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Protein

Megakaryocyte-associated tyrosine-protein kinase

Gene

MATK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei262 – 2621ATPPROSITE-ProRule annotation
Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi241 – 2499ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: GO_Central
  • cell migration Source: GO_Central
  • cell proliferation Source: ProtInc
  • innate immune response Source: GO_Central
  • mesoderm development Source: ProtInc
  • morphogenesis of an epithelium Source: GO_Central
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • positive regulation of cell proliferation Source: ProtInc
  • protein phosphorylation Source: ProtInc
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_115755. Signaling by ERBB2.
SignaLinkiP42679.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MATK
Synonyms:CTK, HYL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6906. MATK.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Membrane 1 Publication

  • Note: In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30649.

Polymorphism and mutation databases

BioMutaiMATK.
DMDMi1169123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Megakaryocyte-associated tyrosine-protein kinasePRO_0000088073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei501 – 5011Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP42679.
PaxDbiP42679.
PRIDEiP42679.

PTM databases

PhosphoSiteiP42679.

Expressioni

Tissue specificityi

Expressed in various myeloid cell lines, detected in brain and lung.

Gene expression databases

BgeeiP42679.
CleanExiHS_MATK.
ExpressionAtlasiP42679. baseline and differential.
GenevisibleiP42679. HS.

Organism-specific databases

HPAiHPA004847.

Interactioni

Subunit structurei

Interacts with KIT.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP102754EBI-751664,EBI-608057
ERBB2P046262EBI-751664,EBI-641062
HSP90AB1P082382EBI-751664,EBI-352572
LRRK2Q5S0072EBI-751664,EBI-5323863

Protein-protein interaction databases

BioGridi110315. 11 interactions.
IntActiP42679. 11 interactions.
MINTiMINT-1466004.
STRINGi9606.ENSP00000378485.

Structurei

Secondary structure

1
507
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 576Combined sources
Beta strandi59 – 613Combined sources
Beta strandi74 – 796Combined sources
Beta strandi83 – 919Combined sources
Turni92 – 943Combined sources
Beta strandi97 – 1015Combined sources
Helixi102 – 1043Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi123 – 1264Combined sources
Helixi129 – 1357Combined sources
Beta strandi144 – 1485Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi156 – 1627Combined sources
Beta strandi165 – 17410Combined sources
Beta strandi177 – 18812Combined sources
Helixi189 – 19810Combined sources
Beta strandi203 – 2053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JWOX-ray2.50A117-213[»]
1X6GNMR-A41-108[»]
3US4X-ray1.50A117-213[»]
ProteinModelPortaliP42679.
SMRiP42679. Positions 39-478.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42679.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 11053SH3PROSITE-ProRule annotationAdd
BLAST
Domaini122 – 21190SH2PROSITE-ProRule annotationAdd
BLAST
Domaini235 – 482248Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP42679.
KOiK08888.
OrthoDBiEOG7SV0V5.
PhylomeDBiP42679.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P42679-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGRGSLVSW RAFHGCDSAE ELPRVSPRFL RAWHPPPVSA RMPTRRWAPG
60 70 80 90 100
TQCITKCEHT RPKPGELAFR KGDVVTILEA CENKSWYRVK HHTSGQEGLL
110 120 130 140 150
AAGALREREA LSADPKLSLM PWFHGKISGQ EAVQQLQPPE DGLFLVRESA
160 170 180 190 200
RHPGDYVLCV SFGRDVIHYR VLHRDGHLTI DEAVFFCNLM DMVEHYSKDK
210 220 230 240 250
GAICTKLVRP KRKHGTKSAE EELARAGWLL NLQHLTLGAQ IGEGEFGAVL
260 270 280 290 300
QGEYLGQKVA VKNIKCDVTA QAFLDETAVM TKMQHENLVR LLGVILHQGL
310 320 330 340 350
YIVMEHVSKG NLVNFLRTRG RALVNTAQLL QFSLHVAEGM EYLESKKLVH
360 370 380 390 400
RDLAARNILV SEDLVAKVSD FGLAKAERKG LDSSRLPVKW TAPEALKHGK
410 420 430 440 450
FTSKSDVWSF GVLLWEVFSY GRAPYPKMSL KEVSEAVEKG YRMEPPEGCP
460 470 480 490 500
GPVHVLMSSC WEAEPARRPP FRKLAEKLAR ELRSAGAPAS VSGQDADGST

SPRSQEP
Length:507
Mass (Da):56,469
Last modified:November 1, 1995 - v1
Checksum:i85721C6E024575EF
GO
Isoform 2 (identifier: P42679-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:508
Mass (Da):56,798
Checksum:iCEFD5D74DAC082E5
GO
Isoform 3 (identifier: P42679-3) [UniParc]FASTAAdd to basket

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

Show »
Length:466
Mass (Da):51,899
Checksum:iB2C4DFFE995D5FEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1082ER → DG in AAA16703 (PubMed:8134117).Curated
Sequence conflicti400 – 4001Missing in AAA16703 (PubMed:8134117).Curated
Sequence conflicti466 – 50742ARRPP…RSQEP → PAGHPSANWPRSWPGSYAVQ VPQPPSQGRTPTVHLAPKPG ALTPPGGPWPQRTERVESAA WGH in AAA16703 (PubMed:8134117).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti354 – 3541A → T in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_041679
Natural varianti496 – 4961A → T.1 Publication
Corresponds to variant rs35351680 [ dbSNP | Ensembl ].
VAR_041680
Natural varianti503 – 5031R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041681

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 3. 1 PublicationVSP_044277Add
BLAST
Alternative sequencei1 – 2424MAGRG…EELPR → MQGHFPAERREGRPRRGTRG QQQLL in isoform 2. 1 PublicationVSP_043123Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12113.1. [P42679-2]
CCDS12114.1. [P42679-1]
CCDS42468.1. [P42679-3]
PIRiA49865.
A55625.
RefSeqiNP_002369.2. NM_002378.3. [P42679-2]
NP_647611.1. NM_139354.2. [P42679-3]
NP_647612.1. NM_139355.2. [P42679-1]
XP_011526320.1. XM_011528018.1. [P42679-1]
UniGeneiHs.631845.

Genome annotation databases

EnsembliENST00000310132; ENSP00000308734; ENSG00000007264.
ENST00000395040; ENSP00000378481; ENSG00000007264. [P42679-3]
ENST00000395045; ENSP00000378485; ENSG00000007264. [P42679-2]
ENST00000619596; ENSP00000483213; ENSG00000007264. [P42679-2]
GeneIDi4145.
KEGGihsa:4145.
UCSCiuc002lyt.3. human. [P42679-1]
uc002lyv.3. human. [P42679-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12113.1. [P42679-2]
CCDS12114.1. [P42679-1]
CCDS42468.1. [P42679-3]
PIRiA49865.
A55625.
RefSeqiNP_002369.2. NM_002378.3. [P42679-2]
NP_647611.1. NM_139354.2. [P42679-3]
NP_647612.1. NM_139355.2. [P42679-1]
XP_011526320.1. XM_011528018.1. [P42679-1]
UniGeneiHs.631845.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JWOX-ray2.50A117-213[»]
1X6GNMR-A41-108[»]
3US4X-ray1.50A117-213[»]
ProteinModelPortaliP42679.
SMRiP42679. Positions 39-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110315. 11 interactions.
IntActiP42679. 11 interactions.
MINTiMINT-1466004.
STRINGi9606.ENSP00000378485.

Chemistry

BindingDBiP42679.
ChEMBLiCHEMBL4175.
GuidetoPHARMACOLOGYi2101.

PTM databases

PhosphoSiteiP42679.

Polymorphism and mutation databases

BioMutaiMATK.
DMDMi1169123.

Proteomic databases

MaxQBiP42679.
PaxDbiP42679.
PRIDEiP42679.

Protocols and materials databases

DNASUi4145.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310132; ENSP00000308734; ENSG00000007264.
ENST00000395040; ENSP00000378481; ENSG00000007264. [P42679-3]
ENST00000395045; ENSP00000378485; ENSG00000007264. [P42679-2]
ENST00000619596; ENSP00000483213; ENSG00000007264. [P42679-2]
GeneIDi4145.
KEGGihsa:4145.
UCSCiuc002lyt.3. human. [P42679-1]
uc002lyv.3. human. [P42679-2]

Organism-specific databases

CTDi4145.
GeneCardsiGC19M003777.
HGNCiHGNC:6906. MATK.
HPAiHPA004847.
MIMi600038. gene.
neXtProtiNX_P42679.
PharmGKBiPA30649.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP42679.
KOiK08888.
OrthoDBiEOG7SV0V5.
PhylomeDBiP42679.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_115755. Signaling by ERBB2.
SignaLinkiP42679.

Miscellaneous databases

EvolutionaryTraceiP42679.
GeneWikiiMegakaryocyte-associated_tyrosine_kinase.
GenomeRNAii4145.
NextBioi16280.
PROiP42679.
SOURCEiSearch...

Gene expression databases

BgeeiP42679.
CleanExiHS_MATK.
ExpressionAtlasiP42679. baseline and differential.
GenevisibleiP42679. HS.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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.
  18. "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.
  19. "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.

Entry informationi

Entry nameiMATK_HUMAN
AccessioniPrimary (citable) accession number: P42679
Secondary accession number(s): B3KNZ9, Q9NST8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.