ICAM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ICAM2_HUMAN
• UniProt AC: P13598
• Protein Name: Intercellular adhesion molecule 2
• Gene Name: ICAM2
• Organism: Homo sapiens (Human).
• Sequence Length: 275
• Subcellular Localization: Membrane ; Single-pass type I membrane protein . Cell projection, microvillus . Co-localizes with RDX, EZR and MSN in microvilli.
• Protein Description: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance..
• Protein Sequence: MSSFGYRTLTVALFTLICCPGSDEKVFEVHVRPKKLAVEPKGSLEVNCSTTCNQPEVGGLETSLDKILLDEQAQWKHYLVSNISHDTVLQCHFTCSGKQESMNSNVSVYQPPRQVILTLQPTLVAVGKSFTIECRVPTVEPLDSLTLFLFRGNETLHYETFGKAAPAPQEATATFNSTADREDGHRNFSCLAVLDLMSRGGNIFHKHSAPKMLEIYEPVSDSQMVIIVTVVSVLLSLFVTSVLLCFIFGQHLRQQRMGTYGVRAAWRRLPQAFRP

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
3	Phosphorylation	-----MSSFGYRTLT -----CCCCCHHHHH	22.76	24719451
47	N-linked_Glycosylation	PKGSLEVNCSTTCNQ CCCCEEEECCCCCCC	12.49	9153399
82	N-linked_Glycosylation	WKHYLVSNISHDTVL HHHHEECCCCCCEEE	32.10	9153399
104	Phosphorylation	GKQESMNSNVSVYQP CCCHHCCCCCEEECC	29.93	26552605
105	N-linked_Glycosylation	KQESMNSNVSVYQPP CCHHCCCCCEEECCC	25.69	9153399
107	Phosphorylation	ESMNSNVSVYQPPRQ HHCCCCCEEECCCCE	21.25	26552605
109	Phosphorylation	MNSNVSVYQPPRQVI CCCCCEEECCCCEEE	14.06	26552605
153	N-linked_Glycosylation	TLFLFRGNETLHYET EEEEEECCCEEEEEE	34.52	9153399
153	N-linked_Glycosylation	TLFLFRGNETLHYET EEEEEECCCEEEEEE	34.52	9153399
163	Ubiquitination	LHYETFGKAAPAPQE EEEEEECCCCCCCCC	36.86	-
176	N-linked_Glycosylation	QEATATFNSTADRED CCCEEEECCCCCCCC	33.81	17623646
176	N-linked_Glycosylation	QEATATFNSTADRED CCCEEEECCCCCCCC	33.81	16335952
187	N-linked_Glycosylation	DREDGHRNFSCLAVL CCCCCCCCEEHHHHH	27.75	9153399
189	Phosphorylation	EDGHRNFSCLAVLDL CCCCCCEEHHHHHHH	16.27	30576142
198	Phosphorylation	LAVLDLMSRGGNIFH HHHHHHHHCCCCCCC	34.76	30576142
206	Ubiquitination	RGGNIFHKHSAPKML CCCCCCCCCCCCCEE	28.62	-
259	Phosphorylation	LRQQRMGTYGVRAAW HHHHHHCHHHHHHHH	14.04	26552605
260	Phosphorylation	RQQRMGTYGVRAAWR HHHHHCHHHHHHHHH	14.11	26552605

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ICAM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ICAM2_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 ICAM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MOES_HUMAN	MSN	physical	9472040
YIF1B_HUMAN	YIF1B	physical	26186194
LRFN1_HUMAN	LRFN1	physical	26186194
C1QRF_HUMAN	C1QL1	physical	26186194
RTN2_HUMAN	RTN2	physical	26186194
HBD_HUMAN	HBD	physical	26186194
LEG1_HUMAN	LGALS1	physical	26186194
PRAF3_HUMAN	ARL6IP5	physical	26186194
MD2L2_HUMAN	MAD2L2	physical	26186194
NRP1_HUMAN	NRP1	physical	26186194
DGLB_HUMAN	DAGLB	physical	26186194
BSCL2_HUMAN	BSCL2	physical	26186194
RAB18_HUMAN	RAB18	physical	26186194
TNFL9_HUMAN	TNFSF9	physical	26186194
PRAF3_HUMAN	ARL6IP5	physical	28514442
C1QRF_HUMAN	C1QL1	physical	28514442
RTN2_HUMAN	RTN2	physical	28514442
MD2L2_HUMAN	MAD2L2	physical	28514442
NRP1_HUMAN	NRP1	physical	28514442
YIF1B_HUMAN	YIF1B	physical	28514442
LEG1_HUMAN	LGALS1	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

N-linked Glycosylation

"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-82; ASN-105; ASN-153 ANDASN-176, AND MASS SPECTROMETRY.
PubMed: 19349973

"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-105 AND ASN-176, AND MASSSPECTROMETRY.
PubMed: 16335952