RAB18_HUMAN - dbPTM
RAB18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB18_HUMAN
UniProt AC Q9NP72
Protein Name Ras-related protein Rab-18
Gene Name RAB18
Organism Homo sapiens (Human).
Sequence Length 206
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Plays a role in apical endocytosis/recycling. May be implicated in transport between the plasma membrane and early endosomes. Plays a key role in eye and brain development and neurodegeneration..
Protein Sequence MDEDVLTTLKILIIGESGVGKSSLLLRFTDDTFDPELAATIGVDFKVKTISVDGNKAKLAIWDTAGQERFRTLTPSYYRGAQGVILVYDVTRRDTFVKLDNWLNELETYCTRNDIVNMLVGNKIDKENREVDRNEGLKFARKHSMLFIEASAKTCDGVQCAFEELVEKIIQTPGLWESENQNKGVKLSHREEGQGGGACGGYCSVL
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
1Acetylation-------MDEDVLTT
-------CCHHHHHH		13.2122223895
7Phosphorylation-MDEDVLTTLKILII
-CCHHHHHHEEEEEE		29.9021406692
8PhosphorylationMDEDVLTTLKILIIG
CCHHHHHHEEEEEEC		23.1521406692
17PhosphorylationKILIIGESGVGKSSL
EEEEECCCCCCCCCE		33.3024850871
21 (in isoform 2)Ubiquitination-34.17-
21UbiquitinationIGESGVGKSSLLLRF
ECCCCCCCCCEEEEE		34.17-
22PhosphorylationGESGVGKSSLLLRFT
CCCCCCCCCEEEEEC		21.9325072903
23PhosphorylationESGVGKSSLLLRFTD
CCCCCCCCEEEEECC		26.9025072903
29PhosphorylationSSLLLRFTDDTFDPE
CCEEEEECCCCCCHH		26.9119060867
29O-linked_GlycosylationSSLLLRFTDDTFDPE
CCEEEEECCCCCCHH		26.91OGP
48UbiquitinationIGVDFKVKTISVDGN
CCCEEEEEEEEECCC		40.51-
48AcetylationIGVDFKVKTISVDGN
CCCEEEEEEEEECCC		40.5127452117
49PhosphorylationGVDFKVKTISVDGNK
CCEEEEEEEEECCCE		22.8223312004
56UbiquitinationTISVDGNKAKLAIWD
EEEECCCEEEEEEEE		53.0521906983
58MalonylationSVDGNKAKLAIWDTA
EECCCEEEEEEEECC		39.8126320211
58AcetylationSVDGNKAKLAIWDTA
EECCCEEEEEEEECC		39.8125953088
58UbiquitinationSVDGNKAKLAIWDTA
EECCCEEEEEEEECC		39.81-
72PhosphorylationAGQERFRTLTPSYYR
CCCHHHHHCCHHHHC		32.07-
74PhosphorylationQERFRTLTPSYYRGA
CHHHHHCCHHHHCCC		15.02-
74AcetylationQERFRTLTPSYYRGA
CHHHHHCCHHHHCCC		15.0219608861
74UbiquitinationQERFRTLTPSYYRGA
CHHHHHCCHHHHCCC		15.0219608861
76PhosphorylationRFRTLTPSYYRGAQG
HHHHCCHHHHCCCCE		29.57-
77PhosphorylationFRTLTPSYYRGAQGV
HHHCCHHHHCCCCEE		9.82-
78PhosphorylationRTLTPSYYRGAQGVI
HHCCHHHHCCCCEEE		13.60-
123UbiquitinationVNMLVGNKIDKENRE
HHHHHCCCCCHHHCC		46.4821906983
138AcetylationVDRNEGLKFARKHSM
CCHHHHHHHHHHCCE		48.0819608861
138MalonylationVDRNEGLKFARKHSM
CCHHHHHHHHHHCCE		48.0826320211
138UbiquitinationVDRNEGLKFARKHSM
CCHHHHHHHHHHCCE		48.0819608861
142MalonylationEGLKFARKHSMLFIE
HHHHHHHHCCEEEEE		36.2826320211
142UbiquitinationEGLKFARKHSMLFIE
HHHHHHHHCCEEEEE		36.28-
144PhosphorylationLKFARKHSMLFIEAS
HHHHHHCCEEEEEEC		21.8823927012
151PhosphorylationSMLFIEASAKTCDGV
CEEEEEECCCCCCCC		19.94-
152 (in isoform 2)Ubiquitination-20.44-
167 (in isoform 2)Ubiquitination-51.68-
167AcetylationCAFEELVEKIIQTPG
HHHHHHHHHHHCCCC		51.6819608861
167UbiquitinationCAFEELVEKIIQTPG
HHHHHHHHHHHCCCC		51.6819608861
172PhosphorylationLVEKIIQTPGLWESE
HHHHHHCCCCCCCCC		14.6526846344
173 (in isoform 2)Phosphorylation-21.3627251275
178PhosphorylationQTPGLWESENQNKGV
CCCCCCCCCCCCCCC		30.2026846344
183UbiquitinationWESENQNKGVKLSHR
CCCCCCCCCCCCEEC		56.152190698
186UbiquitinationENQNKGVKLSHREEG
CCCCCCCCCEECCCC		53.60-
199S-palmitoylationEGQGGGACGGYCSVL
CCCCCCCCCCCEECC		5.00-
202PhosphorylationGGGACGGYCSVL---
CCCCCCCCEECC---		2.7020736484
203MethylationGGACGGYCSVL----
CCCCCCCEECC----		2.28-
203GeranylgeranylationGGACGGYCSVL----
CCCCCCCEECC----		2.28-
212 (in isoform 2)Ubiquitination--
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 RAB18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB18_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 RAB18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE6D_HUMANPDE6Dphysical
16169070
Drug and Disease Associations
Kegg Disease
H00792 Warburg micro syndrome
OMIM Disease
614222Warburg micro syndrome 3 (WARBM3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAB18_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-138, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29, AND MASSSPECTROMETRY.

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