dbPTM

GDIB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GDIB_HUMAN
UniProt AC	P50395
Protein Name	Rab GDP dissociation inhibitor beta
Gene Name	GDI2
Organism	Homo sapiens (Human).
Sequence Length	445
Subcellular Localization	Cytoplasm. Membrane Peripheral membrane protein.
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..
Protein Sequence	MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPGSPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQDVIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNIYKRMTGSEFDFEEMKRKKNDIYGED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNEEYDVI -------CCCCCCEE	14.90	19413330
5	Phosphorylation	---MNEEYDVIVLGT ---CCCCCCEEEECC	14.88	25159151
20	Phosphorylation	GLTECILSGIMSVNG CHHHHHHHCHHCCCC	13.32	22210691
24	Phosphorylation	CILSGIMSVNGKKVL HHHHCHHCCCCEEEE	15.54	22210691
29	Ubiquitination	IMSVNGKKVLHMDRN HHCCCCEEEEECCCC	51.97	-
35	Methylation	KKVLHMDRNPYYGGE EEEEECCCCCCCCCC	38.15	-
38	Phosphorylation	LHMDRNPYYGGESAS EECCCCCCCCCCCCC	20.49	28152594
39	Phosphorylation	HMDRNPYYGGESASI ECCCCCCCCCCCCCC	21.66	28152594
53	Phosphorylation	ITPLEDLYKRFKIPG CCCHHHHHHHCCCCC	16.67	-
54	Acetylation	TPLEDLYKRFKIPGS CCHHHHHHHCCCCCC	59.67	23236377
54	Ubiquitination	TPLEDLYKRFKIPGS CCHHHHHHHCCCCCC	59.67	21890473
54	Ubiquitination	TPLEDLYKRFKIPGS CCHHHHHHHCCCCCC	59.67	21890473
57	Malonylation	EDLYKRFKIPGSPPE HHHHHHCCCCCCCCH	52.61	26320211
57	Succinylation	EDLYKRFKIPGSPPE HHHHHHCCCCCCCCH	52.61	-
57	Succinylation	EDLYKRFKIPGSPPE HHHHHHCCCCCCCCH	52.61	-
57	Ubiquitination	EDLYKRFKIPGSPPE HHHHHHCCCCCCCCH	52.61	-
61	Phosphorylation	KRFKIPGSPPESMGR HHCCCCCCCCHHHCC	31.74	29255136
65	Phosphorylation	IPGSPPESMGRGRDW CCCCCCHHHCCCCCC	32.10	30266825
66	Sulfoxidation	PGSPPESMGRGRDWN CCCCCHHHCCCCCCC	3.96	28465586
68	Methylation	SPPESMGRGRDWNVD CCCHHHCCCCCCCCC	28.47	-
70	Methylation	PESMGRGRDWNVDLI CHHHCCCCCCCCCHH	44.40	-
79	Ubiquitination	WNVDLIPKFLMANGQ CCCCHHHHHHHHCCC	44.10	-
82	Sulfoxidation	DLIPKFLMANGQLVK CHHHHHHHHCCCEEE	2.83	21406390
93	Phosphorylation	QLVKMLLYTEVTRYL CEEEHHHHHCHHHHC	9.26	24927040
94	Phosphorylation	LVKMLLYTEVTRYLD EEEHHHHHCHHHHCC	24.77	19060867
97	Ubiquitination	MLLYTEVTRYLDFKV HHHHHCHHHHCCEEE	13.83	21890473
105	Phosphorylation	RYLDFKVTEGSFVYK HHCCEEECCCEEEEE	34.91	21406692
108	Phosphorylation	DFKVTEGSFVYKGGK CEEECCCEEEEECCE	12.81	21406692
111	Nitration	VTEGSFVYKGGKIYK ECCCEEEEECCEEEE	11.25	-
111	Phosphorylation	VTEGSFVYKGGKIYK ECCCEEEEECCEEEE	11.25	20068231
112	Acetylation	TEGSFVYKGGKIYKV CCCEEEEECCEEEEC	56.75	19608861
112	Methylation	TEGSFVYKGGKIYKV CCCEEEEECCEEEEC	56.75	19608861
112	Ubiquitination	TEGSFVYKGGKIYKV CCCEEEEECCEEEEC	56.75	21906983
117	Phosphorylation	VYKGGKIYKVPSTEA EEECCEEEECCCHHH	14.93	20090780
121	Phosphorylation	GKIYKVPSTEAEALA CEEEECCCHHHHHHH	41.70	25159151
122	Phosphorylation	KIYKVPSTEAEALAS EEEECCCHHHHHHHH	32.90	25159151
129	Phosphorylation	TEAEALASSLMGLFE HHHHHHHHHHHHHHH	25.51	28857561
130	Phosphorylation	EAEALASSLMGLFEK HHHHHHHHHHHHHHH	19.44	28857561
132	Sulfoxidation	EALASSLMGLFEKRR HHHHHHHHHHHHHHC	4.78	30846556
137	Acetylation	SLMGLFEKRRFRKFL HHHHHHHHHCHHHEE	41.35	23236377
142	Acetylation	FEKRRFRKFLVYVAN HHHHCHHHEEEEEEC	40.10	25953088
142	Ubiquitination	FEKRRFRKFLVYVAN HHHHCHHHEEEEEEC	40.10	21906983
153	Acetylation	YVANFDEKDPRTFEG EEECCCCCCCCCCCC	74.91	23954790
153	Ubiquitination	YVANFDEKDPRTFEG EEECCCCCCCCCCCC	74.91	21906983
164	Acetylation	TFEGIDPKKTTMRDV CCCCCCCCCCCHHHH	60.03	23749302
164	Ubiquitination	TFEGIDPKKTTMRDV CCCCCCCCCCCHHHH	60.03	21906983
174	Ubiquitination	TMRDVYKKFDLGQDV CHHHHHHHCCCCCCE	26.82	21890473
176	Ubiquitination	RDVYKKFDLGQDVID HHHHHHCCCCCCEEE	59.79	21890473
194	Phosphorylation	HALALYRTDDYLDQP CHHHHHCCCCCCCCC	21.48	27251275
197	Phosphorylation	ALYRTDDYLDQPCYE HHHCCCCCCCCCHHH	18.26	28152594
202	S-nitrosocysteine	DDYLDQPCYETINRI CCCCCCCHHHHHHHH	3.89	-
202	S-nitrosylation	DDYLDQPCYETINRI CCCCCCCHHHHHHHH	3.89	18335467
202	S-palmitoylation	DDYLDQPCYETINRI CCCCCCCHHHHHHHH	3.89	26865113
203	Phosphorylation	DYLDQPCYETINRIK CCCCCCHHHHHHHHH	23.84	27273156
205	Phosphorylation	LDQPCYETINRIKLY CCCCHHHHHHHHHHH	9.33	28796482
210	Ubiquitination	YETINRIKLYSESLA HHHHHHHHHHHHHHH	37.83	-
212	Phosphorylation	TINRIKLYSESLARY HHHHHHHHHHHHHHH	12.85	21406692
213	Phosphorylation	INRIKLYSESLARYG HHHHHHHHHHHHHHC	31.01	21406692
215	Phosphorylation	RIKLYSESLARYGKS HHHHHHHHHHHHCCC	22.76	21406692
219	Phosphorylation	YSESLARYGKSPYLY HHHHHHHHCCCCCEE	24.25	24076635
221	Acetylation	ESLARYGKSPYLYPL HHHHHHCCCCCEECC	39.05	66724635
221	Methylation	ESLARYGKSPYLYPL HHHHHHCCCCCEECC	39.05	-
221	Ubiquitination	ESLARYGKSPYLYPL HHHHHHCCCCCEECC	39.05	21906983
222	Phosphorylation	SLARYGKSPYLYPLY HHHHHCCCCCEECCC	17.89	20068231
224	Acetylation	ARYGKSPYLYPLYGL HHHCCCCCEECCCCC	26.42	19608861
224	Phosphorylation	ARYGKSPYLYPLYGL HHHCCCCCEECCCCC	26.42	20068231
224	Ubiquitination	ARYGKSPYLYPLYGL HHHCCCCCEECCCCC	26.42	19608861
226	Phosphorylation	YGKSPYLYPLYGLGE HCCCCCEECCCCCCC	5.83	20068231
229	Nitration	SPYLYPLYGLGELPQ CCCEECCCCCCCCCC	13.05	-
229	Phosphorylation	SPYLYPLYGLGELPQ CCCEECCCCCCCCCC	13.05	20068231
245	Phosphorylation	FARLSAIYGGTYMLN HHHHHHHHCCCEECC	14.82	-
253	Acetylation	GGTYMLNKPIEEIIV CCCEECCCCHHEEEE	43.33	26051181
253	Ubiquitination	GGTYMLNKPIEEIIV CCCEECCCCHHEEEE	43.33	21906983
269	Sumoylation	NGKVIGVKSEGEIAR CCEEEEECCHHHHHH	37.26	-
269	Acetylation	NGKVIGVKSEGEIAR CCEEEEECCHHHHHH	37.26	19608861
269	Sumoylation	NGKVIGVKSEGEIAR CCEEEEECCHHHHHH	37.26	19608861
269	Ubiquitination	NGKVIGVKSEGEIAR CCEEEEECCHHHHHH	37.26	21906983
270	Phosphorylation	GKVIGVKSEGEIARC CEEEEECCHHHHHHH	48.72	30622161
278	Ubiquitination	EGEIARCKQLICDPS HHHHHHHEEEECCHH	42.45	-
285	Phosphorylation	KQLICDPSYVKDRVE EEEECCHHHHHHHHH	29.34	28152594
286	Phosphorylation	QLICDPSYVKDRVEK EEECCHHHHHHHHHH	19.53	28152594
288	Acetylation	ICDPSYVKDRVEKVG ECCHHHHHHHHHHHH	31.42	23749302
288	Ubiquitination	ICDPSYVKDRVEKVG ECCHHHHHHHHHHHH	31.42	-
293	Acetylation	YVKDRVEKVGQVIRV HHHHHHHHHHHHHHH	49.13	25953088
293	Malonylation	YVKDRVEKVGQVIRV HHHHHHHHHHHHHHH	49.13	26320211
293	Ubiquitination	YVKDRVEKVGQVIRV HHHHHHHHHHHHHHH	49.13	-
305	Phosphorylation	IRVICILSHPIKNTN HHHHHHHCCCCCCCC	13.80	28348404
309	Acetylation	CILSHPIKNTNDANS HHHCCCCCCCCCCCC	63.27	25953088
309	Ubiquitination	CILSHPIKNTNDANS HHHCCCCCCCCCCCC	63.27	-
316	Phosphorylation	KNTNDANSCQIIIPQ CCCCCCCCCEEEEEH	14.77	21712546
329	Ubiquitination	PQNQVNRKSDIYVCM EHHHCCCCCCEEEEE	47.48	-
330	Phosphorylation	QNQVNRKSDIYVCMI HHHCCCCCCEEEEEH	26.46	28064214
333	Phosphorylation	VNRKSDIYVCMISFA CCCCCCEEEEEHHCC	7.81	27155012
349	Phosphorylation	NVAAQGKYIAIVSTT HHHHCCCEEEEEEEE	11.47	-
355	Phosphorylation	KYIAIVSTTVETKEP CEEEEEEEEECCCCC	24.78	-
360	Ubiquitination	VSTTVETKEPEKEIR EEEEECCCCCHHHHH	58.74	21906983
364	Acetylation	VETKEPEKEIRPALE ECCCCCHHHHHHHHH	69.98	25953088
364	Ubiquitination	VETKEPEKEIRPALE ECCCCCHHHHHHHHH	69.98	-
373	Ubiquitination	IRPALELLEPIEQKF HHHHHHHHHHHHHHC	5.55	21890473
379	Ubiquitination	LLEPIEQKFVSISDL HHHHHHHHCCCHHHH	34.64	-
382	Phosphorylation	PIEQKFVSISDLLVP HHHHHCCCHHHHCCC	21.36	28450419
384	Phosphorylation	EQKFVSISDLLVPKD HHHCCCHHHHCCCCC	18.07	29523821
390	Ubiquitination	ISDLLVPKDLGTESQ HHHHCCCCCCCCCCE	59.09	-
394	Phosphorylation	LVPKDLGTESQIFIS CCCCCCCCCCEEEEE	39.50	26846344
396	Phosphorylation	PKDLGTESQIFISRT CCCCCCCCEEEEEEE	28.54	26846344
401	Phosphorylation	TESQIFISRTYDATT CCCEEEEEEECCCCC	14.07	26846344
403	Phosphorylation	SQIFISRTYDATTHF CEEEEEEECCCCCCE	20.97	23401153
404	Phosphorylation	QIFISRTYDATTHFE EEEEEEECCCCCCEE	11.50	23401153
407	Phosphorylation	ISRTYDATTHFETTC EEEECCCCCCEEEHH	20.22	23401153
408	Phosphorylation	SRTYDATTHFETTCD EEECCCCCCEEEHHH	26.70	23401153
412	Phosphorylation	DATTHFETTCDDIKN CCCCCEEEHHHHHHH	31.61	23401153
413	Phosphorylation	ATTHFETTCDDIKNI CCCCEEEHHHHHHHH	13.52	23401153
418	Acetylation	ETTCDDIKNIYKRMT EEHHHHHHHHHHHHH	44.26	25953088
418	Ubiquitination	ETTCDDIKNIYKRMT EEHHHHHHHHHHHHH	44.26	21906983
422	Ubiquitination	DDIKNIYKRMTGSEF HHHHHHHHHHHCCCC	31.71	-
424	Sulfoxidation	IKNIYKRMTGSEFDF HHHHHHHHHCCCCCH	4.32	21406390
425	Phosphorylation	KNIYKRMTGSEFDFE HHHHHHHHCCCCCHH	41.40	25849741
427	Phosphorylation	IYKRMTGSEFDFEEM HHHHHHCCCCCHHHH	26.39	23403867
435	Acetylation	EFDFEEMKRKKNDIY CCCHHHHHHHHCCCC	65.43	27452117
435	Ubiquitination	EFDFEEMKRKKNDIY CCCHHHHHHHHCCCC	65.43	2190698
438	Ubiquitination	FEEMKRKKNDIYGED HHHHHHHHCCCCCCC	64.98	-
442	Phosphorylation	KRKKNDIYGED---- HHHHCCCCCCC----	19.82	25884760

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 GDIB_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB11A_HUMAN	RAB11A	physical	10512627
RAB9A_HUMAN	RAB9A	physical	10512627
RAB5A_HUMAN	RAB5A	physical	10512627
RAB4A_HUMAN	RAB4A	physical	10512627
RAB2A_HUMAN	RAB2A	physical	10512627
RAB8A_HUMAN	RAB8A	physical	10512627
RB11B_HUMAN	RAB11B	physical	22939629
RAB1A_HUMAN	RAB1A	physical	22939629
GLRA2_HUMAN	GLRA2	physical	21988832
DUT_HUMAN	DUT	physical	22863883
CLIC3_HUMAN	CLIC3	physical	26344197
EZRI_HUMAN	EZR	physical	26344197
FUMH_HUMAN	FH	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
PLIN3_HUMAN	PLIN3	physical	26344197
PPCE_HUMAN	PREP	physical	26344197
RAB7A_HUMAN	RAB7A	physical	26344197
RADI_HUMAN	RDX	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
STMN1_HUMAN	STMN1	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
TXND5_HUMAN	TXNDC5	physical	26344197
FINC_HUMAN	FN1	physical	28514442
CJ088_HUMAN	C10orf88	physical	28514442
H2AY_HUMAN	H2AFY	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 GDIB_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-61, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-269, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-61, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 SER-61, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, AND MASSSPECTROMETRY.	18083107 [Abstract]