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Non-receptor tyrosine-protein kinase TNK1 (EC 2.7.10.2) (Kinase of embryonic stem cells)

 TNK1_MOUSE              Reviewed;         666 AA.
Q99ML2; Q8CCC4; Q8K0X9; Q91V11;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 2.
22-NOV-2017, entry version 131.
RecName: Full=Non-receptor tyrosine-protein kinase TNK1;
EC=2.7.10.2;
AltName: Full=Kinase of embryonic stem cells;
Name=Tnk1 {ECO:0000312|EMBL:AAK35164.1};
Synonyms=Kos1 {ECO:0000312|MGI:MGI:1930958};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL09413.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), FUNCTION,
AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-148, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
STRAIN=129/Sv {ECO:0000312|EMBL:AAL09412.1};
TISSUE=Embryonic stem cell;
PubMed=12789265; DOI=10.1038/sj.onc.1206480;
Hoare K., Hoare S., Smith O.M., Kalmaz G., Small D., May W.S. Jr.;
"Kos1, a nonreceptor tyrosine kinase that suppresses Ras signaling.";
Oncogene 22:3562-3577(2003).
[2] {ECO:0000305, ECO:0000312|EMBL:AAK35164.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hoehn G.T., Felschow D.M., Civin C.I.;
"Cloning of the murine Tnk1 tyrosine kinase and evidence that it plays
a role in cell adhesion.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:AAH29623.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH55303.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH29623.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-666 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Colon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18974114; DOI=10.1158/0008-5472.CAN-08-1467;
Hoare S., Hoare K., Reinhard M.K., Lee Y.J., Oh S.P., May W.S. Jr.;
"Tnk1/Kos1 knockout mice develop spontaneous tumors.";
Cancer Res. 68:8723-8732(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May function in signaling pathways utilized broadly
during fetal development and more selectively in adult tissues and
in cells of the lymphohematopoietic system. Could specifically be
involved in phospholipid signal transduction (By similarity).
Involved in negative regulation of cell growth. Has tumor
suppressor properties. Plays a negative regulatory role in the
Ras-MAPK pathway. {ECO:0000250, ECO:0000269|PubMed:12789265,
ECO:0000269|PubMed:18974114}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Interacts with the SH3 domain of PLCG1 via its Pro-rich
domain. {ECO:0000250|UniProtKB:Q13470}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:12789265}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|Ref.2};
IsoId=Q99ML2-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:12789265};
IsoId=Q99ML2-2; Sequence=VSP_051664, VSP_051665;
-!- TISSUE SPECIFICITY: Expressed in whole embryo and all adult
tissues examined including liver, kidney, heart, brain, skeletal
muscle and intestine. Also detected in various myeloid- and
lymphoid-derived cell lines. {ECO:0000269|PubMed:12789265}.
-!- DEVELOPMENTAL STAGE: Expression during embryogenesis increases
between E7 and E11. Levels of expression subsequently decrease and
reach a steady-state level by E17. {ECO:0000269|PubMed:12789265}.
-!- PTM: Autophosphorylated on tyrosine residues.
{ECO:0000269|PubMed:12789265}.
-!- DISRUPTION PHENOTYPE: Mice develop spontaneous tumors, including
lymphomas and carcinomas at high rates.
{ECO:0000269|PubMed:18974114}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AF307745; AAL09412.1; -; Genomic_DNA.
EMBL; AF307746; AAL09413.1; -; mRNA.
EMBL; AF332512; AAK35164.1; -; mRNA.
EMBL; BC029623; AAH29623.1; -; mRNA.
EMBL; BC055303; AAH55303.1; -; mRNA.
EMBL; AK033440; BAC28288.1; -; mRNA.
CCDS; CCDS24917.1; -. [Q99ML2-1]
RefSeq; NP_114086.3; NM_031880.3. [Q99ML2-1]
RefSeq; XP_006534617.1; XM_006534554.3. [Q99ML2-1]
UniGene; Mm.28874; -.
UniGene; Mm.358793; -.
ProteinModelPortal; Q99ML2; -.
SMR; Q99ML2; -.
STRING; 10090.ENSMUSP00000001626; -.
iPTMnet; Q99ML2; -.
PhosphoSitePlus; Q99ML2; -.
PaxDb; Q99ML2; -.
PRIDE; Q99ML2; -.
Ensembl; ENSMUST00000001626; ENSMUSP00000001626; ENSMUSG00000001583. [Q99ML2-1]
Ensembl; ENSMUST00000108626; ENSMUSP00000104266; ENSMUSG00000001583. [Q99ML2-2]
GeneID; 83813; -.
KEGG; mmu:83813; -.
UCSC; uc007jsb.2; mouse. [Q99ML2-1]
UCSC; uc007jsc.2; mouse. [Q99ML2-2]
CTD; 8711; -.
MGI; MGI:1930958; Tnk1.
eggNOG; KOG0199; Eukaryota.
eggNOG; ENOG410XPRC; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000231055; -.
HOVERGEN; HBG055513; -.
InParanoid; Q99ML2; -.
KO; K08885; -.
OMA; EADLLCY; -.
TreeFam; TF316643; -.
PRO; PR:Q99ML2; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000001583; -.
CleanEx; MM_TNK1; -.
ExpressionAtlas; Q99ML2; baseline and differential.
Genevisible; Q99ML2; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; SH3 domain; Transferase; Tyrosine-protein kinase.
CHAIN 1 666 Non-receptor tyrosine-protein kinase
TNK1.
/FTId=PRO_0000088174.
DOMAIN 116 383 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 381 441 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
NP_BIND 122 130 ATP. {ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159}.
COMPBIAS 507 560 Pro-rich.
ACT_SITE 245 245 Proton acceptor.
{ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028}.
BINDING 148 148 ATP. {ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000250|UniProtKB:Q13470}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:Q13470}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 510 510 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13470}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000250|UniProtKB:Q13470}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000250|UniProtKB:Q13470}.
VAR_SEQ 381 434 AWLSEGRCVREVTEPGALRMEPGDPITIIEGSLDTATWKGQ
NGRTLKVGNFPAS -> VRIPNSPYTHIAFLPCILSPSVPC
RRQTRLGAWAGIWNSAQNQVQSLPAGSAEP (in
isoform 2).
{ECO:0000303|PubMed:12789265}.
/FTId=VSP_051664.
VAR_SEQ 435 666 Missing (in isoform 2).
{ECO:0000303|PubMed:12789265}.
/FTId=VSP_051665.
MUTAGEN 148 148 K->A: Loss of autophosphorylation.
{ECO:0000269|PubMed:12789265}.
CONFLICT 46 46 L -> V (in Ref. 2; AAK35164).
{ECO:0000305}.
CONFLICT 59 59 L -> I (in Ref. 2; AAK35164).
{ECO:0000305}.
CONFLICT 206 206 A -> T (in Ref. 3; AAH29623/AAH55303).
{ECO:0000305}.
CONFLICT 534 534 P -> S (in Ref. 2; AAK35164).
{ECO:0000305}.
SEQUENCE 666 AA; 73099 MW; 5AE6A48D99BADE8B CRC64;
MLPEASSLWL LRLLRDVQLA QFYRPILEEL NVTRPEHFDF VRPEDLDNIG MGRPAQRRLN
EALKRYRSGV KSKNWVYKIL GGFAPEQKEI PPRSDSPLCF HEPEGGLKCL IPEGAVRRGE
LLGSGCFGVV HRGLWTLPSG QSIPVAVKSL RVGPEGPMGT ELGDFLREVS VMMKLEHPHV
LRLHGLVLGQ PLQMVMELAP LGSLHARLTA PAPTPPLPVA LLCLFLRQLA GAMAYLGSCG
LVHRDLATRN LLLASPRMIK VADFGLVRPL GGARGRYVMG GPRPIPYAWC APESLRQGAF
SSASDVWMFG VTLWEMFSGG EEPWAGVPPY LILQRLEKDR ARLPKPPLCS RALYSLALRC
WAPHPADRPS FSNLEGLLQE AWLSEGRCVR EVTEPGALRM EPGDPITIIE GSLDTATWKG
QNGRTLKVGN FPASAVTLAD LGGSPVTHPA HRGSPAHGEK CRGGTDGDRE KATLQDLPPA
RSHRTKMPLQ RMRGISKSLE SVLSLGPRPT GGGSSPPELR RTRAMPQRLP DLPPRPPDLP
PRPPIICNSS QPTQPHKARP KRESSHNHRT GAPGASKATV PSGGPLSDPE WQRKVVEVEL
SVHGVTYQEC QVALRTTGGD VASAIRNLKV DQLFHLSNRS RADCRRILEH HQWDLSAASR
YILARS


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