CXAR_HUMAN - dbPTM
CXAR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CXAR_HUMAN
UniProt AC P78310
Protein Name Coxsackievirus and adenovirus receptor
Gene Name CXADR
Organism Homo sapiens (Human).
Sequence Length 365
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein . Basolateral cell membrane
Single-pass type I membrane protein . Cell junction, tight junction . Cell junction, adherens junction . In epithelial cells localizes to the apical junction
Protein Description Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair.; (Microbial infection) Acts as a receptor for adenovirus type C.; (Microbial infection) Acts as a receptor for Coxsackievirus B1 to B6..
Protein Sequence MALLLCFVLLCGVVDFARSLSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQVIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQCKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSLPLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVGSDQCLLRLNVVPPSNKAGLIAGAIIGTLLALALIGLIIFCCRKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERTPQSPTLPPAKVAAPNLSRMGAIPVMIPAQSKDGSIV
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
88UbiquitinationDDYYPDLKGRVHFTS
CCCCCCCCCCEEEEC		52.6429967540
88AcetylationDDYYPDLKGRVHFTS
CCCCCCCCCCEEEEC		52.6420167786
94PhosphorylationLKGRVHFTSNDLKSG
CCCCEEEECCCCCCC		16.2521082442
99AcetylationHFTSNDLKSGDASIN
EEECCCCCCCCCEEE		56.0820167786
100PhosphorylationFTSNDLKSGDASINV
EECCCCCCCCCEEEE		49.56-
106N-linked_GlycosylationKSGDASINVTNLQLS
CCCCCEEEEEEEEHH		31.87UniProtKB CARBOHYD
108PhosphorylationGDASINVTNLQLSDI
CCCEEEEEEEEHHHC		26.2321082442
121AcetylationDIGTYQCKVKKAPGV
HCEEEEEEEEECCCC		41.3820167786
151PhosphorylationARCYVDGSEEIGSDF
CEEEECCCCCCCCCC		27.8224173317
177UbiquitinationPLQYEWQKLSDSQKM
CCEEEEEECCCCCCC		51.5429967540
178 (in isoform 4)Phosphorylation-4.0524719451
182 (in isoform 4)Phosphorylation-51.5724719451
201N-linked_GlycosylationSSVISVKNASSEYSG
HCEEEEECCCCCCCE		42.79UniProtKB CARBOHYD
203PhosphorylationVISVKNASSEYSGTY
EEEEECCCCCCCEEE		32.8525907765
204PhosphorylationISVKNASSEYSGTYS
EEEECCCCCCCEEEE		37.8425907765
206PhosphorylationVKNASSEYSGTYSCT
EECCCCCCCEEEEEE		17.8525907765
207PhosphorylationKNASSEYSGTYSCTV
ECCCCCCCEEEEEEE		22.1725907765
209PhosphorylationASSEYSGTYSCTVRN
CCCCCCEEEEEEEEC		13.3025907765
210PhosphorylationSSEYSGTYSCTVRNR
CCCCCEEEEEEEECC		12.7925907765
211PhosphorylationSEYSGTYSCTVRNRV
CCCCEEEEEEEECCC		11.8025907765
213PhosphorylationYSGTYSCTVRNRVGS
CCEEEEEEEECCCCC		19.2925907765
230 (in isoform 5)Phosphorylation-5.8524719451
233PhosphorylationRLNVVPPSNKAGLIA
EEEECCCCCCHHHHH		44.9121406692
234 (in isoform 5)Phosphorylation-43.9324719451
259S-palmitoylationLIGLIIFCCRKKRRE
HHHHHHHHHHHHHHH		1.2212021372
260S-palmitoylationIGLIIFCCRKKRREE
HHHHHHHHHHHHHHH		5.0712021372
268UbiquitinationRKKRREEKYEKEVHH
HHHHHHHHHHHHHCC		54.6923000965
271UbiquitinationRREEKYEKEVHHDIR
HHHHHHHHHHCCHHH		63.0423000965
274UbiquitinationEKYEKEVHHDIREDV
HHHHHHHCCHHHHCC		17.6221906983
285UbiquitinationREDVPPPKSRTSTAR
HHCCCCCCCCCCHHH		59.3429967540
286PhosphorylationEDVPPPKSRTSTARS
HCCCCCCCCCCHHHH		46.7126074081
288PhosphorylationVPPPKSRTSTARSYI
CCCCCCCCCHHHHHC		37.2029449344
289PhosphorylationPPPKSRTSTARSYIG
CCCCCCCCHHHHHCC		20.9630576142
290PhosphorylationPPKSRTSTARSYIGS
CCCCCCCHHHHHCCC		26.0229449344
293PhosphorylationSRTSTARSYIGSNHS
CCCCHHHHHCCCCCC		20.7321945579
294PhosphorylationRTSTARSYIGSNHSS
CCCHHHHHCCCCCCC		12.0721945579
297PhosphorylationTARSYIGSNHSSLGS
HHHHHCCCCCCCCCC		23.0821945579
300PhosphorylationSYIGSNHSSLGSMSP
HHCCCCCCCCCCCCC		31.3521945579
301PhosphorylationYIGSNHSSLGSMSPS
HCCCCCCCCCCCCCC		29.2421945579
304PhosphorylationSNHSSLGSMSPSNME
CCCCCCCCCCCCCCC		22.7521945579
306PhosphorylationHSSLGSMSPSNMEGY
CCCCCCCCCCCCCCC		27.2021945579
308PhosphorylationSLGSMSPSNMEGYSK
CCCCCCCCCCCCCCC		41.3121945579
313PhosphorylationSPSNMEGYSKTQYNQ
CCCCCCCCCCCCCCC		8.1621945579
314PhosphorylationPSNMEGYSKTQYNQV
CCCCCCCCCCCCCCC		39.8321945579
315 (in isoform 2)Ubiquitination-31.0321906983
315 (in isoform 1)Ubiquitination-31.0321906983
315UbiquitinationSNMEGYSKTQYNQVP
CCCCCCCCCCCCCCC		31.0322817900
316PhosphorylationNMEGYSKTQYNQVPS
CCCCCCCCCCCCCCH		30.2824732914
318PhosphorylationEGYSKTQYNQVPSED
CCCCCCCCCCCCHHH		16.8825159151
319UbiquitinationGYSKTQYNQVPSEDF
CCCCCCCCCCCHHHH		26.9321906983
323PhosphorylationTQYNQVPSEDFERTP
CCCCCCCHHHHCCCC		51.4419664994
329PhosphorylationPSEDFERTPQSPTLP
CHHHHCCCCCCCCCC		20.6230266825
332PhosphorylationDFERTPQSPTLPPAK
HHCCCCCCCCCCHHH		22.5119664994
334PhosphorylationERTPQSPTLPPAKVA
CCCCCCCCCCHHHHC		58.0830266825
339UbiquitinationSPTLPPAKVAAPNLS
CCCCCHHHHCCCCCC		37.8729967540
339AcetylationSPTLPPAKVAAPNLS
CCCCCHHHHCCCCCC		37.877675287
345UbiquitinationAKVAAPNLSRMGAIP
HHHCCCCCCCCCCCC		3.1529967540
346PhosphorylationKVAAPNLSRMGAIPV
HHCCCCCCCCCCCCE		27.1928355574
350 (in isoform 6)Phosphorylation-8.1230631047
359PhosphorylationPVMIPAQSKDGSIV-
CEEEECCCCCCCCC-		34.5229514088
360UbiquitinationVMIPAQSKDGSIV--
EEEECCCCCCCCC--		54.7729967540
360 (in isoform 1)Ubiquitination-54.7721906983
363PhosphorylationPAQSKDGSIV-----
ECCCCCCCCC-----		30.2528258704
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 CXAR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
259CPalmitoylation

12021372
260CPalmitoylation

12021372
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 CXAR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EWS_HUMANEWSR1physical
16189514
GRHPR_HUMANGRHPRphysical
22939629
NCOA1_HUMANNCOA1physical
15572376
NCOR1_HUMANNCOR1physical
15572376
JAML_HUMANAMICA1physical
21982860
CXAR_HUMANCXADRphysical
21982860
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 CXAR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASSSPECTROMETRY.
"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 SER-306 AND SER-332, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASSSPECTROMETRY.

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