RSU1_HUMAN - dbPTM
RSU1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSU1_HUMAN
UniProt AC Q15404
Protein Name Ras suppressor protein 1
Gene Name RSU1
Organism Homo sapiens (Human).
Sequence Length 277
Subcellular Localization
Protein Description Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro..
Protein Sequence MSKSLKKLVEESREKNQPEVDMSDRGISNMLDVNGLFTLSHITQLVLSHNKLTMVPPNIAELKNLEVLNFFNNQIEELPTQISSLQKLKHLNLGMNRLNTLPRGFGSLPALEVLDLTYNNLSENSLPGNFFYLTTLRALYLSDNDFEILPPDIGKLTKLQILSLRDNDLISLPKEIGELTQLKELHIQGNRLTVLPPELGNLDLTGQKQVFKAENNPWVTPIADQFQLGVSHVFEYIRSETYKYLYGRHMQANPEPPKKNNDKSKKISRKPLAAKNR
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
2Acetylation------MSKSLKKLV
------CCHHHHHHH
30.8322814378
6Ubiquitination--MSKSLKKLVEESR
--CCHHHHHHHHHHH
51.67-
7Ubiquitination-MSKSLKKLVEESRE
-CCHHHHHHHHHHHH
64.1624816145
12PhosphorylationLKKLVEESREKNQPE
HHHHHHHHHHHCCCC
32.0320068231
34UbiquitinationISNMLDVNGLFTLSH
HHHHCCCCCCCHHHH
40.9129967540
54SulfoxidationLSHNKLTMVPPNIAE
HHCCCCCCCCCCHHH
6.5421406390
87UbiquitinationTQISSLQKLKHLNLG
HHHHHHHHHHHCCCC
65.8729967540
89UbiquitinationISSLQKLKHLNLGMN
HHHHHHHHHCCCCCH
53.75-
100PhosphorylationLGMNRLNTLPRGFGS
CCCHHHCCCCCCCCC
42.6127535140
102UbiquitinationMNRLNTLPRGFGSLP
CHHHCCCCCCCCCCC
32.1023000965
105UbiquitinationLNTLPRGFGSLPALE
HCCCCCCCCCCCHHH
6.7521890473
105UbiquitinationLNTLPRGFGSLPALE
HCCCCCCCCCCCHHH
6.7523000965
121UbiquitinationLDLTYNNLSENSLPG
HHCCCCCCCCCCCCC
6.3929967540
130UbiquitinationENSLPGNFFYLTTLR
CCCCCCCEEHHHHHH
5.4423000965
142PhosphorylationTLRALYLSDNDFEIL
HHHHHHCCCCCCCCC
22.32-
155UbiquitinationILPPDIGKLTKLQIL
CCCCCHHHCCEEEEE
54.0023000965
158UbiquitinationPDIGKLTKLQILSLR
CCHHHCCEEEEEECC
49.1623000965
158AcetylationPDIGKLTKLQILSLR
CCHHHCCEEEEEECC
49.1625953088
158MalonylationPDIGKLTKLQILSLR
CCHHHCCEEEEEECC
49.1626320211
159UbiquitinationDIGKLTKLQILSLRD
CHHHCCEEEEEECCC
3.0123503661
171PhosphorylationLRDNDLISLPKEIGE
CCCCCCCCCCHHHHH
46.0120873877
174UbiquitinationNDLISLPKEIGELTQ
CCCCCCCHHHHHHHC
68.2229967540
180PhosphorylationPKEIGELTQLKELHI
CHHHHHHHCCEEEEE
27.7920068231
183UbiquitinationIGELTQLKELHIQGN
HHHHHCCEEEEECCC
48.7023000965
190UbiquitinationKELHIQGNRLTVLPP
EEEEECCCEEEECCC
21.2923000965
206UbiquitinationLGNLDLTGQKQVFKA
CCCCCCCCCEEEEEC
39.7324816145
208UbiquitinationNLDLTGQKQVFKAEN
CCCCCCCEEEEECCC
50.1833845483
212UbiquitinationTGQKQVFKAENNPWV
CCCEEEEECCCCCCC
56.8023503661
217UbiquitinationVFKAENNPWVTPIAD
EEECCCCCCCCCCHH
38.2024816145
220PhosphorylationAENNPWVTPIADQFQ
CCCCCCCCCCHHHHH
12.7125159151
243UbiquitinationYIRSETYKYLYGRHM
HHHHHHHHHHHHHHC
35.8823000965
243MalonylationYIRSETYKYLYGRHM
HHHHHHHHHHHHHHC
35.8826320211
244PhosphorylationIRSETYKYLYGRHMQ
HHHHHHHHHHHHHCC
8.51-
259UbiquitinationANPEPPKKNNDKSKK
CCCCCCCCCCCCCCC
67.7524816145
268PhosphorylationNDKSKKISRKPLAAK
CCCCCCCCCCCHHHC
43.03-
270UbiquitinationKSKKISRKPLAAKNR
CCCCCCCCCHHHCCC
37.2824816145

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 RSU1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSU1_HUMAN !!

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 RSU1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PARVA_HUMANPARVAphysical
26186194
PARVB_HUMANPARVBphysical
26186194
ILK_HUMANILKphysical
26186194
LIMS1_HUMANLIMS1physical
26186194
CBS_HUMANCBSphysical
26344197
ROA3_HUMANHNRNPA3physical
26344197
ILK_HUMANILKphysical
26344197
LIMS1_HUMANLIMS1physical
26344197
NDUA8_HUMANNDUFA8physical
26344197
NTM1A_HUMANNTMT1physical
26344197
PARVA_HUMANPARVAphysical
26344197
PFKAP_HUMANPFKPphysical
26344197
TIAR_HUMANTIAL1physical
26344197
TKT_HUMANTKTphysical
26344197
PARVA_HUMANPARVAphysical
28514442
PARVB_HUMANPARVBphysical
28514442
ILK_HUMANILKphysical
28514442
LIMS1_HUMANLIMS1physical
28514442

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.
Regulatory Network of RSU1_HUMAN

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Related Literatures of Post-Translational Modification

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