TEC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TEC_HUMAN
• UniProt AC: P42680
• Protein Name: Tyrosine-protein kinase Tec
• Gene Name: TEC
• Organism: Homo sapiens (Human).
• Sequence Length: 631
• Subcellular Localization: Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Following B-cell or T-cell receptors activation by antigen, translocates to the plasma membrane through its PH domain. Thrombin and integrin engagement induces translocat
• Protein Description: 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..
• Protein Sequence: MNFNTILEEILIKRSQQKKKTSPLNYKERLFVLTKSMLTYYEGRAEKKYRKGFIDVSKIKCVEIVKNDDGVIPCQNKYPFQVVHDANTLYIFAPSPQSRDLWVKKLKEEIKNNNNIMIKYHPKFWTDGSYQCCRQTEKLAPGCEKYNLFESSIRKALPPAPETKKRRPPPPIPLEEEDNSEEIVVAMYDFQAAEGHDLRLERGQEYLILEKNDVHWWRARDKYGNEGYIPSNYVTGKKSNNLDQYEWYCRNMNRSKAEQLLRSEDKEGGFMVRDSSQPGLYTVSLYTKFGGEGSSGFRHYHIKETTTSPKKYYLAEKHAFGSIPEIIEYHKHNAAGLVTRLRYPVSVKGKNAPTTAGFSYEKWEINPSELTFMRELGSGLFGVVRLGKWRAQYKVAIKAIREGAMCEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMERGCLLNFLRQRQGHFSRDVLLSMCQDVCEGMEYLERNSFIHRDLAARNCLVSEAGVVKVSDFGMARYVLDDQYTSSSGAKFPVKWCPPEVFNYSRFSSKSDVWSFGVLMWEVFTEGRMPFEKYTNYEVVTMVTRGHRLYQPKLASNYVYEVMLRCWQEKPEGRPSFEDLLRTIDELVECEETFGR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MNFNTILEEILI ---CCHHHHHHHHHH	23.85	26261332
15	Ubiquitination	EEILIKRSQQKKKTS HHHHHHHHHHCCCCC	31.77	21890473
36	Phosphorylation	RLFVLTKSMLTYYEG HHHHHHHHHHHHCCC	17.49	29083192
39	Phosphorylation	VLTKSMLTYYEGRAE HHHHHHHHHCCCHHC	18.53	29083192
40	Phosphorylation	LTKSMLTYYEGRAEK HHHHHHHHCCCHHCH	8.78	29083192
41	Phosphorylation	TKSMLTYYEGRAEKK HHHHHHHCCCHHCHH	13.48	29083192
47	Ubiquitination	YYEGRAEKKYRKGFI HCCCHHCHHHHCCCE	54.87	22817900
48	Ubiquitination	YEGRAEKKYRKGFID CCCHHCHHHHCCCEE	41.62	22817900
51	Ubiquitination	RAEKKYRKGFIDVSK HHCHHHHCCCEEHHH	55.90	21890473
60	Ubiquitination	FIDVSKIKCVEIVKN CEEHHHCEEEEEEEC	35.64	-
88	Phosphorylation	QVVHDANTLYIFAPS EEEEECCEEEEECCC	23.74	-
90	Phosphorylation	VHDANTLYIFAPSPQ EEECCEEEEECCCCC	7.61	-
120	Phosphorylation	NNNIMIKYHPKFWTD CCCEEEEECCCCCCC	16.66	-
129	Phosphorylation	PKFWTDGSYQCCRQT CCCCCCCCHHHHCCC	18.16	22461510
130	Phosphorylation	KFWTDGSYQCCRQTE CCCCCCCHHHHCCCC	15.88	22461510
151	Phosphorylation	EKYNLFESSIRKALP HHHCCCHHHHHHHCC	24.59	28857561
152	Phosphorylation	KYNLFESSIRKALPP HHCCCHHHHHHHCCC	21.15	28857561
155	Malonylation	LFESSIRKALPPAPE CCHHHHHHHCCCCCC	53.24	26320211
155	Ubiquitination	LFESSIRKALPPAPE CCHHHHHHHCCCCCC	53.24	-
164	Malonylation	LPPAPETKKRRPPPP CCCCCCCCCCCCCCC	42.49	26320211
188	Phosphorylation	EEIVVAMYDFQAAEG CEEEEEEEEEHHHCC	12.13	27642862
206	Phosphorylation	RLERGQEYLILEKND EECCCCEEEEEECCC	7.37	29978859
223	Phosphorylation	WWRARDKYGNEGYIP EEEECCCCCCCCCCC	29.49	28152594
228	Phosphorylation	DKYGNEGYIPSNYVT CCCCCCCCCCCCCCC	11.95	22322096
231	Phosphorylation	GNEGYIPSNYVTGKK CCCCCCCCCCCCCCC	31.10	27642862
233	Phosphorylation	EGYIPSNYVTGKKSN CCCCCCCCCCCCCCC	12.06	22322096
235	Phosphorylation	YIPSNYVTGKKSNNL CCCCCCCCCCCCCCH	32.68	27642862
245	Phosphorylation	KSNNLDQYEWYCRNM CCCCHHHHHHHHHHC	14.22	24362263
275	Phosphorylation	GGFMVRDSSQPGLYT CCEECCCCCCCCEEE	21.95	28450419
276	Phosphorylation	GFMVRDSSQPGLYTV CEECCCCCCCCEEEE	44.69	28450419
281	Phosphorylation	DSSQPGLYTVSLYTK CCCCCCEEEEEEEEE	15.83	27642862
282	Phosphorylation	SSQPGLYTVSLYTKF CCCCCEEEEEEEEEE	14.52	28450419
284	Phosphorylation	QPGLYTVSLYTKFGG CCCEEEEEEEEEECC	14.09	28450419
286	Phosphorylation	GLYTVSLYTKFGGEG CEEEEEEEEEECCCC	10.61	23917254
287	Phosphorylation	LYTVSLYTKFGGEGS EEEEEEEEEECCCCC	25.78	28450419
322	Phosphorylation	AEKHAFGSIPEIIEY EHHHCCCCHHHHHHH	28.63	24247654
329	Phosphorylation	SIPEIIEYHKHNAAG CHHHHHHHHHHCCCC	13.03	27642862
343	Phosphorylation	GLVTRLRYPVSVKGK CCEEEEECEEEECCC	16.75	-
360	Phosphorylation	PTTAGFSYEKWEINP CCCCCCCEEECEECH	21.19	-
378	Phosphorylation	TFMRELGSGLFGVVR HHHHHHCCCCEEHHH	44.97	20071362
513	Phosphorylation	SDFGMARYVLDDQYT CCCCCEEEEECCCCC	8.88	21945579
519	Phosphorylation	RYVLDDQYTSSSGAK EEEECCCCCCCCCCC	18.65	21945579
520	Phosphorylation	YVLDDQYTSSSGAKF EEECCCCCCCCCCCC	19.25	21945579
521	Phosphorylation	VLDDQYTSSSGAKFP EECCCCCCCCCCCCC	19.99	21945579
522	Phosphorylation	LDDQYTSSSGAKFPV ECCCCCCCCCCCCCC	25.62	21945579
523	Phosphorylation	DDQYTSSSGAKFPVK CCCCCCCCCCCCCCC	42.40	21945579
526	Ubiquitination	YTSSSGAKFPVKWCP CCCCCCCCCCCCCCC	54.44	29967540
591	Phosphorylation	LYQPKLASNYVYEVM CCCCHHHHCHHHHHH	38.85	20071362
595	Phosphorylation	KLASNYVYEVMLRCW HHHHCHHHHHHHHHH	7.76	20071362
618	Phosphorylation	SFEDLLRTIDELVEC CHHHHHHHHHHHHHH	32.52	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
206	Y	Phosphorylation	Kinase	BTK	Q06187	PSP
206	Y	Phosphorylation	Kinase	ITK	Q08881	PSP
206	Y	Phosphorylation	Kinase	TEC	P42680	PSP
519	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
519	Y	Phosphorylation	Kinase	LYN	P07948	Uniprot
519	Y	Phosphorylation	Kinase	TEC	P42680	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TEC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TEC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRLR_HUMAN	PRLR	physical	11328862
VAV_HUMAN	VAV1	physical	11328862
P85B_HUMAN	PIK3R2	physical	9178903
LYN_HUMAN	LYN	physical	11071635
KIT_HUMAN	KIT	physical	11071635
DOK1_HUMAN	DOK1	physical	11071635
WASP_HUMAN	WAS	physical	8892607
KIT_HUMAN	KIT	physical	7526158
DOK1_HUMAN	DOK1	physical	11825908
SOCS1_HUMAN	SOCS1	physical	9341160
GNA12_HUMAN	GNA12	genetic	12515866
GNA13_HUMAN	GNA13	genetic	12515866
ARHGC_HUMAN	ARHGEF12	genetic	12515866
GNA12_HUMAN	GNA12	physical	12515866
ARHGC_HUMAN	ARHGEF12	physical	12515866
JAK2_HUMAN	JAK2	physical	9473212

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206; TYR-228 ANDSER-275, AND MASS SPECTROMETRY.
PubMed: 19369195

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, AND MASSSPECTROMETRY.
PubMed: 19690332

"Identification of phosphorylation sites within the SH3 domains of Tecfamily 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).
Cited for: PROTEIN SEQUENCE OF 203-206, AND PHOSPHORYLATION AT TYR-206.
PubMed: 12573241