IBP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IBP5_HUMAN
• UniProt AC: P24593
• Protein Name: Insulin-like growth factor-binding protein 5
• Gene Name: IGFBP5
• Organism: Homo sapiens (Human).
• Sequence Length: 272
• 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..
• Protein Sequence: MVLLTAVLLLLAAYAGPAQSLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYREQVKIERDSREHEEPTTSEMAEETYSPKIFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRIISAPEMRQESEQGPCRRHMEASLQELKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHTFDSSNVE

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
41	Phosphorylation	ALSMCPPSPLGCELV HHHCCCCCCCCCEEC	20.21	28348404
116	Phosphorylation	QVKIERDSREHEEPT HHCCCCCCCCCCCCC	45.87	17496250
123	Phosphorylation	SREHEEPTTSEMAEE CCCCCCCCHHHHHHH	46.35	26657352
123	O-linked_Glycosylation	SREHEEPTTSEMAEE CCCCCCCCHHHHHHH	46.35	55833671
124	Phosphorylation	REHEEPTTSEMAEET CCCCCCCHHHHHHHH	33.14	26657352
125	Phosphorylation	EHEEPTTSEMAEETY CCCCCCHHHHHHHHC	28.05	27362937
131	O-linked_Glycosylation	TSEMAEETYSPKIFR HHHHHHHHCCCCCCC	22.32	55833677
131	Phosphorylation	TSEMAEETYSPKIFR HHHHHHHHCCCCCCC	22.32	29759185
132	Phosphorylation	SEMAEETYSPKIFRP HHHHHHHCCCCCCCC	26.67	24505115
133	Phosphorylation	EMAEETYSPKIFRPK HHHHHHCCCCCCCCC	27.43	24505115
142	Phosphorylation	KIFRPKHTRISELKA CCCCCCCCCHHHHHH	35.51	24505115
145	Phosphorylation	RPKHTRISELKAEAV CCCCCCHHHHHHHHH	33.32	24505115
161	Phosphorylation	KDRRKKLTQSKFVGG HHHHHHHHHCCCCCC	39.41	24505115
163	Phosphorylation	RRKKLTQSKFVGGAE HHHHHHHCCCCCCCC	23.87	24505115
172	O-linked_Glycosylation	FVGGAENTAHPRIIS CCCCCCCCCCCCCCC	20.18	9883900
172	O-linked_Glycosylation	FVGGAENTAHPRIIS CCCCCCCCCCCCCCC	20.18	9883900
179	Phosphorylation	TAHPRIISAPEMRQE CCCCCCCCCHHHHHH	35.09	25850435
199	Phosphorylation	CRRHMEASLQELKAS HHHHHHHHHHHHHCC	19.78	24505115
206	Phosphorylation	SLQELKASPRMVPRA HHHHHHCCCCCCCCE	16.08	28348404
215	Phosphorylation	RMVPRAVYLPNCDRK CCCCCEEECCCCCCC	18.56	-
247	Phosphorylation	ICWCVDKYGMKLPGM EEEEECCCCCCCCCC	20.28	-
268	Phosphorylation	FQCHTFDSSNVE--- CEEEECCCCCCC---	21.44	17496250
269	Phosphorylation	QCHTFDSSNVE---- EEEECCCCCCC----	46.90	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
116	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IBP5_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 IBP5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAG6_HUMAN	BAG6	physical	16169070
FHL2_HUMAN	FHL2	physical	11821401
VTNC_HUMAN	VTN	physical	11751588

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

O-linked Glycosylation

"Isolation and characterization of circulating 13-kDa C-terminalfragments of human insulin-like growth factor binding protein-5.";
Standker L., Wobst P., Mark S., Forssmann W.-G.;
FEBS Lett. 441:281-286(1998).
Cited for: PROTEIN SEQUENCE OF 141-178 AND 209-223, AND GLYCOSYLATION AT THR-172.
PubMed: 9883900