P24604 (TEC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Tec
EC=2.7.10.2

Gene names

Name:

Tec

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor tyrosine kinase that contributes to signaling from many receptors and participates as a signal transducer in multiple downstream pathways, including regulation of the actin cytoskeleton. 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Enzyme regulation	Activated by tyrosine phosphorylation by a wide range of cytokine stimulations. When T-cells or B-cells receptors are activated, a series of phosphorylation leads to the recruitment of TEC to the cell membrane, where it is phosphorylated at Tyr-518. Also activated in response to SCF. Integrin engagement induces tyrosine phosphorylation of TEC in platelets. STAP1 participates in a positive feedback loop by increasing the activity of TEC. SOCS1 is an inhibitor of TEC kinase activity. Ref.5 Ref.6 Ref.8 Ref.9
Subunit structure	Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10 and KIT By similarity. Interacts with VAV1 and JAK2. Interacts with LYN. Ref.5 Ref.9
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasm › cytoskeleton. Note: Following B-cell or T-cell receptors activation by antigen, translocates to the plasma membrane through its PH domain. Thrombin and integrin engagement induces translocation of TEC to the cytoskeleton during platelet activation. In cardiac myocytes, assumes a diffuse intracellular localization under basal conditions but is recruited to striated structures upon various stimuli, including ATP By similarity. Ref.10 Ref.11 Ref.14
Tissue specificity	Preferentially expressed in liver. Expression is also seen in the hematopoietic cells such as bone marrow, thymus and spleen. Lower expression is seen in the heart, kidney and ovary.
Domain	The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain. Ref.10 The SH3 domain is essential for its targeting to activated CD28 costimulatory molecule By similarity. Ref.10
Post-translational modification	Following B-cell or T-cell receptors engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-518. Undergoes also tyrosine phosphorylation during platelet activation. Ref.5 Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily. Contains 1 Btk-type zinc finger. Contains 1 PH domain. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	SH2 domain SH3 domain Zinc-finger
Ligand	ATP-binding Lipid-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P24604-1)

Also known as: TecIV;

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.

Isoform 2 (identifier: P24604-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MNFNTILEEI...DANTLYIFAP → MMVSFPVKINFHS
     224-245: Missing.

Isoform 3 (identifier: P24604-3)

Also known as: TecIIb;

The sequence of this isoform differs from the canonical sequence as follows:
     604-630: RPEGRPSLEDLLRTIDELVECEETFGR → ESCLCRVAQDLSSKNLIGSRF

Isoform 4 (identifier: P24604-4)

Also known as: TecIIa;

The sequence of this isoform differs from the canonical sequence as follows:
     224-245: Missing.
     604-630: RPEGRPSLEDLLRTIDELVECEETFGR → ESCLCRVAQDLSSKNLIGSRF

Isoform 5 (identifier: P24604-5)

Also known as: TecIII;

The sequence of this isoform differs from the canonical sequence as follows:
     224-245: Missing.

Isoform 6 (identifier: P24604-6)

Also known as: TecI;

The sequence of this isoform differs from the canonical sequence as follows:
     82-100: VVHDANTLYIFAPSPQSRD → STKQGPMGEEVKRRNKEQQ
     101-630: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 630

630

Tyrosine-protein kinase Tec

PRO_0000088171

Regions

Domain

4 – 111

108

PH

Domain

178 – 238

61

SH3

Domain

246 – 344

99

SH2

Domain

369 – 622

254

Protein kinase

Zinc finger

113 – 149

37

Btk-type

Nucleotide binding

375 – 383

9

ATP By similarity

Sites

Active site

488

1

Proton acceptor By similarity

Metal binding

121

1

Zinc By similarity

Metal binding

132

1

Zinc By similarity

Metal binding

133

1

Zinc By similarity

Metal binding

143

1

Zinc By similarity

Binding site

397

1

ATP By similarity

Amino acid modifications

Modified residue

205

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

227

1

Phosphotyrosine By similarity

Modified residue

518

1

Phosphotyrosine; by autocatalysis, LYN and JAK2 Ref.7 Ref.12

Natural variations

Alternative sequence

1 – 94

94

MNFNT…YIFAP → MMVSFPVKINFHS in isoform 2.

VSP_005012

Alternative sequence

82 – 100

19

VVHDA…PQSRD → STKQGPMGEEVKRRNKEQQ in isoform 6.

VSP_005013

Alternative sequence

101 – 630

530

Missing in isoform 6.

VSP_005014

Alternative sequence

224 – 245

22

Missing in isoform 2, isoform 4 and isoform 5.

VSP_005015

Alternative sequence

604 – 630

27

RPEGR…ETFGR → ESCLCRVAQDLSSKNLIGSR F in isoform 3 and isoform 4.

VSP_005016

Experimental info

Mutagenesis

397

1

K → M: Impairs kinase activity. Ref.6

Sequence conflict

23

1

L → P in AAD43404. Ref.2

Sequence conflict

23

1

L → P in AAD43402. Ref.2

Sequence conflict

23

1

L → P in AAD43405. Ref.2

Sequence conflict

23

1

L → P in AAD43406. Ref.2

Sequence conflict

23

1

L → P in AAD43407. Ref.2

Sequence conflict

31

1

C → F in AAD43404. Ref.2

Sequence conflict

31

1

C → F in AAD43402. Ref.2

Sequence conflict

31

1

C → F in AAD43405. Ref.2

Sequence conflict

31

1

C → F in AAD43406. Ref.2

Sequence conflict

31

1

C → F in AAD43407. Ref.2

Sequence conflict

34

1

P → T in AAD43404. Ref.2

Sequence conflict

34

1

P → T in AAD43402. Ref.2

Sequence conflict

34

1

P → T in AAD43405. Ref.2

Sequence conflict

34

1

P → T in AAD43406. Ref.2

Sequence conflict

34

1

P → T in AAD43407. Ref.2

Sequence conflict

535

1

V → E in AAA40018. Ref.4

Sequence conflict

550 – 553

4

FGVL → YGIP in AAA40018. Ref.4

Sequence conflict

590

1

T → S in AAD43402. Ref.2

Sequence conflict

590

1

T → S in AAD43405. Ref.2

Sequence conflict

590

1

T → S in AAD43406. Ref.2

Sequence conflict

590

1

T → S in AAD43407. Ref.2

Sequence conflict

611

1

L → F in AAD43404. Ref.2

Sequence conflict

611

1

L → F in AAD43402. Ref.2

Sequence conflict

611

1

L → F in AAD43405. Ref.2

Sequence conflict

611

1

L → F in AAD43406. Ref.2

Sequence conflict

611

1

L → F in AAD43407. Ref.2

Sequence conflict

611

1

L → F in CAA39196. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

630

Helix Strand Turn

Details...

Beta strand

183 – 185

3

Beta strand

192 – 196

5

Beta strand

204 – 209

6

Beta strand

211 – 219

9

Beta strand

221 – 223

3

Beta strand

225 – 229

5

Beta strand

232 – 236

5

Turn

237 – 241

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TecIV) [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 262640EE90D4A6D2	FASTA	630	73,426
	10 20 30 40 50 60 MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK 70 80 90 100 110 120 CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY 130 140 150 160 170 180 HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE 190 200 210 220 230 240 EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGSEGYIPS NYVTGKKSNN 250 260 270 280 290 300 LDQYEWYCRN TNRSKAEQLL RTEDKEGGFM VRDSSQPGLY TVSLYTKFGG EGSSGFRHYH 310 320 330 340 350 360 IKETATSPKK YYLAEKHAFG SIPEIIEYHK HNAAGLVTRL RYPVSTKGKN APTTAGFSYD 370 380 390 400 410 420 KWEINPSELT FMRELGSGLF GVVRLGKWRA QYKVAIKAIR EGAMCEEDFI EEAKVMMKLT 430 440 450 460 470 480 HPKLVQLYGV CTQQKPIYIV TEFMERGCLL NFLRQRQGHF SRDMLLSMCQ DVCEGMEYLE 490 500 510 520 530 540 RNSFIHRDLA ARNCLVNEAG VVKVSDFGMA RYVLDDQYTS SSGAKFPVKW CPPEVFNYSR 550 560 570 580 590 600 FSSKSDVWSF GVLMWEIFTE GRMPFEKNTN YEVVTMVTRG HRLHRPKLAT KYLYEVMLRC 610 620 630 WQERPEGRPS LEDLLRTIDE LVECEETFGR
	Isoform 2 [UniParc]. Checksum: 72819611523F0872	FASTA	527	61,523
	10 20 30 40 50 60 MMVSFPVKIN FHSSPQSRDR WVKKLKEEIK NNNNIMIKYH PKFWADGSYQ CCRQTEKLAP 70 80 90 100 110 120 GCEKYNLFES SIRKTLPPAP EIKKRRPPPP IPPEEENTEE IVVAMYDFQA TEAHDLRLER 130 140 150 160 170 180 GQEYIILEKN DLHWWRARDK YGWYCRNTNR SKAEQLLRTE DKEGGFMVRD SSQPGLYTVS 190 200 210 220 230 240 LYTKFGGEGS SGFRHYHIKE TATSPKKYYL AEKHAFGSIP EIIEYHKHNA AGLVTRLRYP 250 260 270 280 290 300 VSTKGKNAPT TAGFSYDKWE INPSELTFMR ELGSGLFGVV RLGKWRAQYK VAIKAIREGA 310 320 330 340 350 360 MCEEDFIEEA KVMMKLTHPK LVQLYGVCTQ QKPIYIVTEF MERGCLLNFL RQRQGHFSRD 370 380 390 400 410 420 MLLSMCQDVC EGMEYLERNS FIHRDLAARN CLVNEAGVVK VSDFGMARYV LDDQYTSSSG 430 440 450 460 470 480 AKFPVKWCPP EVFNYSRFSS KSDVWSFGVL MWEIFTEGRM PFEKNTNYEV VTMVTRGHRL 490 500 510 520 HRPKLATKYL YEVMLRCWQE RPEGRPSLED LLRTIDELVE CEETFGR
	Isoform 3 (TecIIb) [UniParc]. Checksum: 196018BC9EC862A5	FASTA	624	72,592
	10 20 30 40 50 60 MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK 70 80 90 100 110 120 CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY 130 140 150 160 170 180 HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE 190 200 210 220 230 240 EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGSEGYIPS NYVTGKKSNN 250 260 270 280 290 300 LDQYEWYCRN TNRSKAEQLL RTEDKEGGFM VRDSSQPGLY TVSLYTKFGG EGSSGFRHYH 310 320 330 340 350 360 IKETATSPKK YYLAEKHAFG SIPEIIEYHK HNAAGLVTRL RYPVSTKGKN APTTAGFSYD 370 380 390 400 410 420 KWEINPSELT FMRELGSGLF GVVRLGKWRA QYKVAIKAIR EGAMCEEDFI EEAKVMMKLT 430 440 450 460 470 480 HPKLVQLYGV CTQQKPIYIV TEFMERGCLL NFLRQRQGHF SRDMLLSMCQ DVCEGMEYLE 490 500 510 520 530 540 RNSFIHRDLA ARNCLVNEAG VVKVSDFGMA RYVLDDQYTS SSGAKFPVKW CPPEVFNYSR 550 560 570 580 590 600 FSSKSDVWSF GVLMWEIFTE GRMPFEKNTN YEVVTMVTRG HRLHRPKLAT KYLYEVMLRC 610 620 WQEESCLCRV AQDLSSKNLI GSRF
	Isoform 4 (TecIIa) [UniParc]. Checksum: B213B18A8519E4F5	FASTA	602	70,104
	10 20 30 40 50 60 MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK 70 80 90 100 110 120 CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY 130 140 150 160 170 180 HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE 190 200 210 220 230 240 EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGWYCRNTN RSKAEQLLRT 250 260 270 280 290 300 EDKEGGFMVR DSSQPGLYTV SLYTKFGGEG SSGFRHYHIK ETATSPKKYY LAEKHAFGSI 310 320 330 340 350 360 PEIIEYHKHN AAGLVTRLRY PVSTKGKNAP TTAGFSYDKW EINPSELTFM RELGSGLFGV 370 380 390 400 410 420 VRLGKWRAQY KVAIKAIREG AMCEEDFIEE AKVMMKLTHP KLVQLYGVCT QQKPIYIVTE 430 440 450 460 470 480 FMERGCLLNF LRQRQGHFSR DMLLSMCQDV CEGMEYLERN SFIHRDLAAR NCLVNEAGVV 490 500 510 520 530 540 KVSDFGMARY VLDDQYTSSS GAKFPVKWCP PEVFNYSRFS SKSDVWSFGV LMWEIFTEGR 550 560 570 580 590 600 MPFEKNTNYE VVTMVTRGHR LHRPKLATKY LYEVMLRCWQ EESCLCRVAQ DLSSKNLIGS RF
	Isoform 5 (TecIII) [UniParc]. Checksum: C43EF410FD030DA1	FASTA	608	70,938
	10 20 30 40 50 60 MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK 70 80 90 100 110 120 CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY 130 140 150 160 170 180 HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE 190 200 210 220 230 240 EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGWYCRNTN RSKAEQLLRT 250 260 270 280 290 300 EDKEGGFMVR DSSQPGLYTV SLYTKFGGEG SSGFRHYHIK ETATSPKKYY LAEKHAFGSI 310 320 330 340 350 360 PEIIEYHKHN AAGLVTRLRY PVSTKGKNAP TTAGFSYDKW EINPSELTFM RELGSGLFGV 370 380 390 400 410 420 VRLGKWRAQY KVAIKAIREG AMCEEDFIEE AKVMMKLTHP KLVQLYGVCT QQKPIYIVTE 430 440 450 460 470 480 FMERGCLLNF LRQRQGHFSR DMLLSMCQDV CEGMEYLERN SFIHRDLAAR NCLVNEAGVV 490 500 510 520 530 540 KVSDFGMARY VLDDQYTSSS GAKFPVKWCP PEVFNYSRFS SKSDVWSFGV LMWEIFTEGR 550 560 570 580 590 600 MPFEKNTNYE VVTMVTRGHR LHRPKLATKY LYEVMLRCWQ ERPEGRPSLE DLLRTIDELV ECEETFGR
	Isoform 6 (TecI) [UniParc]. Checksum: 32AB0BC0567F2CEC	FASTA	100	11,723
	10 20 30 40 50 60 MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK 70 80 90 100 CVEIVKNDDG VIPCQNKFPF QSTKQGPMGE EVKRRNKEQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a novel form of Tec kinase in hematopoietic cells and mapping of the gene to chromosome 5 near Kit." Mano H., Mano K., Tang B., Koehler M., Yi T., Gilbert D.J., Jenkins N.A., Copeland N.G., Ihle J.N. Oncogene 8:417-424(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Splice variants of the mouse Tec gene are differentially expressed in vivo." Merkel A.L., Atmosukarto I.I.C., Stevens K., Rathjen P.D., Booker G.W. Cytogenet. Cell Genet. 84:132-139(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6). Strain: 129.
[3]	"A novel protein-tyrosine kinase, tec, is preferentially expressed in liver." Mano H., Ishikawa F., Nishida J., Hirai H., Takaku F. Oncogene 5:1781-1786(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-630 (ISOFORM 2). Strain: BALB/c. Tissue: Liver.
[4]	"The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family." Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J. Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 485-553.
[5]	"Tec protein tyrosine kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor." Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H. Cell Growth Differ. 7:1135-1139(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, ENZYME REGULATION, INTERACTION WITH VAV1.
[6]	"Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase." Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K. FASEB J. 10:637-642(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY LYN, ENZYME REGULATION, MUTAGENESIS OF LYS-397.
[7]	"Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription." Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K., Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H. Blood 91:1496-1507(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION OF JAK2, PHOSPHORYLATION AT TYR-518.
[8]	"Tec kinase is involved in transcriptional regulation of IL-2 and IL-4 in the CD28 pathway." Yang W.C., Olive D. Eur. J. Immunol. 29:1842-1849(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, FUNCTION IN THE CD28 SIGNALING PATHWAY.
[9]	"The role of Tec protein-tyrosine kinase in T cell signaling." Yang W.C., Ghiotto M., Barbarat B., Olive D. J. Biol. Chem. 274:607-617(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CD28, ENZYME REGULATION, FUNCTION IN PHOSPHORYLATION OF DOK1.
[10]	"The SH3 domain of Tec kinase is essential for its targeting to activated CD28 costimulatory molecule." Garcon F., Ghiotto M., Gerard A., Yang W.C., Olive D., Nunes J.A. Eur. J. Immunol. 34:1972-1980(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
[11]	"Dynamic regulation of Tec kinase localization in membrane-proximal vesicles of a T cell clone revealed by total internal reflection fluorescence and confocal microscopy." Kane L.P., Watkins S.C. J. Biol. Chem. 280:21949-21954(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, MASS SPECTROMETRY. Tissue: Mast cell.
[13]	"The protein tyrosine kinase Tec regulates mast cell function." Schmidt U., Abramova A., Boucheron N., Eckelhart E., Schebesta A., Bilic I., Kneidinger M., Unger B., Hammer M., Sibilia M., Valent P., Ellmeier W. Eur. J. Immunol. 39:3228-3238(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Stress signaling by Tec tyrosine kinase in the ischemic myocardium." Zhang M.J., Franklin S., Li Y., Wang S., Ru X., Mitchell-Jordan S.A., Mano H., Stefani E., Ping P., Vondriska T.M. Am. J. Physiol. 299:H713-H722(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"TEC protein tyrosine kinase is involved in the Erk signaling pathway induced by HGF." Li F., Jiang Y., Zheng Q., Yang X., Wang S. Biochem. Biophys. Res. Commun. 404:79-85(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE HGF-INDUCED ERK SIGNALING PATHWAY.
[16]	"The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain." Pursglove S.E., Mulhern T.D., Mackay J.P., Hinds M.G., Booker G.W. J. Biol. Chem. 277:755-762(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 179-245.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S53716 mRNA. Translation: AAA13515.2.
AF071938, AF071936, AF071937 Genomic DNA. Translation: AAD43404.1.
AF071946 , AF071936, AF071937, AF071938, AF071939, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43402.1.
AF071946 , AF071936, AF071937, AF071938, AF071939, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43405.1.
AF071946 , AF071936, AF071937, AF071938, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43406.1.
AF071946 , AF071936, AF071937, AF071938, AF071940, AF071941, AF071942, AF071943, AF071944, AF071945 Genomic DNA. Translation: AAD43407.1.
X55663 mRNA. Translation: CAA39196.1.
M33427 mRNA. Translation: AAA40018.1.

IPI

IPI00108628.
IPI00227790.
IPI00227791.
IPI00227792.
IPI00227793.
IPI00227794.

PIR

JU0215.
S13763.
T01380.

RefSeq

NP_001106931.1. NM_001113460.1.
NP_001106932.1. NM_001113461.1.
NP_001106935.1. NM_001113464.1.

UniGene

Mm.319581.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GL5	NMR	-	A	181-244	[»]

ProteinModelPortal

P24604.

SMR

P24604. Positions 1-623.

ModBase

Search...

Protein-protein interaction databases

IntAct

P24604. 1 interaction.

PTM databases

PhosphoSite

P24604.

Proteomic databases

PRIDE

P24604.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENSMUST00000138842; ENSMUSP00000120155; ENSMUSG00000029217.
ENSMUST00000149533; ENSMUSP00000123258; ENSMUSG00000029217.

GeneID

21682.

KEGG

mmu:21682.

Organism-specific databases

CTD

7006.

MGI

MGI:98662. Tec.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00640000091251.

HOGENOM

HOG000233859.

HOVERGEN

HBG008761.

InParanoid

P24604.

KO

K07364.

OrthoDB

EOG4XKV6H.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Gene expression databases

ArrayExpress

P24604.

Bgee

P24604.

Genevestigator

P24604.

GermOnline

ENSMUSG00000029217. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.
3.30.505.10. 1 hit.

InterPro

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.
[Graphical view]

Pfam

PF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.

SMART

SM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50003. PH_DOMAIN. 1 hit.
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.
PS51113. ZF_BTK. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24604.

NextBio

300992.

SOURCE

Search...

Entry information

Entry name

TEC_MOUSE

Accession

Primary (citable) accession number: P24604
Secondary accession number(s): Q9R1M9 , Q9WVN0, Q9WVN1, Q9WVN2, Q9WVN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program