dbPTM

RAB23_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB23_HUMAN
UniProt AC	Q9ULC3
Protein Name	Ras-related protein Rab-23
Gene Name	RAB23
Organism	Homo sapiens (Human).
Sequence Length	237
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Cytoplasm . Cytoplasmic vesicle, autophagosome . Endosome membrane . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane Lipid-anchor Cytoplasmic side . Recruited to phagosome
Protein Description	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Together with SUFU, prevents nuclear import of GLI1, and thereby inhibits GLI1 transcription factor activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes..
Protein Sequence	MLEEDMEVAIKMVVVGNGAVGKSSMIQRYCKGIFTKDYKKTIGVDFLERQIQVNDEDVRLMLWDTAGQEEFDAITKAYYRGAQACVLVFSTTDRESFEAVSSWREKVVAEVGDIPTVLVQNKIDLLDDSCIKNEEAEALAKRLKLRFYRTSVKEDLNVNEVFKYLAEKYLQKLKQQIAEDPELTHSSSNKIGVFNTSGGSHSGQNSGTLNGGDVINLRPNKQRTKKNRNPFSSCSIP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
96	Phosphorylation	FSTTDRESFEAVSSW EECCCHHHHHHHHHH	29.31	28348404
101	Phosphorylation	RESFEAVSSWREKVV HHHHHHHHHHHHHHH	31.09	28348404
122	Ubiquitination	PTVLVQNKIDLLDDS CCEEECCCCCCCCHH	22.10	-
132	Ubiquitination	LLDDSCIKNEEAEAL CCCHHHCCCHHHHHH	63.73	-
141	Acetylation	EEAEALAKRLKLRFY HHHHHHHHHHHHHHH	60.14	25953088
141	Malonylation	EEAEALAKRLKLRFY HHHHHHHHHHHHHHH	60.14	26320211
148	Phosphorylation	KRLKLRFYRTSVKED HHHHHHHHCCCCCCC	13.42	-
163	Ubiquitination	LNVNEVFKYLAEKYL CCHHHHHHHHHHHHH	44.52	21890473
164	Phosphorylation	NVNEVFKYLAEKYLQ CHHHHHHHHHHHHHH	10.32	-
168	Acetylation	VFKYLAEKYLQKLKQ HHHHHHHHHHHHHHH	45.73	25953088
168	Malonylation	VFKYLAEKYLQKLKQ HHHHHHHHHHHHHHH	45.73	26320211
174	Ubiquitination	EKYLQKLKQQIAEDP HHHHHHHHHHHHHCC	47.38	-
184	Phosphorylation	IAEDPELTHSSSNKI HHHCCCCCCCCCCEE	20.32	29255136
186	Phosphorylation	EDPELTHSSSNKIGV HCCCCCCCCCCEEEE	30.17	30266825
187	Phosphorylation	DPELTHSSSNKIGVF CCCCCCCCCCEEEEE	30.26	30266825
188	Phosphorylation	PELTHSSSNKIGVFN CCCCCCCCCEEEEEE	45.19	30266825
196	Phosphorylation	NKIGVFNTSGGSHSG CEEEEEECCCCCCCC	19.79	25850435
197	Phosphorylation	KIGVFNTSGGSHSGQ EEEEEECCCCCCCCC	42.11	22496350
200	Phosphorylation	VFNTSGGSHSGQNSG EEECCCCCCCCCCCC	20.29	23927012
202	Phosphorylation	NTSGGSHSGQNSGTL ECCCCCCCCCCCCCC	43.71	23403867
206	Phosphorylation	GSHSGQNSGTLNGGD CCCCCCCCCCCCCCC	25.85	23927012
208	Phosphorylation	HSGQNSGTLNGGDVI CCCCCCCCCCCCCEE	19.51	23927012
234	Methylation	NRNPFSSCSIP---- CCCCCCCCCCC----	4.07	-
234	Geranylgeranylation	NRNPFSSCSIP---- CCCCCCCCCCC----	4.07	-

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 RAB23_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAB23_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 RAB23_HUMAN !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Disease
H00458	Craniosynostosis, including: Pfeiffer syndrome; Apert syndrome; Crouzon syndrome; Jackson-Weiss synd
OMIM Disease
201000	Carpenter syndrome 1 (CRPT1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RAB23_HUMAN

Related Literatures of Post-Translational Modification