ID C9J1X3_HUMAN Unreviewed; 1040 AA.
AC C9J1X3;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=TNK2 {ECO:0000313|Ensembl:ENSP00000392546.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000392546.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0007829|PubMed:15592455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [2] {ECO:0007829|PubMed:17081983}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [3] {ECO:0000313|Ensembl:ENSP00000392546.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4] {ECO:0007829|PubMed:18691976}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6] {ECO:0007829|PubMed:19369195}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8] {ECO:0000313|Ensembl:ENSP00000392546.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AC124944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001294975.1; NM_001308046.1.
DR AlphaFoldDB; C9J1X3; -.
DR SMR; C9J1X3; -.
DR IntAct; C9J1X3; 1.
DR MassIVE; C9J1X3; -.
DR MaxQB; C9J1X3; -.
DR PeptideAtlas; C9J1X3; -.
DR ProteomicsDB; 8138; -.
DR Antibodypedia; 4095; 824 antibodies from 40 providers.
DR DNASU; 10188; -.
DR Ensembl; ENST00000428187.7; ENSP00000392546.1; ENSG00000061938.21.
DR GeneID; 10188; -.
DR UCSC; uc003fvs.2; human.
DR CTD; 10188; -.
DR HGNC; HGNC:19297; TNK2.
DR VEuPathDB; HostDB:ENSG00000061938; -.
DR GeneTree; ENSGT00940000160853; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 10188; 11 hits in 1191 CRISPR screens.
DR ChiTaRS; TNK2; human.
DR GenomeRNAi; 10188; -.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000061938; Expressed in right hemisphere of cerebellum and 192 other cell types or tissues.
DR ExpressionAtlas; C9J1X3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd14328; UBA_TNK1; 1.
DR Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR037085; Cdc42-bd-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021619; Mig-6.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1.
DR PANTHER; PTHR14254:SF6; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF11555; Inhibitor_Mig-6; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|EPD:C9J1X3,
KW ECO:0007829|MaxQB:C9J1X3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 158..417
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 420..480
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 122..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1040 AA; 114950 MW; C2E28B9C4BBCF45F CRC64;
MPAARRFPGL ELSFPLLARL RRRLYTRLGG GRMQPEEGTG WLLELLSEVQ LQQYFLRLRD
DLNVTRLSHF EYVKNEDLEK IGMGRPGQRR LWEAVKRRKA LCKRKSWMSK VFSGKRLEAE
FPPHHSQSTF RKTSPAPGGP AGEGPLQSLT CLIGEKDLRL LEKLGDGSFG VVRRGEWDAP
SGKTVSVAVK CLKPDVLSQP EAMDDFIREV NAMHSLDHRN LIRLYGVVLT PPMKMVTELA
PLGSLLDRLR KHQGHFLLGT LSRYAVQVAE GMGYLESKRF IHRDLAARNL LLATRDLVKI
GDFGLMRALP QNDDHYVMQE HRKVPFAWCA PESLKTRTFS HASDTWMFGV TLWEMFTYGQ
EPWIGLNGSQ ILHKIDKEGE RLPRPEDCPQ DIYNVMVQCW AHKPEDRPTF VALRDFLLEA
QPTDMRALQD FEEPDKLHIQ MNDVITVIEG RAENYWWRGQ NTRTLCVGPF PRNVVTSVAG
LSAQDISQPL QNSFIHTGHG DSDPRHCWGF PDRIDELYLG NPMDPPDLLS VELSTSRPPQ
HLGGVKKPTY DPVSEDQDPL SSDFKRLGLR KPGLPRGLWL AKPSARVPGT KASRGSGAEV
TLIDFGEEPV VPALRPCAPS LAQLAMDACS LLDETPPQSP TRALPRPLHP TPVVDWDARP
LPPPPAYDDV AQDEDDFEIC SINSTLVGAG VPAGPSQGQT NYAFVPEQAR PPPPLEDNLF
LPPQGGGKPP SSAQTAEIFQ ALQQECMRQL QAPAGSPAPS PSPGGDDKPQ VPPRVPIPPR
PTRPHVQLSP APPGEEETSQ WPGPASPPRV PPREPLSPQG SRTPSPLVPP GSSPLPPRLS
SSPGKTMPTT QSFASDPKYA TPQVIQAPGP RAGPCILPIV RDGKKVSSTH YYLLPERPSY
LERYQRFLRE AQSPEEPTPL PVPLLLPPPS TPAPAAPTAT VRPMPQAALD PKANFSTNNS
NPGARPPPPR ATARLPQRGC PGDGPEAGRP ADKIQMVEQL FGLGLRPRGE CHKVLEMFDW
NLEQAGCHLL GSWGPAHHKR
//
