dbPTM

FSTL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FSTL3_HUMAN
UniProt AC	O95633
Protein Name	Follistatin-related protein 3
Gene Name	FSTL3
Organism	Homo sapiens (Human).
Sequence Length	263
Subcellular Localization	Isoform 1: Secreted. Isoform 2: Nucleus. Although alternative initiation has been demonstrated and resulted in different localization, the major source of nuclear FSTL3 appears not to depend on translation initiation at Met-27 according to.
Protein Description	Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10..
Protein Sequence	MRPGAPGPLWPLPWGALAWAVGFVSSMGSGNPAPGGVCWLQQGQEATCSLVLQTDVTRAECCASGNIDTAWSNLTHPGNKINLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPRCECAPDCSGLPARLQVCGSDGATYRDECELRAARCRGHPDLSVMYRGRCRKSCEHVVCPRPQSCVVDQTGSAHCVVCRAAPCPVPSSPGQELCGNNNVTYISSCHMRQATCFLGRSIGVRHAGSCAGTPEEPPGGESAEEEENFV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
73	N-linked_Glycosylation	NIDTAWSNLTHPGNK CCCCCHHHCCCCCCC	37.95	22052913
137	Phosphorylation	ARLQVCGSDGATYRD EEEEECCCCCCCCHH	27.95	28270605
141	Phosphorylation	VCGSDGATYRDECEL ECCCCCCCCHHHHHH	25.31	28270605
142	Phosphorylation	CGSDGATYRDECELR CCCCCCCCHHHHHHH	18.61	28270605
205	Phosphorylation	APCPVPSSPGQELCG CCCCCCCCCCCCCCC	27.29	21712546
215	N-linked_Glycosylation	QELCGNNNVTYISSC CCCCCCCCEEEEECC	31.35	18768470
242	Phosphorylation	IGVRHAGSCAGTPEE CCEECCCCCCCCCCC	11.11	23090842
246	Phosphorylation	HAGSCAGTPEEPPGG CCCCCCCCCCCCCCC	14.70	23090842
255	Phosphorylation	EEPPGGESAEEEENF CCCCCCCCHHHHHCC	44.23	22617229

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
255	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FSTL3_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 FSTL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of FSTL3_HUMAN !!

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 FSTL3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structure of myostatin.follistatin-like 3: N-terminal domains offollistatin-type molecules exhibit alternate modes of binding."; Cash J.N., Angerman E.B., Kattamuri C., Nolan K., Zhao H., Sidis Y.,Keutmann H.T., Thompson T.B.; J. Biol. Chem. 287:1043-1053(2012). Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 36-244 IN COMPLEX WITH MOUSEGDF8, GLYCOSYLATION AT ASN-73, AND DISULFIDE BONDS.	22052913 [Abstract]
"The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity."; Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A.,Thompson T.B.; J. Biol. Chem. 283:32831-32838(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 27-263 IN COMPLEX WITHINHBA, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-215.	18768470 [Abstract]