EKS-MUM-00108
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-MUM-00108
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
TK/Tec491.31.2E-147347597251
StatusReviewed
Ensembl ProteinENSMUSP00000073509
UniProt AccessionP24604; Q9R1M9; Q9WVN0; Q9WVN1; Q9WVN2; Q9WVN3;
Protein NameTyrosine-protein kinase Tec
Protein Synonyms/Alias
Gene NameTec
Gene Synonyms/Alias Tec;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSMUSG00000029217ENSMUSP00000073509ENSMUST00000073843
ENSMUSG00000029217ENSMUSP00000109224ENSMUST00000113594
ENSMUSG00000029217ENSMUSP00000118980ENSMUST00000155342
ENSMUSG00000029217ENSMUSP00000071836ENSMUST00000071944
ENSMUSG00000029217ENSMUSP00000120155ENSMUST00000138842
ENSMUSG00000029217ENSMUSP00000123606ENSMUST00000126481
ENSMUSG00000029217ENSMUSP00000123258ENSMUST00000149533
OrganismMus musculus
Functional DescriptionNon-receptor tyrosine kinase that contributes tosignaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskekleton. Plays a redundant role to ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. Required for TCR-dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific substrate, and contributes to CD28-signaling. Mediates signals that negatively regulate IL2RA expression induced by TCR cross-linking. Plays a redundant role to BTK in BCR-signaling for B-cell development and activation, especially by phosphorylating STAP1, a BCR-signaling protein. Required in mast cells for efficient cytokine production. Involved in both growth and differentiation mechanisms of myeloid cells through activation by the granulocyte colony-stimulating factor CSF3, a critical cytokine to promoting the growth, differentiation, and functional activation of myeloid cells. Participates in platelet signaling downstream of integrin activation. Cooperates with JAK2 through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. GRB10, a negative modifier of the FOS activation pathway, is another substrate of TEC. TEC is involved in G protein-coupled receptor- and integrin-mediated signalings in blood platelets. Plays a role in hepatocyte proliferation and liver regeneration and is involved in HGF-induced ERK signaling pathway. TEC regulates also FGF2 unconventional secretion (endoplasmic reticulum (ER)/Golgi-independent mechanism) under various physiological conditions through phosphorylation of FGF2 'Tyr-82'. May also be involved in the regulation of osteoclast differentiation.
Protein Length608
Protein Sequence
(FASTA)
MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSVLSY YEGRAEKKYR KGVIDISKIK 60
CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY 120
HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE 180
EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGWYCRNTN RSKAEQLLRT 240
EDKEGGFMVR DSSQPGLYTV SLYTKFGGEG SSGFRHYHIK ETATSPKKYY LAEKHAFGSI 300
PEIIEYHKHN AAGLVTRLRY PVSTKGKNAP TTAGFSYDKW EINPSELTFM RELGSGLFGV 360
VRLGKWRAQY KVAIKAIREG AMCEEDFIEE AKVMMKLTHP KLVQLYGVCT QQKPIYIVTE 420
FMERGCLLNF LRQRQGHFSR DMLLSMCQDV CEGMEYLERN SFIHRDLAAR NCLVNEAGVV 480
KVSDFGMARY VLDDQYTSSS GAKFPVKWCP PEVFNYSRFS SKSDVWSFGV LMWEIFTEGR 540
MPFEKNTNYE VVTMVTRGHR LHRPKLASKY LYEVMLRCWQ ERPEGRPSFE DLLRTIDELV 600
ECEETFGR 608
Nucleotide Sequence
(FASTA)
ATGAATTTCA ACACTATCCT AGAAGAGATT CTTATTAAAA GGTCCCAGCA GAAAAAGAAG 60
ACATCACCCT TAAACTACAA AGAGAGACTT TTTGTACTTA CAAAATCCGT GTTGAGCTAC 120
TATGAGGGTC GAGCGGAGAA GAAATACAGA AAGGGCGTCA TTGATATTTC CAAAATCAAG 180
TGTGTGGAGA TAGTGAAGAA CGATGATGGT GTCATTCCCT GTCAAAATAA ATTTCCATTC 240
CAGGTTGTTC ATGATGCTAA TACACTTTAT ATTTTTGCAC CTAGTCCACA AAGCAGGGAC 300
CGATGGGTGA AGAAGTTAAA AGAAGAAATA AAGAACAACA ATAATATCAT GATTAAATAC 360
CATCCTAAAT TCTGGGCAGA TGGGAGTTAC CAGTGTTGTA GACAAACAGA AAAACTAGCA 420
CCCGGATGTG AGAAGTACAA TCTTTTTGAG AGTAGTATAA GAAAGACCCT GCCTCCCGCG 480
CCAGAAATAA AGAAGAGAAG GCCTCCTCCA CCAATTCCCC CAGAGGAAGA AAATACTGAA 540
GAAATCGTTG TAGCGATGTA TGACTTCCAA GCGACGGAAG CACATGACCT CAGGTTAGAG 600
AGAGGCCAAG AGTATATCAT CCTGGAAAAG AATGACCTCC ATTGGTGGAG AGCGAGAGAT 660
AAGTATGGGT GGTACTGCAG AAATACCAAC AGAAGCAAAG CAGAACAGCT CCTCAGAACG 720
GAAGATAAAG AAGGTGGTTT TATGGTGAGA GACTCCAGTC AACCAGGCTT GTACACTGTC 780
TCCCTTTACA CAAAGTTTGG GGGAGAAGGC TCATCAGGTT TCAGGCATTA TCACATAAAG 840
GAAACAGCAA CATCCCCAAA GAAGTATTAC CTGGCAGAGA AGCATGCTTT CGGGTCCATT 900
CCTGAGATCA TTGAATATCA CAAGCACAAT GCGGCAGGGC TTGTCACCAG GCTGCGGTAC 960
CCGGTCAGTA CAAAGGGGAA GAACGCTCCC ACTACTGCCG GCTTCAGCTA TGATAAGTGG 1020
GAGATTAACC CATCAGAGCT GACCTTTATG AGAGAGTTGG GGAGCGGACT GTTTGGAGTG 1080
GTGAGGCTTG GCAAGTGGCG GGCCCAGTAC AAAGTGGCCA TCAAAGCTAT CCGGGAAGGC 1140
GCCATGTGTG AAGAGGATTT CATAGAGGAA GCTAAAGTCA TGATGAAGCT GACACACCCC 1200
AAGCTGGTAC AGCTCTATGG TGTATGCACC CAGCAGAAGC CCATCTACAT CGTTACCGAG 1260
TTCATGGAAC GGGGCTGCCT TCTGAATTTC CTCCGGCAGA GACAAGGCCA TTTCAGCAGA 1320
GACATGCTGC TAAGCATGTG TCAAGATGTC TGTGAAGGGA TGGAGTACCT GGAGAGAAAC 1380
AGCTTCATCC ACAGAGACCT GGCTGCCAGA AATTGTCTAG TGAATGAAGC AGGAGTTGTC 1440
AAAGTATCTG ATTTTGGAAT GGCCAGGTAC GTTCTGGATG ATCAGTACAC AAGTTCTTCT 1500
GGCGCCAAGT TCCCTGTGAA GTGGTGTCCC CCAGAAGTGT TTAATTACAG CCGCTTTAGC 1560
AGCAAGTCAG ACGTCTGGTC GTTTGGTGTG CTAATGTGGG AAATATTCAC AGAAGGCAGG 1620
ATGCCCTTTG AGAAGAACAC CAATTACGAA GTGGTAACCA TGGTGACTCG TGGCCACCGC 1680
CTCCACCGGC CAAAGCTGGC TTCCAAATAT TTGTATGAGG TGATGCTGAG ATGCTGGCAA 1740
GAGAGACCAG AGGGAAGGCC TTCCTTTGAA GACTTGCTGC GTACGATAGA TGAACTAGTT 1800
GAATGTGAAG AAACTTTTGG AAGATGA 1827
Domain Profile
S: 1     ltllkelgsgqfgvvklgkwrakidvaikaikegamseedfieeakvmmklshpklvqly  60
         lt+++elgsg fgvv+lgkwra+++vaikai+egam+eedfieeakvmmkl+hpklvqly
Q: 347   LTFMRELGSGLFGVVRLGKWRAQYKVAIKAIREGAMCEEDFIEEAKVMMKLTHPKLVQLY  406
         79**********************************************************
S: 61    gvclkqkpiyivteylengcllnylrekkkklekelllemckdvcegmeylerksfihrd  120
         gvc++qkpiyivte++e+gclln+lr++++++++++ll+mc+dvcegmeyler+sfihrd
Q: 407   GVCTQQKPIYIVTEFMERGCLLNFLRQRQGHFSRDMLLSMCQDVCEGMEYLERNSFIHRD  466
         ************************************************************
S: 121   laarnclvdeelvvkvsdfglaryvlddqyvssvgakfpvkwsppevlsyskyssksdvw  180
         laarnclv+e+ vvkvsdfg+aryvlddqy+ss+gakfpvkw+ppev++ys++ssksdvw
Q: 467   LAARNCLVNEAGVVKVSDFGMARYVLDDQYTSSSGAKFPVKWCPPEVFNYSRFSSKSDVW  526
         ************************************************************
S: 181   afgvlmwevfsegklpyekksnsevvekvsrglrlyrpklaskkvyevmkscwkekpeer  240
         +fgvlmwe+f+eg++p+ek++n+evv++v+rg+rl+rpklask++yevm +cw+e+pe+r
Q: 527   SFGVLMWEIFTEGRMPFEKNTNYEVVTMVTRGHRLHRPKLASKYLYEVMLRCWQERPEGR  586
         ************************************************************
S: 241   ptfkellsale  251
         p+f++ll+++ 
Q: 587   PSFEDLLRTID  597
         ********995
Domain Sequence
(FASTA)
LTFMRELGSG LFGVVRLGKW RAQYKVAIKA IREGAMCEED FIEEAKVMMK LTHPKLVQLY 60
GVCTQQKPIY IVTEFMERGC LLNFLRQRQG HFSRDMLLSM CQDVCEGMEY LERNSFIHRD 120
LAARNCLVNE AGVVKVSDFG MARYVLDDQY TSSSGAKFPV KWCPPEVFNY SRFSSKSDVW 180
SFGVLMWEIF TEGRMPFEKN TNYEVVTMVT RGHRLHRPKL ASKYLYEVML RCWQERPEGR 240
PSFEDLLRTI D 251
Keyword3D-structure; Adaptive immunity; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Immunity; Kinase; Lipid-binding; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase; Zinc; Zinc-finger.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Danio rerio"; ?>Dasypus novemcinctus"; ?>Equus caballus"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00097
EKS-ANC-00101
EKS-BOT-00107
EKS-CAJ-00108
EKS-CAF-00108
EKS-CAP-00102
EKS-CII-00053
EKS-DAR-00358
EKS-DAN-00037
EKS-EQC-00105
EKS-GAG-00087
EKS-GAA-00126
EKS-GOG-00107
EKS-HOS-00109
EKS-LAC-00110
EKS-LOA-00103
EKS-MAM-00102
EKS-MEG-00082
EKS-MOD-00105
EKS-MUP-00109
EKS-MYL-00120
EKS-NOL-00099
EKS-ORN-00131
EKS-ORA-00088
EKS-ORC-00098
EKS-OTG-00113
EKS-PAT-00097
EKS-PES-00090
EKS-POA-00099
EKS-RAN-00105
EKS-SAH-00099
EKS-SUS-00093
EKS-TAG-00136
EKS-XIM-00129
Gene Ontology
GO:0005737; C:cytoplasm
GO:0005856; C:cytoskeleton
GO:0005886; C:plasma membrane
GO:0005524; F:ATP binding
GO:0046872; F:metal ion binding
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity
GO:0005543; F:phospholipid binding
GO:0035556; P:intracellular signal transduction
KEGG
mmu:21682;
InterPros
IPR011009; Kinase-like_dom.
IPR011993; PH_like_dom.
IPR001849; Pleckstrin_homology.
IPR000719; Prot_kinase_cat_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.
IPR001562; Znf_Btk_motif.
Pfam
PF00779; BTK; 1.
PF00169; PH; 1.
PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
SMARTs
SM00107; BTK; 1.
SM00233; PH; 1.
SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
Prosites
PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PS51113; ZF_BTK; 1.
Prints
PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00402; TECBTKDOMAIN.
PR00109; TYRKINASE.
Created Date20-Feb-2013