Reviewed,
UniProtKB/Swiss-Prot Q92834 (RPGR_HUMAN)
Last modified
November 3, 2009.
Version 105.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: X-linked retinitis pigmentosa GTPase regulator | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1020 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Could be a guanine-nucleotide releasing factor. |
| Subunit structure | Interacts with RPGRIP1. Ref.8 |
| Subcellular location | Golgi apparatus By similarity. |
| Tissue specificity | Heart, brain, placenta, lung, liver, muscle, kidney, retina, pancreas and fetal retinal pigment epithelium. Isoform 3 is found only in the retina. Colocalizes with RPGRIP1 in the outer segment of rod photoreceptors and cone outer segments. Ref.9 |
| Post-translational modification | Prenylated By similarity. |
| Involvement in disease | Defects in RPGR are the cause of retinitis pigmentosa type 3 (RP3) [MIM:300389]; also known as X-linked retinitis pigmentosa 3 (XLRP-3). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP3 is a form of choroidoretinal degeneration which is distinguished from other types by the presence in heterozygous women, with no visual defects, of a brilliant, scintillating, golden-hued, patchy appearance most striking around the macula, called a tapetal-like retinal reflex. Ref.1 Ref.2 Ref.7 Ref.10 Ref.11 Ref.12 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Defects in RPGR are the cause of retinitis pigmentosa type 15 (RP15) [MIM:300029]. RP15 belongs to the X-linked forms of retinitis pigmentosa (XLRP) which are among the most severe, because of their early onset, often leading to significant vision loss before the 4th decade. Defects in RPGR are the cause of retinitis pigmentosa with deafness and sinorespiratory infections (RPDSI) [MIM:300455]. RPDSI is characterized by the association of primary ciliary dyskinesia and Usher syndrome features. The phenotype has similarities with primary ciliary dyskinesia and Usher syndrome. Defects in RPGR are the cause of cone-rod dystrophy X-linked type 1 (CORDX1) [MIM:304020]; also known as cone dystrophy 1 (CO1). CORDs are inherited retinal dystrophies belonging to the group of pigmentary retinopathies. CORDs are characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. In CORDX1 the degree of rod-photoreceptor involvement can be variable, with degeneration increasing as the disease progresses. Affected individuals (essentially all of whom are males) present with decreased visual acuity, myopia, photophobia, abnormal color vision, full peripheral visual fields, decreased photopic electroretinographic responses, and granularity of the macular retinal pigment epithelium. Although penetrance appears to be nearly 100%, there is variable expressivity with respect to age at onset and severity of symptoms. Ref.19 |
| Sequence similarities | Contains 6 RCC1 repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Sensory transduction Vision |
| Cellular component | Golgi apparatus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Cone-rod dystrophy Deafness Disease mutation Retinitis pigmentosa |
| Domain | Repeat |
| Molecular function | Guanine-nucleotide releasing factor |
| PTM | Lipoprotein Methylation Prenylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | intracellular protein transport Traceable author statement. Source: ProtInc response to stimulusInferred from electronic annotation. Source: UniProtKB-KW visual perception Ref.10Inferred from mutant phenotype. Source: UniProtKB |
| Cellular component | Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW protein bindingTraceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: Q92834-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q92834-2) The sequence of this isoform differs from the canonical sequence as follows: 585-789: Missing. | ||||||
| Isoform 3 (identifier: Q92834-3) The sequence of this isoform differs from the canonical sequence as follows: 585-789: Missing. 841-851: DHEFSKTEELK → YSASHSQIVSV 852-1020: Missing. | ||||||
| Isoform 4 (identifier: Q92834-4) The sequence of this isoform differs from the canonical sequence as follows: 354-415: Missing. 585-789: Missing. | ||||||
| Isoform 5 (identifier: Q92834-5) The sequence of this isoform differs from the canonical sequence as follows: 473-480: YLLDEMTK → THHEPEFQ 481-1020: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1017 | 1017 | X-linked retinitis pigmentosa GTPase regulator | PRO_0000206638 | |||||
| Propeptide | 1018 – 1020 | 3 | Removed in mature form Potential | PRO_0000370844 | |||||
Regions | |||||||||
| Repeat | 54 – 105 | 52 | RCC1 1 | ||||||
| Repeat | 106 – 158 | 53 | RCC1 2 | ||||||
| Repeat | 159 – 208 | 50 | RCC1 3 | ||||||
| Repeat | 209 – 261 | 53 | RCC1 4 | ||||||
| Repeat | 262 – 313 | 52 | RCC1 5 | ||||||
| Repeat | 314 – 367 | 54 | RCC1 6 | ||||||
| Compositional bias | 530 – 903 | 374 | Glu-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1017 | 1 | Cysteine methyl ester Potential | ||||||
| Lipidation | 1017 | 1 | S-geranylgeranyl cysteine Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 354 – 415 | 62 | Missing in isoform 4. | VSP_005547 | |||||
| Alternative sequence | 473 – 480 | 8 | YLLDEMTK → THHEPEFQ in isoform 5. | VSP_009183 | |||||
| Alternative sequence | 481 – 1020 | 540 | Missing in isoform 5. | VSP_009184 | |||||
| Alternative sequence | 585 – 789 | 205 | Missing in isoform 2, isoform 3 and isoform 4. | VSP_005548 | |||||
| Alternative sequence | 841 – 851 | 11 | DHEFSKTEELK → YSASHSQIVSV in isoform 3. | VSP_005549 | |||||
| Alternative sequence | 852 – 1020 | 169 | Missing in isoform 3. | VSP_005550 | |||||
| Natural variant | 43 | 1 | G → E in RP3. Ref.17 | VAR_018057 | |||||
| Natural variant | 43 | 1 | G → R in RP3. Ref.17 | VAR_018058 | |||||
| Natural variant | 60 | 1 | G → V in RP3. Ref.10 Ref.11 Ref.17 | VAR_008501 | |||||
| Natural variant | 75 | 1 | I → V in RP3; could be a polymorphism. Ref.10 | VAR_008503 | |||||
| Natural variant | 76 | 1 | S → I: dbSNP rs1801685. Ref.13 | VAR_013624 | |||||
| Natural variant | 98 | 1 | H → Q in RP3. Ref.1 Ref.7 | VAR_008504 | |||||
| Natural variant | 99 | 1 | T → N in RP3. Ref.12 | VAR_013625 | |||||
| Natural variant | 127 | 1 | R → G in RP3. Ref.17 Ref.20 | VAR_018059 | |||||
| Natural variant | 130 | 1 | F → C in RP3. Ref.2 | VAR_006850 | |||||
| Natural variant | 152 | 1 | S → L in RP3. Ref.22 | VAR_025949 | |||||
| Natural variant | 173 | 1 | G → R in RP3 and RPDSI. Ref.20 Ref.24 | VAR_018060 | |||||
| Natural variant | 184 | 1 | Q → H: dbSNP rs5963403. | VAR_033259 | |||||
| Natural variant | 215 | 1 | G → V in RP3. Ref.1 Ref.22 | VAR_008505 | |||||
| Natural variant | 235 | 1 | P → S in RP3. Ref.2 | VAR_006851 | |||||
| Natural variant | 250 | 1 | C → R in RP3. Ref.1 Ref.7 | VAR_008506 | |||||
| Natural variant | 250 | 1 | C → Y in RP3. Ref.20 | VAR_018061 | |||||
| Natural variant | 258 | 1 | Missing in RP3. | VAR_018062 | |||||
| Natural variant | 262 | 1 | A → G in RP3; could be a polymorphism. Ref.10 | VAR_008507 | |||||
| Natural variant | 267 | 1 | G → E in RP3. | VAR_018063 | |||||
| Natural variant | 267 | 1 | G → R in RP3. Ref.20 | VAR_026127 | |||||
| Natural variant | 275 | 1 | G → S in RP3. Ref.2 | VAR_006852 | |||||
| Natural variant | 285 | 1 | E → G in RP3. Ref.20 | VAR_026128 | |||||
| Natural variant | 289 | 1 | I → V in RP3. Ref.12 | VAR_013626 | |||||
| Natural variant | 296 – 300 | 5 | Missing in RP3. | VAR_013627 | |||||
| Natural variant | 302 | 1 | C → R in RP3. Ref.15 | VAR_011561 | |||||
| Natural variant | 302 | 1 | C → Y in RP3. Ref.17 | VAR_018064 | |||||
| Natural variant | 312 | 1 | D → N in RP3. Ref.21 | VAR_018065 | |||||
| Natural variant | 312 | 1 | D → Y in RP3. Ref.21 | VAR_018066 | |||||
| Natural variant | 320 | 1 | G → R in RP3. Ref.21 | VAR_018067 | |||||
| Natural variant | 345 | 1 | N → D Rare polymorphism. dbSNP rs41305223. Ref.17 Ref.19 | VAR_018068 | |||||
| Natural variant | 425 | 1 | R → K: dbSNP rs1801687. Ref.10 Ref.17 Ref.13 Ref.16 | VAR_008508 | |||||
| Natural variant | 431 | 1 | I → V | VAR_008509 | |||||
| Natural variant | 436 | 1 | G → D in RP3. Ref.17 Ref.18 Ref.20 | VAR_008510 | |||||
| Natural variant | 526 | 1 | Missing | VAR_011562 | |||||
| Natural variant | 533 | 1 | T → M: dbSNP rs41312104. Ref.16 | VAR_011563 | |||||
| Natural variant | 566 | 1 | G → E: dbSNP rs1801688. Ref.10 Ref.17 Ref.13 Ref.16 | VAR_008511 | |||||
Experimental info | |||||||||
| Sequence conflict | 1 – 3 | 3 | MRE → MAKLRRSTTTAL Ref.4 | ||||||
| Sequence conflict | 190 | 1 | K → N in CAC86116. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3)." Meindl A., Dry K.L., Herrmann K., Manson F.D., Ciccodicola A., Edgar A.J., Carvalho M.R.S., Achatz H., Hellebrand H., Lennon A.A., Migliaccio C., Porter K., Zrenner E., Bird A.C., Jay M., Lorenz B., Wittwer B., D'Urso M., Meitinger T., Wright A.F. Nat. Genet. 13:35-42(1996) [PubMed: 8673101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), VARIANTS RP3 GLN-98; VAL-215; ARG-250 AND 296-THR--ILE-300 DEL. |
| [2] | "Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1." Roepman R., van Duijnhoven G., Rosenberg T., Pinckers A.J.L.G., Bleeker-Wagemakers L.M., Bergen A.A.B., Post J., Beck A., Reinhardt R., Ropers H.-H., Cremers F., Berger W. Hum. Mol. Genet. 5:1035-1041(1996) [PubMed: 8817343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS RP3 CYS-130; SER-235 AND SER-275. Tissue: Retina. |
| [3] | Berger W. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [4] | "RPGR transcription studies in mouse and human tissues reveal a retina-specific isoform that is disrupted in a patient with X-linked retinitis pigmentosa." Kirschner R., Rosenberg T., Schultz-Heienbrok R., Lenzner S., Feil S., Roepman R., Cremers F.P.M., Ropers H.-H., Berger W. Hum. Mol. Genet. 8:1571-1578(1999) [PubMed: 10401007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). Tissue: Retina. |
| [5] | "DNA sequence comparison of human and mouse retinitis pigmentosa GTPase regulator (RPGR) identifies tissue-specific exons and putative regulatory elements." Kirschner R., Erturk D., Zeitz C., Sahin S., Ramser J., Cremers F.P.M., Ropers H.-H., Berger W. Hum. Genet. 109:271-278(2001) [PubMed: 11702207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). |
| [7] | "Mutational hot spot within a new RPGR exon in X-linked retinitis pigmentosa." Vervoort R., Lennon A.A., Bird A.C., Tulloch B., Axton R., Miano M.G., Meindl A., Meitinger T., Ciccodicola A., Wright A.F. Nat. Genet. 25:462-466(2000) [PubMed: 10932196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 525-840 (ISOFORM 1), VARIANTS RP3 GLN-98 AND ARG-250. |
| [8] | "The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors." Roepman R., Bernoud-Hubac N., Schick D.E., Maugeri A., Berger W., Ropers H.-H., Cremers F.P.M., Ferreira P.A. Hum. Mol. Genet. 9:2095-2105(2000) [PubMed: 10958648] [Abstract] Cited for: INTERACTION WITH RPGRIP1. |
| [9] | "Species-specific subcellular localization of RPGR and RPGRIP isoforms: implications for the phenotypic variability of congenital retinopathies among species." Mavlyutov T.A., Zhao H., Ferreira P.A. Hum. Mol. Genet. 11:1899-1907(2002) [PubMed: 12140192] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [10] | "Spectrum of mutations in the RPGR gene that are identified in 20% of families with X-linked retinitis pigmentosa." Buraczynska M., Wu W., Fujita R., Buraczynska K., Phelps E., Andreasson S., Bennett J., Birch D.G., Fishman G.A., Hoffman D.R., Inana G., Jacobson S.G., Musarella M.A., Sieving P.A., Swaroop A. Am. J. Hum. Genet. 61:1287-1292(1997) [PubMed: 9399904] [Abstract] Cited for: VARIANTS RP3 VAL-60; VAL-75 AND GLY-262, VARIANTS LYS-425; VAL-431 AND GLU-566. |
| [11] | "X-linked retinitis pigmentosa in two families with a missense mutation in the RPGR gene and putative change of glycine to valine at codon 60." Fishman G.A., Grover S., Jacobson S.G., Alexander K.R., Derlacki D.J., Wu W., Buraczynska M., Swaroop A. Ophthalmology 105:2286-2296(1998) [PubMed: 9855162] [Abstract] Cited for: VARIANT RP3 VAL-60. |
| [12] | "Mutation analysis of the RPGR gene reveals novel mutations in south European patients with X-linked retinitis pigmentosa." Miano M.G., Testa F., Strazzullo M., Trujillo M., De Bernardo C., Grammatico B., Simonelli F., Mangino M., Torrente I., Ruberto G., Beneyto M., Antinolo G., Rinaldi E., Danesino C., Ventruto V., D'Urso M., Ayuso C., Baiget M., Ciccodicola A. Eur. J. Hum. Genet. 7:687-694(1999) [PubMed: 10482958] [Abstract] Cited for: VARIANTS RP3 ASN-99 AND VAL-289. |
| [13] | "Identification of novel RPGR (retinitis pigmentosa GTPase regulator) mutations in a subset of X-linked retinitis pigmentosa families segregating with the RP3 locus." Zito I., Thiselton D.L., Gorin M.B., Stout J.T., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J. Hum. Genet. 105:57-62(1999) [PubMed: 10480356] [Abstract] Cited for: VARIANTS ILE-76; LYS-425 AND GLU-566. |
| [14] | "Remapping of the RP15 locus for X-linked cone-rod degeneration to Xp11.4-p21.1, and identification of a de novo insertion in the RPGR exon ORF15." Mears A.J., Hiriyanna S., Vervoort R., Yashar B., Gieser L., Fahrner S., Daiger S.P., Heckenlively J.R., Sieving P.A., Wright A.F., Swaroop A. Am. J. Hum. Genet. 67:1000-1003(2000) [PubMed: 10970770] [Abstract] Cited for: INVOLVEMENT IN RP15. |
| [15] | "Novel mutations of the RPGR gene in RP3 families." Zito I., Gorin M.B., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J. Hum. Mutat. 15:386-386(2000) [PubMed: 10737996] [Abstract] Cited for: VARIANT RP3 ARG-302. |
| [16] | "Sequence variation within the RPGR gene: evidence for a founder complex allele." Zito I., Morris A., Tyson P., Winship I., Sharp D., Gilbert D., Thiselton D.L., Bhattacharya S.S., Hardcastle A.J. Hum. Mutat. 16:273-274(2000) [PubMed: 10980543] [Abstract] Cited for: VARIANTS LYS-425; GLN-526 DEL; MET-533 AND GLU-566. |
| [17] | "X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function." Sharon D., Bruns G.A.P., McGee T.L., Sandberg M.A., Berson E.L., Dryja T.P. Invest. Ophthalmol. Vis. Sci. 41:2712-2721(2000) [PubMed: 10937588] [Abstract] Cited for: VARIANTS RP3 ARG-43; GLU-43; VAL-60; GLY-127; TYR-302 AND ASP-436, VARIANTS ASP-345; LYS-425; VAL-431 AND GLU-566. |
| [18] | "Five novel RPGR mutations in families with X-linked retinitis pigmentosa." Guevara-Fujita M., Fahrner S., Buraczynska K., Cook J., Wheaton D., Cortes F., Vicencio C., Pena M., Fishman G.A., Mintz-Hittner H., Birch D.G., Hoffman D.R., Mears A.J., Fujita R., Swaroop A. Hum. Mutat. 17:151-151(2001) [PubMed: 11180598] [Abstract] Cited for: VARIANT RP3 ASP-436. |
| [19] | "X-linked cone-rod dystrophy (locus COD1): identification of mutations in RPGR exon ORF15." Demirci F.Y.K., Rigatti B.W., Wen G., Radak A.L., Mah T.S., Baic C.L., Traboulsi E.I., Alitalo T., Ramser J., Gorin M.B. Am. J. Hum. Genet. 70:1049-1053(2002) [PubMed: 11857109] [Abstract] Cited for: INVOLVEMENT IN CORDX1, VARIANT ASP-345. |
| [20] | "A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa." Breuer D.K., Yashar B.M., Filippova E., Hiriyanna S., Lyons R.H., Mears A.J., Asaye B., Acar C., Vervoort R., Wright A.F., Musarella M.A., Wheeler P., MacDonald I., Iannaccone A., Birch D., Hoffman D.R., Fishman G.A., Heckenlively J.R. Swaroop A.Am. J. Hum. Genet. 70:1545-1554(2002) [PubMed: 11992260] [Abstract] Cited for: VARIANTS RP3 GLY-127; ARG-173; TYR-250; LEU-258 DEL; ARG-267; GLY-285 AND ASP-436. |
| [21] | "RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa." Sharon D., Sandberg M.A., Rabe V.W., Stillberger M., Dryja T.P., Berson E.L. Am. J. Hum. Genet. 73:1131-1146(2003) [PubMed: 14564670] [Abstract] Cited for: VARIANTS RP3 ASN-312; TYR-312 AND ARG-320. |
| [22] | "X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15." Bader I., Brandau O., Achatz H., Apfelstedt-Sylla E., Hergersberg M., Lorenz B., Wissinger B., Wittwer B., Rudolph G., Meindl A., Meitinger T. Invest. Ophthalmol. Vis. Sci. 44:1458-1463(2003) [PubMed: 12657579] [Abstract] Cited for: VARIANTS RP3 LEU-152 AND VAL-215. |
| [23] | "RPGR mutation associated with retinitis pigmentosa, impaired hearing, and sinorespiratory infections." Zito I., Downes S.M., Patel R.J., Cheetham M.E., Ebenezer N.D., Jenkins S.A., Bhattacharya S.S., Webster A.R., Holder G.E., Bird A.C., Bamiou D.E., Hardcastle A.J. J. Med. Genet. 40:609-615(2003) [PubMed: 12920075] [Abstract] Cited for: INVOLVEMENT IN RPDSI. |
| [24] | "Clinical and immunohistochemical evidence for an X linked retinitis pigmentosa syndrome with recurrent infections and hearing loss in association with an RPGR mutation." Iannaccone A., Breuer D.K., Wang X.F., Kuo S.F., Normando E.M., Filippova E., Baldi A., Hiriyanna S., MacDonald C.B., Baldi F., Cosgrove D., Morton C.C., Swaroop A., Jablonski M.M. J. Med. Genet. 40:E118-E118(2003) [PubMed: 14627685] [Abstract] Cited for: VARIANT RPDSI ARG-173. |
| + | Additional computationally mapped references. |
Web resources
| Mutations of the RPGR gene Retina International's Scientific Newsletter |
| GeneReviews |
Cross-references
Sequence databases | |
|---|---|
| U57629 mRNA. Translation: AAC50481.1. X97668 mRNA. Translation: CAA66258.1. AJ238395 mRNA. Translation: CAB54002.1. AJ318463 Genomic DNA. Translation: CAC86116.1. BC031624 mRNA. Translation: AAH31624.1. AF286471 Genomic DNA. Translation: AAG00550.1. | |
| IPI | IPI00023757. IPI00215806. IPI00215807. IPI00215808. IPI00397031. |
| RefSeq | NP_000319.1. |
| UniGene | Hs.61438 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I2M based on UniProtKB P18754. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q92834. |
PTM databases | |
| PhosphoSite | Q92834. |
Proteomic databases | |
| PRIDE | Q92834. |
Genome annotation databases | |
| Ensembl | ENST00000309513; ENSP00000308783; ENSG00000156313; Homo sapiens. [Genome view] ENST00000318842; ENSP00000322219; ENSG00000156313; Homo sapiens. [Genome view] ENST00000338898; ENSP00000340208; ENSG00000156313; Homo sapiens. [Genome view] ENST00000339363; ENSP00000343671; ENSG00000156313; Homo sapiens. [Genome view] ENST00000342811; ENSP00000339531; ENSG00000156313; Homo sapiens. [Genome view] ENST00000378505; ENSP00000367766; ENSG00000156313; Homo sapiens. [Genome view] |
| GeneID | 6103. |
| KEGG | hsa:6103. |
| UCSC | uc004deb.1. human. |
Organism-specific databases | |
| CTD | 6103. |
| GeneCards | GC0XM038013. |
| H-InvDB | HIX0016727. |
| HGNC | HGNC:10295. RPGR. |
| HPA | HPA001593. |
| MIM | 300029. phenotype. 300389. phenotype. 300455. phenotype. 304020. phenotype. 312610. gene. |
| Orphanet | 49382. Achromatopsia. 1872. Cone rod dystrophy. 244. Primary ciliary dyskinesia. 791. Retinitis pigmentosa. |
| PharmGKB | PA34656. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q92834. |
| OMA | NNNEPLP. |
Gene expression databases | |
| ArrayExpress | Q92834. |
| Bgee | Q92834. |
| CleanEx | HS_RPGR. |
| Genevestigator | Q92834. |
| GermOnline | ENSG00000156313. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000408. Reg_chr_condens. IPR009091. Reg_csome_cond/b-lactamase_inh. [Graphical view] |
| Gene3D | G3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 1 hit. |
| Pfam | PF00415. RCC1. 4 hits. [Graphical view] |
| PRINTS | PR00633. RCCNDNSATION. |
| PROSITE | PS00625. RCC1_1. False negative. PS00626. RCC1_2. 4 hits. PS50012. RCC1_3. 6 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 23741. |
| SOURCE | Search... |
Entry information
| Entry name | RPGR_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q92834 Secondary accession number(s): O00702 Q9UMR1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


