IBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IBP1_HUMAN
• UniProt AC: P08833
• Protein Name: Insulin-like growth factor-binding protein 1
• Gene Name: IGFBP1
• Organism: Homo sapiens (Human).
• Sequence Length: 259
• Subcellular Localization: Secreted.
• Protein Description: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration..
• Protein Sequence: MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN

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
23	Phosphorylation	LTVQVGVTAGAPWQC HHHHHCCCCCCCCCC	17.28	22210691
34	Phosphorylation	PWQCAPCSAEKLALC CCCCCCCCHHHHCCC	38.10	24505115
45	Phosphorylation	LALCPPVSASCSEVT HCCCCCCCCCCCHHH	21.90	26091039
52	O-linked_Glycosylation	SASCSEVTRSAGCGC CCCCCHHHHHCCCCC	18.17	OGP
83	Phosphorylation	ARCARGLSCRALPGE HHHHCCCCCCCCCCC	12.37	-
98	O-linked_Glycosylation	QQPLHALTRGQGACV CCCHHHHHCCCCCEE	33.27	OGP
108	Phosphorylation	QGACVQESDASAPHA CCCEEECCCCCCCCH	22.76	7678248
120	Phosphorylation	PHAAEAGSPESPEST CCHHHCCCCCCCCCC	32.32	19765076
123	Phosphorylation	AEAGSPESPESTEIT HHCCCCCCCCCCCCC	37.03	18772238
126	Phosphorylation	GSPESPESTEITEEE CCCCCCCCCCCCHHH	34.42	18772238
127	Phosphorylation	SPESPESTEITEEEL CCCCCCCCCCCHHHH	29.73	24275569
144	Phosphorylation	NFHLMAPSEEDHSIL HCCCCCCCHHHHCHH	44.04	18772238
156	Phosphorylation	SILWDAISTYDGSKA CHHHHHHHCCCCCCE	23.72	26091039
157	Phosphorylation	ILWDAISTYDGSKAL HHHHHHHCCCCCCEE	21.37	26091039
158	Phosphorylation	LWDAISTYDGSKALH HHHHHHCCCCCCEEE	16.12	26091039
167	O-linked_Glycosylation	GSKALHVTNIKKWKE CCCEEEECCCCCCCC	22.07	OGP
181	Phosphorylation	EPCRIELYRVVESLA CCCHHHHHHHHHHHH	6.64	-
193	Phosphorylation	SLAKAQETSGEEISK HHHHHHHCCCCCCHH	29.92	30242111
194	Phosphorylation	LAKAQETSGEEISKF HHHHHHCCCCCCHHC	43.38	18772238
199	Phosphorylation	ETSGEEISKFYLPNC HCCCCCCHHCCCCCC	21.71	30242111
242	Phosphorylation	NGKRIPGSPEIRGDP CCEECCCCCCCCCCC	17.63	15489334

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
45	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
126	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
126	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
144	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
144	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
156	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
157	T	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
193	T	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
194	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
194	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
194	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
199	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
242	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IBP1_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 IBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN3_HUMAN	PTPN3	physical	28514442
TRIP6_HUMAN	TRIP6	physical	28514442
SUSD5_HUMAN	SUSD5	physical	28514442
ATS1_HUMAN	ADAMTS1	physical	28514442
ZN696_HUMAN	ZNF696	physical	28514442
TIMP1_HUMAN	TIMP1	physical	28514442
IGF2_HUMAN	IGF2	physical	28514442
PXDC2_HUMAN	PLXDC2	physical	28514442
GBB2_HUMAN	GNB2	physical	28514442
ZN664_HUMAN	ZNF664	physical	28514442
SMOC1_HUMAN	SMOC1	physical	28514442
GTPB2_HUMAN	GTPBP2	physical	28514442
LMF2_HUMAN	LMF2	physical	28514442
TIMP3_HUMAN	TIMP3	physical	28514442
CD59_HUMAN	CD59	physical	28514442
CTBP1_HUMAN	CTBP1	physical	28514442
NDST2_HUMAN	NDST2	physical	28514442
UBP46_HUMAN	USP46	physical	28514442
CTBP2_HUMAN	CTBP2	physical	28514442
TPA_HUMAN	PLAT	physical	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Identification of the sites of phosphorylation in insulin-like growthfactor binding protein-1. Regulation of its affinity byphosphorylation of serine 101.";
Jones J.I., Busby W.H. Jr., Wright G., Smith C.E., Kimack N.M.,Clemmons D.R.;
J. Biol. Chem. 268:1125-1131(1993).
Cited for: PHOSPHORYLATION AT SER-126; SER-144 AND SER-194, AND PARTIAL PROTEINSEQUENCE.
PubMed: 7678248

"Identification of the amniotic fluid insulin-like growth factorbinding protein-1 phosphorylation sites and propensity to proteolysisof the isoforms.";
Dolcini L., Sala A., Campagnoli M., Labo S., Valli M., Visai L.,Minchiotti L., Monaco H.L., Galliano M.;
FEBS J. 276:6033-6046(2009).
Cited for: PROTEIN SEQUENCE OF 26-53; 95-152 AND 182-208, CLEAVAGE OF INITIATORMETHIONINE, PHOSPHORYLATION AT SER-120; SER-123; SER-126; SER-144 ANDSER-194, AND MASS SPECTROMETRY.
PubMed: 19765076