RANG_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RANG_MOUSE
• UniProt AC: P34022
• Protein Name: Ran-specific GTPase-activating protein
• Gene Name: Ranbp1
• Organism: Mus musculus (Mouse).
• Sequence Length: 203
• 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. [PubMed: 9428644 Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (By similarity Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L]
• Protein Sequence: MAAAKDSHEDHDTSTENADESNHDPQFEPIVSLPEQEIKTLEEDEEELFKMRAKLFRFASENDLPEWKERGTGDVKLLKHKEKGTIRLLMRRDKTLKICANHYITPMMELKPNAGSDRAWVWNTHADFADECPKPELLAIRFLNAENAQKFKTKFEECRKEIEEREKKGPGKNDNAEKVAEKLEALSVREAREEAEEKSEEKQ

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAKDSHE ------CCCCCCCCC	19.00	-
7	Phosphorylation	-MAAAKDSHEDHDTS -CCCCCCCCCCCCCC	28.24	22802335
13	Phosphorylation	DSHEDHDTSTENADE CCCCCCCCCCCCCCC	33.84	21082442
14	Phosphorylation	SHEDHDTSTENADES CCCCCCCCCCCCCCC	39.52	21082442
15	Phosphorylation	HEDHDTSTENADESN CCCCCCCCCCCCCCC	35.04	22942356
21	Phosphorylation	STENADESNHDPQFE CCCCCCCCCCCCCCC	39.76	22942356
32	Phosphorylation	PQFEPIVSLPEQEIK CCCCCCCCCCHHHCC	38.64	25159016
50	Acetylation	EDEEELFKMRAKLFR HCHHHHHHHHHHHHH	39.85	23236377
50	Ubiquitination	EDEEELFKMRAKLFR HCHHHHHHHHHHHHH	39.85	22790023
60	Phosphorylation	AKLFRFASENDLPEW HHHHHHHCCCCCHHH	33.93	26824392
68	Ubiquitination	ENDLPEWKERGTGDV CCCCHHHHHCCCCCC	35.55	22790023
76	Ubiquitination	ERGTGDVKLLKHKEK HCCCCCCEEECCCCC	53.49	27667366
99	Glutathionylation	RDKTLKICANHYITP CCCCCHHHCCCCCCC	2.72	24333276
103	Phosphorylation	LKICANHYITPMMEL CHHHCCCCCCCCEEC	13.29	-
111	Acetylation	ITPMMELKPNAGSDR CCCCEECCCCCCCCC	23.95	22826441
132	Glutathionylation	HADFADECPKPELLA CCCCCHHCCCHHHEE	5.59	24333276
134	Acetylation	DFADECPKPELLAIR CCCHHCCCHHHEEHE	63.88	22826441
150	Ubiquitination	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	-
150	Acetylation	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	23806337
150	Succinylation	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	23806337
150	Succinylation	LNAENAQKFKTKFEE CCHHHHHHHHHHHHH	46.55	-
154	Acetylation	NAQKFKTKFEECRKE HHHHHHHHHHHHHHH	51.90	22826441
182	Succinylation	NAEKVAEKLEALSVR CHHHHHHHHHHHHHH	41.72	23806337
182	Acetylation	NAEKVAEKLEALSVR CHHHHHHHHHHHHHH	41.72	23806337
187	Phosphorylation	AEKLEALSVREAREE HHHHHHHHHHHHHHH	26.61	27180971
199	Phosphorylation	REEAEEKSEEKQ--- HHHHHHHHHHCC---	55.02	29895711

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RANG_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RANG_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RANG_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RCC1_HUMAN	RCC1	physical	26496610
IMB1_HUMAN	KPNB1	physical	26496610
RAN_HUMAN	RAN	physical	26496610
DSCR3_HUMAN	DSCR3	physical	26496610
COMD3_HUMAN	COMMD3	physical	26496610
TFP11_HUMAN	TFIP11	physical	26496610
PGAP2_HUMAN	PGAP2	physical	26496610
CCD22_HUMAN	CCDC22	physical	26496610
COMD5_HUMAN	COMMD5	physical	26496610
COMD9_HUMAN	COMMD9	physical	26496610
COMD2_HUMAN	COMMD2	physical	26496610
COMDA_HUMAN	COMMD10	physical	26496610
VPS29_HUMAN	VPS29	physical	26496610
CCD93_HUMAN	CCDC93	physical	26496610
COMD4_HUMAN	COMMD4	physical	26496610
COMD8_HUMAN	COMMD8	physical	26496610
CP062_HUMAN	C16orf62	physical	26496610
COMD1_HUMAN	COMMD1	physical	26496610
COMD6_HUMAN	COMMD6	physical	26496610
FA45A_HUMAN	FAM45A	physical	26496610

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.
PubMed: 14729942