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Protein

Tyrosine-protein kinase Tec

Gene

TEC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Cofactori

Zn2+By similarityNote: 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)DescriptionActionsGraphical viewLength
Metal bindingi121ZincBy similarity1
Metal bindingi132ZincBy similarity1
Metal bindingi133ZincBy similarity1
Metal bindingi143ZincBy similarity1
Binding sitei398ATPPROSITE-ProRule annotation1
Active sitei489Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri113 – 149Btk-typePROSITE-ProRule annotationAdd BLAST37
Nucleotide bindingi376 – 384ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • phospholipid binding Source: BHF-UCL

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • B cell receptor signaling pathway Source: UniProtKB
  • cell differentiation Source: GO_Central
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • innate immune response Source: GO_Central
  • integrin-mediated signaling pathway Source: UniProtKB
  • intracellular signal transduction Source: ProtInc
  • peptidyl-tyrosine autophosphorylation Source: BHF-UCL
  • peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • protein phosphorylation Source: ProtInc
  • regulation of cell proliferation Source: GO_Central
  • regulation of platelet activation Source: UniProtKB
  • tissue regeneration Source: GO_Central
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
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

BioCyciZFISH:HS06035-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-1433557. Signaling by SCF-KIT.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-512988. Interleukin-3, 5 and GM-CSF signaling.
SignaLinkiP42680.
SIGNORiP42680.

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
Proteomesi
  • UP000005640 Componenti: 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi7006.
MalaCardsiTEC.
OpenTargetsiENSG00000135605.
PharmGKBiPA36436.

Chemistry databases

ChEMBLiCHEMBL4246.
GuidetoPHARMACOLOGYi2238.

Polymorphism and mutation databases

BioMutaiTEC.
DMDMi158518392.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000881701 – 631Tyrosine-protein kinase TecAdd BLAST631

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei206Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei228PhosphotyrosineCombined sources1
Modified residuei519Phosphotyrosine; by autocatalysis, LYN and JAK2Combined sources1

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

EPDiP42680.
MaxQBiP42680.
PaxDbiP42680.
PeptideAtlasiP42680.
PRIDEiP42680.

PTM databases

iPTMnetiP42680.
PhosphoSitePlusiP42680.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000135605.
CleanExiHS_TEC.
ExpressionAtlasiP42680. baseline and differential.
GenevisibleiP42680. HS.

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).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112865. 23 interactors.
IntActiP42680. 18 interactors.
MINTiMINT-1498364.
STRINGi9606.ENSP00000370912.

Chemistry databases

BindingDBiP42680.

Structurei

Secondary structure

1631
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 14Combined sources12
Beta strandi19 – 21Combined sources3
Beta strandi26 – 41Combined sources16
Beta strandi45 – 47Combined sources3
Beta strandi53 – 55Combined sources3
Helixi56 – 58Combined sources3
Beta strandi61 – 64Combined sources4
Beta strandi69 – 71Combined sources3
Beta strandi74 – 76Combined sources3
Beta strandi78 – 83Combined sources6
Beta strandi88 – 92Combined sources5
Helixi96 – 110Combined sources15
Beta strandi118 – 120Combined sources3
Beta strandi132 – 134Combined sources3
Beta strandi143 – 145Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LULNMR-A1-154[»]
ProteinModelPortaliP42680.
SMRiP42680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 111PHPROSITE-ProRule annotationAdd BLAST108
Domaini179 – 239SH3PROSITE-ProRule annotationAdd BLAST61
Domaini247 – 345SH2PROSITE-ProRule annotationAdd BLAST99
Domaini370 – 623Protein kinasePROSITE-ProRule annotationAdd BLAST254

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

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation
Contains 1 Btk-type zinc finger.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri113 – 149Btk-typePROSITE-ProRule annotationAdd BLAST37

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiP42680.
KOiK07364.
OMAiRNMNRSK.
OrthoDBiEOG091G0D46.
PhylomeDBiP42680.
TreeFamiTF351634.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 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

        10         20         30         40         50
MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSMLTY YEGRAEKKYR
60 70 80 90 100
KGFIDVSKIK CVEIVKNDDG VIPCQNKYPF QVVHDANTLY IFAPSPQSRD
110 120 130 140 150
LWVKKLKEEI KNNNNIMIKY HPKFWTDGSY QCCRQTEKLA PGCEKYNLFE
160 170 180 190 200
SSIRKALPPA PETKKRRPPP PIPLEEEDNS EEIVVAMYDF QAAEGHDLRL
210 220 230 240 250
ERGQEYLILE KNDVHWWRAR DKYGNEGYIP SNYVTGKKSN NLDQYEWYCR
260 270 280 290 300
NMNRSKAEQL LRSEDKEGGF MVRDSSQPGL YTVSLYTKFG GEGSSGFRHY
310 320 330 340 350
HIKETTTSPK KYYLAEKHAF GSIPEIIEYH KHNAAGLVTR LRYPVSVKGK
360 370 380 390 400
NAPTTAGFSY EKWEINPSEL TFMRELGSGL FGVVRLGKWR AQYKVAIKAI
410 420 430 440 450
REGAMCEEDF IEEAKVMMKL THPKLVQLYG VCTQQKPIYI VTEFMERGCL
460 470 480 490 500
LNFLRQRQGH FSRDVLLSMC QDVCEGMEYL ERNSFIHRDL AARNCLVSEA
510 520 530 540 550
GVVKVSDFGM ARYVLDDQYT SSSGAKFPVK WCPPEVFNYS RFSSKSDVWS
560 570 580 590 600
FGVLMWEVFT EGRMPFEKYT NYEVVTMVTR GHRLYQPKLA SNYVYEVMLR
610 620 630
CWQEKPEGRP SFEDLLRTID ELVECEETFG R
Length:631
Mass (Da):73,581
Last modified:September 11, 2007 - v2
Checksum:iF55DECBF9916E1F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti514V → F in BAA06171 (PubMed:7934162).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04185044R → Q.1 PublicationCorresponds to variant rs35374286dbSNPEnsembl.1
Natural variantiVAR_041851563R → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LULNMR-A1-154[»]
ProteinModelPortaliP42680.
SMRiP42680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112865. 23 interactors.
IntActiP42680. 18 interactors.
MINTiMINT-1498364.
STRINGi9606.ENSP00000370912.

Chemistry databases

BindingDBiP42680.
ChEMBLiCHEMBL4246.
GuidetoPHARMACOLOGYi2238.

PTM databases

iPTMnetiP42680.
PhosphoSitePlusiP42680.

Polymorphism and mutation databases

BioMutaiTEC.
DMDMi158518392.

Proteomic databases

EPDiP42680.
MaxQBiP42680.
PaxDbiP42680.
PeptideAtlasiP42680.
PRIDEiP42680.

Protocols and materials databases

DNASUi7006.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381501; ENSP00000370912; ENSG00000135605.
GeneIDi7006.
KEGGihsa:7006.
UCSCiuc003gxz.4. human.

Organism-specific databases

CTDi7006.
DisGeNETi7006.
GeneCardsiTEC.
HGNCiHGNC:11719. TEC.
HPAiHPA005733.
MalaCardsiTEC.
MIMi600583. gene.
neXtProtiNX_P42680.
OpenTargetsiENSG00000135605.
PharmGKBiPA36436.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiP42680.
KOiK07364.
OMAiRNMNRSK.
OrthoDBiEOG091G0D46.
PhylomeDBiP42680.
TreeFamiTF351634.

Enzyme and pathway databases

BioCyciZFISH:HS06035-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-1433557. Signaling by SCF-KIT.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-512988. Interleukin-3, 5 and GM-CSF signaling.
SignaLinkiP42680.
SIGNORiP42680.

Miscellaneous databases

ChiTaRSiTEC. human.
GeneWikiiTEC_(gene).
GenomeRNAii7006.
PROiP42680.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135605.
CleanExiHS_TEC.
ExpressionAtlasiP42680. baseline and differential.
GenevisibleiP42680. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 170 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.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.