CD52_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CD52_HUMAN
• UniProt AC: P31358
• Protein Name: CAMPATH-1 antigen
• Gene Name: CD52
• Organism: Homo sapiens (Human).
• Sequence Length: 61
• Subcellular Localization: Cell membrane; Lipid-anchor, GPI-anchor.
• Protein Description: May play a role in carrying and orienting carbohydrate, as well as having a more specific role..
• Protein Sequence: MKRFLFLLLTISLLVMVQIQTGLSGQNDTSQTSSPSASSNISGGIFLFFVANAIIHLFCFS

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
27	N-linked_Glycosylation	QTGLSGQNDTSQTSS HHCCCCCCCCCCCCC	59.04	UniProtKB CARBOHYD
27	N-linked_Glycosylation	QTGLSGQNDTSQTSS HHCCCCCCCCCCCCC	59.04	7890742
36	GPI-anchor	TSQTSSPSASSNISG CCCCCCCCCCCCCCH	42.61	7688956
40	N-linked_Glycosylation	SSPSASSNISGGIFL CCCCCCCCCCHHHHH	29.92	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of CD52_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CD52_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 CD52_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CD52_HUMAN !!

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
• D02802: Alemtuzumab (genetical recombination) (JAN); Alemtuzumab (USAN/INN); Campath (TN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

GPI-anchor

"Structure of the CAMPATH-1 antigen, a glycosylphosphatidylinositol-anchored glycoprotein which is an exceptionally good target forcomplement lysis.";
Xia M.Q., Hale G., Lifely M.R., Ferguson M.A., Campbell D.,Packman L., Waldmann H.;
Biochem. J. 293:633-640(1993).
Cited for: GPI-ANCHOR AT SER-36.
PubMed: 7688956