dbPTM

ICAM5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ICAM5_HUMAN
UniProt AC	Q9UMF0
Protein Name	Intercellular adhesion molecule 5
Gene Name	ICAM5
Organism	Homo sapiens (Human).
Sequence Length	924
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)..
Protein Sequence	MPGPSPGLRRALLGLWAALGLGLFGLSAVSQEPFWADLQPRVAFVERGGSLWLNCSTNCPRPERGGLETSLRRNGTQRGLRWLARQLVDIREPETQPVCFFRCARRTLQARGLIRTFQRPDRVELMPLPPWQPVGENFTLSCRVPGAGPRASLTLTLLRGAQELIRRSFAGEPPRARGAVLTATVLARREDHGANFSCRAELDLRPHGLGLFENSSAPRELRTFSLSPDAPRLAAPRLLEVGSERPVSCTLDGLFPASEARVYLALGDQNLSPDVTLEGDAFVATATATASAEQEGARQLVCNVTLGGENRETRENVTIYSFPAPLLTLSEPSVSEGQMVTVTCAAGAQALVTLEGVPAAVPGQPAQLQLNATENDDRRSFFCDATLDVDGETLIKNRSAELRVLYAPRLDDSDCPRSWTWPEGPEQTLRCEARGNPEPSVHCARSDGGAVLALGLLGPVTRALSGTYRCKAANDQGEAVKDVTLTVEYAPALDSVGCPERITWLEGTEASLSCVAHGVPPPDVICVRSGELGAVIEGLLRVAREHAGTYRCEATNPRGSAAKNVAVTVEYGPRFEEPSCPSNWTWVEGSGRLFSCEVDGKPQPSVKCVGSGGATEGVLLPLAPPDPSPRAPRIPRVLAPGIYVCNATNRHGSVAKTVVVSAESPPEMDESTCPSHQTWLEGAEASALACAARGRPSPGVRCSREGIPWPEQQRVSREDAGTYHCVATNAHGTDSRTVTVGVEYRPVVAELAASPPGGVRPGGNFTLTCRAEAWPPAQISWRAPPGALNIGLSSNNSTLSVAGAMGSHGGEYECAATNAHGRHARRITVRVAGPWLWVAVGGAAGGAALLAAGAGLAFYVQSTACKKGEYNVQEAESSGEAVCLNGAGGGAGGAAGAEGGPEAAGGAAESPAEGEVFAIQLTSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	N-linked_Glycosylation	RGGSLWLNCSTNCPR CCCEEEEECCCCCCC	13.20	18691975
69	Phosphorylation	PERGGLETSLRRNGT CCCCCCCHHHHHCCC	37.80	26270265
70	Phosphorylation	ERGGLETSLRRNGTQ CCCCCCHHHHHCCCH	15.54	26270265
74	N-linked_Glycosylation	LETSLRRNGTQRGLR CCHHHHHCCCHHHHH	51.97	18691975
107	O-linked_Glycosylation	FFRCARRTLQARGLI HHHCHHHHHHHHCHH	20.05	30620550
137	N-linked_Glycosylation	PWQPVGENFTLSCRV CCCCCCCCEEEEEEC	29.31	18691975
139	Phosphorylation	QPVGENFTLSCRVPG CCCCCCEEEEEECCC	29.37	29083192
141	Phosphorylation	VGENFTLSCRVPGAG CCCCEEEEEECCCCC	9.23	29083192
152	Phosphorylation	PGAGPRASLTLTLLR CCCCCCHHHHHHHHH	24.14	22985185
156	Phosphorylation	PRASLTLTLLRGAQE CCHHHHHHHHHHHHH	20.64	22985185
182	Phosphorylation	RARGAVLTATVLARR CHHCEEEEEEEEECC	17.43	14729942
184	Phosphorylation	RGAVLTATVLARRED HCEEEEEEEEECCCC	15.71	14729942
195	N-linked_Glycosylation	RREDHGANFSCRAEL CCCCCCCCCEEEEEE	33.68	18691975
214	N-linked_Glycosylation	HGLGLFENSSAPREL CCCCCCCCCCCCCCC	33.65	18691975
303	N-linked_Glycosylation	GARQLVCNVTLGGEN CCEEEEEEEEECCCC	23.48	UniProtKB CARBOHYD
316	N-linked_Glycosylation	ENRETRENVTIYSFP CCCCCCCCEEEEEEC	32.70	UniProtKB CARBOHYD
371	N-linked_Glycosylation	QPAQLQLNATENDDR CCEEEEEECCCCCCC	31.68	UniProtKB CARBOHYD
397	N-linked_Glycosylation	DGETLIKNRSAELRV CCCEEEECCCEEEEE	35.82	UniProtKB CARBOHYD
418	Phosphorylation	DDSDCPRSWTWPEGP CCCCCCCCCCCCCCC	17.63	-
446	Phosphorylation	PSVHCARSDGGAVLA CCCEEEECCCCEEEE	23.29	24732914
465	Phosphorylation	GPVTRALSGTYRCKA HHHHHHHCCCEEEEE	28.27	22115753
467	Phosphorylation	VTRALSGTYRCKAAN HHHHHCCCEEEEECC	12.38	22115753
583	N-linked_Glycosylation	EEPSCPSNWTWVEGS CCCCCCCCCEEEECC	25.91	UniProtKB CARBOHYD
646	N-linked_Glycosylation	APGIYVCNATNRHGS CCCEEEEECCCCCCC	39.49	UniProtKB CARBOHYD
737	Phosphorylation	AHGTDSRTVTVGVEY CCCCCCEEEEEEEEE	25.20	27794612
739	Phosphorylation	GTDSRTVTVGVEYRP CCCCEEEEEEEEECC	15.78	27794612
764	N-linked_Glycosylation	GGVRPGGNFTLTCRA CCCCCCCCEEEEEEE	32.42	UniProtKB CARBOHYD
780	Phosphorylation	AWPPAQISWRAPPGA ECCCCEEEEECCCCC	9.83	24719451
795	N-linked_Glycosylation	LNIGLSSNNSTLSVA EEEECCCCCCCEEEE	42.99	UniProtKB CARBOHYD
796	N-linked_Glycosylation	NIGLSSNNSTLSVAG EEECCCCCCCEEEEE	38.02	UniProtKB CARBOHYD
828	Phosphorylation	GRHARRITVRVAGPW CCCCEEEEEEEECCE	10.64	-

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
Oops, there are no upstream regulatory protein records of ICAM5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
54	N	Glycosylation		18691975
Glycosylation at Asn-54 is critical for functional folding.

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 ICAM5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ICAM5_HUMAN !!

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 ICAM5_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"An unusual allosteric mobility of the C-terminal helix of a high-affinity alphaL integrin I domain variant bound to ICAM-5."; Zhang H., Casasnovas J.M., Jin M., Liu J.H., Gahmberg C.G.,Springer T.A., Wang J.H.; Mol. Cell 31:432-437(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-227 IN COMPLEX WITH ITGAL,GLYCOSYLATION AT ASN-54; ASN-74; ASN-137; ASN-195 AND ASN-214, ANDDISULFIDE BONDS.	18691975 [Abstract]
Phosphorylation
Reference	PubMed
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND THR-184, ANDMASS SPECTROMETRY.	15144186 [Abstract]

show