dbPTM

RGAP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RGAP1_MOUSE
UniProt AC	Q9WVM1
Protein Name	Rac GTPase-activating protein 1
Gene Name	Racgap1 {ECO:0000312\|MGI:MGI:1349423}
Organism	Mus musculus (Mouse).
Sequence Length	628
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasm, cytoskeleton, spindle . Cytoplasmic vesicle, secretory vesicle, acrosome . Cleavage furrow . Midbody, Midbody ring . Cell membrane Peripheral membrane protein Cytoplasmic side . During interphase, localized to the
Protein Description	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells..
Protein Sequence	MDTTMVNLWTLFEQLVRRMEIINEGNESIEFIQVVKDFEDFRKKYQRTNQELEKFKDLLLKAETGRSALDVKLKHARNQVDVEIKRRQRAEAECAKLEQQIQLIRDILMCDTSGSIQLSEEQKSALAFLNRGQASSGHAGNNRLSTIDESGSILSDISFDKTDESLDWDSSLVKNFKMKKREKRRSNSRQFIDGPPGPVKKTCSIGSTVDQANESIVAKTTVTVPSDGGPIEAVSTIETLPSWTRSRGKSGPLQPVNSDSALNSRPLEPRTDTDNLGTPQNTGGMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRLVSHPECRDRCPLPCIPPLVGTPVKIGEGMLADFVSQASPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHVICSLLKDFLRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVSQSPDTKMDIANLAKVFGPTIVAHTVPNPDPVTMFQDIKRQLKVVERLLSLPLEYWNQFMMVDQENIDSQRGNGNSTPRTPDVKVSLLGPVTTPEFQLVKTPLSSSLSQRLYNLSKSTPRFGNKSKSATNLGQQGKFFPAPYLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDTTMVNL -------CCCHHHHH	10.49	-
119	Phosphorylation	TSGSIQLSEEQKSAL CCCCEECCHHHHHHH	23.78	28973931
123	Ubiquitination	IQLSEEQKSALAFLN EECCHHHHHHHHHHH	40.76	-
124	Phosphorylation	QLSEEQKSALAFLNR ECCHHHHHHHHHHHH	28.36	26824392
145	Phosphorylation	HAGNNRLSTIDESGS CCCCCCCCCCCCCCC	21.78	18846507
146	Phosphorylation	AGNNRLSTIDESGSI CCCCCCCCCCCCCCC	36.72	26643407
150	Phosphorylation	RLSTIDESGSILSDI CCCCCCCCCCCCCCC	33.81	26643407
152	Phosphorylation	STIDESGSILSDISF CCCCCCCCCCCCCCC	29.63	26643407
155	Phosphorylation	DESGSILSDISFDKT CCCCCCCCCCCCCCC	31.09	26643407
158	Phosphorylation	GSILSDISFDKTDES CCCCCCCCCCCCCCC	32.17	26643407
162	Phosphorylation	SDISFDKTDESLDWD CCCCCCCCCCCCCCC	47.01	26643407
165	Phosphorylation	SFDKTDESLDWDSSL CCCCCCCCCCCCHHH	34.14	26643407
170	Phosphorylation	DESLDWDSSLVKNFK CCCCCCCHHHHHHHH	22.71	26370283
171	Phosphorylation	ESLDWDSSLVKNFKM CCCCCCHHHHHHHHC	34.41	22817900
174	Acetylation	DWDSSLVKNFKMKKR CCCHHHHHHHHCHHH	63.06	7614671
186	Phosphorylation	KKREKRRSNSRQFID HHHHHHHHCCCCCCC	43.09	26643407
188	Phosphorylation	REKRRSNSRQFIDGP HHHHHHCCCCCCCCC	28.80	26643407
202	Phosphorylation	PPGPVKKTCSIGSTV CCCCCCCCCCCCCCC	13.03	25619855
204	Phosphorylation	GPVKKTCSIGSTVDQ CCCCCCCCCCCCCCC	34.90	25619855
207	Phosphorylation	KKTCSIGSTVDQANE CCCCCCCCCCCCCCC	24.48	25619855
208	Phosphorylation	KTCSIGSTVDQANES CCCCCCCCCCCCCCC	23.92	25619855
215	Phosphorylation	TVDQANESIVAKTTV CCCCCCCCEEEEEEE	23.36	25619855
220	Phosphorylation	NESIVAKTTVTVPSD CCCEEEEEEEEECCC	19.43	26643407
221	Phosphorylation	ESIVAKTTVTVPSDG CCEEEEEEEEECCCC	17.30	26643407
223	Phosphorylation	IVAKTTVTVPSDGGP EEEEEEEEECCCCCE	25.30	26643407
226	Phosphorylation	KTTVTVPSDGGPIEA EEEEEECCCCCEEEE	44.55	26643407
235	Phosphorylation	GGPIEAVSTIETLPS CCEEEEEEEEEECCH	30.62	26643407
236	Phosphorylation	GPIEAVSTIETLPSW CEEEEEEEEEECCHH	19.08	26643407
249	Acetylation	SWTRSRGKSGPLQPV HHHHCCCCCCCCCCC	51.64	23806337
250	Phosphorylation	WTRSRGKSGPLQPVN HHHCCCCCCCCCCCC	48.76	26824392
258	Phosphorylation	GPLQPVNSDSALNSR CCCCCCCCCCCHHCC	32.93	26824392
260	Phosphorylation	LQPVNSDSALNSRPL CCCCCCCCCHHCCCC	34.18	26643407
264	Phosphorylation	NSDSALNSRPLEPRT CCCCCHHCCCCCCCC	35.80	22817900
278	Phosphorylation	TDTDNLGTPQNTGGM CCCCCCCCCCCCCCC	25.52	25263469
282	Phosphorylation	NLGTPQNTGGMRLHD CCCCCCCCCCCCHHH	29.84	26643407
293	Ubiquitination	RLHDFVSKTVIKPES CHHHHHHCCCCCCHH	41.32	-
297	Acetylation	FVSKTVIKPESCVPC HHHCCCCCCHHHCCC	38.09	15607653
300	Phosphorylation	KTVIKPESCVPCGKR CCCCCCHHHCCCCCE	29.01	22067460
306	Acetylation	ESCVPCGKRIKFGKL HHHCCCCCEEEECCE	58.63	15607663
314	Phosphorylation	RIKFGKLSLKCRDCR EEEECCEEEEECCCE	29.30	22067460
343	Phosphorylation	CIPPLVGTPVKIGEG CCCCCCCCCEEECCC	19.89	26824392
388	Phosphorylation	EAGLYRISGCDRTVK HHHCHHHCCCCHHHH	25.11	-
406	Phosphorylation	EKFLKVKTVPLLSKV HHHCCCCCCCCCCCC	30.28	21743459
411	Phosphorylation	VKTVPLLSKVDDIHV CCCCCCCCCCCHHHH	38.01	21743459
491	Ubiquitination	VSQSPDTKMDIANLA HHCCCCCHHHHHHHH	41.79	-
560	Phosphorylation	SQRGNGNSTPRTPDV CCCCCCCCCCCCCCC	40.98	24759943
561	Phosphorylation	QRGNGNSTPRTPDVK CCCCCCCCCCCCCCE	22.31	25263469
564	Phosphorylation	NGNSTPRTPDVKVSL CCCCCCCCCCCEEEE	25.66	25263469
570	Phosphorylation	RTPDVKVSLLGPVTT CCCCCEEEEECCCCC	16.50	23984901
576	Phosphorylation	VSLLGPVTTPEFQLV EEEECCCCCCCEEEE	39.50	26239621
577	Phosphorylation	SLLGPVTTPEFQLVK EEECCCCCCCEEEEE	22.51	26824392
584	Ubiquitination	TPEFQLVKTPLSSSL CCCEEEEECCCCCHH	53.68	-
585	Phosphorylation	PEFQLVKTPLSSSLS CCEEEEECCCCCHHH	23.22	26824392
588	Phosphorylation	QLVKTPLSSSLSQRL EEEECCCCCHHHHHH	21.05	26745281
589	Phosphorylation	LVKTPLSSSLSQRLY EEECCCCCHHHHHHH	42.87	26745281
590	Phosphorylation	VKTPLSSSLSQRLYN EECCCCCHHHHHHHH	28.76	26745281
592	Phosphorylation	TPLSSSLSQRLYNLS CCCCCHHHHHHHHHH	18.40	26745281
596	Phosphorylation	SSLSQRLYNLSKSTP CHHHHHHHHHHCCCC	19.08	26643407
599	Phosphorylation	SQRLYNLSKSTPRFG HHHHHHHHCCCCCCC	22.41	26643407
601	Phosphorylation	RLYNLSKSTPRFGNK HHHHHHCCCCCCCCC	40.02	25263469
602	Phosphorylation	LYNLSKSTPRFGNKS HHHHHCCCCCCCCCC	23.40	25263469
609	Phosphorylation	TPRFGNKSKSATNLG CCCCCCCCCCCCCCC	35.52	28066266
611	Phosphorylation	RFGNKSKSATNLGQQ CCCCCCCCCCCCCCC	47.63	28066266
613	Phosphorylation	GNKSKSATNLGQQGK CCCCCCCCCCCCCCC	37.76	28066266
626	Phosphorylation	GKFFPAPYLK----- CCCCCCCCCC-----	29.27	-

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
150	S	Phosphorylation	Kinase	PLK1	Q07832	Uniprot
158	S	Phosphorylation	Kinase	PLK1	Q07832	Uniprot
165	S	Phosphorylation	Kinase	PLK1	Q07832	Uniprot
171	S	Phosphorylation	Kinase	PLK1	Q07832	Uniprot
388	S	Phosphorylation	Kinase	AURKB	O70126	Uniprot
411	S	Phosphorylation	Kinase	AURKB	O70126	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
158	S	Phosphorylation	-
Phosphorylation on Ser-158 does not appear to contribute to binding to ECT2 (By similarity).
165	S	Phosphorylation	-
Phosphorylation on Ser-165 plays a major role in mediating interaction with ECT2 (By similarity).
388	S	Phosphorylation	-
Phosphorylation by AURKB on Ser-388 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA (By similarity).

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 RGAP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KIF23_HUMAN	KIF23	physical	20360068
MICA3_HUMAN	MICAL3	physical	20360068
PRC1_HUMAN	PRC1	physical	20360068
RGAP1_HUMAN	RACGAP1	physical	20360068
SH3K1_HUMAN	SH3KBP1	physical	20360068
CD2AP_HUMAN	CD2AP	physical	20360068
SHCBP_HUMAN	SHCBP1	physical	20360068
ACTA_HUMAN	ACTA2	physical	26496610
ANX11_HUMAN	ANXA11	physical	26496610
DDX3X_HUMAN	DDX3X	physical	26496610
IF5A1_HUMAN	EIF5A	physical	26496610
FLNA_HUMAN	FLNA	physical	26496610
NAB1_HUMAN	NAB1	physical	26496610
RASN_HUMAN	NRAS	physical	26496610
PAK2_HUMAN	PAK2	physical	26496610
RPB3_HUMAN	POLR2C	physical	26496610
RPB7_HUMAN	POLR2G	physical	26496610
SAFB1_HUMAN	SAFB	physical	26496610
MANF_HUMAN	MANF	physical	26496610
EEA1_HUMAN	EEA1	physical	26496610
GUAA_HUMAN	GMPS	physical	26496610
FUBP1_HUMAN	FUBP1	physical	26496610
MTA2_HUMAN	MTA2	physical	26496610
KIF23_HUMAN	KIF23	physical	26496610
ML12A_HUMAN	MYL12A	physical	26496610
GA2L1_HUMAN	GAS2L1	physical	26496610
IL24_HUMAN	IL24	physical	26496610
TADBP_HUMAN	TARDBP	physical	26496610
PPIL2_HUMAN	PPIL2	physical	26496610
GPKOW_HUMAN	GPKOW	physical	26496610
NOB1_HUMAN	NOB1	physical	26496610
ASCC1_HUMAN	ASCC1	physical	26496610
PF21A_HUMAN	PHF21A	physical	26496610
FXL19_HUMAN	FBXL19	physical	26496610
ELP3_HUMAN	ELP3	physical	26496610
RCC2_HUMAN	RCC2	physical	26496610
CSN7B_HUMAN	COPS7B	physical	26496610
SHCBP_HUMAN	SHCBP1	physical	26496610
F192A_HUMAN	FAM192A	physical	26496610
CCNL2_HUMAN	CCNL2	physical	26496610
K2013_HUMAN	KIAA2013	physical	26496610
ESCO1_HUMAN	ESCO1	physical	26496610
RB12B_HUMAN	RBM12B	physical	26496610

Drug and Disease Associations

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

Regulatory Network of RGAP1_MOUSE

Related Literatures of Post-Translational Modification

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