OPSD_BOVIN - dbPTM
OPSD_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OPSD_BOVIN
UniProt AC P02699
Protein Name Rhodopsin
Gene Name RHO
Organism Bos taurus (Bovine).
Sequence Length 348
Subcellular Localization Membrane
Multi-pass membrane protein . Cell projection, cilium, photoreceptor outer segment . Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory c
Protein Description Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. [PubMed: 10926528]
Protein Sequence MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA
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-------MNGTEGPN
-------CCCCCCCC		10.616759163
2N-linked_Glycosylation------MNGTEGPNF
------CCCCCCCCE		67.1218818650
15N-linked_GlycosylationNFYVPFSNKTGVVRS
CEECCCCCCCCCCCC		46.4118818650
16AcetylationFYVPFSNKTGVVRSP
EECCCCCCCCCCCCC		45.52-
66AcetylationLYVTVQHKKLRTPLN
HHHHHCCCCCCCHHH		36.09-
67AcetylationYVTVQHKKLRTPLNY
HHHHCCCCCCCHHHH		40.87-
141AcetylationERYVVVCKPMSNFRF
HHEEEEEEECCCCCC		31.95-
296OtherTIPAFFAKTSAVYNP
CCHHHHHCHHHCCCH		37.5410926528
311AcetylationVIYIMMNKQFRNCMV
HHHHHCCHHHCCCEE		32.68-
322S-palmitoylationNCMVTTLCCGKNPLG
CCEEEEEECCCCCCC		2.433350146
323S-palmitoylationCMVTTLCCGKNPLGD
CEEEEEECCCCCCCC		11.063350146
325AcetylationVTTLCCGKNPLGDDE
EEEEECCCCCCCCCC		41.29-
334PhosphorylationPLGDDEASTTVSKTE
CCCCCCCCCCCCCCC		23.6715351781
335PhosphorylationLGDDEASTTVSKTET
CCCCCCCCCCCCCCC		37.9615351781
336PhosphorylationGDDEASTTVSKTETS
CCCCCCCCCCCCCCC		21.9315351781
338PhosphorylationDEASTTVSKTETSQV
CCCCCCCCCCCCCCC		31.5915351781
339AcetylationEASTTVSKTETSQVA
CCCCCCCCCCCCCCC		46.15-
340PhosphorylationASTTVSKTETSQVAP
CCCCCCCCCCCCCCC		36.679169442
342PhosphorylationTTVSKTETSQVAPA-
CCCCCCCCCCCCCC-		29.6815351781
343PhosphorylationTVSKTETSQVAPA--
CCCCCCCCCCCCC--		19.2027458239
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
334SPhosphorylationKinaseGRK1Q15835
PSP
334SPhosphorylationKinasePKC_GROUP-PhosphoELM
334SPhosphorylationKinasePKC-FAMILY-GPS
334SPhosphorylationKinasePRKCAP04409
GPS
335TPhosphorylationKinasePKC_GROUP-PhosphoELM
335TPhosphorylationKinasePKC-FAMILY-GPS
335TPhosphorylationKinasePRKCAP04409
GPS
336TPhosphorylationKinasePKC_GROUP-PhosphoELM
336TPhosphorylationKinasePKC-FAMILY-GPS
336TPhosphorylationKinasePRKCAP04409
GPS
338SPhosphorylationKinasePKC_GROUP-PhosphoELM
338SPhosphorylationKinasePKC-FAMILY-GPS
338SPhosphorylationKinasePRKCAP04409
GPS
338SPhosphorylationKinaseGRK1Q15835
PSP
340TPhosphorylationKinaseGRK1Q15835
PSP
340TPhosphorylationKinaseGRK1P28327
PhosphoELM
342TPhosphorylationKinaseGRK1Q15835
PSP
343SPhosphorylationKinasePRKCAP04409
GPS
343SPhosphorylationKinaseGRK7Q8WMV0
Uniprot
343SPhosphorylationKinaseGRK1Q15835
PSP
343SPhosphorylationKinaseRK-Uniprot
343SPhosphorylationKinaseGRK1P28327
PhosphoELM
343SPhosphorylationKinaseGRK7F1MH44
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OPSD_BOVIN !!
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 OPSD_BOVIN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_HUMANBAG6physical
24806960
UBC_HUMANUBCphysical
24806960
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OPSD_BOVIN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Advances in determination of a high-resolution three-dimensionalstructure of rhodopsin, a model of G-protein-coupled receptors(GPCRs).";
Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.;
Biochemistry 40:7761-7772(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINALCHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, ANDGLYCOSYLATION AT ASN-2 AND ASN-15.
"Rhodopsin carbohydrate. Structure of small oligosaccharides attachedat two sites near the NH2 terminus.";
Fukuda M.N., Papermaster D.S., Hargrave P.A.;
J. Biol. Chem. 254:8201-8207(1979).
Cited for: GLYCOSYLATION AT ASN-2 AND ASN-15.
"Rhodopsin and bacteriorhodopsin: structure-function relationships.";
Ovchinnikov Y.A.;
FEBS Lett. 148:179-191(1982).
Cited for: PROTEIN SEQUENCE.
Palmitoylation
ReferencePubMed
"Advances in determination of a high-resolution three-dimensionalstructure of rhodopsin, a model of G-protein-coupled receptors(GPCRs).";
Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.;
Biochemistry 40:7761-7772(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINALCHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, ANDGLYCOSYLATION AT ASN-2 AND ASN-15.
"Palmitylation of a G-protein coupled receptor. Direct analysis bytandem mass spectrometry.";
Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R.;
J. Biol. Chem. 267:16889-16894(1992).
Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
"Two adjacent cysteine residues in the C-terminal cytoplasmic fragmentof bovine rhodopsin are palmitylated.";
Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S.;
FEBS Lett. 230:1-5(1988).
Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
Phosphorylation
ReferencePubMed
"Conformational changes in the phosphorylated C-terminal domain ofrhodopsin during rhodopsin arrestin interactions.";
Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A.;
J. Biol. Chem. 279:51203-51207(2004).
Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUALARRESTIN, AND PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338;THR-340; THR-342 AND SER-343.
"The arrestin-bound conformation and dynamics of the phosphorylatedcarboxy-terminal region of rhodopsin.";
Kisselev O.G., McDowell J.H., Hargrave P.A.;
FEBS Lett. 564:307-311(2004).
Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUALARRESTIN, AND PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338;THR-340; THR-342 AND SER-343.
"Mechanistic studies on rhodopsin kinase. Light-dependentphosphorylation of C-terminal peptides of rhodopsin.";
Brown N.G., Fowles C., Sharma R., Akhtar M.;
Eur. J. Biochem. 208:659-667(1992).
Cited for: PHOSPHORYLATION AT SER-343.

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