| UniProt ID | ICAM1_HUMAN | |
|---|---|---|
| UniProt AC | P05362 | |
| Protein Name | Intercellular adhesion molecule 1 | |
| Gene Name | ICAM1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 532 | |
| 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). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation.; (Microbial infection) Acts as a receptor for major receptor group rhinovirus A-B capsid proteins.; (Microbial infection) Acts as a receptor for Coxsackievirus A21 capsid proteins.; (Microbial infection) Upon Kaposi's sarcoma-associated herpesvirus/HHV-8 infection, is degraded by viral E3 ubiquitin ligase MIR2, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes and NK cell.. | |
| Protein Sequence | MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 30 | Phosphorylation | GPGNAQTSVSPSKVI CCCCCCCCCCCCEEE | 14.44 | 30301811 | |
| 32 | Phosphorylation | GNAQTSVSPSKVILP CCCCCCCCCCEEEEC | 24.19 | 30301811 | |
| 43 | Phosphorylation | VILPRGGSVLVTCST EEECCCCEEEEEEEC | 18.33 | 30576142 | |
| 47 | O-linked_Glycosylation | RGGSVLVTCSTSCDQ CCCEEEEEEECCCCC | 9.14 | OGP | |
| 49 | Phosphorylation | GSVLVTCSTSCDQPK CEEEEEEECCCCCCC | 17.62 | 30576142 | |
| 51 | Phosphorylation | VLVTCSTSCDQPKLL EEEEEECCCCCCCCC | 10.21 | 30576142 | |
| 56 | Acetylation | STSCDQPKLLGIETP ECCCCCCCCCCCCCC | 51.19 | 26051181 | |
| 62 | Phosphorylation | PKLLGIETPLPKKEL CCCCCCCCCCCCCCE | 28.36 | - | |
| 62 | O-linked_Glycosylation | PKLLGIETPLPKKEL CCCCCCCCCCCCCCE | 28.36 | 55830671 | |
| 67 | 2-Hydroxyisobutyrylation | IETPLPKKELLLPGN CCCCCCCCCEECCCC | 52.21 | - | |
| 101 | O-linked_Glycosylation | SNCPDGQSTAKTFLT CCCCCCCCCCCEEEE | 35.54 | OGP | |
| 130 | N-linked_Glycosylation | SWQPVGKNLTLRCQV CCCCCCCCEEEEEEE | 32.12 | 9539702 | |
| 132 | Phosphorylation | QPVGKNLTLRCQVEG CCCCCCEEEEEEEEC | 22.88 | 24719451 | |
| 145 | N-linked_Glycosylation | EGGAPRANLTVVLLR ECCCCCCCEEEEEEE | 37.21 | 12526797 | |
| 145 | N-linked_Glycosylation | EGGAPRANLTVVLLR ECCCCCCCEEEEEEE | 37.21 | 12526797 | |
| 183 | N-linked_Glycosylation | RRDHHGANFSCRTEL ECCCCCCCCEEEEEC | 33.68 | 9539702 | |
| 202 | N-linked_Glycosylation | QGLELFENTSAPYQL CCEEECCCCCCCEEE | 31.81 | 12526797 | |
| 202 | N-linked_Glycosylation | QGLELFENTSAPYQL CCEEECCCCCCCEEE | 31.81 | 12526797 | |
| 207 | Phosphorylation | FENTSAPYQLQTFVL CCCCCCCEEEEEEEE | 22.90 | - | |
| 211 | Phosphorylation | SAPYQLQTFVLPATP CCCEEEEEEEECCCC | 25.05 | - | |
| 217 | Phosphorylation | QTFVLPATPPQLVSP EEEEECCCCCCCCCC | 33.30 | - | |
| 217 | O-linked_Glycosylation | QTFVLPATPPQLVSP EEEEECCCCCCCCCC | 33.30 | OGP | |
| 223 | Phosphorylation | ATPPQLVSPRVLEVD CCCCCCCCCCEEEEC | 18.64 | - | |
| 260 | N-linked_Glycosylation | ALGDQRLNPTVTYGN ECCCCCCCCEEEECC | 32.17 | 19159218 | |
| 267 | N-linked_Glycosylation | NPTVTYGNDSFSAKA CCEEEECCCCCEEEE | 31.19 | 15099525 | |
| 267 | N-linked_Glycosylation | NPTVTYGNDSFSAKA CCEEEECCCCCEEEE | 31.19 | 15099525 | |
| 275 | Phosphorylation | DSFSAKASVSVTAED CCCEEEEEEEEEECC | 17.76 | - | |
| 296 | N-linked_Glycosylation | TCAVILGNQSQETLQ EEEEEECCCCCCEEE | 34.58 | 15099525 | |
| 323 | Phosphorylation | ILTKPEVSEGTEVTV EEECCCCCCCCEEEE | 28.75 | 20068231 | |
| 326 | Phosphorylation | KPEVSEGTEVTVKCE CCCCCCCCEEEEEEE | 24.19 | 20068231 | |
| 329 | Phosphorylation | VSEGTEVTVKCEAHP CCCCCEEEEEEEECC | 14.17 | 20068231 | |
| 359 | Ubiquitination | PRAQLLLKATPEDNG HHHEEEEECCCCCCC | 50.62 | 21906983 | |
| 385 | N-linked_Glycosylation | AGQLIHKNQTRELRV HHHEECCCCCCEEEE | 34.00 | 15099525 | |
| 406 | N-linked_Glycosylation | DERDCPGNWTWPENS CCCCCCCCCCCCCCC | 20.39 | UniProtKB CARBOHYD | |
| 467 | Phosphorylation | RSTQGEVTRKVTVNV ECCCCCEEEEEEEEE | 22.07 | 22210691 | |
| 471 | Phosphorylation | GEVTRKVTVNVLSPR CCEEEEEEEEECCCC | 14.92 | 22210691 | |
| 495 | Phosphorylation | AAAVIMGTAGLSTYL HHHHHHCCCCHHHHH | 10.52 | 22210691 | |
| 501 | Phosphorylation | GTAGLSTYLYNRQRK CCCCHHHHHHHHHHH | 12.10 | 22817900 | |
| 512 | Phosphorylation | RQRKIKKYRLQQAQK HHHHHHHHHHHHHHC | 16.14 | 28152594 | |
| 519 | Ubiquitination | YRLQQAQKGTPMKPN HHHHHHHCCCCCCCC | 68.70 | - | |
| 521 | Phosphorylation | LQQAQKGTPMKPNTQ HHHHHCCCCCCCCCC | 27.52 | 25159151 | |
| 524 | Ubiquitination | AQKGTPMKPNTQATP HHCCCCCCCCCCCCC | 36.00 | 21906983 | |
| 527 | Phosphorylation | GTPMKPNTQATPP-- CCCCCCCCCCCCC-- | 28.27 | 29255136 | |
| 530 | Phosphorylation | MKPNTQATPP----- CCCCCCCCCC----- | 26.69 | 29255136 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| - | K | Ubiquitination | E3 ubiquitin ligase | MARCHF9 | Q86YJ5 | PMID:17174307 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXO4 | Q9UKT5 | PMID:29137327 |
| - | K | Ubiquitination | E3 ubiquitin ligase | K5 | P90489 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ICAM1_HUMAN !! | ||||||
* 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 ICAM1_HUMAN !! | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Structural basis for dimerization of ICAM-1 on the cell surface."; Yang Y., Jun C.D., Liu J.H., Zhang R., Joachimiak A., Springer T.A.,Wang J.H.; Mol. Cell 14:269-276(2004). Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDEBONDS, AND GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385. | |
| "Structures of the alpha L I domain and its complex with ICAM-1 reveala shape-shifting pathway for integrin regulation."; Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D.,McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H.,Springer T.A.; Cell 112:99-111(2003). Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 28-318 IN COMPLEX WITH ITGALVWFA DOMAIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-130; ASN-145;ASN-183 AND ASN-202. | |
| "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-145 AND ASN-267, AND MASSSPECTROMETRY. | |
| "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-202; ASN-260 AND ASN-267,AND MASS SPECTROMETRY. | |
| "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-267, AND MASSSPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, ANDMASS SPECTROMETRY. | |
