RAC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAC2_HUMAN
• UniProt AC: P15153
• Protein Name: Ras-related C3 botulinum toxin substrate 2
• Gene Name: RAC2
• Organism: Homo sapiens (Human).
• Sequence Length: 192
• Subcellular Localization: Cytoplasm. Membrane-associated when activated.
• 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 secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase..
• Protein Sequence: MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRQQKRACSLL

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	-
5	Acetylation	---MQAIKCVVVGDG ---CCCCEEEEECCC	24.80	25953088
6	S-palmitoylation	--MQAIKCVVVGDGA --CCCCEEEEECCCC	1.99	29575903
6	S-nitrosylation	--MQAIKCVVVGDGA --CCCCEEEEECCCC	1.99	2212679
17	O-linked_Glycosylation	GDGAVGKTCLLISYT CCCCCCCEEEEEEEE	11.49	24141704
32	O-linked_Glycosylation	TNAFPGEYIPTVFDN CCCCCCCCCCCEECC	20.37	24141704
32	Phosphorylation	TNAFPGEYIPTVFDN CCCCCCCCCCCEECC	20.37	22817900
39	ADP-ribosylation	YIPTVFDNYSANVMV CCCCEECCCEEEEEE	22.61	-
39	ADP-ribosylation	YIPTVFDNYSANVMV CCCCEECCCEEEEEE	22.61	-
41	O-linked_Glycosylation	PTVFDNYSANVMVDS CCEECCCEEEEEECC	21.44	24141704
64	Phosphorylation	DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC	11.38	28796482
71	Phosphorylation	YDRLRPLSYPQTDVF HHHCCCCCCCCCCEE	37.13	18669648
96	Ubiquitination	SYENVRAKWFPEVRH HHHCHHHHHCHHHHH	38.51	21890473
105	S-nitrosylation	FPEVRHHCPSTPIIL CHHHHHHCCCCCEEE	2.02	22126794
107	Phosphorylation	EVRHHCPSTPIILVG HHHHHCCCCCEEEEE	52.81	24719451
116	Ubiquitination	PIILVGTKLDLRDDK CEEEEEECCCCCCCH	33.79	-
123	Ubiquitination	KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH	62.15	21890473
123	Acetylation	KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH	62.15	23749302
123	Methylation	KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH	62.15	23644510
125	Phosphorylation	DLRDDKDTIEKLKEK CCCCCHHHHHHHHHC	36.45	24961811
128	Acetylation	DDKDTIEKLKEKKLA CCHHHHHHHHHCCCC	62.09	26822725
128	Ubiquitination	DDKDTIEKLKEKKLA CCHHHHHHHHHCCCC	62.09	-
130	Trimethylation	KDTIEKLKEKKLAPI HHHHHHHHHCCCCCC	77.79	-
130	Methylation	KDTIEKLKEKKLAPI HHHHHHHHHCCCCCC	77.79	23644510
133	Ubiquitination	IEKLKEKKLAPITYP HHHHHHCCCCCCCCH	51.47	21890473
147	Ubiquitination	PQGLALAKEIDSVKY HHHHHHHHHCCCCCE	56.93	21890473
147	Acetylation	PQGLALAKEIDSVKY HHHHHHHHHCCCCCE	56.93	19608861
153	Ubiquitination	AKEIDSVKYLECSAL HHHCCCCCEEEHHHH	48.33	-
153	Acetylation	AKEIDSVKYLECSAL HHHCCCCCEEEHHHH	48.33	23749302
154	Phosphorylation	KEIDSVKYLECSALT HHCCCCCEEEHHHHH	12.94	28152594
157	S-palmitoylation	DSVKYLECSALTQRG CCCCEEEHHHHHHHH	2.38	29575903
161	Phosphorylation	YLECSALTQRGLKTV EEEHHHHHHHHHHHH	18.88	25850435
163	Methylation	ECSALTQRGLKTVFD EHHHHHHHHHHHHHH	47.37	-
166	Ubiquitination	ALTQRGLKTVFDEAI HHHHHHHHHHHHHHH	45.53	21890473
166	Acetylation	ALTQRGLKTVFDEAI HHHHHHHHHHHHHHH	45.53	26822725
167	Phosphorylation	LTQRGLKTVFDEAIR HHHHHHHHHHHHHHH	31.29	21082442
178	S-nitrosylation	EAIRAVLCPQPTRQQ HHHHHHHCCCCCHHH	2.06	24105792
189	Geranylgeranylation	TRQQKRACSLL---- CHHHHHHHHCC----	3.23	1903399
189	Methylation	TRQQKRACSLL---- CHHHHHHHHCC----	3.23	-
189	Geranylgeranylation	TRQQKRACSLL---- CHHHHHHHHCC----	3.23	1903399

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

Oops, there are no upstream regulatory protein records of RAC2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAC2_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 RAC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL1_HUMAN	CUL1	physical	11445862
DOCK2_HUMAN	DOCK2	physical	10559471
NOS2_HUMAN	NOS2	physical	11457725
GDIR2_HUMAN	ARHGDIB	physical	10655614
SCG1_HUMAN	CHGB	physical	21900206
AFG32_HUMAN	AFG3L2	physical	21900206
RAC3_HUMAN	RAC3	physical	28514442
DOCK1_HUMAN	DOCK1	physical	28514442
ELMO2_HUMAN	ELMO2	physical	28514442
GDS1_HUMAN	RAP1GDS1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 608203: Neutrophil immunodeficiency syndrome (NEUID)
• 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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND MASS SPECTROMETRY.
PubMed: 19608861

Prenylation

"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteinsencoded by rac1, rac2, and ralA.";
Kinsella B.T., Erdman R.A., Maltese W.A.;
J. Biol. Chem. 266:9786-9794(1991).
Cited for: ISOPRENYLATION AT CYS-189, AND MUTAGENESIS OF CYS-189.
PubMed: 1903399