CD38_HUMAN - dbPTM
CD38_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD38_HUMAN
UniProt AC P28907
Protein Name ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Gene Name CD38
Organism Homo sapiens (Human).
Sequence Length 300
Subcellular Localization Membrane
Single-pass type II membrane protein.
Protein Description Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system..
Protein Sequence MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI
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
13UbiquitinationFSPVSGDKPCCRLSR
ECCCCCCCCCHHHHH
43.40-
51PhosphorylationPRWRQQWSGPGTTKR
HHHHHHCCCCCCCCC
30.6728842319
100N-linked_GlycosylationFISKHPCNITEEDYQ
HHCCCCCCCCHHHCH
48.9819159218
158PhosphorylationGYLADDLTWCGEFNT
HHHHCCCCEECCCCC
26.2130576142
164N-linked_GlycosylationLTWCGEFNTSKINYQ
CCEECCCCCCCCCCC
38.86UniProtKB CARBOHYD
166PhosphorylationWCGEFNTSKINYQSC
EECCCCCCCCCCCCC
32.4230576142
181PhosphorylationPDWRKDCSNNPVSVF
CCHHHHCCCCCCHHH
50.1827732954
186PhosphorylationDCSNNPVSVFWKTVS
HCCCCCCHHHHHHHH
16.9227732954
209N-linked_GlycosylationDVVHVMLNGSRSKIF
CEEEEECCCCCCCCC
28.4419159218
219N-linked_GlycosylationRSKIFDKNSTFGSVE
CCCCCCCCCCCCCEE
48.3919159218
219N-linked_GlycosylationRSKIFDKNSTFGSVE
CCCCCCCCCCCCCEE
48.3919349973
220O-linked_GlycosylationSKIFDKNSTFGSVEV
CCCCCCCCCCCCEEE
30.74OGP
221O-linked_GlycosylationKIFDKNSTFGSVEVH
CCCCCCCCCCCEEEE
41.21OGP
229N-linked_GlycosylationFGSVEVHNLQPEKVQ
CCCEEEECCCHHHEE
45.6119349973
229N-linked_GlycosylationFGSVEVHNLQPEKVQ
CCCEEEECCCHHHEE
45.6119349973
258PhosphorylationRDLCQDPTIKELESI
CHHHCCCHHHHHHHH
53.63-
264PhosphorylationPTIKELESIISKRNI
CHHHHHHHHHHHCCC
37.5324719451
2682-HydroxyisobutyrylationELESIISKRNIQFSC
HHHHHHHHCCCEEEC
38.77-

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 CD38_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD38_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 CD38_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FCG3A_HUMANFCGR3Aphysical
11895784
CD3E_HUMANCD3Ephysical
14523017
CD3Z_HUMANCD247physical
14523017
LCK_HUMANLCKphysical
14523017
ZAP70_HUMANZAP70physical
14523017

Drug and Disease Associations
Kegg Disease
H00005 Chronic lymphocytic leukemia (CLL)
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 CD38_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-219, 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-100; ASN-209 AND ASN-219,AND MASS SPECTROMETRY.

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