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P42680

- TEC_HUMAN

UniProt

P42680 - TEC_HUMAN

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Protein

Tyrosine-protein kinase Tec

Gene
TEC, PSCTK4
Organism
Homo sapiens (Human)
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-215'. May also be involved in the regulation of osteoclast differentiation.4 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-519. 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 sitei398 – 3981ATP By similarity
Active sitei489 – 4891Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typeAdd
BLAST
Nucleotide bindingi376 – 3849ATP 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
  5. protein binding Source: IntAct

GO - Biological processi

  1. B cell receptor signaling pathway Source: UniProtKB
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. innate immune response Source: Reactome
  4. integrin-mediated signaling pathway Source: UniProtKB
  5. intracellular signal transduction Source: ProtInc
  6. peptidyl-tyrosine phosphorylation Source: GOC
  7. protein phosphorylation Source: ProtInc
  8. regulation of platelet activation Source: UniProtKB
  9. tissue regeneration Source: Ensembl
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. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
SignaLinkiP42680.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Tec (EC:2.7.10.2)
Gene namesi
Name:TEC
Synonyms:PSCTK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11719. 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.2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631Tyrosine-protein kinase TecPRO_0000088170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061Phosphotyrosine; by autocatalysis2 Publications
Modified residuei228 – 2281Phosphotyrosine1 Publication
Modified residuei519 – 5191Phosphotyrosine; by autocatalysis, LYN and JAK21 Publication

Post-translational modificationi

Following B-cell or T-cell receptors engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-519. Undergoes also tyrosine phosphorylation during platelet activation.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP42680.
PaxDbiP42680.
PRIDEiP42680.

PTM databases

PhosphoSiteiP42680.

Expressioni

Tissue specificityi

Expressed in a wide range of cells, including hematopoietic cell lines like myeloid, B-, and T-cell lineages.

Gene expression databases

ArrayExpressiP42680.
BgeeiP42680.
CleanExiHS_TEC.
GenevestigatoriP42680.

Organism-specific databases

HPAiHPA005733.

Interactioni

Subunit structurei

Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with CD28, FASLG, FGF2, GRB10, LYN and KIT. Interacts with VAV1 and JAK2 By similarity.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GAB1Q134802EBI-1383480,EBI-517684
METP085812EBI-1383480,EBI-1039152

Protein-protein interaction databases

BioGridi112865. 23 interactions.
IntActiP42680. 16 interactions.
MINTiMINT-1498364.
STRINGi9606.ENSP00000370912.

Structurei

Secondary structure

1
631
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412
Beta strandi19 – 213
Beta strandi26 – 4116
Beta strandi45 – 473
Beta strandi53 – 553
Helixi56 – 583
Beta strandi61 – 644
Beta strandi69 – 713
Beta strandi74 – 763
Beta strandi78 – 836
Beta strandi88 – 925
Helixi96 – 11015
Beta strandi118 – 1203
Beta strandi132 – 1343
Beta strandi143 – 1453

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LULNMR-A1-154[»]
ProteinModelPortaliP42680.
SMRiP42680. Positions 1-154, 182-624.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 111108PHAdd
BLAST
Domaini179 – 23961SH3Add
BLAST
Domaini247 – 34599SH2Add
BLAST
Domaini370 – 623254Protein 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.
The SH3 domain is essential for its targeting to activated CD28 costimulatory molecule By similarity.

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.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiP42680.
KOiK07364.
OMAiCTQQKPI.
OrthoDBiEOG7KM5SC.
PhylomeDBiP42680.
TreeFamiTF351634.

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]

Sequencei

Sequence statusi: Complete.

P42680-1 [UniParc]FASTAAdd to Basket

« Hide

MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSMLTY YEGRAEKKYR    50
KGFIDVSKIK CVEIVKNDDG VIPCQNKYPF QVVHDANTLY IFAPSPQSRD 100
LWVKKLKEEI KNNNNIMIKY HPKFWTDGSY QCCRQTEKLA PGCEKYNLFE 150
SSIRKALPPA PETKKRRPPP PIPLEEEDNS EEIVVAMYDF QAAEGHDLRL 200
ERGQEYLILE KNDVHWWRAR DKYGNEGYIP SNYVTGKKSN NLDQYEWYCR 250
NMNRSKAEQL LRSEDKEGGF MVRDSSQPGL YTVSLYTKFG GEGSSGFRHY 300
HIKETTTSPK KYYLAEKHAF GSIPEIIEYH KHNAAGLVTR LRYPVSVKGK 350
NAPTTAGFSY EKWEINPSEL TFMRELGSGL FGVVRLGKWR AQYKVAIKAI 400
REGAMCEEDF IEEAKVMMKL THPKLVQLYG VCTQQKPIYI VTEFMERGCL 450
LNFLRQRQGH FSRDVLLSMC QDVCEGMEYL ERNSFIHRDL AARNCLVSEA 500
GVVKVSDFGM ARYVLDDQYT SSSGAKFPVK WCPPEVFNYS RFSSKSDVWS 550
FGVLMWEVFT EGRMPFEKYT NYEVVTMVTR GHRLYQPKLA SNYVYEVMLR 600
CWQEKPEGRP SFEDLLRTID ELVECEETFG R 631
Length:631
Mass (Da):73,581
Last modified:September 11, 2007 - v2
Checksum:iF55DECBF9916E1F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441R → Q.1 Publication
Corresponds to variant rs35374286 [ dbSNP | Ensembl ].
VAR_041850
Natural varianti563 – 5631R → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041851

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti514 – 5141V → F in BAA06171. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29767 mRNA. Translation: BAA06171.1.
CH471069 Genomic DNA. Translation: EAW93055.1.
BC101711 mRNA. Translation: AAI01712.1.
BC101713 mRNA. Translation: AAI01714.1.
BC143487 mRNA. Translation: AAI43488.1.
CCDSiCCDS3481.1.
PIRiI38268.
I56997.
RefSeqiNP_003206.2. NM_003215.2.
UniGeneiHs.479670.

Genome annotation databases

EnsembliENST00000381501; ENSP00000370912; ENSG00000135605.
GeneIDi7006.
KEGGihsa:7006.
UCSCiuc003gxz.3. human.

Polymorphism databases

DMDMi158518392.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29767 mRNA. Translation: BAA06171.1 .
CH471069 Genomic DNA. Translation: EAW93055.1 .
BC101711 mRNA. Translation: AAI01712.1 .
BC101713 mRNA. Translation: AAI01714.1 .
BC143487 mRNA. Translation: AAI43488.1 .
CCDSi CCDS3481.1.
PIRi I38268.
I56997.
RefSeqi NP_003206.2. NM_003215.2.
UniGenei Hs.479670.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LUL NMR - A 1-154 [» ]
ProteinModelPortali P42680.
SMRi P42680. Positions 1-154, 182-624.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112865. 23 interactions.
IntActi P42680. 16 interactions.
MINTi MINT-1498364.
STRINGi 9606.ENSP00000370912.

Chemistry

BindingDBi P42680.
ChEMBLi CHEMBL4246.
GuidetoPHARMACOLOGYi 2238.

PTM databases

PhosphoSitei P42680.

Polymorphism databases

DMDMi 158518392.

Proteomic databases

MaxQBi P42680.
PaxDbi P42680.
PRIDEi P42680.

Protocols and materials databases

DNASUi 7006.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381501 ; ENSP00000370912 ; ENSG00000135605 .
GeneIDi 7006.
KEGGi hsa:7006.
UCSCi uc003gxz.3. human.

Organism-specific databases

CTDi 7006.
GeneCardsi GC04M048137.
HGNCi HGNC:11719. TEC.
HPAi HPA005733.
MIMi 600583. gene.
neXtProti NX_P42680.
PharmGKBi PA36436.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233859.
HOVERGENi HBG008761.
InParanoidi P42680.
KOi K07364.
OMAi CTQQKPI.
OrthoDBi EOG7KM5SC.
PhylomeDBi P42680.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
SignaLinki P42680.

Miscellaneous databases

GeneWikii TEC_(gene).
GenomeRNAii 7006.
NextBioi 27366.
PROi P42680.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42680.
Bgeei P42680.
CleanExi HS_TEC.
Genevestigatori P42680.

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. "Molecular cloning and analysis of the human Tec protein-tyrosine kinase."
    Sato K., Mano H., Ariyama T., Inazawa J., Yazaki Y., Hirai H.
    Leukemia 8:1663-1672(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. "Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases."
    Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A., Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.
    Biochim. Biophys. Acta 1645:123-132(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 203-206, PHOSPHORYLATION AT TYR-206.
  5. "Tec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor binding."
    Tang B., Mano H., Yi T., Ihle J.N.
    Mol. Cell. Biol. 14:8432-8437(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH KIT, ENZYME REGULATION.
  6. "Integrin-dependent tyrosine phosphorylation and cytoskeletal translocation of Tec in thrombin-activated platelets."
    Laffargue M., Monnereau L., Tuech J., Ragab A., Ragab-Thomas J., Payrastre B., Raynal P., Chap H.
    Biochem. Biophys. Res. Commun. 238:247-251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  7. Cited for: ENZYME REGULATION.
  8. Cited for: INTERACTION WITH GRB10, FUNCTION IN PHOSPHORYLATION OF GRB10.
  9. "Tec is involved in G protein-coupled receptor- and integrin-mediated signalings in human blood platelets."
    Hamazaki Y., Kojima H., Mano H., Nagata Y., Todokoro K., Abe T., Nagasawa T.
    Oncogene 16:2773-2779(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
  10. "Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase."
    Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A., Yamashita Y., Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.
    Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STAP1, ENZYME REGULATION.
  11. "SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase."
    Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.
    J. Biol. Chem. 279:55089-55096(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5D AND INPPL1.
  12. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206 AND TYR-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Tec protein tyrosine kinase inhibits CD25 expression in human T-lymphocyte."
    Susaki K., Kitanaka A., Dobashi H., Kubota Y., Kittaka K., Kameda T., Yamaoka G., Mano H., Mihara K., Ishida T.
    Immunol. Lett. 127:135-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion."
    Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H., Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.
    Traffic 11:813-826(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FGF2, INTERACTION WITH FGF2.
  17. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-44 AND LYS-563.

Entry informationi

Entry nameiTEC_HUMAN
AccessioniPrimary (citable) accession number: P42680
Secondary accession number(s): B7ZKZ6, Q3MIS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

It is uncertain whether Met-1 is the initiator.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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