dbPTM

RAGP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAGP1_MOUSE
UniProt AC	P46061
Protein Name	Ran GTPase-activating protein 1
Gene Name	Rangap1
Organism	Mus musculus (Mouse).
Sequence Length	589
Subcellular Localization	Cytoplasm . Nucleus, nucleoplasm . Nucleus envelope . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Cytoplasmic during interphase (PubMed:26506250). Detected at the nuclear envelope during interphase (PubMed:9442102, PubMed
Protein Description	GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export. [PubMed: 18305100 Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity Required for postimplantation embryonic development]
Protein Sequence	MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEPPQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASEDIAKL ------CCHHHHHHH	22.94	-
3	Phosphorylation	-----MASEDIAKLA -----CCHHHHHHHH	34.21	-
8	Acetylation	MASEDIAKLAETLAK CCHHHHHHHHHHHHH	48.87	23806337
15	Ubiquitination	KLAETLAKTQVAGGQ HHHHHHHHHCCCCCC	42.47	-
24	Phosphorylation	QVAGGQLSFKGKGLK CCCCCCCEECCCCCC	19.61	23140645
60	Phosphorylation	ALRLEGNTVGVEAAR EEEECCCCHHHHHHH	29.50	21082442
71	Succinylation	EAARVIAKALEKKSE HHHHHHHHHHHHHHH	42.24	24315375
169	S-palmitoylation	LAAALTECHRKSSAQ HHHHHHHHHHHHCCC	2.95	26165157
296	Ubiquitination	RGGLPKLKELNLSFC HCCCCHHHHCCCCHH	67.30	-
301	Phosphorylation	KLKELNLSFCEIKRD HHHHCCCCHHCCHHH	27.12	-
356	Phosphorylation	NMAKVLASLSDDEGE CHHHHHHHCCCCCCC	25.01	25338131
358	Phosphorylation	AKVLASLSDDEGEDE HHHHHHCCCCCCCCC	40.29	23649490
405	Phosphorylation	EEPPQRGSGEEPATP CCCCCCCCCCCCCCC	45.26	25521595
411	Phosphorylation	GSGEEPATPSRKILD CCCCCCCCCCCCCCC	32.29	26824392
413	Phosphorylation	GEEPATPSRKILDPN CCCCCCCCCCCCCCC	41.68	25159016
421	Phosphorylation	RKILDPNSGEPAPVL CCCCCCCCCCCCCCC	50.34	21659604
429	Phosphorylation	GEPAPVLSSPTPTDL CCCCCCCCCCCCCCH	34.21	27087446
430	Phosphorylation	EPAPVLSSPTPTDLS CCCCCCCCCCCCCHH	28.73	26824392
432	Phosphorylation	APVLSSPTPTDLSTF CCCCCCCCCCCHHHH	40.54	26824392
434	Phosphorylation	VLSSPTPTDLSTFLS CCCCCCCCCHHHHHH	52.64	27087446
437	Phosphorylation	SPTPTDLSTFLSFPS CCCCCCHHHHHHCCC	21.66	27087446
438	Phosphorylation	PTPTDLSTFLSFPSP CCCCCHHHHHHCCCH	35.57	27087446
441	Phosphorylation	TDLSTFLSFPSPEKL CCHHHHHHCCCHHHH	30.81	22942356
444	Phosphorylation	STFLSFPSPEKLLRL HHHHHCCCHHHHHHH	43.62	26824392
526	Sumoylation	LIHMGLLKSEDKIKA HHHHCCCCCHHHHHC	57.76	-
526	Sumoylation	LIHMGLLKSEDKIKA HHHHCCCCCHHHHHC	57.76	28289178
526	Acetylation	LIHMGLLKSEDKIKA HHHHCCCCCHHHHHC	57.76	23236377
567	Ubiquitination	LLLAFVTKPNGALET HHHHHHCCCCCHHHH	31.05	-
575	S-palmitoylation	PNGALETCSFARHNL CCCHHHHCHHHHHHH	1.99	26165157

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
411	T	Phosphorylation	Kinase	CDK1	P06493	PSP
411	T	Phosphorylation	Kinase	CDK2	P24941	PSP
411	T	Phosphorylation	Kinase	CDK2	P97377	Uniprot
444	S	Phosphorylation	Kinase	CDK1	P06493	PSP
444	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAGP1_MOUSE !!

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 RAGP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBP2_HUMAN	RANBP2	physical	9456312
FYB1_MOUSE	Fyb	physical	29127148
UBC9_MOUSE	Ube2i	physical	29127148

Drug and Disease Associations

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

Regulatory Network of RAGP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASSSPECTROMETRY.	19131326 [Abstract]
*"RanGAP1SUMO1 is phosphorylated at the onset of mitosis and remainsassociated with RanBP2 upon NPC disassembly.";** Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L.,Melchior F.; J. Cell Biol. 164:965-971(2004). Cited for: PHOSPHORYLATION AT THR-411 AND SER-444, AND MUTAGENESIS OF THR-411 ANDSER-444.	15037602 [Abstract]
Sumoylation
Reference	PubMed
"SUMO modification through rapamycin-mediated heterodimerizationreveals a dual role for Ubc9 in targeting RanGAP1 to nuclear porecomplexes."; Zhu S., Zhang H., Matunis M.J.; Exp. Cell Res. 312:1042-1049(2006). Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF LYS-526.	16469311 [Abstract]
"SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex."; Matunis M.J., Wu J., Blobel G.; J. Cell Biol. 140:499-509(1998). Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF LYS-526 AND PHE-564.	9456312 [Abstract]
"Molecular characterization of the SUMO-1 modification of RanGAP1 andits role in nuclear envelope association."; Mahajan R., Gerace L., Melchior F.; J. Cell Biol. 140:259-270(1998). Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF LYS-526.	9442102 [Abstract]