FSTL1_HUMAN - dbPTM
FSTL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FSTL1_HUMAN
UniProt AC Q12841
Protein Name Follistatin-related protein 1
Gene Name FSTL1
Organism Homo sapiens (Human).
Sequence Length 308
Subcellular Localization Secreted .
Protein Description May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity)..
Protein Sequence MWKRWLALALALVAVAWVRAEEELRSKSKICANVFCGAGRECAVTEKGEPTCLCIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHCKEKKSVSPSASPVVCYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYPDQENNKLLRGLCVDALIELSDENADWKLSFQEFLKCLNPSFNPPEKKCALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKNQKGAQTQTEEEMTRYVQELQKHQETAEKTKRVSTKEI
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 Orthologous
Protein Cluster
88PhosphorylationRDACLTGSKIQVDYD
CCCCCCCCEEEECCC
22.7330631047
103PhosphorylationGHCKEKKSVSPSASP
CCCCCCCCCCCCCCC
38.6125003641
105PhosphorylationCKEKKSVSPSASPVV
CCCCCCCCCCCCCEE
21.8924505115
107O-linked_GlycosylationEKKSVSPSASPVVCY
CCCCCCCCCCCEEEE
33.59OGP
107PhosphorylationEKKSVSPSASPVVCY
CCCCCCCCCCCEEEE
33.5927251275
109PhosphorylationKSVSPSASPVVCYQS
CCCCCCCCCEEEECC
23.6727251275
114PhosphorylationSASPVVCYQSNRDEL
CCCCEEEECCCHHHH
11.9027251275
116PhosphorylationSPVVCYQSNRDELRR
CCEEEECCCHHHHHH
13.8327251275
141UbiquitinationIPDGWFSKGSNYSEI
CCCCCCCCCCCHHHH
57.81-
144N-linked_GlycosylationGWFSKGSNYSEILDK
CCCCCCCCHHHHHHH
53.68UniProtKB CARBOHYD
161PhosphorylationKNFDNGDSRLDSSEF
HCCCCCCCCCCHHHH
35.8222617229
165PhosphorylationNGDSRLDSSEFLKFV
CCCCCCCHHHHHHHH
36.0419664994
166PhosphorylationGDSRLDSSEFLKFVE
CCCCCCHHHHHHHHH
31.8429255136
175N-linked_GlycosylationFLKFVEQNETAINIT
HHHHHHCCCCCEECC
34.7716335952
180N-linked_GlycosylationEQNETAINITTYPDQ
HCCCCCEECCCCCCH
24.0816335952
231UbiquitinationPSFNPPEKKCALEDE
CCCCCCCCCCCCCCC
59.95-
277PhosphorylationKNQKGAQTQTEEEMT
CCCCCCCCCCHHHHH
36.6021406692
279PhosphorylationQKGAQTQTEEEMTRY
CCCCCCCCHHHHHHH
49.0721406692
284PhosphorylationTQTEEEMTRYVQELQ
CCCHHHHHHHHHHHH
23.3321406692
286PhosphorylationTEEEMTRYVQELQKH
CHHHHHHHHHHHHHH
9.41-

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
165SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FSTL1_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 FSTL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APBP2_HUMANAPPBP2physical
19060904

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 FSTL1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-175 AND ASN-180, AND MASSSPECTROMETRY.

TOP