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P42679

- MATK_HUMAN

UniProt

P42679 - MATK_HUMAN

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Protein

Megakaryocyte-associated tyrosine-protein kinase

Gene
MATK, CTK, HYL
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei262 – 2621ATP By similarity
Active sitei352 – 3521Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi241 – 2499ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein binding Source: IntAct
  4. protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. mesoderm development Source: ProtInc
  3. peptidyl-tyrosine phosphorylation Source: GOC
  4. positive regulation of cell proliferation Source: ProtInc
  5. protein phosphorylation Source: ProtInc
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: Chromosome 19

Organism-specific databases

HGNCiHGNC:6906. MATK.

Subcellular locationi

Cytoplasm. Membrane
Note: In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation.1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30649.

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

ArrayExpressiP42679.
BgeeiP42679.
CleanExiHS_MATK.
GenevestigatoriP42679.

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

Protein-protein interaction databases

BioGridi110315. 12 interactions.
IntActiP42679. 7 interactions.
MINTiMINT-1466004.
STRINGi9606.ENSP00000313859.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP42679.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 11053SH3Add
BLAST
Domaini122 – 21190SH2Add
BLAST
Domaini235 – 482248Protein kinaseAdd
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
KOiK08888.
OMAiYRAKHHA.
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. Align

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

MAGRGSLVSW RAFHGCDSAE ELPRVSPRFL RAWHPPPVSA RMPTRRWAPG    50
TQCITKCEHT RPKPGELAFR KGDVVTILEA CENKSWYRVK HHTSGQEGLL 100
AAGALREREA LSADPKLSLM PWFHGKISGQ EAVQQLQPPE DGLFLVRESA 150
RHPGDYVLCV SFGRDVIHYR VLHRDGHLTI DEAVFFCNLM DMVEHYSKDK 200
GAICTKLVRP KRKHGTKSAE EELARAGWLL NLQHLTLGAQ IGEGEFGAVL 250
QGEYLGQKVA VKNIKCDVTA QAFLDETAVM TKMQHENLVR LLGVILHQGL 300
YIVMEHVSKG NLVNFLRTRG RALVNTAQLL QFSLHVAEGM EYLESKKLVH 350
RDLAARNILV SEDLVAKVSD FGLAKAERKG LDSSRLPVKW TAPEALKHGK 400
FTSKSDVWSF GVLLWEVFSY GRAPYPKMSL KEVSEAVEKG YRMEPPEGCP 450
GPVHVLMSSC WEAEPARRPP FRKLAEKLAR ELRSAGAPAS VSGQDADGST 500
SPRSQEP 507
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

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. VSP_044277Add
BLAST
Alternative sequencei1 – 2424MAGRG…EELPR → MQGHFPAERREGRPRRGTRG QQQLL in isoform 2. VSP_043123Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1082ER → DG in AAA16703. 1 Publication
Sequence conflicti400 – 4001Missing in AAA16703. 1 Publication
Sequence conflicti466 – 50742ARRPP…RSQEP → PAGHPSANWPRSWPGSYAVQ VPQPPSQGRTPTVHLAPKPG ALTPPGGPWPQRTERVESAA WGH in AAA16703. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.631845.

Genome annotation databases

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

Polymorphism databases

DMDMi1169123.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12113.1. [P42679-2 ]
CCDS12114.1. [P42679-1 ]
CCDS42468.1. [P42679-3 ]
PIRi A49865.
A55625.
RefSeqi NP_002369.2. NM_002378.3. [P42679-2 ]
NP_647611.1. NM_139354.2. [P42679-3 ]
NP_647612.1. NM_139355.2. [P42679-1 ]
UniGenei Hs.631845.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P42679.
SMRi P42679. Positions 39-478.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110315. 12 interactions.
IntActi P42679. 7 interactions.
MINTi MINT-1466004.
STRINGi 9606.ENSP00000313859.

Chemistry

BindingDBi P42679.
ChEMBLi CHEMBL4175.
GuidetoPHARMACOLOGYi 2101.

PTM databases

PhosphoSitei P42679.

Polymorphism databases

DMDMi 1169123.

Proteomic databases

MaxQBi P42679.
PaxDbi P42679.
PRIDEi P42679.

Protocols and materials databases

DNASUi 4145.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310132 ; ENSP00000308734 ; ENSG00000007264 . [P42679-1 ]
ENST00000395040 ; ENSP00000378481 ; ENSG00000007264 . [P42679-3 ]
ENST00000395045 ; ENSP00000378485 ; ENSG00000007264 . [P42679-2 ]
GeneIDi 4145.
KEGGi hsa:4145.
UCSCi uc002lyt.3. human. [P42679-1 ]
uc002lyv.3. human. [P42679-2 ]

Organism-specific databases

CTDi 4145.
GeneCardsi GC19M003777.
HGNCi HGNC:6906. MATK.
HPAi HPA004847.
MIMi 600038. gene.
neXtProti NX_P42679.
PharmGKBi PA30649.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
KOi K08888.
OMAi YRAKHHA.
OrthoDBi EOG7SV0V5.
PhylomeDBi P42679.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_115755. Signaling by ERBB2.
SignaLinki P42679.

Miscellaneous databases

EvolutionaryTracei P42679.
GeneWikii Megakaryocyte-associated_tyrosine_kinase.
GenomeRNAii 4145.
NextBioi 16280.
PROi P42679.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42679.
Bgeei P42679.
CleanExi HS_MATK.
Genevestigatori P42679.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 158 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

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