RAB30_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB30_HUMAN
• UniProt AC: Q15771
• Protein Name: Ras-related protein Rab-30
• Gene Name: RAB30
• Organism: Homo sapiens (Human).
• Sequence Length: 203
• Subcellular Localization: Membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus, trans-Golgi network . Cytoplasm . Golgi apparatus .
• Protein Description: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Required for maintaining the structural integrity of the Golgi apparatus, possibly by mediating interactions with cytoplasmic scaffolding proteins..
• Protein Sequence: MSMEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGNKIDLAERREVSQQRAEEFSEAQDMYYLETSAKESDNVEKLFLDLACRLISEARQNTLVNNVSSPLPGEGKSISYLTCCNFN

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
6	Phosphorylation	--MSMEDYDFLFKIV --CCHHHHHHEEEEE	8.69	27642862
57	Ubiquitination	TVEINGEKVKLQIWD EEEECCEEEEEEEEC	46.17	-
59	Malonylation	EINGEKVKLQIWDTA EECCEEEEEEEECCC	45.82	26320211
59	Ubiquitination	EINGEKVKLQIWDTA EECCEEEEEEEECCC	45.82	-
65	Phosphorylation	VKLQIWDTAGQERFR EEEEEECCCCHHHHH	20.07	28857561
73	Phosphorylation	AGQERFRSITQSYYR CCHHHHHHHHHHHHH	27.55	30108239
75	Phosphorylation	QERFRSITQSYYRSA HHHHHHHHHHHHHHC	16.83	30108239
117	Phosphorylation	YASNKVITVLVGNKI HHCCCCEEEEECCCC	15.69	-
133	Phosphorylation	LAERREVSQQRAEEF HHHHHHHHHHHHHHH	18.82	22468782
147	Phosphorylation	FSEAQDMYYLETSAK HHHHHHHHHHHCCCC	17.12	22468782
152	Phosphorylation	DMYYLETSAKESDNV HHHHHHCCCCCCCCH	28.15	22468782
161	Ubiquitination	KESDNVEKLFLDLAC CCCCCHHHHHHHHHH	40.01	-
172	Phosphorylation	DLACRLISEARQNTL HHHHHHHHHHHHCCC	29.78	22210691
178	Phosphorylation	ISEARQNTLVNNVSS HHHHHHCCCCCCCCC	24.60	27251275
184	Phosphorylation	NTLVNNVSSPLPGEG CCCCCCCCCCCCCCC	28.50	25159151
185	Phosphorylation	TLVNNVSSPLPGEGK CCCCCCCCCCCCCCC	26.61	25159151
199	Geranylgeranylation	KSISYLTCCNFN--- CEEEEEEEECCC---	1.32	-
200	Methylation	SISYLTCCNFN---- EEEEEEEECCC----	5.69	-
200	Geranylgeranylation	SISYLTCCNFN---- EEEEEEEECCC----	5.69	-

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

Oops, there are no upstream regulatory protein records of RAB30_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAB30_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 RAB30_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BICL2_MOUSE	Ccdc64b	physical	20360680
HD_HUMAN	HTT	physical	28514442
RAE2_HUMAN	CHML	physical	28514442
F8I2_HUMAN	F8A1	physical	28514442
RAE1_HUMAN	CHM	physical	28514442
UBP4_HUMAN	USP4	physical	28514442
D2HDH_HUMAN	D2HGDH	physical	28514442
MOG1_HUMAN	RANGRF	physical	28514442
URFB1_HUMAN	UHRF1BP1	physical	28514442
PHLB3_HUMAN	PHLDB3	physical	28514442
TPC10_HUMAN	TRAPPC10	physical	28514442
TPPC9_HUMAN	TRAPPC9	physical	28514442
VP13C_HUMAN	VPS13C	physical	28514442
VASP_HUMAN	VASP	physical	28514442
CUX1_HUMAN	CUX1	physical	28514442
CASP_HUMAN	CUX1	physical	28514442
ACOX1_HUMAN	ACOX1	physical	28514442
TPPC4_HUMAN	TRAPPC4	physical	28514442
DPH1_HUMAN	DPH1	physical	28514442
DTNA_HUMAN	DTNA	physical	28514442
UBB_HUMAN	UBB	physical	28514442
XPP1_HUMAN	XPNPEP1	physical	28514442
L2GL2_HUMAN	LLGL2	physical	28514442
PGTA_HUMAN	RABGGTA	physical	28514442
COG4_HUMAN	COG4	physical	28514442

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY.
PubMed: 18691976