dbPTM

GDIA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GDIA_HUMAN
UniProt AC	P31150
Protein Name	Rab GDP dissociation inhibitor alpha
Gene Name	GDI1
Organism	Homo sapiens (Human).
Sequence Length	447
Subcellular Localization	Cytoplasm . Golgi apparatus, trans-Golgi network .
Protein Description	Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes..
Protein Sequence	MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLEGPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVPSTETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQTTSMRDVYRKFDLGQDVIDFTGHALALYRTDDYLDQPCLETVNRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVRKAGQVIRIICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETTDPEKEVEPALELLEPIDQKFVAISDLYEPIDDGCESQVFCSCSYDATTHFETTCNDIKDIYKRMAGTAFDFENMKRKQNDVFGEAEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDEEYDVI -------CCCCCEEE	15.33	-
5	Phosphorylation	---MDEEYDVIVLGT ---CCCCCEEEEECC	17.29	28270605
12	Phosphorylation	YDVIVLGTGLTECIL CEEEEECCCHHHHHH	25.51	28270605
15	Phosphorylation	IVLGTGLTECILSGI EEECCCHHHHHHHCH	30.10	28270605
20	Phosphorylation	GLTECILSGIMSVNG CHHHHHHHCHHCCCC	13.32	28270605
24	Phosphorylation	CILSGIMSVNGKKVL HHHHCHHCCCCEEEE	15.54	28270605
29	Acetylation	IMSVNGKKVLHMDRN HHCCCCEEEEECCCC	51.97	27452117
29	Ubiquitination	IMSVNGKKVLHMDRN HHCCCCEEEEECCCC	51.97	-
35	Methylation	KKVLHMDRNPYYGGE EEEEECCCCCCCCCC	38.15	-
38	Phosphorylation	LHMDRNPYYGGESSS EECCCCCCCCCCCCC	20.49	20068231
39	Phosphorylation	HMDRNPYYGGESSSI ECCCCCCCCCCCCCC	21.66	20068231
43	Phosphorylation	NPYYGGESSSITPLE CCCCCCCCCCCCCHH	32.43	20068231
44	Phosphorylation	PYYGGESSSITPLEE CCCCCCCCCCCCHHH	22.81	20068231
45	Phosphorylation	YYGGESSSITPLEEL CCCCCCCCCCCHHHH	39.50	20068231
47	Phosphorylation	GGESSSITPLEELYK CCCCCCCCCHHHHHH	24.62	20068231
53	Phosphorylation	ITPLEELYKRFQLLE CCCHHHHHHHHHHHH	11.91	20068231
54	Ubiquitination	TPLEELYKRFQLLEG CCHHHHHHHHHHHHC	60.40	21890473
65	Phosphorylation	LLEGPPESMGRGRDW HHHCCCHHCCCCCCC	32.10	21712546
66	Sulfoxidation	LEGPPESMGRGRDWN HHCCCHHCCCCCCCC	3.96	21406390
68	Methylation	GPPESMGRGRDWNVD CCCHHCCCCCCCCCC	28.47	-
70	Methylation	PESMGRGRDWNVDLI CHHCCCCCCCCCCHH	44.40	-
79	Ubiquitination	WNVDLIPKFLMANGQ CCCCHHHHHHHHCCC	44.10	-
93	Phosphorylation	QLVKMLLYTEVTRYL CEEEHHHHHHHHHHC	9.26	24927040
94	Phosphorylation	LVKMLLYTEVTRYLD EEEHHHHHHHHHHCC	24.77	19060867
99	Phosphorylation	LYTEVTRYLDFKVVE HHHHHHHHCCEEEEE	10.97	-
111	Phosphorylation	VVEGSFVYKGGKIYK EEEEEEEEECCEEEE	11.25	22817900
112	Acetylation	VEGSFVYKGGKIYKV EEEEEEEECCEEEEC	56.75	26051181
112	Ubiquitination	VEGSFVYKGGKIYKV EEEEEEEECCEEEEC	56.75	-
112	2-Hydroxyisobutyrylation	VEGSFVYKGGKIYKV EEEEEEEECCEEEEC	56.75	-
115	Ubiquitination	SFVYKGGKIYKVPST EEEEECCEEEECCCH	52.08	-
117	Phosphorylation	VYKGGKIYKVPSTET EEECCEEEECCCHHH	14.93	22817900
121	Phosphorylation	GKIYKVPSTETEALA CEEEECCCHHHHHHH	41.69	28348404
122	Phosphorylation	KIYKVPSTETEALAS EEEECCCHHHHHHHH	40.64	28348404
124	Phosphorylation	YKVPSTETEALASNL EECCCHHHHHHHHHH	27.01	28348404
132	Sulfoxidation	EALASNLMGMFEKRR HHHHHHHHHHHHHHH	4.23	21406390
137	Ubiquitination	NLMGMFEKRRFRKFL HHHHHHHHHHHHEEE	37.29	21890473
165	Phosphorylation	FEGVDPQTTSMRDVY CCCCCCCCCCHHHHH	26.65	25022875
168	Sulfoxidation	VDPQTTSMRDVYRKF CCCCCCCHHHHHHHC	3.89	21406390
169	Methylation	DPQTTSMRDVYRKFD CCCCCCHHHHHHHCC	29.97	-
174	Ubiquitination	SMRDVYRKFDLGQDV CHHHHHHHCCCCCCE	26.08	-
205	Phosphorylation	LDQPCLETVNRIKLY CCCHHHHHHHHHHHH	15.33	21210654
210	Acetylation	LETVNRIKLYSESLA HHHHHHHHHHHHHHH	37.83	25953088
210	Ubiquitination	LETVNRIKLYSESLA HHHHHHHHHHHHHHH	37.83	21890473
210	2-Hydroxyisobutyrylation	LETVNRIKLYSESLA HHHHHHHHHHHHHHH	37.83	-
212	Phosphorylation	TVNRIKLYSESLARY HHHHHHHHHHHHHHH	12.85	21406692
213	Phosphorylation	VNRIKLYSESLARYG HHHHHHHHHHHHHHC	31.01	21406692
215	Phosphorylation	RIKLYSESLARYGKS HHHHHHHHHHHHCCC	22.76	21406692
219	Phosphorylation	YSESLARYGKSPYLY HHHHHHHHCCCCCEE	24.25	24076635
221	Methylation	ESLARYGKSPYLYPL HHHHHHCCCCCEECC	39.05	-
221	Ubiquitination	ESLARYGKSPYLYPL HHHHHHCCCCCEECC	39.05	21890473
221	Acetylation	ESLARYGKSPYLYPL HHHHHHCCCCCEECC	39.05	23954790
222	Phosphorylation	SLARYGKSPYLYPLY HHHHHCCCCCEECCC	17.89	20068231
224	Phosphorylation	ARYGKSPYLYPLYGL HHHCCCCCEECCCCC	26.42	20068231
226	Phosphorylation	YGKSPYLYPLYGLGE HCCCCCEECCCCCCC	5.83	20068231
229	Phosphorylation	SPYLYPLYGLGELPQ CCCEECCCCCCCCCC	13.05	20068231
242	Phosphorylation	PQGFARLSAIYGGTY CCHHHHHHHHHCCCE	13.68	23663014
245	Phosphorylation	FARLSAIYGGTYMLN HHHHHHHHCCCEECC	14.82	23663014
248	Phosphorylation	LSAIYGGTYMLNKPV HHHHHCCCEECCCCH	11.03	23663014
249	Phosphorylation	SAIYGGTYMLNKPVD HHHHCCCEECCCCHH	11.68	23663014
253	Ubiquitination	GGTYMLNKPVDDIIM CCCEECCCCHHEEEE	42.32	-
264	Methylation	DIIMENGKVVGVKSE EEEEECCEEEEECCC	45.38	-
269	Ubiquitination	NGKVVGVKSEGEVAR CCEEEEECCCCCHHH	36.54	21890473
269	2-Hydroxyisobutyrylation	NGKVVGVKSEGEVAR CCEEEEECCCCCHHH	36.54	-
269	Acetylation	NGKVVGVKSEGEVAR CCEEEEECCCCCHHH	36.54	22424773
278	Ubiquitination	EGEVARCKQLICDPS CCCHHHEEEEEECHH	42.45	-
285	Phosphorylation	KQLICDPSYIPDRVR EEEEECHHHCCHHHH	23.57	21406692
286	Phosphorylation	QLICDPSYIPDRVRK EEEECHHHCCHHHHH	23.12	21406692
290	Methylation	DPSYIPDRVRKAGQV CHHHCCHHHHHHHHE	25.45	-
309	Acetylation	CILSHPIKNTNDANS EEECCCCCCCCCCCC	63.27	26051181
309	Ubiquitination	CILSHPIKNTNDANS EEECCCCCCCCCCCC	63.27	-
316	Phosphorylation	KNTNDANSCQIIIPQ CCCCCCCCCEEEEEH	14.77	21712546
317	S-nitrosylation	NTNDANSCQIIIPQN CCCCCCCCEEEEEHH	3.19	2212679
330	Phosphorylation	QNQVNRKSDIYVCMI HHHCCCCCCEEEEEE	26.46	-
333	Phosphorylation	VNRKSDIYVCMISYA CCCCCCEEEEEEECC	7.81	22817900
338	Phosphorylation	DIYVCMISYAHNVAA CEEEEEEECCCHHHH	6.86	-
339	Phosphorylation	IYVCMISYAHNVAAQ EEEEEEECCCHHHHC	10.85	19060867
349	Phosphorylation	NVAAQGKYIAIASTT HHHHCCCEEEEEEEE	11.47	21406692
354	Phosphorylation	GKYIAIASTTVETTD CCEEEEEEEEEECCC	20.63	21406692
355	Phosphorylation	KYIAIASTTVETTDP CEEEEEEEEEECCCH	26.32	21406692
356	Phosphorylation	YIAIASTTVETTDPE EEEEEEEEEECCCHH	17.53	21406692
359	Phosphorylation	IASTTVETTDPEKEV EEEEEEECCCHHHCC	31.96	21406692
360	Phosphorylation	ASTTVETTDPEKEVE EEEEEECCCHHHCCH	35.73	21406692
401	O-linked_Glycosylation	CESQVFCSCSYDATT CCCEEEEEECCCCCC	8.47	OGP
413	Phosphorylation	ATTHFETTCNDIKDI CCCCEECCHHHHHHH	11.34	18452278
435	Ubiquitination	AFDFENMKRKQNDVF CCCHHHHHHHHCCCC	68.94	21890473
437	Ubiquitination	DFENMKRKQNDVFGE CHHHHHHHHCCCCCC	48.19	21890473

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 GDIA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GDIA_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 GDIA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB1B_HUMAN	RAB1B	physical	8836150
CDC42_HUMAN	CDC42	physical	11583574
RAB9A_HUMAN	RAB9A	physical	7744738
RB11B_HUMAN	RAB11B	physical	22939629
RAB1A_HUMAN	RAB1A	physical	22939629
PIMT_HUMAN	PCMT1	physical	22939629
BACH_HUMAN	ACOT7	physical	22863883
AL9A1_HUMAN	ALDH9A1	physical	22863883
ARLY_HUMAN	ASL	physical	22863883
GGH_HUMAN	GGH	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
HEXA_HUMAN	HEXA	physical	22863883
NEDD8_HUMAN	NEDD8	physical	22863883
RCC2_HUMAN	RCC2	physical	22863883
SCRN1_HUMAN	SCRN1	physical	22863883
SGTA_HUMAN	SGTA	physical	22863883
LNX1_HUMAN	LNX1	physical	25416956
MOES_HUMAN	MSN	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
EMD_HUMAN	EMD	physical	26496610
RAB8A_HUMAN	RAB8A	physical	26496610
RAB1A_HUMAN	RAB1A	physical	26496610
RAB4A_HUMAN	RAB4A	physical	26496610
RAB5B_HUMAN	RAB5B	physical	26496610
RAB6A_HUMAN	RAB6A	physical	26496610
RAB13_HUMAN	RAB13	physical	26496610
RAB5C_HUMAN	RAB5C	physical	26496610
RAB7A_HUMAN	RAB7A	physical	26496610
FUBP3_HUMAN	FUBP3	physical	26496610
RAB9A_HUMAN	RAB9A	physical	26496610
TIF1B_HUMAN	TRIM28	physical	26496610
RAB10_HUMAN	RAB10	physical	26496610
PLPL6_HUMAN	PNPLA6	physical	26496610
RAB35_HUMAN	RAB35	physical	26496610
RAB31_HUMAN	RAB31	physical	26496610
EXOS7_HUMAN	EXOSC7	physical	26496610
FA98A_HUMAN	FAM98A	physical	26496610
REPI1_HUMAN	REPIN1	physical	26496610
RAB14_HUMAN	RAB14	physical	26496610
INT13_HUMAN	ASUN	physical	26496610
DYHC2_HUMAN	DYNC2H1	physical	26496610
RAB34_HUMAN	RAB34	physical	26496610
SPT2_HUMAN	SPTY2D1	physical	26496610
RAB12_HUMAN	RAB12	physical	26496610
RB22A_HUMAN	RAB22A	physical	28514442
RAB12_HUMAN	RAB12	physical	28514442
RAB24_HUMAN	RAB24	physical	28514442
RAB4A_HUMAN	RAB4A	physical	28514442
RAB8A_HUMAN	RAB8A	physical	28514442
UBP25_HUMAN	USP25	physical	28514442
RAB34_HUMAN	RAB34	physical	28514442
RASEF_HUMAN	RASEF	physical	28514442
RAB5B_HUMAN	RAB5B	physical	28514442
RAB4B_HUMAN	RAB4B	physical	28514442
RAB6A_HUMAN	RAB6A	physical	28514442
RAB21_HUMAN	RAB21	physical	28514442
RAB14_HUMAN	RAB14	physical	28514442
RAB10_HUMAN	RAB10	physical	28514442
RAB13_HUMAN	RAB13	physical	28514442
RAB35_HUMAN	RAB35	physical	28514442
RAB7A_HUMAN	RAB7A	physical	28514442
GDIB_HUMAN	GDI2	physical	28514442
RAB18_HUMAN	RAB18	physical	28514442
RAB2A_HUMAN	RAB2A	physical	28514442
ACAP2_HUMAN	ACAP2	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300849	Mental retardation, X-linked 41 (MRX41)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GDIA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-333, AND MASSSPECTROMETRY.	15592455 [Abstract]