CD151_HUMAN - dbPTM
CD151_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD151_HUMAN
UniProt AC P48509
Protein Name CD151 antigen
Gene Name CD151
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Essential for the proper assembly of the glomerular and tubular basement membranes in kidney.; (Microbial infection) Plays a role in human papillomavirus 16/HPV-16 endocytosis upon binding to cell surface receptor..
Protein Sequence MGEFNEKKTTCGTVCLKYLLFTYNCCFWLAGLAVMAVGIWTLALKSDYISLLASGTYLATAYILVVAGTVVMVTGVLGCCATFKERRNLLRLYFILLLIIFLLEIIAGILAYAYYQQLNTELKENLKDTMTKRYHQPGHEAVTSAVDQLQQEFHCCGSNNSQDWRDSEWIRSQEAGGRVVPDSCCKTVVALCGQRDHASNIYKVEGGCITKLETFIQEHLRVIGAVGIGIACVQVFGMIFTCCLYRSLKLEHY
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
7Ubiquitination-MGEFNEKKTTCGTV
-CCCCCCCCCCHHHH		57.4318713730
72-Hydroxyisobutyrylation-MGEFNEKKTTCGTV
-CCCCCCCCCCHHHH		57.43-
8UbiquitinationMGEFNEKKTTCGTVC
CCCCCCCCCCHHHHH		42.778713730
11S-palmitoylationFNEKKTTCGTVCLKY
CCCCCCCHHHHHHHH		5.3511907260
15S-palmitoylationKTTCGTVCLKYLLFT
CCCHHHHHHHHHHHH		2.4511907260
17UbiquitinationTCGTVCLKYLLFTYN
CHHHHHHHHHHHHHH		28.821871373
48PhosphorylationTLALKSDYISLLASG
HHHHCCCHHHHHHHC		10.25-
79S-palmitoylationMVTGVLGCCATFKER
HHCCCHHHHHCHHHH		0.9412110679
80S-palmitoylationVTGVLGCCATFKERR
HCCCHHHHHCHHHHH		3.6612110679
132UbiquitinationNLKDTMTKRYHQPGH
HHHHHHHHHCCCCCH		39.89-
159N-linked_GlycosylationEFHCCGSNNSQDWRD
HHCCCCCCCCCCCCC		37.14UniProtKB CARBOHYD
167PhosphorylationNSQDWRDSEWIRSQE
CCCCCCCCHHHHCHH		26.6823927012
184S-palmitoylationGRVVPDSCCKTVVAL
CCCCCHHHHHHHHHH		3.4429575903
185S-palmitoylationRVVPDSCCKTVVALC
CCCCHHHHHHHHHHH		4.8529575903
186UbiquitinationVVPDSCCKTVVALCG
CCCHHHHHHHHHHHC		48.99-
187O-linked_GlycosylationVPDSCCKTVVALCGQ
CCHHHHHHHHHHHCC		13.29OGP
192S-palmitoylationCKTVVALCGQRDHAS
HHHHHHHHCCCCCCC		2.9229575903
199PhosphorylationCGQRDHASNIYKVEG
HCCCCCCCCEEEEEC		21.9721406692
202PhosphorylationRDHASNIYKVEGGCI
CCCCCCEEEEECCHH		17.1521406692
2032-HydroxyisobutyrylationDHASNIYKVEGGCIT
CCCCCEEEEECCHHH		29.97-
203UbiquitinationDHASNIYKVEGGCIT
CCCCCEEEEECCHHH		29.97-
211UbiquitinationVEGGCITKLETFIQE
EECCHHHHHHHHHHH		25.14-
242S-palmitoylationVFGMIFTCCLYRSLK
HHHHHHHHHHHHHHC		0.7511907260
243S-palmitoylationFGMIFTCCLYRSLKL
HHHHHHHHHHHHHCC		3.2111907260
249UbiquitinationCCLYRSLKLEHY---
HHHHHHHCCCCC---		53.7421890473
253PhosphorylationRSLKLEHY-------
HHHCCCCC-------		15.7527642862
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 CD151_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD151_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 CD151_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCP_HUMANCD46physical
10741407
ITA3_HUMANITGA3physical
10734060
FPRP_HUMANPTGFRNphysical
11278880
ITB1_HUMANITGB1physical
12175627
GRM1C_HUMANGRAMD1Cphysical
25416956
Drug and Disease Associations
Kegg Disease
H00928 Nephropathy with pretibial epidermolysis bullosa and deafness
OMIM Disease
609057Nephropathy with pretibial epidermolysis bullosa and deafness (NPEBD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD151_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Palmitoylation of tetraspanin proteins: modulation of CD151 lateralinteractions, subcellular distribution, and integrin-dependent cellmorphology.";
Yang X., Claas C., Kraeft S.K., Chen L.B., Wang Z., Kreidberg J.A.,Hemler M.E.;
Mol. Biol. Cell 13:767-781(2002).
Cited for: PALMITOYLATION AT CYS-11; CYS-15; CYS-242 AND CYS-243.

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