dbPTM

RANG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RANG_HUMAN
UniProt AC	P43487
Protein Name	Ran-specific GTPase-activating protein
Gene Name	RANBP1
Organism	Homo sapiens (Human).
Sequence Length	201
Subcellular Localization
Protein Description	Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. [PubMed: 20485264 Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN]
Protein Sequence	MAAAKDTHEDHDTSTENTDESNHDPQFEPIVSLPEQEIKTLEEDEEELFKMRAKLFRFASENDLPEWKERGTGDVKLLKHKEKGAIRLLMRRDKTLKICANHYITPMMELKPNAGSDRAWVWNTHADFADECPKPELLAIRFLNAENAQKFKTKFEECRKEIEEREKKAGSGKNDHAEKVAEKLEALSVKEETKEDAEEKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAKDTHE ------CCCCCCCCC	19.00	19413330
5	Acetylation	---MAAAKDTHEDHD ---CCCCCCCCCCCC	59.44	23954790
7	Phosphorylation	-MAAAKDTHEDHDTS -CCCCCCCCCCCCCC	26.85	26503892
13	Phosphorylation	DTHEDHDTSTENTDE CCCCCCCCCCCCCCC	33.84	22167270
14	Phosphorylation	THEDHDTSTENTDES CCCCCCCCCCCCCCC	39.52	22167270
15	Phosphorylation	HEDHDTSTENTDESN CCCCCCCCCCCCCCC	35.03	22167270
18	Phosphorylation	HDTSTENTDESNHDP CCCCCCCCCCCCCCC	34.61	22167270
21	Phosphorylation	STENTDESNHDPQFE CCCCCCCCCCCCCCC	42.13	22167270
32	Phosphorylation	PQFEPIVSLPEQEIK CCCCCCCCCCHHHCC	38.64	23927012
39	Ubiquitination	SLPEQEIKTLEEDEE CCCHHHCCCCHHCHH	46.43	-
50	Acetylation	EDEEELFKMRAKLFR HCHHHHHHHHHHHHH	39.85	23236377
50	Ubiquitination	EDEEELFKMRAKLFR HCHHHHHHHHHHHHH	39.85	-
54	Acetylation	ELFKMRAKLFRFASE HHHHHHHHHHHHHCC	37.48	18527719
60	Phosphorylation	AKLFRFASENDLPEW HHHHHHHCCCCCHHH	33.93	19664994
68	Ubiquitination	ENDLPEWKERGTGDV CCCCHHHHHCCCCCC	35.55	21890473
68	Acetylation	ENDLPEWKERGTGDV CCCCHHHHHCCCCCC	35.55	25953088
68	Ubiquitination	ENDLPEWKERGTGDV CCCCHHHHHCCCCCC	35.55	21890473
68	Methylation	ENDLPEWKERGTGDV CCCCHHHHHCCCCCC	35.55	18527727
76	Ubiquitination	ERGTGDVKLLKHKEK HCCCCCCEEECHHHH	53.49	21890473
76	Ubiquitination	ERGTGDVKLLKHKEK HCCCCCCEEECHHHH	53.49	21890473
76	Acetylation	ERGTGDVKLLKHKEK HCCCCCCEEECHHHH	53.49	25953088
79	Acetylation	TGDVKLLKHKEKGAI CCCCEEECHHHHHHH	64.17	18527735
97	Acetylation	MRRDKTLKICANHYI HCCCCCHHHHCCCCC	40.76	25953088
99	Glutathionylation	RDKTLKICANHYITP CCCCHHHHCCCCCCC	2.72	22555962
103	Phosphorylation	LKICANHYITPMMEL HHHHCCCCCCCCEEC	13.29	28796482
105	Phosphorylation	ICANHYITPMMELKP HHCCCCCCCCEECCC	9.66	-
111	Ubiquitination	ITPMMELKPNAGSDR CCCCEECCCCCCCCC	23.95	21906983
111	Ubiquitination	ITPMMELKPNAGSDR CCCCEECCCCCCCCC	23.95	21890473
111	Acetylation	ITPMMELKPNAGSDR CCCCEECCCCCCCCC	23.95	20167786
132	Glutathionylation	HADFADECPKPELLA CCCCCHHCCCHHHEE	5.59	22555962
134	Acetylation	DFADECPKPELLAIR CCCHHCCCHHHEEHE	63.88	23954790
134	Ubiquitination	DFADECPKPELLAIR CCCHHCCCHHHEEHE	63.88	21906983
134	Ubiquitination	DFADECPKPELLAIR CCCHHCCCHHHEEHE	63.88	21890473
137	Phosphorylation	DECPKPELLAIRFLN HHCCCHHHEEHEECC	5.48	27251275
150	Ubiquitination	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	21890473
150	Acetylation	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	19608861
150	Succinylation	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	-
150	Succinylation	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	19608861
150	Ubiquitination	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	21890473
152	Acetylation	AENAQKFKTKFEECR HHHHHHHHHHHHHHH	58.82	20167786
154	Acetylation	NAQKFKTKFEECRKE HHHHHHHHHHHHHHH	51.90	23749302
154	Ubiquitination	NAQKFKTKFEECRKE HHHHHHHHHHHHHHH	51.90	-
160	Acetylation	TKFEECRKEIEEREK HHHHHHHHHHHHHHH	74.77	30583473
179	Acetylation	GKNDHAEKVAEKLEA CCCHHHHHHHHHHHH	47.75	25953088
182	Ubiquitination	DHAEKVAEKLEALSV HHHHHHHHHHHHHCC	62.25	21890473
182	Ubiquitination	DHAEKVAEKLEALSV HHHHHHHHHHHHHCC	62.25	19608861
182	Acetylation	DHAEKVAEKLEALSV HHHHHHHHHHHHHCC	62.25	19608861
183	Ubiquitination	HAEKVAEKLEALSVK HHHHHHHHHHHHCCC	41.72	21906983
183	Acetylation	HAEKVAEKLEALSVK HHHHHHHHHHHHCCC	41.72	19608861
188	Phosphorylation	AEKLEALSVKEETKE HHHHHHHCCCHHHHH	37.89	23401153
190	Acetylation	KLEALSVKEETKEDA HHHHHCCCHHHHHHH	46.59	26051181
190	Ubiquitination	KLEALSVKEETKEDA HHHHHCCCHHHHHHH	46.59	-
190	Sumoylation	KLEALSVKEETKEDA HHHHHCCCHHHHHHH	46.59	28112733
190	Sumoylation	KLEALSVKEETKEDA HHHHHCCCHHHHHHH	46.59	-
193	Phosphorylation	ALSVKEETKEDAEEK HHCCCHHHHHHHHHH	40.60	30108239
194	Acetylation	LSVKEETKEDAEEKQ HCCCHHHHHHHHHHC	57.80	26051181
200	Acetylation	TKEDAEEKQ------ HHHHHHHHC------	53.46	30583485
265	Phosphorylation	----------------------------------------------------------------------- -----------------------------------------------------------------------		27251275

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 RANG_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IMB1_HUMAN	KPNB1	physical	10473610
RAN_HUMAN	RAN	physical	10811801
XPO1_HUMAN	XPO1	physical	10601307
RAN_HUMAN	RAN	physical	10779340
IMB1_HUMAN	KPNB1	physical	10779340
RAN_HUMAN	RAN	physical	9111043
MDM2_HUMAN	MDM2	physical	12393906
RAN_HUMAN	RAN	physical	22939629
RCC1_HUMAN	RCC1	physical	22939629
RNA1_SCHPO	rna1	physical	11832950
IDHC_HUMAN	IDH1	physical	22863883
PLST_HUMAN	PLS3	physical	22863883
HERC5_HUMAN	HERC5	physical	24693865
VATD_HUMAN	ATP6V1D	physical	26344197
GOLP3_HUMAN	GOLPH3	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAN_HUMAN	RAN	physical	26344197
RNB3L_HUMAN	RANBP3L	physical	26344197
TADBP_HUMAN	TARDBP	physical	26344197

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 RANG_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-60, 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-150 AND LYS-183, 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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-60, 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 THR-7; THR-13; SER-14;THR-18 AND SER-21, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-14; THR-15;THR-18 AND SER-21, AND MASS SPECTROMETRY.	17287340 [Abstract]