RAC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAC3_HUMAN
• UniProt AC: P60763
• Protein Name: Ras-related C3 botulinum toxin substrate 3
• Gene Name: RAC3
• Organism: Homo sapiens (Human).
• Sequence Length: 192
• Subcellular Localization: Cytoplasm. Endomembrane system. Cell projection, lamellipodium. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton. Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodi
• Protein Description: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner..
• Protein Sequence: MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF

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
5	Ubiquitination	---MQAIKCVVVGDG ---CCCCEEEEECCC	24.80	-
6	S-palmitoylation	--MQAIKCVVVGDGA --CCCCEEEEECCCC	1.99	29575903
32	Phosphorylation	TNAFPGEYIPTVFDN CCCCCCCCCCCEECC	20.37	22817900
32	O-linked_Glycosylation	TNAFPGEYIPTVFDN CCCCCCCCCCCEECC	20.37	24141704
64	Phosphorylation	DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC	11.38	28796482
71	Phosphorylation	YDRLRPLSYPQTDVF HHHCCCCCCCCCCEE	37.13	18669648
89	Phosphorylation	FSLVSPASFENVRAK EECCCHHHHHCHHHH	36.16	-
96	Ubiquitination	SFENVRAKWYPEVRH HHHCHHHHCCHHHHH	36.37	27667366
96	Acetylation	SFENVRAKWYPEVRH HHHCHHHHCCHHHHH	36.37	25953088
98	Phosphorylation	ENVRAKWYPEVRHHC HCHHHHCCHHHHHHC	6.71	28152594
116	Ubiquitination	PILLVGTKLDLRDDK CEEEEEEECCCCCCH	33.79	32015554
133	Ubiquitination	IERLRDKKLAPITYP HHHHHHCCCCCCCCC	54.92	29967540
139	Phosphorylation	KKLAPITYPQGLAMA CCCCCCCCCHHHHHH	8.35	-
153	Ubiquitination	AREIGSVKYLECSAL HHHHCCEEEEECHHH	45.90	27667366
154	Phosphorylation	REIGSVKYLECSALT HHHCCEEEEECHHHH	12.94	28152594
157	S-palmitoylation	GSVKYLECSALTQRG CCEEEEECHHHHHHC	2.38	29575903
161	Phosphorylation	YLECSALTQRGLKTV EEECHHHHHHCHHHH	18.88	25850435
163	Methylation	ECSALTQRGLKTVFD ECHHHHHHCHHHHHH	47.37	-
166	Ubiquitination	ALTQRGLKTVFDEAI HHHHHCHHHHHHHHH	45.53	23000965
167	Phosphorylation	LTQRGLKTVFDEAIR HHHHCHHHHHHHHHH	31.29	21082442
183	Neddylation	VLCPPPVKKPGKKCT HCCCCCCCCCCCCCC	60.05	32015554
183	Ubiquitination	VLCPPPVKKPGKKCT HCCCCCCCCCCCCCC	60.05	21139048
183	Malonylation	VLCPPPVKKPGKKCT HCCCCCCCCCCCCCC	60.05	26320211
184	Ubiquitination	LCPPPVKKPGKKCTV CCCCCCCCCCCCCCC	60.27	29967540
189	Methylation	VKKPGKKCTVF---- CCCCCCCCCCC----	4.46	-
189	Geranylgeranylation	VKKPGKKCTVF---- CCCCCCCCCCC----	4.46	-

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

Oops, there are no upstream regulatory protein records of RAC3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAC3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RAC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CIB1_HUMAN	CIB1	physical	11756406
GDIR2_HUMAN	ARHGDIB	physical	21900206
GDIR1_HUMAN	ARHGDIA	physical	21900206
ESR1_HUMAN	ESR1	physical	21217774
FXL19_HUMAN	FBXL19	physical	24684802

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-167, AND MASSSPECTROMETRY.
PubMed: 18669648