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P24604

- TEC_MOUSE

UniProt

P24604 - TEC_MOUSE

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Protein

Tyrosine-protein kinase Tec

Gene
Tec
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Enzyme regulationi

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211Zinc By similarity
Metal bindingi132 – 1321Zinc By similarity
Metal bindingi133 – 1331Zinc By similarity
Metal bindingi143 – 1431Zinc By similarity
Binding sitei397 – 3971ATP By similarity
Active sitei488 – 4881Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typeAdd
BLAST
Nucleotide bindingi375 – 3839ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. lipid binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  5. protein binding Source: MGI

GO - Biological processi

  1. immune system process Source: UniProtKB-KW
  2. intracellular signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

ATP-binding, Lipid-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188578. Signaling by SCF-KIT.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Tec (EC:2.7.10.2)
Gene namesi
Name:Tec
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:98662. Tec.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasmcytoskeleton
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.3 Publications

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi397 – 3971K → M: Impairs kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 630630Tyrosine-protein kinase TecPRO_0000088171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051Phosphotyrosine; by autocatalysis By similarity
Modified residuei227 – 2271Phosphotyrosine By similarity
Modified residuei518 – 5181Phosphotyrosine; by autocatalysis, LYN and JAK23 Publications

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP24604.

PTM databases

PhosphoSiteiP24604.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiP24604.
BgeeiP24604.
GenevestigatoriP24604.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi204103. 2 interactions.
IntActiP24604. 1 interaction.
MINTiMINT-5167157.

Structurei

Secondary structure

1
630
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi183 – 1853
Beta strandi192 – 1965
Beta strandi204 – 2096
Beta strandi211 – 2199
Beta strandi221 – 2233
Beta strandi225 – 2295
Beta strandi232 – 2365
Turni237 – 2415

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GL5NMR-A181-244[»]
ProteinModelPortaliP24604.
SMRiP24604. Positions 1-623.

Miscellaneous databases

EvolutionaryTraceiP24604.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 111108PHAdd
BLAST
Domaini178 – 23861SH3Add
BLAST
Domaini246 – 34499SH2Add
BLAST
Domaini369 – 622254Protein kinaseAdd
BLAST

Domaini

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.1 Publication
The SH3 domain is essential for its targeting to activated CD28 costimulatory molecule By similarity.1 Publication

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 SH2 domain.
Contains 1 SH3 domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typeAdd
BLAST

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091251.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiP24604.
KOiK07364.
OrthoDBiEOG7KM5SC.
PhylomeDBiP24604.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_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]
PfamiPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTiSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50003. 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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P24604-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR    50
KGVIDISKIK CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD 100
RWVKKLKEEI KNNNNIMIKY HPKFWADGSY QCCRQTEKLA PGCEKYNLFE 150
SSIRKTLPPA PEIKKRRPPP PIPPEEENTE EIVVAMYDFQ ATEAHDLRLE 200
RGQEYIILEK NDLHWWRARD KYGSEGYIPS NYVTGKKSNN LDQYEWYCRN 250
TNRSKAEQLL RTEDKEGGFM VRDSSQPGLY TVSLYTKFGG EGSSGFRHYH 300
IKETATSPKK YYLAEKHAFG SIPEIIEYHK HNAAGLVTRL RYPVSTKGKN 350
APTTAGFSYD KWEINPSELT FMRELGSGLF GVVRLGKWRA QYKVAIKAIR 400
EGAMCEEDFI EEAKVMMKLT HPKLVQLYGV CTQQKPIYIV TEFMERGCLL 450
NFLRQRQGHF SRDMLLSMCQ DVCEGMEYLE RNSFIHRDLA ARNCLVNEAG 500
VVKVSDFGMA RYVLDDQYTS SSGAKFPVKW CPPEVFNYSR FSSKSDVWSF 550
GVLMWEIFTE GRMPFEKNTN YEVVTMVTRG HRLHRPKLAT KYLYEVMLRC 600
WQERPEGRPS LEDLLRTIDE LVECEETFGR 630
Length:630
Mass (Da):73,426
Last modified:November 1, 1995 - v2
Checksum:i262640EE90D4A6D2
GO
Isoform 2 (identifier: P24604-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:527
Mass (Da):61,523
Checksum:i72819611523F0872
GO
Isoform 3 (identifier: P24604-3) [UniParc]FASTAAdd to Basket

Also known as: TecIIb

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

Show »
Length:624
Mass (Da):72,592
Checksum:i196018BC9EC862A5
GO
Isoform 4 (identifier: P24604-4) [UniParc]FASTAAdd to Basket

Also known as: TecIIa

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

Show »
Length:602
Mass (Da):70,104
Checksum:iB213B18A8519E4F5
GO
Isoform 5 (identifier: P24604-5) [UniParc]FASTAAdd to Basket

Also known as: TecIII

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

Show »
Length:608
Mass (Da):70,938
Checksum:iC43EF410FD030DA1
GO
Isoform 6 (identifier: P24604-6) [UniParc]FASTAAdd to Basket

Also known as: TecI

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

Show »
Length:100
Mass (Da):11,723
Checksum:i32AB0BC0567F2CEC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9494MNFNT…YIFAP → MMVSFPVKINFHS in isoform 2. VSP_005012Add
BLAST
Alternative sequencei82 – 10019VVHDA…PQSRD → STKQGPMGEEVKRRNKEQQ in isoform 6. VSP_005013Add
BLAST
Alternative sequencei101 – 630530Missing in isoform 6. VSP_005014Add
BLAST
Alternative sequencei224 – 24522Missing in isoform 2, isoform 4 and isoform 5. VSP_005015Add
BLAST
Alternative sequencei604 – 63027RPEGR…ETFGR → ESCLCRVAQDLSSKNLIGSR F in isoform 3 and isoform 4. VSP_005016Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231L → P in AAD43404. 1 Publication
Sequence conflicti23 – 231L → P in AAD43402. 1 Publication
Sequence conflicti23 – 231L → P in AAD43405. 1 Publication
Sequence conflicti23 – 231L → P in AAD43406. 1 Publication
Sequence conflicti23 – 231L → P in AAD43407. 1 Publication
Sequence conflicti31 – 311C → F in AAD43404. 1 Publication
Sequence conflicti31 – 311C → F in AAD43402. 1 Publication
Sequence conflicti31 – 311C → F in AAD43405. 1 Publication
Sequence conflicti31 – 311C → F in AAD43406. 1 Publication
Sequence conflicti31 – 311C → F in AAD43407. 1 Publication
Sequence conflicti34 – 341P → T in AAD43404. 1 Publication
Sequence conflicti34 – 341P → T in AAD43402. 1 Publication
Sequence conflicti34 – 341P → T in AAD43405. 1 Publication
Sequence conflicti34 – 341P → T in AAD43406. 1 Publication
Sequence conflicti34 – 341P → T in AAD43407. 1 Publication
Sequence conflicti535 – 5351V → E in AAA40018. 1 Publication
Sequence conflicti550 – 5534FGVL → YGIP in AAA40018. 1 Publication
Sequence conflicti590 – 5901T → S in AAD43402. 1 Publication
Sequence conflicti590 – 5901T → S in AAD43405. 1 Publication
Sequence conflicti590 – 5901T → S in AAD43406. 1 Publication
Sequence conflicti590 – 5901T → S in AAD43407. 1 Publication
Sequence conflicti611 – 6111L → F in AAD43404. 1 Publication
Sequence conflicti611 – 6111L → F in AAD43402. 1 Publication
Sequence conflicti611 – 6111L → F in AAD43405. 1 Publication
Sequence conflicti611 – 6111L → F in AAD43406. 1 Publication
Sequence conflicti611 – 6111L → F in AAD43407. 1 Publication
Sequence conflicti611 – 6111L → F in CAA39196. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS51515.1. [P24604-5]
CCDS51516.1. [P24604-1]
PIRiJU0215.
S13763.
T01380.
RefSeqiNP_001106931.1. NM_001113460.2.
NP_001106932.1. NM_001113461.2.
NP_001106935.1. NM_001113464.2.
XP_006503908.1. XM_006503845.1.
XP_006503909.1. XM_006503846.1.
UniGeneiMm.319581.

Genome annotation databases

EnsembliENSMUST00000138842; ENSMUSP00000120155; ENSMUSG00000029217.
ENSMUST00000149533; ENSMUSP00000123258; ENSMUSG00000029217.
GeneIDi21682.
KEGGimmu:21682.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS51515.1. [P24604-5 ]
CCDS51516.1. [P24604-1 ]
PIRi JU0215.
S13763.
T01380.
RefSeqi NP_001106931.1. NM_001113460.2.
NP_001106932.1. NM_001113461.2.
NP_001106935.1. NM_001113464.2.
XP_006503908.1. XM_006503845.1.
XP_006503909.1. XM_006503846.1.
UniGenei Mm.319581.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GL5 NMR - A 181-244 [» ]
ProteinModelPortali P24604.
SMRi P24604. Positions 1-623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204103. 2 interactions.
IntActi P24604. 1 interaction.
MINTi MINT-5167157.

PTM databases

PhosphoSitei P24604.

Proteomic databases

PRIDEi P24604.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000138842 ; ENSMUSP00000120155 ; ENSMUSG00000029217 .
ENSMUST00000149533 ; ENSMUSP00000123258 ; ENSMUSG00000029217 .
GeneIDi 21682.
KEGGi mmu:21682.

Organism-specific databases

CTDi 7006.
MGIi MGI:98662. Tec.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091251.
HOGENOMi HOG000233859.
HOVERGENi HBG008761.
InParanoidi P24604.
KOi K07364.
OrthoDBi EOG7KM5SC.
PhylomeDBi P24604.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188578. Signaling by SCF-KIT.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

Miscellaneous databases

EvolutionaryTracei P24604.
NextBioi 300992.
PROi P24604.
SOURCEi Search...

Gene expression databases

ArrayExpressi P24604.
Bgeei P24604.
Genevestigatori P24604.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_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 ]
Pfami PF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTi SM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  13. Cited for: FUNCTION.
  14. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: SUBCELLULAR LOCATION.
  16. "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.
  17. "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.

Entry informationi

Entry nameiTEC_MOUSE
AccessioniPrimary (citable) accession number: P24604
Secondary accession number(s): Q9R1M9
, Q9WVN0, Q9WVN1, Q9WVN2, Q9WVN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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