RPE65_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPE65_HUMAN
• UniProt AC: Q16518
• Protein Name: Retinoid isomerohydrolase
• Gene Name: RPE65
• Organism: Homo sapiens (Human).
• Sequence Length: 533
• Subcellular Localization: Cytoplasm . Cell membrane ; Lipid-anchor . Microsome membrane . Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. Undergoes light-dependent intracellular transport to become more concentrated
• Protein Description: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. [PubMed: 16116091 Essential for the production of 11-cis retinal for both rod and cone photoreceptors]
• Protein Sequence: MSIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEIVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYLNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKYCGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS

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
2	Acetylation	------MSIQVEHPA ------CCCEEECCC	23.02	-
18	Phosphorylation	GYKKLFETVEELSSP HHHHHHHHHHHHCCC	26.36	-
78	Phosphorylation	DFKEGHVTYHRRFIR CCCCCCEEEEEHHHH	14.13	22210691
79	Phosphorylation	FKEGHVTYHRRFIRT CCCCCEEEEEHHHHH	7.70	22210691
89	Phosphorylation	RFIRTDAYVRAMTEK HHHHHHHHHHHHHCC	8.02	22817900
101	Phosphorylation	TEKRIVITEFGTCAF HCCEEEEEECCCCCC	17.86	22817900
105	Phosphorylation	IVITEFGTCAFPDPC EEEEECCCCCCCCHH	13.14	22817900
112	S-palmitoylation	TCAFPDPCKNIFSRF CCCCCCHHHHHHHHH	7.41	19049981
113	Acetylation	CAFPDPCKNIFSRFF CCCCCHHHHHHHHHH	59.47	19049981
117	Phosphorylation	DPCKNIFSRFFSYFR CHHHHHHHHHHHHHC	25.12	15557452
146	S-palmitoylation	VGEDYYACTETNFIT CCCCEEEEECCCEEE	1.72	30914787
231	S-palmitoylation	EIVVQFPCSDRFKPS EEEEEEECCCCCCCC	7.54	17122102
304	Phosphorylation	KKYLNNKYRTSPFNL HHHHCCCCCCCCCCC	22.65	-
329	S-palmitoylation	GFLIVDLCCWKGFEF CEEEEEEECCCCHHH	1.94	17122102
330	S-palmitoylation	FLIVDLCCWKGFEFV EEEEEEECCCCHHHH	5.67	17122102
376	Acetylation	VLPLNIDKADTGKNL EEECCCCHHCCCCCC	44.35	20167786
379	Phosphorylation	LNIDKADTGKNLVTL CCCCHHCCCCCCEEC	55.72	-
410	Phosphorylation	LEPEVLFSGPRQAFE CCCEEEECCCCCCCC	43.67	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RPE65_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPE65_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RPE65_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S27A1_HUMAN	SLC27A1	physical	20356843
ZMYM2_HUMAN	ZMYM2	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442

Drug and Disease Associations

• Kegg Disease
• H00527: Retinitis pigmentosa (RP)
• H00837: Leber congenital amaurosis (LCR)
• OMIM Disease
• 204100: Leber congenital amaurosis 2 (LCA2)
• 613794: Retinitis pigmentosa 20 (RP20)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Identification of a novel palmitylation site essential for membraneassociation and isomerohydrolase activity of RPE65.";
Takahashi Y., Moiseyev G., Ablonczy Z., Chen Y., Crouch R.K., Ma J.X.;
J. Biol. Chem. 284:3211-3218(2009).
Cited for: PROTEIN SEQUENCE OF 98-118, PHOSPHORYLATION AT THR-101; THR-105 ANDSER-117, PALMITOYLATION AT CYS-112, MUTAGENESIS OF CYS-106 ANDCYS-112, ACETYLATION AT LYS-113, AND MASS SPECTROMETRY.
PubMed: 19049981

Palmitoylation

"Identification of a novel palmitylation site essential for membraneassociation and isomerohydrolase activity of RPE65.";
Takahashi Y., Moiseyev G., Ablonczy Z., Chen Y., Crouch R.K., Ma J.X.;
J. Biol. Chem. 284:3211-3218(2009).
Cited for: PROTEIN SEQUENCE OF 98-118, PHOSPHORYLATION AT THR-101; THR-105 ANDSER-117, PALMITOYLATION AT CYS-112, MUTAGENESIS OF CYS-106 ANDCYS-112, ACETYLATION AT LYS-113, AND MASS SPECTROMETRY.
PubMed: 19049981

Phosphorylation

"Identification of a novel palmitylation site essential for membraneassociation and isomerohydrolase activity of RPE65.";
Takahashi Y., Moiseyev G., Ablonczy Z., Chen Y., Crouch R.K., Ma J.X.;
J. Biol. Chem. 284:3211-3218(2009).
Cited for: PROTEIN SEQUENCE OF 98-118, PHOSPHORYLATION AT THR-101; THR-105 ANDSER-117, PALMITOYLATION AT CYS-112, MUTAGENESIS OF CYS-106 ANDCYS-112, ACETYLATION AT LYS-113, AND MASS SPECTROMETRY.
PubMed: 19049981