dbPTM

RAB5A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB5A_HUMAN
UniProt AC	P20339
Protein Name	Ras-related protein Rab-5A
Gene Name	RAB5A
Organism	Homo sapiens (Human).
Sequence Length	215
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Early endosome membrane Lipid-anchor . Melanosome . Cytoplasmic vesicle . Cell projection, ruffle . Membrane . Cytoplasm, cytosol. Cytoplasmic vesicle, phagosome membrane . Endosome membrane . Enric
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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. [PubMed: 10818110]
Protein Sequence	MASRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPTQPTRNQCCSN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASRGATRP ------CCCCCCCCC	14.13	-
3	Phosphorylation	-----MASRGATRPN -----CCCCCCCCCC	29.92	25159151
4	Methylation	----MASRGATRPNG ----CCCCCCCCCCC	29.27	115489929
7	Phosphorylation	-MASRGATRPNGPNT -CCCCCCCCCCCCCC	49.86	-
14	Phosphorylation	TRPNGPNTGNKICQF CCCCCCCCCCCCCEE	45.31	28348404
22	Acetylation	GNKICQFKLVLLGES CCCCCEEEEEEECCC	16.29	25953088
29	Phosphorylation	KLVLLGESAVGKSSL EEEEECCCCCCCCHH	26.84	23911959
33	Ubiquitination	LGESAVGKSSLVLRF ECCCCCCCCHHHHHH	30.21	-
33	Ubiquitination	LGESAVGKSSLVLRF ECCCCCCCCHHHHHH	30.21	-
35	Phosphorylation	ESAVGKSSLVLRFVK CCCCCCCHHHHHHHC	26.44	20860994
51	Phosphorylation	QFHEFQESTIGAAFL CCHHHHHHHHCHHEE	17.97	26126808
52	Phosphorylation	FHEFQESTIGAAFLT CHHHHHHHHCHHEEE	23.76	26126808
59	Phosphorylation	TIGAAFLTQTVCLDD HHCHHEEEEEEECCC	18.75	26126808
61	Phosphorylation	GAAFLTQTVCLDDTT CHHEEEEEEECCCCE	14.14	26126808
82	Phosphorylation	DTAGQERYHSLAPMY CCCCCCCCHHHCCCH	8.60	25106551
84	Phosphorylation	AGQERYHSLAPMYYR CCCCCCHHHCCCHHC	19.79	28857561
88	Sulfoxidation	RYHSLAPMYYRGAQA CCHHHCCCHHCCCCE	3.69	28183972
102	Ubiquitination	AAIVVYDITNEESFA EEEEEEECCCHHHHH	2.14	21890473
116	Acetylation	ARAKNWVKELQRQAS HHHHHHHHHHHHHCC	44.30	26051181
116	Ubiquitination	ARAKNWVKELQRQAS HHHHHHHHHHHHHCC	44.30	21890473
116	Ubiquitination	ARAKNWVKELQRQAS HHHHHHHHHHHHHCC	44.30	2189047
120	Ubiquitination	NWVKELQRQASPNIV HHHHHHHHHCCCCEE	46.81	-
123	Phosphorylation	KELQRQASPNIVIAL HHHHHHCCCCEEEEE	15.33	25159151
134	Ubiquitination	VIALSGNKADLANKR EEEECCCHHHHCCCC	46.96	-
140	Ubiquitination	NKADLANKRAVDFQE CHHHHCCCCCCCHHH	35.81	-
160	Sulfoxidation	DDNSLLFMETSAKTS CCCCEEEEECCCCCC	5.76	30846556
165	Ubiquitination	LFMETSAKTSMNVNE EEEECCCCCCCCHHH	40.68	-
193	Phosphorylation	PQNPGANSARGRGVD CCCCCCCCCCCCCCC	20.86	29255136
197	Methylation	GANSARGRGVDLTEP CCCCCCCCCCCCCCC	36.09	115489935
202	Phosphorylation	RGRGVDLTEPTQPTR CCCCCCCCCCCCCCC	35.14	18669648
205	Phosphorylation	GVDLTEPTQPTRNQC CCCCCCCCCCCCCCC	40.73	18669648
208	Phosphorylation	LTEPTQPTRNQCCSN CCCCCCCCCCCCCCC	32.22	18669648
212	Geranylgeranylation	TQPTRNQCCSN---- CCCCCCCCCCC----	2.91	7991565
212	Geranylgeranylation	TQPTRNQCCSN---- CCCCCCCCCCC----	2.91	7991565
213	Geranylgeranylation	QPTRNQCCSN----- CCCCCCCCCC-----	2.92	7991565
213	Geranylgeranylation	QPTRNQCCSN----- CCCCCCCCCC-----	2.92	7991565

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
7	T	Phosphorylation	Kinase	PRKCE	Q02156	GPS
84	S	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot
123	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
84	S	Phosphorylation		29125462
Phosphorylation of Ser-84 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including RAB GDP dissociation inhibitors GDI1 and GDI2.

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 RAB5A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SDCB1_HUMAN	SDCBP	physical	15014045
EEA1_HUMAN	EEA1	physical	14600265
RIN3_HUMAN	RIN3	physical	12972505
KIF3B_HUMAN	KIF3B	physical	12832475
RABE1_HUMAN	RABEP1	physical	9524117
RABE1_HUMAN	RABEP1	physical	8521472
RIN1_HUMAN	RIN1	physical	11703925
EEA1_HUMAN	EEA1	physical	11718716
RABE1_HUMAN	RABEP1	physical	11718716
EEA1_HUMAN	EEA1	physical	11493665
AGTR1_HUMAN	AGTR1	physical	11682489
RAB4A_BOVIN	RAB4A	physical	11788822
RABE2_BOVIN	RABEP2	physical	11788822
RBNS5_HUMAN	RBSN	physical	11062261
VPS45_HUMAN	VPS45	physical	11062261
RIN2_HUMAN	RIN2	physical	11733506
RAB37_HUMAN	RAB37	physical	10722846
DP13A_HUMAN	APPL1	physical	15016378
VPS45_HUMAN	VPS45	physical	15016378
PK3C3_HUMAN	PIK3C3	physical	15016378
EEA1_HUMAN	EEA1	physical	15016378
DP13B_HUMAN	APPL2	physical	15016378
P85A_HUMAN	PIK3R1	physical	15377662
EEA1_HUMAN	EEA1	physical	10720461
RABE1_HUMAN	RABEP1	physical	10720461
RABX5_HUMAN	RABGEF1	physical	10720461
RABE2_HUMAN	RABEP2	physical	10720461
SH3K1_HUMAN	SH3KBP1	physical	22833562
RIN1_HUMAN	RIN1	physical	17403676
KCNA5_HUMAN	KCNA5	physical	18755741
EEA1_HUMAN	EEA1	physical	15328530
RABE1_HUMAN	RABEP1	physical	15328530
PK3C3_HUMAN	PIK3C3	physical	15328530
PK3CB_HUMAN	PIK3CB	physical	15328530
RBNS5_HUMAN	RBSN	physical	15328530
ANFY1_HUMAN	ANKFY1	physical	15328530
RB11A_HUMAN	RAB11A	physical	16354686
TRFE_HUMAN	TF	physical	16354686
GRIK4_HUMAN	GRIK4	physical	15782196
RUFY1_HUMAN	RUFY1	physical	14617813
RABX5_HUMAN	RABGEF1	physical	23048039
SYUA_HUMAN	SNCA	physical	15207266
RAB7A_HUMAN	RAB7A	physical	22939629
DP13A_HUMAN	APPL1	physical	17581628
SUN2_HUMAN	SUN2	physical	21988832
PRAF1_HUMAN	RABAC1	physical	21988832
VGFR2_HUMAN	KDR	physical	23393387
ANFY1_HUMAN	ANKFY1	physical	24102721
EEA1_HUMAN	EEA1	physical	20534488
RBNS5_HUMAN	RBSN	physical	20534488
RB11B_HUMAN	RAB11B	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
RAB8A_HUMAN	RAB8A	physical	26344197
RAB8B_HUMAN	RAB8B	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
ENTP6_HUMAN	ENTPD6	physical	26496610
CO1A2_HUMAN	COL1A2	physical	26496610
ZEP1_HUMAN	HIVEP1	physical	26496610
RAB5C_HUMAN	RAB5C	physical	26496610
TAF12_HUMAN	TAF12	physical	26496610
MKNK1_HUMAN	MKNK1	physical	26496610
NCOR1_HUMAN	NCOR1	physical	26496610
SUN2_HUMAN	SUN2	physical	26496610
M3K20_HUMAN	ZAK	physical	26496610
RABL6_HUMAN	RABL6	physical	26496610
ANM9_HUMAN	PRMT9	physical	26496610
CYTSB_HUMAN	SPECC1	physical	26496610
MIC13_HUMAN	C19orf70	physical	26496610
CA052_HUMAN	C1orf52	physical	26496610
CAVN1_HUMAN	PTRF	physical	26496610
HTAI2_HUMAN	HTATIP2	physical	21252234
ACSL4_HUMAN	ACSL4	physical	21252234
SHLB1_HUMAN	SH3GLB1	physical	21252234
RABE1_HUMAN	RABEP1	physical	26430212
RAB5C_HUMAN	RAB5C	physical	28514442
RAE1_HUMAN	CHM	physical	28514442
GDIA_HUMAN	GDI1	physical	28514442
RAE2_HUMAN	CHML	physical	28514442
PGTA_HUMAN	RABGGTA	physical	28514442
GDIB_HUMAN	GDI2	physical	28514442
ATE1_HUMAN	ATE1	physical	28514442
PGTB2_HUMAN	RABGGTB	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.

Regulatory Network of RAB5A_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]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202; THR-205 ANDTHR-208, AND MASS SPECTROMETRY.	18669648 [Abstract]
Prenylation
Reference	PubMed
"Rab geranylgeranyl transferase catalyzes the geranylgeranylation ofadjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."; Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.; Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994). Cited for: NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-212 AND CYS-213, ANDMASS SPECTROMETRY.	7991565 [Abstract]

show