CD166_HUMAN - dbPTM
CD166_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD166_HUMAN
UniProt AC Q13740
Protein Name CD166 antigen
Gene Name ALCAM
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, axon . Cell projection, dendrite . Detected at the immunological synapse, i.e, at the contact zone between antigen-presenting dendritic cells and T-cells (PubMed:15294938, PubMed:
Protein Description Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. [PubMed: 7760007]
Protein Sequence MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA
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 Orthologous
Protein Cluster
11 (in isoform 4)Phosphorylation-5.1529116813
12 (in isoform 4)Phosphorylation-1.1529116813
52SulfoxidationLDVPQNLMFGKWKYE
CCCCCCCEECEEEEE		5.6621406390
64PhosphorylationKYEKPDGSPVFIAFR
EEECCCCCEEEEEEE		25.85110750185
80PhosphorylationSTKKSVQYDDVPEYK
CCCCCCCCCCCCCHH		16.3822817900
86PhosphorylationQYDDVPEYKDRLNLS
CCCCCCCHHHHCCCC		16.4822817900
87UbiquitinationYDDVPEYKDRLNLSE
CCCCCCHHHHCCCCC		34.4121906983
87 (in isoform 2)Ubiquitination-34.4121906983
87 (in isoform 1)Ubiquitination-34.4121906983
872-HydroxyisobutyrylationYDDVPEYKDRLNLSE
CCCCCCHHHHCCCCC		34.41-
87UbiquitinationYDDVPEYKDRLNLSE
CCCCCCHHHHCCCCC		34.4121906983
91N-linked_GlycosylationPEYKDRLNLSENYTL
CCHHHHCCCCCCEEE		42.2712754519
95N-linked_GlycosylationDRLNLSENYTLSISN
HHCCCCCCEEEEEEC		31.5412754519
95N-linked_GlycosylationDRLNLSENYTLSISN
HHCCCCCCEEEEEEC		31.5412754519
117PhosphorylationRFVCMLVTEDNVFEA
CEEEEEECCCCEECC		33.3920639409
126PhosphorylationDNVFEAPTIVKVFKQ
CCEECCCCEEECCCC		45.5120639409
1522-HydroxyisobutyrylationFLETEQLKKLGDCIS
HHCHHHHHHHHCCCC		45.72-
167N-linked_GlycosylationEDSYPDGNITWYRNG
CCCCCCCCEEEEECC		35.5812754519
167N-linked_GlycosylationEDSYPDGNITWYRNG
CCCCCCCCEEEEECC		35.5812754519
196PhosphorylationKKEMDPVTQLYTMTS
ECCCCCCCEEEEEEE		20.4624905233
199PhosphorylationMDPVTQLYTMTSTLE
CCCCCEEEEEEEEEE		5.6624905233
200PhosphorylationDPVTQLYTMTSTLEY
CCCCEEEEEEEEEEE		23.6724905233
202PhosphorylationVTQLYTMTSTLEYKT
CCEEEEEEEEEEEEE		15.6824905233
203PhosphorylationTQLYTMTSTLEYKTT
CEEEEEEEEEEEEEC		21.8524905233
204PhosphorylationQLYTMTSTLEYKTTK
EEEEEEEEEEEEECC		17.9124905233
207PhosphorylationTMTSTLEYKTTKADI
EEEEEEEEEECCCCE		19.4229116813
209PhosphorylationTSTLEYKTTKADIQM
EEEEEEEECCCCEEC		32.4024905233
210PhosphorylationSTLEYKTTKADIQMP
EEEEEEECCCCEECC		21.7824905233
265N-linked_GlycosylationNAIKEGDNITLKCLG
CCCCCCCCEEEEECC		39.75UniProtKB CARBOHYD
265N-linked_GlycosylationNAIKEGDNITLKCLG
CCCCCCCCEEEEECC		39.7516335952
298PhosphorylationGIRSSNTYTLTDVRR
CCCCCCEEEEECCHH		12.19110750197
306N-linked_GlycosylationTLTDVRRNATGDYKC
EEECCHHHCCCCCEE		31.15UniProtKB CARBOHYD
308PhosphorylationTDVRRNATGDYKCSL
ECCHHHCCCCCEEEE		33.8526699800
311PhosphorylationRRNATGDYKCSLIDK
HHHCCCCCEEEECCC		18.4226699800
314PhosphorylationATGDYKCSLIDKKSM
CCCCCEEEECCCCHH		24.9826699800
343O-linked_GlycosylationLNPSGEVTRQIGDAL
CCCCCCHHEECCCEE		16.74OGP
361N-linked_GlycosylationCTISASRNATVVWMK
EEEEECCCCEEEEEE		37.1519349973
361N-linked_GlycosylationCTISASRNATVVWMK
EEEEECCCCEEEEEE		37.1519349973
375PhosphorylationKDNIRLRSSPSFSSL
ECCEEECCCCCCCCC		51.7128348404
376PhosphorylationDNIRLRSSPSFSSLH
CCEEECCCCCCCCCE		20.3728348404
378PhosphorylationIRLRSSPSFSSLHYQ
EEECCCCCCCCCEEE		39.4428348404
380PhosphorylationLRSSPSFSSLHYQDA
ECCCCCCCCCEEECC		36.0128348404
381PhosphorylationRSSPSFSSLHYQDAG
CCCCCCCCCEEECCC		19.7028348404
407PhosphorylationEGLKKRESLTLIVEG
CCCCCCCCEEEEEEC		30.5926091039
409PhosphorylationLKKRESLTLIVEGKP
CCCCCCEEEEEECCC		24.5826091039
457N-linked_GlycosylationTGSGSVINQTEESPY
ECCCCCCCCCCCCCC		40.3319349973
457N-linked_GlycosylationTGSGSVINQTEESPY
ECCCCCCCCCCCCCC		40.3319159218
466N-linked_GlycosylationTEESPYINGRYYSKI
CCCCCCCCCEEEEEE		24.0519349973
466N-linked_GlycosylationTEESPYINGRYYSKI
CCCCCCCCCEEEEEE		24.0519349973
480N-linked_GlycosylationIIISPEENVTLTCTA
EEECCCCCEEEEEEC		30.3412754519
480N-linked_GlycosylationIIISPEENVTLTCTA
EEECCCCCEEEEEEC		30.3412754519
496N-linked_GlycosylationNQLERTVNSLNVSAI
HHHHHHHHEECEEEE		39.9219349973
496N-linked_GlycosylationNQLERTVNSLNVSAI
HHHHHHHHEECEEEE		39.9219349973
499N-linked_GlycosylationERTVNSLNVSAISIP
HHHHHEECEEEEECC		26.0612754519
499N-linked_GlycosylationERTVNSLNVSAISIP
HHHHHEECEEEEECC		26.0612754519
501 (in isoform 2)Phosphorylation-20.8622617229
518N-linked_GlycosylationADEISDENREKVNDQ
HHCCCHHHHHHHHHH		63.5019349973
518N-linked_GlycosylationADEISDENREKVNDQ
HHCCCHHHHHHHHHH		63.5019349973
550 (in isoform 2)Ubiquitination-7.85-
559 (in isoform 2)Ubiquitination-49.4621906983
559AcetylationKKSKTASKHVNKDLG
CCCHHHHHHHCHHCC		49.4619666643
560 (in isoform 2)Ubiquitination-26.3621906983
563UbiquitinationTASKHVNKDLGNMEE
HHHHHHCHHCCCHHH		53.92-
563AcetylationTASKHVNKDLGNMEE
HHHHHHCHHCCCHHH		53.9219666651
567 (in isoform 2)Ubiquitination-41.8321906983
572 (in isoform 1)Ubiquitination-63.1121906983
572UbiquitinationLGNMEENKKLEENNH
CCCHHHHHHHHHCCC		63.1121906983
573 (in isoform 1)Ubiquitination-73.1121906983
573UbiquitinationGNMEENKKLEENNHK
CCHHHHHHHHHCCCC		73.112190698
580 (in isoform 1)Ubiquitination-50.6221906983
580UbiquitinationKLEENNHKTEA----
HHHHCCCCCCC----		50.6221906983
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
-KUbiquitinationE3 ubiquitin ligaseK5P90489
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD166_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

Oops, there are no SNP-PTM records of CD166_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD6_HUMANCD6physical
7543097
NAR3_HUMANART3physical
21988832
LEG1_HUMANLGALS1physical
28514442
FBX2_HUMANFBXO2physical
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 CD166_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-457 AND ASN-466, 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-91; ASN-95; ASN-457 ANDASN-480, 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-95; ASN-265 AND ASN-499,AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-91; ASN-167; ASN-480 AND ASN-499.

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