TGFB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TGFB1_HUMAN
• UniProt AC: P01137
• Protein Name: Transforming growth factor beta-1
• Gene Name: TGFB1
• Organism: Homo sapiens (Human).
• Sequence Length: 390
• Subcellular Localization: Secreted, extracellular space, extracellular matrix .
• Protein Description: Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP). [PubMed: 25310401 Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells. Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus]
• Protein Sequence: MPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS

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
42	Sumoylation	TIDMELVKRKRIEAI CCCHHHHHHHHHHHH	65.90	-
42	Ubiquitination	TIDMELVKRKRIEAI CCCHHHHHHHHHHHH	65.90	-
42	Sumoylation	TIDMELVKRKRIEAI CCCHHHHHHHHHHHH	65.90	-
55	Phosphorylation	AIRGQILSKLRLASP HHHHHHHHHHHCCCC	31.13	24719451
56	Ubiquitination	IRGQILSKLRLASPP HHHHHHHHHHCCCCC	33.89	-
82	N-linked_Glycosylation	EAVLALYNSTRDRVA HHHHHHHHCCCCCCC	37.44	28117447
82	N-linked_Glycosylation	EAVLALYNSTRDRVA HHHHHHHHCCCCCCC	37.44	16335952
106	Ubiquitination	PEADYYAKEVTRVLM CCHHHHHHHHEEEEE	36.27	2190698
123	Ubiquitination	THNEIYDKFKQSTHS CCHHHHHHHHHCCCE	37.17	21890473
127	Phosphorylation	IYDKFKQSTHSIYMF HHHHHHHCCCEEEEE	28.78	24719451
128	Phosphorylation	YDKFKQSTHSIYMFF HHHHHHCCCEEEEEE	19.69	24043423
130	Phosphorylation	KFKQSTHSIYMFFNT HHHHCCCEEEEEEEH	18.59	24043423
132	Phosphorylation	KQSTHSIYMFFNTSE HHCCCEEEEEEEHHH	7.29	24043423
136	N-linked_Glycosylation	HSIYMFFNTSELREA CEEEEEEEHHHHHHH	31.28	16263699
137	Phosphorylation	SIYMFFNTSELREAV EEEEEEEHHHHHHHC	20.58	24043423
138	Phosphorylation	IYMFFNTSELREAVP EEEEEEHHHHHHHCC	35.42	24719451
163	Ubiquitination	RLLRLKLKVEQHVEL HHHHHHCHHHHHHHH	41.98	-
176	N-linked_Glycosylation	ELYQKYSNNSWRYLS HHHHHHCCCCHHHHH	43.39	17660510
274	Phosphorylation	RAQHLQSSRHRRALD HHHHHHHHHHHHHCC	21.10	24719451
291	Ubiquitination	YCFSSTEKNCCVRQL CCCCCCCCCEEEEEH	56.21	-
309	Ubiquitination	FRKDLGWKWIHEPKG EHHHHCCCCCCCCCC	34.18	-
317	Phosphorylation	WIHEPKGYHANFCLG CCCCCCCCCCCEECC	12.13	-

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

Oops, there are no upstream regulatory protein records of TGFB1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TGFB1_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 TGFB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FNTA_HUMAN	FNTA	physical	8599089
CO2A1_HUMAN	COL2A1	physical	10085302
PGS2_HUMAN	DCN	physical	8093006
PGS1_HUMAN	BGN	physical	8093006
FMOD_HUMAN	FMOD	physical	8093006
FCN1_HUMAN	FCN1	physical	7686157
TSP1_HUMAN	THBS1	physical	1550960
1433E_HUMAN	YWHAE	physical	11172812
FKB1A_HUMAN	FKBP1A	physical	11960000
LAMB1_HUMAN	LAMB1	physical	20936779
EPS15_HUMAN	EPS15	physical	19109251
FKB1A_HUMAN	FKBP1A	physical	23734213
CCD33_HUMAN	CCDC33	physical	25416956
NMT1_HUMAN	NMT1	physical	26186194
NMT2_HUMAN	NMT2	physical	26186194
FEM1B_HUMAN	FEM1B	physical	26186194
LAMC1_HUMAN	LAMC1	physical	26186194
UBR1_HUMAN	UBR1	physical	26186194
RMD5A_HUMAN	RMND5A	physical	26186194
IF1AX_HUMAN	EIF1AX	physical	26186194
AGR3_HUMAN	AGR3	physical	25640309
ANGL4_HUMAN	ANGPTL4	physical	25640309
BCAS3_HUMAN	BCAS3	physical	25640309
BLID_HUMAN	BLID	physical	25640309
CCL5_HUMAN	CCL5	physical	25640309
CYTM_HUMAN	CST6	physical	25640309
DIRA3_HUMAN	DIRAS3	physical	25640309
GREB1_HUMAN	GREB1	physical	25640309
HXC6_HUMAN	HOXC6	physical	25640309
KLK5_HUMAN	KLK5	physical	25640309
KLK7_HUMAN	KLK7	physical	25640309
KLK9_HUMAN	KLK9	physical	25640309
MTA3_HUMAN	MTA3	physical	25640309
PDLI2_HUMAN	PDLIM2	physical	25640309
HOP2_HUMAN	PSMC3IP	physical	25640309
SG3A1_HUMAN	SCGB3A1	physical	25640309
SNAI1_HUMAN	SNAI1	physical	25640309
ST14_HUMAN	ST14	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
TSP50_HUMAN	PRSS50	physical	25640309
NSD3_HUMAN	WHSC1L1	physical	25640309
A4_HUMAN	APP	physical	25241761
MMP9_HUMAN	MMP9	physical	25241761
DAXX_HUMAN	DAXX	physical	25241761
ERP44_HUMAN	ERP44	physical	28514442
NMT2_HUMAN	NMT2	physical	28514442
UBR1_HUMAN	UBR1	physical	28514442
NMT1_HUMAN	NMT1	physical	28514442
LAMC1_HUMAN	LAMC1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 131300: Camurati-Engelmann disease (CAEND)
• 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

N-linked Glycosylation

"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, AND MASS SPECTROMETRY.
PubMed: 16263699

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, AND MASS SPECTROMETRY.
PubMed: 16335952