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Reviewed, UniProtKB/Swiss-Prot P42679 (MATK_HUMAN)

Last modified November 25, 2008. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Megakaryocyte-associated tyrosine-protein kinase
    EC=2.7.10.2
Alternative name(s):
    Tyrosine-protein kinase CTK
    Protein kinase HYL
    Hematopoietic consensus tyrosine-lacking kinase
Gene names
Name: MATK
Synonyms: CTK, HYL
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Catalytic activity

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

Subcellular location

Cytoplasm.

Tissue specificity

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

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Megakaryocyte-associated tyrosine-protein kinase
PRO_0000088073

Regions

Domain58 – 11053SH3
Domain122 – 21190SH2
Domain235 – 482248Protein kinase
Nucleotide binding241 – 2499ATP By similarity

Sites

Active site3521Proton acceptor By similarity
Binding site2621ATP By similarity

Amino acid modifications

Modified residue5011Phosphoserine
Modified residue5041Phosphoserine

Natural variations

Natural variant3541A → T in an ovarian mucinous carcinoma sample; somatic mutation.
VAR_041679
Natural variant4961A → T
VAR_041680
Natural variant5031R → Q in a colorectal adenocarcinoma sample; somatic mutation.
VAR_041681

Experimental info

Sequence conflict107 – 1082ER → DG in AAA16703. Ref.1
Sequence conflict4001Missing in AAA16703. Ref.1
Sequence conflict466 – 50742ARRPP…RSQEP → PAGHPSANWPRSWPGSYAVQ VPQPPSQGRTPTVHLAPKPG ALTPPGGPWPQRTERVESAA WGH in AAA16703. Ref.1

Secondary structure

................................ 507
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42679-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 85721C6E024575EF

FASTA50756,469
        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 

« Hide

References

« Hide '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: 8134117] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8288563] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 7530249] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[4]"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. expand/collapse author list , 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: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Eye.
[6]"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: 7936664] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501 AND SER-504, MASS SPECTROMETRY.
[9]"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-501, MASS SPECTROMETRY.
[10]"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.
[11]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-354; THR-496 AND GLN-503.
+Additional computationally mapped references.

Cross-references

Sequence databases

L18974 mRNA. Translation: AAA16703.1.
X77278 mRNA. Translation: CAA54493.1.
S75168 expand/collapse EMBL AC list , S75145, S75147, S75166, S75151, S75153, S75155, S75156, S75158, S75159, S75162, S75164 Genomic DNA. Translation: AAC60645.1.
AC005777 Genomic DNA. Translation: AAC62843.1.
BC000114 mRNA. Translation: AAH00114.1.
BC003109 mRNA. Translation: AAH03109.1.
PIRA49865.
A55625.
RefSeqNP_647612.1.
UniGeneHs.631845

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JWOX-ray2.50A117-213[»]
1X6GNMR-A39-108[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP42679.

PTM databases

PhosphoSiteP42679.

Genome annotation databases

EnsemblENSG00000007264. Homo sapiens. [Contig view]
GeneID4145.
KEGGhsa:4145.

Organism-specific databases

HGNCHGNC:6906. MATK.
HPAHPA004847.
MIM600038. gene.
PharmGKBPA30649.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP42679.

Gene expression databases

ArrayExpressP42679.
CleanExHS_MATK.
GermOnlineENSG00000007264. Homo sapiens.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR000980. SH2.
IPR001452. SH3.
IPR015773. Tyr_kinase_megakaryocyte-assoc.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PANTHERPTHR23256:SF134. MATK. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. 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]
ProtoNetSearch...

Other Resources

LinkHubP42679.
NextBio16280.
SOURCESearch...

Entry information

Entry nameMATK_HUMAN
AccessionPrimary (citable) accession number: P42679
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents