RAC2_MOUSE - dbPTM
RAC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAC2_MOUSE
UniProt AC Q05144
Protein Name Ras-related C3 botulinum toxin substrate 2
Gene Name Rac2
Organism Mus musculus (Mouse).
Sequence Length 192
Subcellular Localization Cytoplasm. Membrane
Lipid-anchor. 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 MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKDIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRQQKRPCSLL
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 Orthologous
Protein Cluster
17PhosphorylationGDGAVGKTCLLISYT
CCCCCCCEEEEEEEE
11.49-
22PhosphorylationGKTCLLISYTTNAFP
CCEEEEEEEECCCCC
19.18-
23PhosphorylationKTCLLISYTTNAFPG
CEEEEEEEECCCCCC
15.58-
24PhosphorylationTCLLISYTTNAFPGE
EEEEEEEECCCCCCC
13.54-
64PhosphorylationDTAGQEDYDRLRPLS
CCCCCCCHHHCCCCC
11.38-
105GlutathionylationFPEVRHHCPSTPIIL
CHHHHHHCCCCCEEE
2.0224333276
107PhosphorylationEVRHHCPSTPIILVG
HHHHHCCCCCEEEEE
52.8124719451
116UbiquitinationPIILVGTKLDLRDDK
CEEEEEECCCCCCCH
33.79-
123UbiquitinationKLDLRDDKDTIEKLK
CCCCCCCHHHHHHHH
62.1522790023
125PhosphorylationDLRDDKDTIEKLKEK
CCCCCHHHHHHHHHC
36.4529899451
128UbiquitinationDDKDTIEKLKEKKLA
CCHHHHHHHHHCCCC
62.0922790023
147UbiquitinationPQGLALAKDIDSVKY
HHHHHHHCCCCCCCE
56.9427667366
147AcetylationPQGLALAKDIDSVKY
HHHHHHHCCCCCCCE
56.94-
153UbiquitinationAKDIDSVKYLECSAL
HCCCCCCCEEEHHHH
48.33-
157S-nitrosylationDSVKYLECSALTQRG
CCCCEEEHHHHHHHH
2.3822588120
157GlutathionylationDSVKYLECSALTQRG
CCCCEEEHHHHHHHH
2.3824333276
157S-palmitoylationDSVKYLECSALTQRG
CCCCEEEHHHHHHHH
2.3828526873
158PhosphorylationSVKYLECSALTQRGL
CCCEEEHHHHHHHHH
19.5520531401
161PhosphorylationYLECSALTQRGLKTV
EEEHHHHHHHHHHHH
18.8822817900
166UbiquitinationALTQRGLKTVFDEAI
HHHHHHHHHHHHHHH
45.5327667366
167PhosphorylationLTQRGLKTVFDEAIR
HHHHHHHHHHHHHHH
31.2925177544
178GlutathionylationEAIRAVLCPQPTRQQ
HHHHHHHCCCCCCCC
2.0624333276
189GeranylgeranylationTRQQKRPCSLL----
CCCCCCCCCCC----
5.34-
189MethylationTRQQKRPCSLL----
CCCCCCCCCCC----
5.34-

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

Oops, there are no upstream regulatory protein records of RAC2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAC2_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 RAC2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RAC2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAC2_MOUSE

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Related Literatures of Post-Translational Modification

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