dbPTM

RAN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAN_HUMAN
UniProt AC	P62826
Protein Name	GTP-binding nuclear protein Ran
Gene Name	RAN
Organism	Homo sapiens (Human).
Sequence Length	216
Subcellular Localization	Nucleus . Nucleus envelope . Cytoplasm, cytosol . Cytoplasm . Melanosome . Predominantly nuclear during interphase (PubMed:8421051, PubMed:12194828, PubMed:10679025). Becomes dispersed throughout the cytoplasm during mitosis (PubMed:8421051, PubMed:1
Protein Description	GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. [PubMed: 10400640]
Protein Sequence	MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAQGEPQV ------CCCCCCCEE	14.43	22223895
12	Methylation	GEPQVQFKLVLVGDG CCCEEEEEEEEEECC	22.16	115976171
21	Phosphorylation	VLVGDGGTGKTTFVK EEEECCCCCCEEEEE	40.82	29255136
23	2-Hydroxyisobutyrylation	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	-
23	Ubiquitination	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	21890473
23	Acetylation	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	25953088
23	Ubiquitination	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	21890473
24	Phosphorylation	GDGGTGKTTFVKRHL ECCCCCCEEEEEECC	27.15	23186163
25	Phosphorylation	DGGTGKTTFVKRHLT CCCCCCEEEEEECCC	29.89	-
28	Ubiquitination	TGKTTFVKRHLTGEF CCCEEEEEECCCCCC	29.88	-
28	Acetylation	TGKTTFVKRHLTGEF CCCEEEEEECCCCCC	29.88	26051181
29	Methylation	GKTTFVKRHLTGEFE CCEEEEEECCCCCCC	25.42	115490227
32	Phosphorylation	TFVKRHLTGEFEKKY EEEEECCCCCCCEEE	28.65	20873877
37	Ubiquitination	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	31075303
37	Acetylation	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	26822725
37	Succinylation	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	23954790
37	Methylation	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	31075303
37	2-Hydroxyisobutyrylation	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	-
38	Acetylation	LTGEFEKKYVATLGV CCCCCCEEEEEEEEC	37.45	23749302
38	Ubiquitination	LTGEFEKKYVATLGV CCCCCCEEEEEEEEC	37.45	-
38	Ubiquitination	LTGEFEKKYVATLGV CCCCCCEEEEEEEEC	37.45	21890473
38	Malonylation	LTGEFEKKYVATLGV CCCCCCEEEEEEEEC	37.45	26320211
39	Phosphorylation	TGEFEKKYVATLGVE CCCCCEEEEEEEECE	13.34	24927040
42	Phosphorylation	FEKKYVATLGVEVHP CCEEEEEEEECEEEE	17.63	28152594
60	2-Hydroxyisobutyrylation	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	-
60	Ubiquitination	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	21890473
60	Ubiquitination	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	21890473
60	Acetylation	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	19608861
60	Methylation	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	19608861
71	2-Hydroxyisobutyrylation	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	-
71	Sumoylation	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	28112733
71	Ubiquitination	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	19608861
71	Acetylation	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	19608861
71	Ubiquitination	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	21890473
79	Phosphorylation	FGGLRDGYYIQAQCA CCCCCCCEEEEEEEE	11.15	24043423
80	Phosphorylation	GGLRDGYYIQAQCAI CCCCCCEEEEEEEEE	7.65	24043423
93	Phosphorylation	AIIMFDVTSRVTYKN EEEEEECCCCCEECC	16.80	21955146
94	Phosphorylation	IIMFDVTSRVTYKNV EEEEECCCCCEECCC	25.30	24043423
98	Phosphorylation	DVTSRVTYKNVPNWH ECCCCCEECCCCCHH	9.56	21955146
99	Ubiquitination	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	21890473
99	Malonylation	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	26320211
99	2-Hydroxyisobutyrylation	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	-
99	Ubiquitination	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	19608861
99	Acetylation	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	19608861
112	S-nitrosylation	HRDLVRVCENIPIVL HHHHHHHHCCCCEEE	2.02	22178444
112	S-palmitoylation	HRDLVRVCENIPIVL HHHHHHHHCCCCEEE	2.02	29575903
112	S-nitrosocysteine	HRDLVRVCENIPIVL HHHHHHHHCCCCEEE	2.02	-
120	S-nitrosylation	ENIPIVLCGNKVDIK CCCCEEECCCCCCCC	3.80	22178444
120	S-palmitoylation	ENIPIVLCGNKVDIK CCCCEEECCCCCCCC	3.80	29575903
120	S-nitrosocysteine	ENIPIVLCGNKVDIK CCCCEEECCCCCCCC	3.80	-
123	Ubiquitination	PIVLCGNKVDIKDRK CEEECCCCCCCCCCE	26.94	-
123	2-Hydroxyisobutyrylation	PIVLCGNKVDIKDRK CEEECCCCCCCCCCE	26.94	-
123	Acetylation	PIVLCGNKVDIKDRK CEEECCCCCCCCCCE	26.94	25953088
127	Succinylation	CGNKVDIKDRKVKAK CCCCCCCCCCEEECE	47.20	23954790
127	Malonylation	CGNKVDIKDRKVKAK CCCCCCCCCCEEECE	47.20	26320211
127	Acetylation	CGNKVDIKDRKVKAK CCCCCCCCCCEEECE	47.20	25953088
127	Ubiquitination	CGNKVDIKDRKVKAK CCCCCCCCCCEEECE	47.20	-
130	Ubiquitination	KVDIKDRKVKAKSIV CCCCCCCEEECEEEE	59.21	-
134	Ubiquitination	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	21890473
134	Ubiquitination	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	29040603
134	Acetylation	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	29040603
134	2-Hydroxyisobutyrylation	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	-
135	Phosphorylation	DRKVKAKSIVFHRKK CCEEECEEEEEEECC	28.92	23401153
141	Malonylation	KSIVFHRKKNLQYYD EEEEEEECCCCEEEE	37.13	26320211
141	Ubiquitination	KSIVFHRKKNLQYYD EEEEEEECCCCEEEE	37.13	-
142	Malonylation	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	26320211
142	Acetylation	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	23236377
142	2-Hydroxyisobutyrylation	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	-
142	Ubiquitination	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	-
142	Ubiquitination	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	21890473
146	Phosphorylation	HRKKNLQYYDISAKS EECCCCEEEECCCCC	13.28	25159151
147	Nitration	RKKNLQYYDISAKSN ECCCCEEEECCCCCC	8.21	-
147	Phosphorylation	RKKNLQYYDISAKSN ECCCCEEEECCCCCC	8.21	27273156
150	Phosphorylation	NLQYYDISAKSNYNF CCEEEECCCCCCCCC	27.09	28152594
152	Ubiquitination	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	-
152	Sumoylation	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	-
152	Succinylation	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	23954790
152	Acetylation	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	23236377
152	Ubiquitination	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	21890473
153	Phosphorylation	YYDISAKSNYNFEKP EEECCCCCCCCCCCH	44.24	28152594
155	Phosphorylation	DISAKSNYNFEKPFL ECCCCCCCCCCCHHH	28.46	27273156
159	Ubiquitination	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	19608861
159	Succinylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	-
159	Ubiquitination	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	21890473
159	2-Hydroxyisobutyrylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	-
159	Succinylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	19608861
159	Methylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	19608861
159	Acetylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	19608861
159	Sumoylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	19608861
167	Ubiquitination	PFLWLARKLIGDPNL HHHHHHHHHHCCCCC	38.56	-

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
135	S	Phosphorylation	Kinase	PAK4	O96013	PSP
135	S	Phosphorylation	Kinase	PLK1	P53350	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
37	K	Acetylation	31075303
Acetylation at Lys-37 enhances the association with nuclear export components.
37	K	Acetylation	31075303
Deacetylation of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit RELA/p65.
134	K	Acetylation	29040603
Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding.

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 RAN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RANG_HUMAN	RANBP1	physical	7891706
RRP44_YEAST	DIS3	physical	8896453
XPO1_HUMAN	XPO1	physical	12070164
CE126_HUMAN	KIAA1377	physical	16169070
NEK9_HUMAN	NEK9	physical	12101123
RANG_HUMAN	RANBP1	physical	10811801
NTF2_HUMAN	NUTF2	physical	9533885
RCC1_HUMAN	RCC1	physical	10369786
XPO1_HUMAN	XPO1	physical	9323133
TNPO1_HUMAN	TNPO1	physical	10353245
XPO5_HUMAN	XPO5	physical	11777942
XPOT_HUMAN	XPOT	physical	12138183
ABL1_HUMAN	ABL1	physical	11420673
RAGP1_HUMAN	RANGAP1	physical	7744835
RAGP1_HUMAN	RANGAP1	physical	8146159
TNPO2_HUMAN	TNPO2	physical	12384575
TNPO1_HUMAN	TNPO1	physical	12384575
NXF1_HUMAN	NXF1	physical	12384575
RCC1_HUMAN	RCC1	physical	7988569
RCC1_HUMAN	RCC1	physical	7882974
RANG_HUMAN	RANBP1	physical	7882974
RCC1_HUMAN	RCC1	physical	10827954
RAGP1_HUMAN	RANGAP1	physical	20805321
XRCC1_HUMAN	XRCC1	physical	20805321
NTF2_HUMAN	NUTF2	physical	20805321
RANG_HUMAN	RANBP1	physical	20805321
IMB1_HUMAN	KPNB1	physical	10037787
RANG_HUMAN	RANBP1	physical	12649209
IPO7_HUMAN	IPO7	physical	11024021
XPOT_HUMAN	XPOT	physical	11024021
IMB1_HUMAN	KPNB1	physical	11024021
TNPO1_HUMAN	TNPO1	physical	11024021
XPO7_HUMAN	XPO7	physical	11024021
ESR1_HUMAN	ESR1	physical	22266855
IPO13_HUMAN	IPO13	physical	17828378
RBP2_HUMAN	RANBP2	physical	7603572
RANG_HUMAN	RANBP1	physical	7603572
IPO11_HUMAN	IPO11	physical	15545318
MD2L2_HUMAN	MAD2L2	physical	19753112
XPO4_HUMAN	XPO4	physical	10944119
IPO5_HUMAN	IPO5	physical	10944119
IPO7_HUMAN	IPO7	physical	10944119
XPOT_HUMAN	XPOT	physical	10944119
IMB1_HUMAN	KPNB1	physical	10944119
TNPO1_HUMAN	TNPO1	physical	10944119
XPO1_HUMAN	XPO1	physical	10944119
RANG_HUMAN	RANBP1	physical	9315840
XPO1_HUMAN	XPO1	physical	22939629
RCC1_HUMAN	RCC1	physical	22939629
TNPO1_HUMAN	TNPO1	physical	22939629
TPR_HUMAN	TPR	physical	22939629
RBM39_HUMAN	RBM39	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
TRA2B_HUMAN	TRA2B	physical	22939629
SON_HUMAN	SON	physical	22939629
IMA1_HUMAN	KPNA2	physical	9428644
XPO2_HUMAN	CSE1L	physical	9428644
RANG_MOUSE	Ranbp1	physical	9428644
XPO5_HUMAN	XPO5	physical	20951941
RNA1_SCHPO	rna1	physical	11832950
RANG_HUMAN	RANBP1	physical	11832950
RBP2_HUMAN	RANBP2	physical	21988832
RGPD5_HUMAN	RGPD5	physical	21988832
PFD4_HUMAN	PFDN4	physical	22863883
NTF2_HUMAN	NUTF2	physical	25416956
HERC5_HUMAN	HERC5	physical	24693865
BIRC5_HUMAN	BIRC5	physical	23251006
GDE_HUMAN	AGL	physical	26344197
IF6_HUMAN	EIF6	physical	26344197
EXOS2_HUMAN	EXOSC2	physical	26344197
IPO7_HUMAN	IPO7	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
IMA6_HUMAN	KPNA5	physical	26344197
NTF2_HUMAN	NUTF2	physical	26344197
RBP2_HUMAN	RANBP2	physical	26344197
RNBP6_HUMAN	RANBP6	physical	26344197
XPO1_HUMAN	XPO1	physical	26344197
RGPD2_HUMAN	RGPD2	physical	28514442
RGPD8_HUMAN	RGPD8	physical	28514442
MOG1_HUMAN	RANGRF	physical	28514442
RGPD5_HUMAN	RGPD5	physical	28514442
RCC1_HUMAN	RCC1	physical	28514442
NEMP2_HUMAN	TMEM194B	physical	28514442
DLGP5_HUMAN	DLGAP5	physical	28514442
RBP2_HUMAN	RANBP2	physical	28514442
CDCA2_HUMAN	CDCA2	physical	28514442
RAGP1_HUMAN	RANGAP1	physical	28514442
NU153_HUMAN	NUP153	physical	28514442
NEMP1_HUMAN	TMEM194A	physical	28514442
NU214_HUMAN	NUP214	physical	28514442
NTF2_HUMAN	NUTF2	physical	28514442
IMB1_HUMAN	KPNB1	physical	28514442
AKIR1_HUMAN	AKIRIN1	physical	28514442
NUP62_HUMAN	NUP62	physical	28514442
IPO9_HUMAN	IPO9	physical	28514442
IMA3_HUMAN	KPNA4	physical	28514442
IKIP_HUMAN	IKBIP	physical	28514442
PAR14_MOUSE	Parp14	physical	23473667

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 RAN_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]
"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-60; LYS-71; LYS-99 ANDLYS-159, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND MASSSPECTROMETRY.	19534553 [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-147 AND TYR-155, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"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-147, AND MASSSPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASSSPECTROMETRY.	18781797 [Abstract]

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