFR KGDVVTILEA CENKSWYRVK HHTSGQEGLL AAGALREREA LSADPKLSLM 130 140 150 160 170 180 PWFHGKISGQ EAVQQLQPPE DGLFLVRESA RHPGDYVLCV SFGRDVIHYR VLHRDGHLTI 190 200 210 220 230 240 DEAVFFCNLM DMVEHYSKDK GAICTKLVRP KRKHGTKSAE EELARAGWLL NLQHLTLGAQ 250 260 270 280 290 300 IGEGEFGAVL QGEYLGQKVA VKNIKCDVTA QAFLDETAVM TKMQHENLVR LLGVILHQGL 310 320 330 340 350 360 YIVMEHVSKG NLVNFLRTRG RALVNTAQLL QFSLHVAEGM EYLESKKLVH RDLAARNILV 370 380 390 400 410 420 SEDLVAKVSD FGLAKAERKG LDSSRLPVKW TAPEALKHGK FTSKSDVWSF GVLLWEVFSY 430 440 450 460 470 480 GRAPYPKMSL KEVSEAVEKG YRMEPPEGCP GPVHVLMSSC WEAEPARRPP FRKLAEKLAR 490 500 ELRSAGAPAS VSGQDADGST SPRSQEP
	Isoform 2 [UniParc]. Checksum: CEFD5D74DAC082E5	FASTA	508	56,798
	10 20 30 40 50 60 MQGHFPAERR EGRPRRGTRG QQQLLVSPRF LRAWHPPPVS ARMPTRRWAP GTQCITKCEH 70 80 90 100 110 120 TRPKPGELAF RKGDVVTILE ACENKSWYRV KHHTSGQEGL LAAGALRERE ALSADPKLSL 130 140 150 160 170 180 MPWFHGKISG QEAVQQLQPP EDGLFLVRES ARHPGDYVLC VSFGRDVIHY RVLHRDGHLT 190 200 210 220 230 240 IDEAVFFCNL MDMVEHYSKD KGAICTKLVR PKRKHGTKSA EEELARAGWL LNLQHLTLGA 250 260 270 280 290 300 QIGEGEFGAV LQGEYLGQKV AVKNIKCDVT AQAFLDETAV MTKMQHENLV RLLGVILHQG 310 320 330 340 350 360 LYIVMEHVSK GNLVNFLRTR GRALVNTAQL LQFSLHVAEG MEYLESKKLV HRDLAARNIL 370 380 390 400 410 420 VSEDLVAKVS DFGLAKAERK GLDSSRLPVK WTAPEALKHG KFTSKSDVWS FGVLLWEVFS 430 440 450 460 470 480 YGRAPYPKMS LKEVSEAVEK GYRMEPPEGC PGPVHVLMSS CWEAEPARRP PFRKLAEKLA 490 500 RELRSAGAPA SVSGQDADGS TSPRSQEP
	Isoform 3 [UniParc]. Checksum: B2C4DFFE995D5FEE	FASTA	466	51,899
	10 20 30 40 50 60 MPTRRWAPGT QCITKCEHTR PKPGELAFRK GDVVTILEAC ENKSWYRVKH HTSGQEGLLA 70 80 90 100 110 120 AGALREREAL SADPKLSLMP WFHGKISGQE AVQQLQPPED GLFLVRESAR HPGDYVLCVS 130 140 150 160 170 180 FGRDVIHYRV LHRDGHLTID EAVFFCNLMD MVEHYSKDKG AICTKLVRPK RKHGTKSAEE 190 200 210 220 230 240 ELARAGWLLN LQHLTLGAQI GEGEFGAVLQ GEYLGQKVAV KNIKCDVTAQ AFLDETAVMT 250 260 270 280 290 300 KMQHENLVRL LGVILHQGLY IVMEHVSKGN LVNFLRTRGR ALVNTAQLLQ FSLHVAEGME 310 320 330 340 350 360 YLESKKLVHR DLAARNILVS EDLVAKVSDF GLAKAERKGL DSSRLPVKWT APEALKHGKF 370 380 390 400 410 420 TSKSDVWSFG VLLWEVFSYG RAPYPKMSLK EVSEAVEKGY RMEPPEGCPG PVHVLMSSCW 430 440 450 460 EAEPARRPPF RKLAEKLARE LRSAGAPASV SGQDADGSTS PRSQEP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase)." Sakano S., Iwama A., Inazawa J., Ariyama T., Ohno M., Suda T. Oncogene 9:1155-1161(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Identification and characterization of a novel tyrosine kinase from megakaryocytes." Bennett B.D., Cowley S., Jiang S., London R., Deng B., Grabarek J., Groopman J.E., Goeddel D.V., Avraham H. J. Biol. Chem. 269:1068-1074(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Megakaryocyte.
[3]	"Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product." Avraham S., Jiang S., Ota S., Fu Y., Deng B., Dowler L.L., White R.A., Avraham H. J. Biol. Chem. 270:1833-1842(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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). Tissue: Brain.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Testis.
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton 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. , 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].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye.
[9]	"Characterization of mouse non-receptor tyrosine kinase gene, HYL." Hamaguchi I., Iwama A., Yamaguchi N., Sakano S., Matsuda Y., Suda T. Oncogene 9:3371-3374(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets." Hirao A., Hamaguchi I., Suda T., Yamaguchi N. EMBO J. 16:2342-2351(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. Tissue: Platelet.
[11]	"Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes." Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H. J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIT.
[12]	"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor." Roskoski R. Jr. Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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-501, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[17]	"Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 39-108.
[18]	"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] THR-354; THR-496 AND GLN-503.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L18974 mRNA. Translation: AAA16703.1.
X77278 mRNA. Translation: CAA54493.1.
S75164 , S75145, S75147, S75166, S75168, S75151, S75153, S75155, S75156, S75158, S75159, S75162 Genomic DNA. Translation: AAC60645.1.
AK055395 mRNA. Translation: BAG51511.1.
AL137754 mRNA. Translation: CAB70906.2.
AC005777 Genomic DNA. Translation: AAC62843.1.
CH471139 Genomic DNA. Translation: EAW69285.1.
BC000114 mRNA. Translation: AAH00114.1.
BC003109 mRNA. Translation: AAH03109.1.

IPI

IPI00000868.
IPI00477563.

PIR

A49865.
A55625.

RefSeq

NP_002369.2. NM_002378.3.
NP_647611.1. NM_139354.2.
NP_647612.1. NM_139355.2.

UniGene

Hs.631845.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JWO	X-ray	2.50	A	117-213	[»]
1X6G	NMR	-	A	41-108	[»]
3US4	X-ray	1.50	A	117-213	[»]

ProteinModelPortal

P42679.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42679. 3 interactions.

MINT

MINT-1496198.

STRING

9606.ENSP00000313859.

PTM databases

PhosphoSite

P42679.

Polymorphism databases

DMDM

1169123.

Proteomic databases

PaxDb

P42679.

PRIDE

P42679.

Protocols and materials databases

DNASU

4145.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310132; ENSP00000308734; ENSG00000007264.
ENST00000395040; ENSP00000378481; ENSG00000007264.
ENST00000395045; ENSP00000378485; ENSG00000007264.

GeneID

4145.

KEGG

hsa:4145.

UCSC

uc002lyt.3. human.

Organism-specific databases

CTD

4145.

GeneCards

GC19M003777.

HGNC

HGNC:6906. MATK.

HPA

HPA004847.

MIM

600038. gene.

neXtProt

NX_P42679.

PharmGKB

PA30649.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

KO

K08888.

OMA

KHGKFSS.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P42679.

Bgee

P42679.

CleanEx

HS_MATK.

Genevestigator

P42679.

GermOnline

ENSG00000007264. Homo sapiens.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P42679.

ChEMBL

CHEMBL4175.

EvolutionaryTrace

P42679.

GenomeRNAi

4145.

NextBio

16280.

SOURCE

Search...

Entry information

Entry name

MATK_HUMAN

Accession

Primary (citable) accession number: P42679
Secondary accession number(s): B3KNZ9, Q9NST8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.