dbPTM

TGFI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TGFI1_HUMAN
UniProt AC	O43294
Protein Name	Transforming growth factor beta-1-induced transcript 1 protein
Gene Name	TGFB1I1
Organism	Homo sapiens (Human).
Sequence Length	461
Subcellular Localization	Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Associated with the actin cytoskeleton colocalizes with stress fibers.
Protein Description	Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity..
Protein Sequence	MEDLDALLSDLETTTSHMPRSGAPKERPAEPLTPPPSYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKPAAPAAPPFSSSSGVLGTGLCELDRLLQELNATQFNITDEIMSQFPSSKVASGEQKEDQSEDKKRPSLPSSPSPGLPKASATSATLELDRLMASLSDFRVQNHLPASGPTQPPVVSSTNEGSPSPPEPTGKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGDEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECFAPFSGGSFFEHEGRPLCENHFHARRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERAGKPYCQPCFLKLFG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDLDALL -------CHHHHHHH	9.02	22814378
9	Phosphorylation	EDLDALLSDLETTTS HHHHHHHHHHHHHHC	40.79	22199227
13	Phosphorylation	ALLSDLETTTSHMPR HHHHHHHHHHCCCCC	42.54	27732954
14	Phosphorylation	LLSDLETTTSHMPRS HHHHHHHHHCCCCCC	19.54	27732954
15	Phosphorylation	LSDLETTTSHMPRSG HHHHHHHHCCCCCCC	24.85	27732954
16 (in isoform 2)	Phosphorylation	-	18.72	-
16	Phosphorylation	SDLETTTSHMPRSGA HHHHHHHCCCCCCCC	18.72	27732954
21	Phosphorylation	TTSHMPRSGAPKERP HHCCCCCCCCCCCCC	33.17	29759185
27 (in isoform 2)	Phosphorylation	-	41.68	-
32 (in isoform 2)	Phosphorylation	-	9.39	-
33	Phosphorylation	ERPAEPLTPPPSYGH CCCCCCCCCCCCCCC	44.45	28355574
36 (in isoform 2)	Phosphorylation	-	41.19	-
37	Phosphorylation	EPLTPPPSYGHQPQT CCCCCCCCCCCCCCC	49.90	21955146
38	Phosphorylation	PLTPPPSYGHQPQTG CCCCCCCCCCCCCCC	25.13	21955146
44	Phosphorylation	SYGHQPQTGSGESSG CCCCCCCCCCCCCCC	39.74	21955146
46	Phosphorylation	GHQPQTGSGESSGAS CCCCCCCCCCCCCCC	42.65	22199227
49	Phosphorylation	PQTGSGESSGASGDK CCCCCCCCCCCCCCC	37.28	21955146
50	Phosphorylation	QTGSGESSGASGDKD CCCCCCCCCCCCCCC	33.79	22199227
51 (in isoform 2)	Phosphorylation	-	32.80	-
53	Phosphorylation	SGESSGASGDKDHLY CCCCCCCCCCCCCEE	51.56	25850435
60	Phosphorylation	SGDKDHLYSTVCKPR CCCCCCEEEEECCCC	10.01	21945579
61	Phosphorylation	GDKDHLYSTVCKPRS CCCCCEEEEECCCCC	22.26	21945579
62	Phosphorylation	DKDHLYSTVCKPRSP CCCCEEEEECCCCCC	19.16	21945579
65 (in isoform 2)	Phosphorylation	-	38.85	-
68	Phosphorylation	STVCKPRSPKPAAPA EEECCCCCCCCCCCC	45.89	29255136
80	Phosphorylation	APAAPPFSSSSGVLG CCCCCCCCCCCCCCC	34.78	23663014
81	O-linked_Glycosylation	PAAPPFSSSSGVLGT CCCCCCCCCCCCCCC	28.98	31492838
81	Phosphorylation	PAAPPFSSSSGVLGT CCCCCCCCCCCCCCC	28.98	26657352
82	Phosphorylation	AAPPFSSSSGVLGTG CCCCCCCCCCCCCCH	29.88	30266825
83	Phosphorylation	APPFSSSSGVLGTGL CCCCCCCCCCCCCHH	34.56	23663014
88	Phosphorylation	SSSGVLGTGLCELDR CCCCCCCCHHHHHHH	23.87	24117733
102 (in isoform 2)	Ubiquitination	-	18.53	-
105 (in isoform 2)	Phosphorylation	-	6.57	-
109 (in isoform 2)	Ubiquitination	-	39.36	-
120 (in isoform 2)	Phosphorylation	-	5.75	-
122	Phosphorylation	FPSSKVASGEQKEDQ CCCCCCCCCCCCCCC	45.94	26657352
123 (in isoform 2)	Phosphorylation	-	31.45	-
124 (in isoform 2)	Phosphorylation	-	56.86	-
126 (in isoform 2)	Phosphorylation	-	59.98	-
130	Phosphorylation	GEQKEDQSEDKKRPS CCCCCCCCCCCCCCC	61.15	26657352
137	Phosphorylation	SEDKKRPSLPSSPSP CCCCCCCCCCCCCCC	57.87	29255136
140	Phosphorylation	KKRPSLPSSPSPGLP CCCCCCCCCCCCCCC	61.24	29255136
141	Phosphorylation	KRPSLPSSPSPGLPK CCCCCCCCCCCCCCC	27.70	29255136
143	Phosphorylation	PSLPSSPSPGLPKAS CCCCCCCCCCCCCCC	33.28	25463755
150	Phosphorylation	SPGLPKASATSATLE CCCCCCCCCCCHHHH	37.90	20873877
152	Phosphorylation	GLPKASATSATLELD CCCCCCCCCHHHHHH	19.19	26657352
153	Phosphorylation	LPKASATSATLELDR CCCCCCCCHHHHHHH	20.97	26657352
155	Phosphorylation	KASATSATLELDRLM CCCCCCHHHHHHHHH	22.11	30242111
164	Phosphorylation	ELDRLMASLSDFRVQ HHHHHHHHHHHCCHH	17.91	23911959
166	Phosphorylation	DRLMASLSDFRVQNH HHHHHHHHHCCHHHC	32.01	23403867
169 (in isoform 2)	Phosphorylation	-	33.82	-
170 (in isoform 2)	Phosphorylation	-	7.25	-
175 (in isoform 2)	Phosphorylation	-	19.48	-
177	Phosphorylation	VQNHLPASGPTQPPV HHHCCCCCCCCCCCC	43.28	18691976
177 (in isoform 2)	Phosphorylation	-	43.28	-
180	Phosphorylation	HLPASGPTQPPVVSS CCCCCCCCCCCCCCC	58.18	28060719
186	Phosphorylation	PTQPPVVSSTNEGSP CCCCCCCCCCCCCCC	31.51	22167270
187	Phosphorylation	TQPPVVSSTNEGSPS CCCCCCCCCCCCCCC	24.52	22167270
188	Phosphorylation	QPPVVSSTNEGSPSP CCCCCCCCCCCCCCC	29.77	22167270
192	Phosphorylation	VSSTNEGSPSPPEPT CCCCCCCCCCCCCCC	18.94	29255136
194	Phosphorylation	STNEGSPSPPEPTGK CCCCCCCCCCCCCCC	55.58	23401153
199	Phosphorylation	SPSPPEPTGKGSLDT CCCCCCCCCCCCHHH	50.27	29255136
203	Phosphorylation	PEPTGKGSLDTMLGL CCCCCCCCHHHHHHH	26.93	26657352
207	Sulfoxidation	GKGSLDTMLGLLQSD CCCCHHHHHHHHHHH	2.52	30846556
213	Phosphorylation	TMLGLLQSDLSRRGV HHHHHHHHHHHHCCC	40.25	28857561
216	Phosphorylation	GLLQSDLSRRGVPTQ HHHHHHHHHCCCCCC	25.56	26657352
284	Phosphorylation	ECYFERFSPRCGFCN HHHHHCCCCCCCCCC	20.04	28555341
380	Phosphorylation	RECFAPFSGGSFFEH CHHCCCCCCCCCCCC	40.98	26657352
383	Phosphorylation	FAPFSGGSFFEHEGR CCCCCCCCCCCCCCC	30.22	27251275
386 (in isoform 2)	Phosphorylation	-	38.73	-
403	Phosphorylation	HFHARRGSLCATCGL CCHHCCCCCCHHCCC	20.61	26846344
407	Phosphorylation	RRGSLCATCGLPVTG CCCCCCHHCCCCCCC	13.20	23927012
413	Phosphorylation	ATCGLPVTGRCVSAL HHCCCCCCCCHHHHH	19.57	23927012
418	Phosphorylation	PVTGRCVSALGRRFH CCCCCHHHHHCCCCC	22.77	24670416
430	Phosphorylation	RFHPDHFTCTFCLRP CCCCCCEEEEEECCC	13.76	24719451
449	Ubiquitination	SFQERAGKPYCQPCF CHHHHCCCCCCCCHH	31.65	-
458	Ubiquitination	YCQPCFLKLFG---- CCCCHHHHHCC----	22.86	-

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
60	Y	Phosphorylation	Kinase	PYK2	Q14289	PSP
60	Y	Phosphorylation	Kinase	PTK2B	P70600	GPS
60	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TGFI1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TGFI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCR_HUMAN	NR3C1	physical	10848625
FAK2_HUMAN	PTK2B	physical	9422762
FAK2_HUMAN	PTK2B	physical	11856738
FAK1_HUMAN	PTK2	physical	11463817
PAXI_HUMAN	PXN	physical	11463817
FAK1_HUMAN	PTK2	physical	9858471
FAK2_HUMAN	PTK2B	physical	9858471
VINC_HUMAN	VCL	physical	9858471
GIT1_RAT	Git1	physical	12153727
HSPB1_HUMAN	HSPB1	physical	11546764
SMAD3_HUMAN	SMAD3	physical	15561701
CBLC_HUMAN	CBLC	physical	24831009
HSPB1_HUMAN	HSPB1	physical	24831009
HSPB2_HUMAN	HSPB2	physical	24831009
SMAD3_HUMAN	SMAD3	physical	14755691

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.

Regulatory Network of TGFI1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-68 AND SER-186, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-192 AND SER-194,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Suppression of androgen receptor transactivation by Pyk2 viainteraction and phosphorylation of the ARA55 coregulator."; Wang X., Yang Y., Guo X., Sampson E.R., Hsu C.-L., Tsai M.-Y., Yeh S.,Wu G., Guo Y., Chang C.; J. Biol. Chem. 277:15426-15431(2002). Cited for: FUNCTION, INTERACTION WITH PTK2B/PYK2, AND PHOSPHORYLATION AT TYR-60BY FAK2.	11856738 [Abstract]
"Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn."; Ishino M., Aoto H., Sasaski H., Suzuki R., Sasaki T.; FEBS Lett. 474:179-183(2000). Cited for: MUTAGENESIS OF TYR-60, PHOSPHORYLATION AT TYR-60, AND INTERACTION WITHCSK AND PTK2B/PYK2.	10838081 [Abstract]