dbPTM

ICAM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ICAM3_HUMAN
UniProt AC	P32942
Protein Name	Intercellular adhesion molecule 3
Gene Name	ICAM3
Organism	Homo sapiens (Human).
Sequence Length	547
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). [PubMed: 1448173 ICAM3 is also a ligand for integrin alpha-D/beta-2. In association with integrin alpha-L/beta-2, contributes to apoptotic neutrophil phagocytosis by macrophages]
Protein Sequence	MATMVPSVLWPRACWTLLVCCLLTPGVQGQEFLLRVEPQNPVLSAGGSLFVNCSTDCPSSEKIALETSLSKELVASGMGWAAFNLSNVTGNSRILCSVYCNGSQITGSSNITVYRLPERVELAPLPPWQPVGQNFTLRCQVEDGSPRTSLTVVLLRWEEELSRQPAVEEPAEVTATVLASRDDHGAPFSCRTELDMQPQGLGLFVNTSAPRQLRTFVLPVTPPRLVAPRFLEVETSWPVDCTLDGLFPASEAQVYLALGDQMLNATVMNHGDTLTATATATARADQEGAREIVCNVTLGGERREARENLTVFSFLGPIVNLSEPTAHEGSTVTVSCMAGARVQVTLDGVPAAAPGQPAQLQLNATESDDGRSFFCSATLEVDGEFLHRNSSVQLRVLYGPKIDRATCPQHLKWKDKTRHVLQCQARGNPYPELRCLKEGSSREVPVGIPFFVNVTHNGTYQCQASSSRGKYTLVVVMDIEAGSSHFVPVFVAVLLTLGVVTIVLALMYVFREHQRSGSYHVREESTYLPLTSMQPTEAMGEEPSRAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MATMVPSVLW -----CCCCCCCCHH	19.87	23663014
7	Phosphorylation	-MATMVPSVLWPRAC -CCCCCCCCHHHHHH	20.59	23663014
52	N-linked_Glycosylation	AGGSLFVNCSTDCPS CCCCEEEECCCCCCC	13.49	15728350
84	N-linked_Glycosylation	GMGWAAFNLSNVTGN CCCEEEEEECCCCCC	37.52	19349973
84	N-linked_Glycosylation	GMGWAAFNLSNVTGN CCCEEEEEECCCCCC	37.52	19349973
87	N-linked_Glycosylation	WAAFNLSNVTGNSRI EEEEEECCCCCCCEE	38.24	19349973
87	N-linked_Glycosylation	WAAFNLSNVTGNSRI EEEEEECCCCCCCEE	38.24	19349973
91	N-linked_Glycosylation	NLSNVTGNSRILCSV EECCCCCCCEEEEEE	20.81	19349973
91	N-linked_Glycosylation	NLSNVTGNSRILCSV EECCCCCCCEEEEEE	20.81	19349973
101	N-linked_Glycosylation	ILCSVYCNGSQITGS EEEEEEECCCEEECC	35.15	UniProtKB CARBOHYD
110	N-linked_Glycosylation	SQITGSSNITVYRLP CEEECCCCEEEEECC	35.33	15728350
134	N-linked_Glycosylation	PWQPVGQNFTLRCQV CCCCCCCCEEEEEEE	26.41	19349973
134	N-linked_Glycosylation	PWQPVGQNFTLRCQV CCCCCCCCEEEEEEE	26.41	19349973
136	Phosphorylation	QPVGQNFTLRCQVED CCCCCCEEEEEEEEC	22.35	24719451
151	Phosphorylation	GSPRTSLTVVLLRWE CCCCCEEEEEEEEEH	14.34	-
174	O-linked_Glycosylation	VEEPAEVTATVLASR CCCCCEEEEEEEECC	14.23	OGP
206	N-linked_Glycosylation	QGLGLFVNTSAPRQL CCCEEEEECCCCCEE	22.45	16335952
206	N-linked_Glycosylation	QGLGLFVNTSAPRQL CCCEEEEECCCCCEE	22.45	19159218
264	N-linked_Glycosylation	ALGDQMLNATVMNHG HHCCHHCCEEEECCC	28.37	UniProtKB CARBOHYD
295	N-linked_Glycosylation	GAREIVCNVTLGGER CCEEEEEEEEECCCH	20.93	19349973
295	N-linked_Glycosylation	GAREIVCNVTLGGER CCEEEEEEEEECCCH	20.93	19349973
308	N-linked_Glycosylation	ERREARENLTVFSFL CHHHHHCCCEEEEEC	35.14	UniProtKB CARBOHYD
320	N-linked_Glycosylation	SFLGPIVNLSEPTAH EECCCCCCCCCCCCC	38.27	UniProtKB CARBOHYD
325	O-linked_Glycosylation	IVNLSEPTAHEGSTV CCCCCCCCCCCCCEE	36.27	OGP
333	O-linked_Glycosylation	AHEGSTVTVSCMAGA CCCCCEEEEEECCCC	13.54	OGP
363	N-linked_Glycosylation	QPAQLQLNATESDDG CCEEEEECCCCCCCC	31.68	19159218
363	N-linked_Glycosylation	QPAQLQLNATESDDG CCEEEEECCCCCCCC	31.68	16335952
389	N-linked_Glycosylation	DGEFLHRNSSVQLRV CCEEECCCCCEEEEE	28.08	UniProtKB CARBOHYD
401	Ubiquitination	LRVLYGPKIDRATCP EEEEECCCCCCCCCC	53.53	-
412	Ubiquitination	ATCPQHLKWKDKTRH CCCCCCCCCCCCCCE	50.50	-
414	Ubiquitination	CPQHLKWKDKTRHVL CCCCCCCCCCCCEEE	48.00	-
430	Phosphorylation	CQARGNPYPELRCLK EHHCCCCCCCCCEEC	17.22	28102081
453	N-linked_Glycosylation	VGIPFFVNVTHNGTY CCCCEEEEECCCCEE	28.01	UniProtKB CARBOHYD
457	N-linked_Glycosylation	FFVNVTHNGTYQCQA EEEEECCCCEEEEEE	34.83	UniProtKB CARBOHYD
516	Phosphorylation	VFREHQRSGSYHVRE HHHHHHHCCCEEECC	26.06	23401153
518	Phosphorylation	REHQRSGSYHVREES HHHHHCCCEEECCCC	17.20	28857561
519	Phosphorylation	EHQRSGSYHVREEST HHHHCCCEEECCCCC	14.09	24702127
525	Phosphorylation	SYHVREESTYLPLTS CEEECCCCCEEECCC	20.00	23401153
526	Phosphorylation	YHVREESTYLPLTSM EEECCCCCEEECCCC	32.15	23401153
527	Phosphorylation	HVREESTYLPLTSMQ EECCCCCEEECCCCC	18.66	28796482
531	Phosphorylation	ESTYLPLTSMQPTEA CCCEEECCCCCCCCC	21.88	28796482
532	Phosphorylation	STYLPLTSMQPTEAM CCEEECCCCCCCCCC	24.09	28796482
536	Phosphorylation	PLTSMQPTEAMGEEP ECCCCCCCCCCCCCC	21.34	28796482
544	Phosphorylation	EAMGEEPSRAE---- CCCCCCCCCCC----	47.61	26074081

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
518	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ICAM3_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
110	N-linked Glycosylation	115 (5)	R ⇒ G	rs7258015	Systemic lupus erythematosus or rheumatoid arthritis	27193031

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MOES_HUMAN	MSN	physical	9298994
MOES_HUMAN	MSN	physical	11784723
EZRI_HUMAN	EZR	physical	11784723
A4_HUMAN	APP	physical	21832049
TM192_HUMAN	TMEM192	physical	28514442
FUT8_HUMAN	FUT8	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.

Regulatory Network of ICAM3_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"An atomic resolution view of ICAM recognition in a complex betweenthe binding domains of ICAM-3 and integrin alphaLbeta2."; Song G., Yang Y., Liu J.-H., Casasnovas J.M., Shimaoka M.,Springer T.A., Wang J.-H.; Proc. Natl. Acad. Sci. U.S.A. 102:3366-3371(2005). Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 30-115 IN COMPLEX WITHINTEGRIN ALPHALBETA2, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-52 ANDASN-110.	15728350 [Abstract]
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-87; ASN-91;ASN-134; ASN-206; ASN-295 AND ASN-363, AND MASS SPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, AND MASSSPECTROMETRY.	19159218 [Abstract]
"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-206 AND ASN-363, AND MASSSPECTROMETRY.	16335952 [Abstract]