RASD1_HUMAN - dbPTM
RASD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASD1_HUMAN
UniProt AC Q9Y272
Protein Name Dexamethasone-induced Ras-related protein 1
Gene Name RASD1
Organism Homo sapiens (Human).
Sequence Length 281
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cytoplasm, perinuclear region. Nucleus.
Protein Description Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity)..
Protein Sequence MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLRQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVDQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGGDPGDAFGIVAPFARRPSVHSDLMYIREKASAGSQAKDKERCVIS
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
11S-nitrosylationAAMIKKMCPSDSELS
HHHHHHHCCCCCCCC
3.9112498886
11S-nitrosocysteineAAMIKKMCPSDSELS
HHHHHHHCCCCCCCC
3.91-
13PhosphorylationMIKKMCPSDSELSIP
HHHHHCCCCCCCCCC
49.1730631047
15PhosphorylationKKMCPSDSELSIPAK
HHHCCCCCCCCCCCC
44.7830631047
32PhosphorylationYRMVILGSSKVGKTA
EEEEEECCCCCCCHH
24.4430631047
33PhosphorylationRMVILGSSKVGKTAI
EEEEECCCCCCCHHH
29.5730631047
66PhosphorylationDFHRKFYSIRGEVYQ
HHHHHHHCCCCEEEE
14.6724719451
92 (in isoform 2)Phosphorylation-17.4630631047
124PhosphorylationLRQQILDTKSCLKNK
HHHHHHCCHHHHCCC
22.7824702127
182PhosphorylationEISAKKNSSLDQMFR
EEECCCCCCHHHHHH
40.9529978859
183PhosphorylationISAKKNSSLDQMFRA
EECCCCCCHHHHHHH
45.4129978859
199PhosphorylationFAMAKLPSEMSPDLH
HHHHCCCHHCCHHHH
57.2629978859
202PhosphorylationAKLPSEMSPDLHRKV
HCCCHHCCHHHHHHH
15.9429978859
210PhosphorylationPDLHRKVSVQYCDVL
HHHHHHHHHHHHHHH
13.4124719451
219UbiquitinationQYCDVLHKKALRNKK
HHHHHHCHHHHHCCC
35.2632142685
232PhosphorylationKKLLRAGSGGGGGDP
CCCCCCCCCCCCCCH
33.0228355574
254PhosphorylationAPFARRPSVHSDLMY
CCCCCCCCCCCCHHH
30.5629978859
257PhosphorylationARRPSVHSDLMYIRE
CCCCCCCCCHHHHHH
30.2229978859
261PhosphorylationSVHSDLMYIREKASA
CCCCCHHHHHHHHHC
12.2529978859
267PhosphorylationMYIREKASAGSQAKD
HHHHHHHHCCCCCCC
44.2029083192
270PhosphorylationREKASAGSQAKDKER
HHHHHCCCCCCCCCC
27.0429083192
273UbiquitinationASAGSQAKDKERCVI
HHCCCCCCCCCCCCC
62.7930230243
278MethylationQAKDKERCVIS----
CCCCCCCCCCC----
3.14-
278FarnesylationQAKDKERCVIS----
CCCCCCCCCCC----
3.14-

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 RASD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RASD1_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 RASD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAPON_HUMANNOS1APphysical
11086993
NOS1_HUMANNOS1physical
11086993
GNAI1_HUMANGNAI1physical
10840027
GBB1_HUMANGNB1physical
16225846
RBY1F_HUMANRBMY1Fphysical
25416956

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 RASD1_HUMAN

loading...

Related Literatures of Post-Translational Modification
S-nitrosylation
ReferencePubMed
"Nitrosopeptide mapping: a novel methodology reveals s-nitrosylationof dexras1 on a single cysteine residue.";
Jaffrey S.R., Fang M., Snyder S.H.;
Chem. Biol. 9:1329-1335(2002).
Cited for: S-NITROSYLATION AT CYS-11, AND MUTAGENESIS OF CYS-11.

TOP