OSTF1_HUMAN - dbPTM
OSTF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSTF1_HUMAN
UniProt AC Q92882
Protein Name Osteoclast-stimulating factor 1
Gene Name OSTF1
Organism Homo sapiens (Human).
Sequence Length 214
Subcellular Localization Cytoplasm .
Protein Description Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity..
Protein Sequence MSKPPPKPVKPGQVKVFRALYTFEPRTPDELYFEEGDIIYITDMSDTNWWKGTSKGRTGLIPSNYVAEQAESIDNPLHEAAKRGNLSWLRECLDNRVGVNGLDKAGSTALYWACHGGHKDIVEMLFTQPNIELNQQNKLGDTALHAAAWKGYADIVQLLLAKGARTDLRNIEKKLAFDMATNAACASLLKKKQGTDAVRTLSNAEDYLDDEDSD
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
2Acetylation------MSKPPPKPV
------CCCCCCCCC		54.6025944712
21PhosphorylationVKVFRALYTFEPRTP
EEEEEEEEEECCCCC		14.3828152594
22PhosphorylationKVFRALYTFEPRTPD
EEEEEEEEECCCCCC		23.5228152594
39UbiquitinationYFEEGDIIYITDMSD
EECCCCEEEEEECCC		2.1222505724
54PhosphorylationTNWWKGTSKGRTGLI
CCCCCCCCCCCCCEE		41.6121712546
56UbiquitinationWWKGTSKGRTGLIPS
CCCCCCCCCCCEECC		31.9522505724
58PhosphorylationKGTSKGRTGLIPSNY
CCCCCCCCCEECCHH		45.0421712546
63PhosphorylationGRTGLIPSNYVAEQA
CCCCEECCHHHHHHH		33.5221712546
65PhosphorylationTGLIPSNYVAEQAES
CCEECCHHHHHHHHH		12.8427642862
72PhosphorylationYVAEQAESIDNPLHE
HHHHHHHHCCCHHHH		37.9527067055
82AcetylationNPLHEAAKRGNLSWL
CHHHHHHHHCCHHHH		68.8125953088
82UbiquitinationNPLHEAAKRGNLSWL
CHHHHHHHHCCHHHH		68.8122505724
85UbiquitinationHEAAKRGNLSWLREC
HHHHHHCCHHHHHHH		34.6322505724
87PhosphorylationAAKRGNLSWLRECLD
HHHHCCHHHHHHHHH		28.2324719451
111PhosphorylationKAGSTALYWACHGGH
CCCHHHHHHHHHCCC		6.6225147952
119UbiquitinationWACHGGHKDIVEMLF
HHHHCCCHHHHHHHH		53.0421890473
136UbiquitinationPNIELNQQNKLGDTA
CCEECCCCCCCCHHH		48.2121890473
152PhosphorylationHAAAWKGYADIVQLL
HHHHHCCHHHHHHHH		9.4328348404
162UbiquitinationIVQLLLAKGARTDLR
HHHHHHHCCCCHHHH		53.7423000965
165UbiquitinationLLLAKGARTDLRNIE
HHHHCCCCHHHHHHH		37.1221890473
174UbiquitinationDLRNIEKKLAFDMAT
HHHHHHHHHHHHHHH		32.0529967540
181PhosphorylationKLAFDMATNAACASL
HHHHHHHHHHHHHHH		20.8226552605
185GlutathionylationDMATNAACASLLKKK
HHHHHHHHHHHHHHH		2.1622555962
187PhosphorylationATNAACASLLKKKQG
HHHHHHHHHHHHHCC		33.8330576142
190UbiquitinationAACASLLKKKQGTDA
HHHHHHHHHHCCCCH		64.3229967540
195PhosphorylationLLKKKQGTDAVRTLS
HHHHHCCCCHHHHHC		20.4929514088
200PhosphorylationQGTDAVRTLSNAEDY
CCCCHHHHHCCHHHH		28.1220201521
202PhosphorylationTDAVRTLSNAEDYLD
CCHHHHHCCHHHHCC		33.1220201521
207PhosphorylationTLSNAEDYLDDEDSD
HHCCHHHHCCCCCCC		11.9730278072
213PhosphorylationDYLDDEDSD------
HHCCCCCCC------		43.0820201521
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
202SPhosphorylationKinaseRPS6KA1Q15418
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSTF1_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 OSTF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTND_HUMANADI1physical
17353931
KHDR1_HUMANKHDRBS1physical
22745667
CBL_HUMANCBLphysical
15135048
SRC_HUMANSRCphysical
15135048
ACTB_HUMANACTBphysical
15135048
A4_HUMANAPPphysical
21832049
TRI54_HUMANTRIM54physical
25416956
XRP2_HUMANRP2physical
28514442
KLH42_HUMANKLHL42physical
28514442
MYO1E_HUMANMYO1Ephysical
28514442
PXDNL_HUMANPXDNLphysical
28514442
CHM2A_HUMANCHMP2Aphysical
28514442
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 OSTF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-200 AND SER-213, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-202 ANDSER-213, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, ANDMASS SPECTROMETRY.
"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-202 AND SER-213, ANDMASS SPECTROMETRY.
"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-213, AND MASSSPECTROMETRY.

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