RAB28_HUMAN - dbPTM
RAB28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB28_HUMAN
UniProt AC P51157
Protein Name Ras-related protein Rab-28
Gene Name RAB28
Organism Homo sapiens (Human).
Sequence Length 221
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cytoplasm, cytoskeleton, cilium basal body. Expressed in the basal body and ciliary rootlet of the photoreceptors..
Protein Description
Protein Sequence MSDSEEESQDRQLKIVVLGDGASGKTSLTTCFAQETFGKQYKQTIGLDFFLRRITLPGNLNVTLQIWDIGGQTIGGKMLDKYIYGAQGVLLVYDITNYQSFENLEDWYTVVKKVSEESETQPLVALVGNKIDLEHMRTIKPEKHLRFCQENGFSSHFVSAKTGDSVFLCFQKVAAEILGIKLNKAEIEQSQRVVKADIVNYNQEPMSRTVNPPRSSMCAVQ
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
2Phosphorylation------MSDSEEESQ
------CCHHHHHHH
50.2525849741
2 (in isoform 2)Phosphorylation-50.2524719451
2Acetylation------MSDSEEESQ
------CCHHHHHHH
50.2521406692
4Phosphorylation----MSDSEEESQDR
----CCHHHHHHHHC
39.3325849741
4 (in isoform 2)Phosphorylation-39.3324719451
8PhosphorylationMSDSEEESQDRQLKI
CCHHHHHHHHCCEEE
40.4321406692
23PhosphorylationVVLGDGASGKTSLTT
EEECCCCCCCCCHHH
46.4830622161
25UbiquitinationLGDGASGKTSLTTCF
ECCCCCCCCCHHHHH
32.2329967540
26PhosphorylationGDGASGKTSLTTCFA
CCCCCCCCCHHHHHH
32.2830622161
27PhosphorylationDGASGKTSLTTCFAQ
CCCCCCCCHHHHHHH
27.4930622161
29PhosphorylationASGKTSLTTCFAQET
CCCCCCHHHHHHHHH
22.6830622161
39AcetylationFAQETFGKQYKQTIG
HHHHHHHHHHHHHHC
46.3825953088
39UbiquitinationFAQETFGKQYKQTIG
HHHHHHHHHHHHHHC
46.3829967540
44PhosphorylationFGKQYKQTIGLDFFL
HHHHHHHHHCCEEEE
16.9222210691
73PhosphorylationIWDIGGQTIGGKMLD
EEEECCCEECCEECH
25.5122210691
115PhosphorylationYTVVKKVSEESETQP
HHHHHHHCCCCCCCC
44.5230622161
118PhosphorylationVKKVSEESETQPLVA
HHHHCCCCCCCCEEE
41.7230622161
120PhosphorylationKVSEESETQPLVALV
HHCCCCCCCCEEEHH
44.7830622161
130UbiquitinationLVALVGNKIDLEHMR
EEEHHCCCCCHHHHH
31.5029967540
143UbiquitinationMRTIKPEKHLRFCQE
HHCCCHHHHHHHHHH
57.3729967540
184UbiquitinationILGIKLNKAEIEQSQ
HHCCCCCHHHHHHHH
58.8129967540
201PhosphorylationVKADIVNYNQEPMSR
EECCEECCCCCCCCC
13.8228060719
207PhosphorylationNYNQEPMSRTVNPPR
CCCCCCCCCCCCCCC
35.2028060719
209PhosphorylationNQEPMSRTVNPPRSS
CCCCCCCCCCCCCHH
19.82-
218MethylationNPPRSSMCAVQ----
CCCCHHCCCCC----
3.47-
218FarnesylationNPPRSSMCAVQ----
CCCCHHCCCCC----
3.4717411337
218FarnesylationNPPRSSMCAVQ----
CCCCHHCCCCC----
3.4717411337

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 RAB28_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB28_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 RAB28_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PDE6D_HUMANPDE6Dphysical
27173435
NCOA3_HUMANNCOA3physical
27173435
CATL2_HUMANCTSVphysical
27173435
C144A_HUMANCCDC144Aphysical
27173435
HMMR_HUMANHMMRphysical
27173435
KIF7_HUMANKIF7physical
27173435
HSF1_HUMANHSF1physical
27173435
MNS1_HUMANMNS1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615374Cone-rod dystrophy 18 (CORD18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAB28_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Towards complete sets of farnesylated and geranylgeranylatedproteins.";
Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,Eisenhaber F.;
PLoS Comput. Biol. 3:634-648(2007).
Cited for: ISOPRENYLATION AT CYS-218.

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