RPGR_HUMAN - dbPTM
RPGR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPGR_HUMAN
UniProt AC Q92834
Protein Name X-linked retinitis pigmentosa GTPase regulator
Gene Name RPGR
Organism Homo sapiens (Human).
Sequence Length 1020
Subcellular Localization Cytoplasm, cytoskeleton, flagellum axoneme . Golgi apparatus .
Isoform 6: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme.
Protein Description Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes (By similarity). May be involved in microtubule organization and regulation of transport in primary cilia..
Protein Sequence MREPEELMPDSGAVFTFGKSKFAENNPGKFWFKNDVPVHLSCGDEHSAVVTGNNKLYMFGSNNWGQLGLGSKSAISKPTCVKALKPEKVKLAACGRNHTLVSTEGGNVYATGGNNEGQLGLGDTEERNTFHVISFFTSEHKIKQLSAGSNTSAALTEDGRLFMWGDNSEGQIGLKNVSNVCVPQQVTIGKPVSWISCGYYHSAFVTTDGELYVFGEPENGKLGLPNQLLGNHRTPQLVSEIPEKVIQVACGGEHTVVLTENAVYTFGLGQFGQLGLGTFLFETSEPKVIENIRDQTISYISCGENHTALITDIGLMYTFGDGRHGKLGLGLENFTNHFIPTLCSNFLRFIVKLVACGGCHMVVFAAPHRGVAKEIEFDEINDTCLSVATFLPYSSLTSGNVLQRTLSARMRRRERERSPDSFSMRRTLPPIEGTLGLSACFLPNSVFPRCSERNLQESVLSEQDLMQPEEPDYLLDEMTKEAEIDNSSTVESLGETTDILNMTHIMSLNSNEKSLKLSPVQKQKKQQTIGELTQDTALTENDDSDEYEEMSEMKEGKACKQHVSQGIFMTQPATTIEAFSDEEVGNDTGQVGPQADTDGEGLQKEVYRHENNNGVDQLDAKEIEKESDGGHSQKESEAEEIDSEKETKLAEIAGMKDLREREKSTKKMSPFFGNLPDRGMNTESEENKDFVKKRESCKQDVIFDSERESVEKPDSYMEGASESQQGIADGFQQPEAIEFSSGEKEDDEVETDQNIRYGRKLIEQGNEKETKPIISKSMAKYDFKCDRLSEIPEEKEGAEDSKGNGIEEQEVEANEENVKVHGGRKEKTEILSDDLTDKAEDHEFSKTEELKLEDVDEEINAENVESKKKTVGDDESVPTGYHSKTEGAERTNDDSSAETIEKKEKANLEERAICEYNENPKGYMLDDADSSSLEILENSETTPSKDMKKTKKIFLFKRVPSINQKIVKNNNEPLPEIKSIGDQIILKSDNKDADQNHMSQNHQNIPPTNTERRSKSCTIL
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
143UbiquitinationFTSEHKIKQLSAGSN
ECCHHHEEEECCCCC
50.4129967540
335PhosphorylationGLGLENFTNHFIPTL
CCCCCCCCCCCHHHH
39.09-
393PhosphorylationSVATFLPYSSLTSGN
HHHHHCCHHHCCCCC
17.03-
418PhosphorylationRRRERERSPDSFSMR
HHHHHHHCCCCCCCC
28.4530266825
418 (in isoform 6)Phosphorylation-28.4527251275
421PhosphorylationERERSPDSFSMRRTL
HHHHCCCCCCCCCCC
23.7030266825
423PhosphorylationERSPDSFSMRRTLPP
HHCCCCCCCCCCCCC
18.4830266825
512 (in isoform 4)Phosphorylation-43.7929523821
513 (in isoform 4)Phosphorylation-66.4029523821
514PhosphorylationSLNSNEKSLKLSPVQ
ECCCCCCCCCCCHHH
25.2630266825
518 (in isoform 6)Phosphorylation-22.8027251275
518 (in isoform 4)Phosphorylation-22.8029523821
518PhosphorylationNEKSLKLSPVQKQKK
CCCCCCCCHHHHHHH
22.8025159151
518 (in isoform 2)Phosphorylation-22.8024719451
539 (in isoform 6)Phosphorylation-30.2227251275
539PhosphorylationLTQDTALTENDDSDE
HHHCCCCCCCCCCHH
30.2227251275
544PhosphorylationALTENDDSDEYEEMS
CCCCCCCCHHHHHHH
34.8926471730
547PhosphorylationENDDSDEYEEMSEMK
CCCCCHHHHHHHHHH
23.3727642862
574 (in isoform 3)Phosphorylation-34.6829523821
574 (in isoform 2)Phosphorylation-34.6829523821
574 (in isoform 6)Phosphorylation-34.6829523821
575 (in isoform 6)Phosphorylation-20.9429523821
575 (in isoform 3)Phosphorylation-20.9429523821
575 (in isoform 2)Phosphorylation-20.9429523821
580 (in isoform 3)Phosphorylation-51.6829523821
580 (in isoform 2)Phosphorylation-51.6829523821
580 (in isoform 6)Phosphorylation-51.6829523821
585UbiquitinationAFSDEEVGNDTGQVG
ECCCCCCCCCCCCCC
29.5824816145
586UbiquitinationFSDEEVGNDTGQVGP
CCCCCCCCCCCCCCC
49.1724816145
636PhosphorylationGGHSQKESEAEEIDS
CCCCHHHHHHHHCCC
49.4927135362
643PhosphorylationSEAEEIDSEKETKLA
HHHHHCCCHHHHHHH
57.1227135362
682PhosphorylationLPDRGMNTESEENKD
CCCCCCCCCCHHHHH
31.8130576142
684PhosphorylationDRGMNTESEENKDFV
CCCCCCCCHHHHHHH
48.4430576142
696UbiquitinationDFVKKRESCKQDVIF
HHHHHHHHHCCCEEC
30.5524816145
697UbiquitinationFVKKRESCKQDVIFD
HHHHHHHHCCCEECC
3.8324816145
756 (in isoform 2)Phosphorylation-35.0924719451
801 (in isoform 6)Phosphorylation-33.6923879269
828PhosphorylationHGGRKEKTEILSDDL
ECCHHHCEEECCCCC
29.3822985185
866PhosphorylationINAENVESKKKTVGD
HCHHHHHCCCCCCCC
45.5525332170
870PhosphorylationNVESKKKTVGDDESV
HHHCCCCCCCCCCCC
38.3023312004
876PhosphorylationKTVGDDESVPTGYHS
CCCCCCCCCCCCCCC
40.1523312004
879PhosphorylationGDDESVPTGYHSKTE
CCCCCCCCCCCCCCC
48.4923312004
881PhosphorylationDESVPTGYHSKTEGA
CCCCCCCCCCCCCCC
12.8523312004
883PhosphorylationSVPTGYHSKTEGAER
CCCCCCCCCCCCCCC
32.5623312004
885PhosphorylationPTGYHSKTEGAERTN
CCCCCCCCCCCCCCC
42.5423312004
891PhosphorylationKTEGAERTNDDSSAE
CCCCCCCCCCCCCHH
34.2119664994
901UbiquitinationDSSAETIEKKEKANL
CCCHHHHHHHHHCCH
66.5524816145
902UbiquitinationSSAETIEKKEKANLE
CCHHHHHHHHHCCHH
63.4824816145
916PhosphorylationEERAICEYNENPKGY
HHHHHEECCCCCCCE
24.3028796482
931PhosphorylationMLDDADSSSLEILEN
ECCCCCCCCCHHHHC
39.2230576142
932PhosphorylationLDDADSSSLEILENS
CCCCCCCCCHHHHCC
33.6930576142
942PhosphorylationILENSETTPSKDMKK
HHHCCCCCCCCCCHH
22.8630576142
961PhosphorylationFLFKRVPSINQKIVK
EEEEECCCCCHHHHH
31.1723401153
979PhosphorylationEPLPEIKSIGDQIIL
CCCHHHCCCCCEEEE
37.1527966365
1017MethylationTERRSKSCTIL----
CHHHCCCCCCC----
2.93-
1017GeranylgeranylationTERRSKSCTIL----
CHHHCCCCCCC----
2.93-
1101 (in isoform 6)Ubiquitination--
1106 (in isoform 6)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 RPGR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPGR_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 RPGR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPGR1_HUMANRPGRIP1physical
10958648
PDE6D_HUMANPDE6Dphysical
9990021
SMC1A_HUMANSMC1Aphysical
16043481
SMC3_HUMANSMC3physical
16043481
IQCB1_HUMANIQCB1physical
15723066
RPGR1_HUMANRPGRIP1physical
25416956
BIRC6_HUMANBIRC6physical
26638075
NPHP4_HUMANNPHP4physical
26638075
NUDC_HUMANNUDCphysical
26638075
NUDC2_HUMANNUDCD2physical
26638075
NUDC3_HUMANNUDCD3physical
26638075
FTM_HUMANRPGRIP1Lphysical
26638075
UN45A_HUMANUNC45Aphysical
26638075
DNJA1_HUMANDNAJA1physical
26638075
DNJC7_HUMANDNAJC7physical
26638075
DYN2_HUMANDNM2physical
26638075
FKBP4_HUMANFKBP4physical
26638075
RHOA_HUMANRHOAphysical
26638075
TTF2_HUMANTTF2physical
26638075
TBA1A_HUMANTUBA1Aphysical
26638075
TBA1C_HUMANTUBA1Cphysical
26638075
TBB5_HUMANTUBBphysical
26638075
TBB2B_HUMANTUBB2Bphysical
26638075
TBB4A_HUMANTUBB4Aphysical
26638075
TBB4B_HUMANTUBB4Bphysical
26638075
FTM_HUMANRPGRIP1Lphysical
28514442
NPHP4_HUMANNPHP4physical
28514442
ORC2_HUMANORC2physical
28514442
ORC3_HUMANORC3physical
28514442
AT1A4_HUMANATP1A4physical
28514442
NPHP1_HUMANNPHP1physical
28514442
TBB1_HUMANTUBB1physical
28514442
SPSB3_HUMANSPSB3physical
28514442
MTMR1_HUMANMTMR1physical
28514442
PDE6D_HUMANPDE6Dphysical
28514442
IDE_HUMANIDEphysical
28514442
LRWD1_HUMANLRWD1physical
28514442
PDLI7_HUMANPDLIM7physical
28514442
PDE6D_HUMANPDE6Dphysical
27173435
FTM_HUMANRPGRIP1Lphysical
27173435
NEK4_HUMANNEK4physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300029Retinitis pigmentosa 3 (RP3)
300455Retinitis pigmentosa and sinorespiratory infections with or without deafness (RPDSI)
304020Cone-rod dystrophy, X-linked 1 (CORDX1)
300834Macular degeneration, X-linked, atrophic (MDXLA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPGR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASSSPECTROMETRY.

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