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Q92834 (RPGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
X-linked retinitis pigmentosa GTPase regulator
Gene names
Name:RPGR
Synonyms:RP3, XLRP3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1020 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could be a guanine-nucleotide releasing factor. Play a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Ref.20

Subunit structure

Interacts with PDE6D and RPGRIP1. Interacts with NPM1. Interacts with RPGRIP1L. Ref.10 Ref.12 Ref.17 Ref.19

Subcellular location

Golgi apparatus By similarity. Cytoplasm › cytoskeleton › cilium basal body By similarity. Cytoplasm › cytoskeleton › centrosome Ref.17.

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.15

Post-translational modification

Prenylated By similarity.

Involvement in disease

Defects in RPGR are the cause of retinitis pigmentosa type 3 (RP3) [MIM:300029]; also known as X-linked retinitis pigmentosa 3 (XLRP-3) or retinitis pigmentosa type 15 (RP15). A X-linked retinal dystrophy belonging to the group of pigmentary retinopathies. RP is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. 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. In RP3, affected males have a severe phenotype, and carrier females show a wide spectrum of clinical features ranging from completely asymptomatic to severe retinitis pigmentosa. Heterozygous women can manifest a form of choroidoretinal degeneration which is distinguished from other types by the absence of visual defects in the presence of a brilliant, scintillating, golden-hued, patchy appearance most striking around the macula, called a tapetal-like retinal reflex. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Defects in RPGR are the cause of retinitis pigmentosa and sinorespiratory infections with or without deafness (RPDSI) [MIM:300455]. A disease characterized by the association primary ciliary dyskinesia features with retinitis pigmentosa. Some patients also manifest deafness. Ref.16 Ref.32

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.13

Defects in RPGR are a cause of macular degeneration X-linked atrophic (MDXLA) [MIM:300834]. MDXLA is an ocular disorder characterized by macular atrophy causing progressive loss of visual acuity with minimal peripheral visual impairment. Some patients manifest extensive macular degeneration plus peripheral loss of retinal pigment epithelium and choriocapillaries. Full-field electroretinograms (ERGs) show normal cone and rod responses in some affected males despite advanced macular degeneration. Ref.14

Sequence similarities

Contains 6 RCC1 repeats.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10171017X-linked retinitis pigmentosa GTPase regulator
PRO_0000206638
Propeptide1018 – 10203Removed in mature form Potential
PRO_0000370844

Regions

Repeat54 – 10552RCC1 1
Repeat106 – 15853RCC1 2
Repeat159 – 20850RCC1 3
Repeat209 – 26153RCC1 4
Repeat262 – 31352RCC1 5
Repeat314 – 36754RCC1 6
Compositional bias530 – 903374Glu-rich

Amino acid modifications

Modified residue5441Phosphoserine Ref.18
Modified residue10171Cysteine methyl ester Potential
Lipidation10171S-geranylgeranyl cysteine Potential

Natural variations

Alternative sequence354 – 41562Missing in isoform 4.
VSP_005547
Alternative sequence473 – 4808YLLDEMTK → THHEPEFQ in isoform 5.
VSP_009183
Alternative sequence481 – 1020540Missing in isoform 5.
VSP_009184
Alternative sequence585 – 789205Missing in isoform 2, isoform 3 and isoform 4.
VSP_005548
Alternative sequence841 – 85111DHEFSKTEELK → YSASHSQIVSV in isoform 3.
VSP_005549
Alternative sequence852 – 1020169Missing in isoform 3.
VSP_005550
Natural variant431G → E in RP3. Ref.27
VAR_018057
Natural variant431G → R in RP3. Ref.27
VAR_018058
Natural variant601G → V in RP3. Ref.21 Ref.22 Ref.27
VAR_008501
Natural variant751I → V in RP3; could be a polymorphism. Ref.21
VAR_008503
Natural variant761S → I. Ref.24
Corresponds to variant rs1801685 [ dbSNP | Ensembl ].
VAR_013624
Natural variant981H → Q in RP3; reduces interaction with PDE6D. Ref.1 Ref.9 Ref.10
VAR_008504
Natural variant991T → N in RP3. Ref.23
VAR_013625
Natural variant1271R → G in RP3. Ref.27 Ref.29
VAR_018059
Natural variant1301F → C in RP3; reduces interaction with PDE6D. Ref.2 Ref.10
VAR_006850
Natural variant1521S → L in RP3. Ref.31
VAR_025949
Natural variant1731G → R in RP3 and RPDSI. Ref.29 Ref.32
VAR_018060
Natural variant1841Q → H.
Corresponds to variant rs5963403 [ dbSNP | Ensembl ].
VAR_033259
Natural variant2151G → V in RP3; reduces interaction with PDE6D. Ref.1 Ref.10 Ref.31
VAR_008505
Natural variant2351P → S in RP3; reduces interaction with PDE6D. Ref.2 Ref.10
VAR_006851
Natural variant2501C → R in RP3; reduces interaction with PDE6D. Ref.1 Ref.9 Ref.10
VAR_008506
Natural variant2501C → Y in RP3. Ref.29
VAR_018061
Natural variant2581Missing in RP3.
VAR_018062
Natural variant2621A → G in RP3; could be a polymorphism. Ref.21
VAR_008507
Natural variant2671G → E in RP3.
VAR_018063
Natural variant2671G → R in RP3. Ref.29
VAR_026127
Natural variant2751G → S in RP3; reduces interaction with PDE6D. Ref.2 Ref.10
VAR_006852
Natural variant2851E → G in RP3. Ref.29
VAR_026128
Natural variant2891I → V in RP3. Ref.23
VAR_013626
Natural variant296 – 3005Missing in RP3.
VAR_013627
Natural variant3021C → R in RP3. Ref.25
VAR_011561
Natural variant3021C → Y in RP3. Ref.27
VAR_018064
Natural variant3121D → N in RP3. Ref.30
VAR_018065
Natural variant3121D → Y in RP3. Ref.30
VAR_018066
Natural variant3201G → R in RP3. Ref.30
VAR_018067
Natural variant3451N → D Rare polymorphism. Ref.13 Ref.27
Corresponds to variant rs41305223 [ dbSNP | Ensembl ].
VAR_018068
Natural variant4251R → K. Ref.21 Ref.24 Ref.26 Ref.27
Corresponds to variant rs1801687 [ dbSNP | Ensembl ].
VAR_008508
Natural variant4311I → V. Ref.21 Ref.27
VAR_008509
Natural variant4361G → D in RP3. Ref.27 Ref.28 Ref.29
VAR_008510
Natural variant5261Missing.
VAR_011562
Natural variant5331T → M. Ref.26
Corresponds to variant rs41312104 [ dbSNP | Ensembl ].
VAR_011563
Natural variant5661G → E. Ref.21 Ref.24 Ref.26 Ref.27
Corresponds to variant rs1801688 [ dbSNP | Ensembl ].
VAR_008511

Experimental info

Mutagenesis361V → F: Does not reduce interaction with PDE6D. Ref.10
Sequence conflict1 – 33MRE → MAKLRRSTTTAL in CAB54002. Ref.4
Sequence conflict1901K → N in CAC86116. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: EAB16275A9A436C3

FASTA1,020113,387
        10         20         30         40         50         60 
MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV TGNNKLYMFG 

        70         80         90        100        110        120 
SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL VSTEGGNVYA TGGNNEGQLG 

       130        140        150        160        170        180 
LGDTEERNTF HVISFFTSEH KIKQLSAGSN TSAALTEDGR LFMWGDNSEG QIGLKNVSNV 

       190        200        210        220        230        240 
CVPQQVTIGK PVSWISCGYY HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE 

       250        260        270        280        290        300 
IPEKVIQVAC GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 

       310        320        330        340        350        360 
SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI VKLVACGGCH 

       370        380        390        400        410        420 
MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN VLQRTLSARM RRRERERSPD 

       430        440        450        460        470        480 
SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC SERNLQESVL SEQDLMQPEE PDYLLDEMTK 

       490        500        510        520        530        540 
EAEIDNSSTV ESLGETTDIL NMTHIMSLNS NEKSLKLSPV QKQKKQQTIG ELTQDTALTE 

       550        560        570        580        590        600 
NDDSDEYEEM SEMKEGKACK QHVSQGIFMT QPATTIEAFS DEEVGNDTGQ VGPQADTDGE 

       610        620        630        640        650        660 
GLQKEVYRHE NNNGVDQLDA KEIEKESDGG HSQKESEAEE IDSEKETKLA EIAGMKDLRE 

       670        680        690        700        710        720 
REKSTKKMSP FFGNLPDRGM NTESEENKDF VKKRESCKQD VIFDSERESV EKPDSYMEGA 

       730        740        750        760        770        780 
SESQQGIADG FQQPEAIEFS SGEKEDDEVE TDQNIRYGRK LIEQGNEKET KPIISKSMAK 

       790        800        810        820        830        840 
YDFKCDRLSE IPEEKEGAED SKGNGIEEQE VEANEENVKV HGGRKEKTEI LSDDLTDKAE 

       850        860        870        880        890        900 
DHEFSKTEEL KLEDVDEEIN AENVESKKKT VGDDESVPTG YHSKTEGAER TNDDSSAETI 

       910        920        930        940        950        960 
EKKEKANLEE RAICEYNENP KGYMLDDADS SSLEILENSE TTPSKDMKKT KKIFLFKRVP 

       970        980        990       1000       1010       1020 
SINQKIVKNN NEPLPEIKSI GDQIILKSDN KDADQNHMSQ NHQNIPPTNT ERRSKSCTIL

« Hide

Isoform 2 [UniParc].

Checksum: 70D84EAD988348D1
Show »

FASTA81590,245
Isoform 3 [UniParc].

Checksum: BE8E98184F0404A6
Show »

FASTA64670,981
Isoform 4 [UniParc].

Checksum: A84202BD00B84930
Show »

FASTA75383,394
Isoform 5 [UniParc].

Checksum: 6766EA259A232631
Show »

FASTA48052,628

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 DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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).
[9]"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.
[10]"The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase."
Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.
Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999) [PubMed: 9990021] [Abstract]
Cited for: INTERACTION WITH PDE6D, CHARACTERIZATION OF RP3 VARIANTS GLN-98; CYS-130; VAL-215; SER-235; ARG-250 AND SER-275, MUTAGENESIS OF VAL-36.
[11]"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 RP3/RP15.
[12]"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.
[13]"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.
[14]"X-linked recessive atrophic macular degeneration from RPGR mutation."
Ayyagari R., Demirci F.Y., Liu J., Bingham E.L., Stringham H., Kakuk L.E., Boehnke M., Gorin M.B., Richards J.E., Sieving P.A.
Genomics 80:166-171(2002) [PubMed: 12160730] [Abstract]
Cited for: INVOLVEMENT IN MDXLA.
[15]"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.
[16]"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.
[17]"RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin."
Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H., Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U., Vervoort R., Swaroop A., Wright A.F.
Hum. Mol. Genet. 14:1183-1197(2005) [PubMed: 15772089] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NPM1.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[19]"A common allele in RPGRIP1L is a modifier of retinal degeneration in ciliopathies."
Khanna H., Davis E.E., Murga-Zamalloa C.A., Estrada-Cuzcano A., Lopez I., den Hollander A.I., Zonneveld M.N., Othman M.I., Waseem N., Chakarova C.F., Maubaret C., Diaz-Font A., MacDonald I., Muzny D.M., Wheeler D.A., Morgan M., Lewis L.R., Logan C.V. expand/collapse author list , Tan P.L., Beer M.A., Inglehearn C.F., Lewis R.A., Jacobson S.G., Bergmann C., Beales P.L., Attie-Bitach T., Johnson C.A., Otto E.A., Bhattacharya S.S., Hildebrandt F., Gibbs R.A., Koenekoop R.K., Swaroop A., Katsanis N.
Nat. Genet. 41:739-745(2009) [PubMed: 19430481] [Abstract]
Cited for: INTERACTION WITH RPGRIP1L.
[20]"The role of RPGR in cilia formation and actin stability."
Gakovic M., Shu X., Kasioulis I., Carpanini S., Moraga I., Wright A.F.
Hum. Mol. Genet. 20:4840-4850(2011) [PubMed: 21933838] [Abstract]
Cited for: FUNCTION.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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. expand/collapse author list , Jacobson S.G., Sieving P.A., 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.
[30]"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.
[31]"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.
[32]"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

EMBL
GenBank
DDBJ		U57629 mRNA. Translation: AAC50481.1.
X97668 mRNA. Translation: CAA66258.1.
AJ238395 mRNA. Translation: CAB54002.1.
AJ318463 Genomic DNA. Translation: CAC86116.1.
AL606748 Genomic DNA. Translation: CAI95407.1.
CH471141 Genomic DNA. Translation: EAW59441.1.
BC031624 mRNA. Translation: AAH31624.1.
AF286471 Genomic DNA. Translation: AAG00550.1.
IPIIPI00023757.
IPI00215806.
IPI00215807.
IPI00215808.
IPI00397031.
RefSeqNP_000319.1. NM_000328.2.
UniGeneHs.61438.

3D structure databases

ProteinModelPortalQ92834.
SMRQ92834. Positions 7-367.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ92834.

PTM databases

PhosphoSiteQ92834.

Polymorphism databases

DMDM23503098.

Proteomic databases

PRIDEQ92834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339363; ENSP00000343671; ENSG00000156313.
GeneID6103.
KEGGhsa:6103.
UCSCuc004deb.1. human.

Organism-specific databases

CTD6103.
GeneCardsGC0XM038128.
HGNCHGNC:10295. RPGR.
HPAHPA001593.
MIM300029. phenotype.
300455. phenotype.
300834. phenotype.
304020. phenotype.
312610. gene.
neXtProtNX_Q92834.
Orphanet49382. Achromatopsia.
1872. Cone rod dystrophy.
244. Primary ciliary dyskinesia.
247522. Primary ciliary dyskinesia - retinitis pigmentosa.
791. Retinitis pigmentosa.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16592.
GeneTreeENSGT00590000082902.
HOVERGENHBG026899.
PhylomeDBQ92834.

Gene expression databases

ArrayExpressQ92834.
BgeeQ92834.
CleanExHS_RPGR.
GenevestigatorQ92834.
GermOnlineENSG00000156313. Homo sapiens.

Family and domain databases

InterProIPR000408. Reg_chr_condens.
IPR009091. Reg_csome_cond/b-lactamase_inh.
[Graphical view]
Gene3DG3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 1 hit.
PfamPF00415. RCC1. 6 hits.
[Graphical view]
PRINTSPR00633. RCCNDNSATION.
SUPFAMSSF50985. RCC1/BLIP-II. 1 hit.
PROSITEPS00625. RCC1_1. False negative.
PS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio23741.
SOURCESearch...

Entry information

Entry nameRPGR_HUMAN
AccessionPrimary (citable) accession number: Q92834
Secondary accession number(s): B1ARN3 expand/collapse secondary AC list , O00702, O00737, Q8N5T6, Q93039, Q9HD29, Q9UMR1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2002
Last modified: January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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