dbPTM

RAB3D_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB3D_HUMAN
UniProt AC	O95716
Protein Name	Ras-related protein Rab-3D
Gene Name	RAB3D
Organism	Homo sapiens (Human).
Sequence Length	219
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side .
Protein Description	Protein transport. Probably involved in regulated exocytosis (By similarity)..
Protein Sequence	MASAGDTQAGPRDAADQNFDYMFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRTITTAYYRGAMGFLLMYDIANQESFAAVQDWATQIKTYSWDNAQVILVGNKCDLEDERVVPAEDGRRLADDLGFEFFEASAKENINVKQVFERLVDVICEKMNESLEPSSSSGSNGKGPAVGDAPAPQPSSCSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASAGDTQA ------CCCCCCCCC	14.21	22814378
3	Phosphorylation	-----MASAGDTQAG -----CCCCCCCCCC	31.33	25849741
21	Phosphorylation	AADQNFDYMFKLLLI CHHCCCCCEEEEEEE	10.58	-
42	Phosphorylation	KTSFLFRYADDSFTP CEEEEEEECCCCCCC	13.67	22817900
78	Phosphorylation	IKLQIWDTAGQERYR EEEEEEECCCHHHHH	20.07	28857561
84	Phosphorylation	DTAGQERYRTITTAY ECCCHHHHHHHHHHH	16.03	19060867
86	Phosphorylation	AGQERYRTITTAYYR CCHHHHHHHHHHHHH	17.46	29125462
88	Phosphorylation	QERYRTITTAYYRGA HHHHHHHHHHHHHHH	12.54	-
89	Phosphorylation	ERYRTITTAYYRGAM HHHHHHHHHHHHHHH	14.60	20363803
91	Phosphorylation	YRTITTAYYRGAMGF HHHHHHHHHHHHHHH	7.51	20363803
92	Phosphorylation	RTITTAYYRGAMGFL HHHHHHHHHHHHHHH	10.50	20363803
190	Phosphorylation	ICEKMNESLEPSSSS HHHHHHHHCCCCCCC	32.78	-
194	Phosphorylation	MNESLEPSSSSGSNG HHHHCCCCCCCCCCC	33.21	26471730
195	Phosphorylation	NESLEPSSSSGSNGK HHHCCCCCCCCCCCC	38.96	26471730
196	Phosphorylation	ESLEPSSSSGSNGKG HHCCCCCCCCCCCCC	42.95	26471730
197	Phosphorylation	SLEPSSSSGSNGKGP HCCCCCCCCCCCCCC	48.46	26471730
199	Phosphorylation	EPSSSSGSNGKGPAV CCCCCCCCCCCCCCC	44.34	26471730
217	Geranylgeranylation	PAPQPSSCSC----- CCCCCCCCCC-----	5.89	-
219	Methylation	PQPSSCSC------- CCCCCCCC-------	8.30	-
219	Geranylgeranylation	PQPSSCSC------- CCCCCCCC-------	8.30	-

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
86	T	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
86	T	Phosphorylation		29125462
Phosphorylation of Thr-86 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM and CHML.

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 RAB3D_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A16L1_HUMAN	ATG16L1	physical	18448665
A4_HUMAN	APP	physical	21832049
CP2C9_HUMAN	CYP2C9	physical	21163940
CEP55_HUMAN	CEP55	physical	21163940
BICL2_MOUSE	Ccdc64b	physical	20360680

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 RAB3D_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]