RAC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAC1_MOUSE
• UniProt AC: P63001
• Protein Name: Ras-related C3 botulinum toxin substrate 1
• Gene Name: Rac1
• Organism: Mus musculus (Mouse).
• Sequence Length: 192
• Subcellular Localization: Cell membrane; Lipid-anchor; Cytoplasmic side. Melanosome. Cytoplasm. Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine. Found in the ruffled border (a late endosomal-like compartment in the pl
• Protein Description: Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3..
• Protein Sequence: MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL

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
6	S-nitrosylation	--MQAIKCVVVGDGA --CCCCEEEEECCCC	1.99	20925432
6	S-nitrosocysteine	--MQAIKCVVVGDGA --CCCCEEEEECCCC	1.99	-
17	Phosphorylation	GDGAVGKTCLLISYT CCCCCCCEEEEEEEE	11.49	-
22	Phosphorylation	GKTCLLISYTTNAFP CCEEEEEEEECCCCC	19.18	-
23	Phosphorylation	KTCLLISYTTNAFPG CEEEEEEEECCCCCC	15.58	-
24	Phosphorylation	TCLLISYTTNAFPGE EEEEEEEECCCCCCC	13.54	-
58	Phosphorylation	VNLGLWDTAGQEDYD ECEEEECCCCCCCHH	22.55	-
64	Phosphorylation	DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC	11.38	-
96	Ubiquitination	SFENVRAKWYPEVRH HHHCHHHHCCHHHHH	36.37	-
105	S-nitrosocysteine	YPEVRHHCPNTPIIL CHHHHHHCCCCCEEE	1.96	-
105	S-palmitoylation	YPEVRHHCPNTPIIL CHHHHHHCCCCCEEE	1.96	28526873
105	S-nitrosylation	YPEVRHHCPNTPIIL CHHHHHHCCCCCEEE	1.96	24895380
105	Glutathionylation	YPEVRHHCPNTPIIL CHHHHHHCCCCCEEE	1.96	24333276
108	Phosphorylation	VRHHCPNTPIILVGT HHHHCCCCCEEEEEE	10.87	26824392
116	Ubiquitination	PIILVGTKLDLRDDK CEEEEEECCCCCCCH	33.79	-
123	Ubiquitination	KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH	62.15	-
123	Acetylation	KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH	62.15	23806337
125	Phosphorylation	DLRDDKDTIEKLKEK CCCCCHHHHHHHHHC	36.45	29899451
128	Ubiquitination	DDKDTIEKLKEKKLT CCHHHHHHHHHCCCC	62.09	-
132	Acetylation	TIEKLKEKKLTPITY HHHHHHHCCCCCCCC	52.04	7631953
133	Ubiquitination	IEKLKEKKLTPITYP HHHHHHCCCCCCCCH	59.70	-
133	Acetylation	IEKLKEKKLTPITYP HHHHHHCCCCCCCCH	59.70	22826441
135	Phosphorylation	KLKEKKLTPITYPQG HHHHCCCCCCCCHHH	22.86	29899451
147	Ubiquitination	PQGLAMAKEIGAVKY HHHHHHHHHHCCEEE	36.46	-
153	Acetylation	AKEIGAVKYLECSAL HHHHCCEEEEECHHH	43.51	22826441
153	Ubiquitination	AKEIGAVKYLECSAL HHHHCCEEEEECHHH	43.51	-
157	S-palmitoylation	GAVKYLECSALTQRG CCEEEEECHHHHHHC	2.38	28526873
157	S-nitrosylation	GAVKYLECSALTQRG CCEEEEECHHHHHHC	2.38	24895380
157	Glutathionylation	GAVKYLECSALTQRG CCEEEEECHHHHHHC	2.38	24333276
157	S-nitrosocysteine	GAVKYLECSALTQRG CCEEEEECHHHHHHC	2.38	-
158	Phosphorylation	AVKYLECSALTQRGL CEEEEECHHHHHHCH	19.55	20531401
161	Phosphorylation	YLECSALTQRGLKTV EEECHHHHHHCHHHH	18.88	20415495
166	Ubiquitination	ALTQRGLKTVFDEAI HHHHHCHHHHHHHHH	45.53	-
167	Phosphorylation	LTQRGLKTVFDEAIR HHHHCHHHHHHHHHH	31.29	25177544
178	S-nitrosocysteine	EAIRAVLCPPPVKKR HHHHHHCCCCCCCCC	3.70	-
178	Glutathionylation	EAIRAVLCPPPVKKR HHHHHHCCCCCCCCC	3.70	24333276
178	S-nitrosylation	EAIRAVLCPPPVKKR HHHHHHCCCCCCCCC	3.70	24895380
183	Ubiquitination	VLCPPPVKKRKRKCL HCCCCCCCCCCCCEE	53.27	-
184	Ubiquitination	LCPPPVKKRKRKCLL CCCCCCCCCCCCEEC	64.48	-
189	Geranylgeranylation	VKKRKRKCLLL---- CCCCCCCEECC----	3.62	-
189	Methylation	VKKRKRKCLLL---- CCCCCCCEECC----	3.62	-

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

Oops, there are no upstream regulatory protein records of RAC1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAC1_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 RAC1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HACD3_HUMAN	PTPLAD1	genetic	10747961
HACD3_HUMAN	PTPLAD1	physical	10747961
RCC2_HUMAN	RCC2	physical	25074804
GDIR1_MOUSE	Arhgdia	physical	25074804

Drug and Disease Associations

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