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Q92834 (RPGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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. Ref.21

Subunit structure

Interacts with PDE6D and RPGRIP1. Isoform 6 interacts with NPM1 (via C-terminus). Interacts with RPGRIP1L. Isoform 6 interacts with SMC1A and SMC3. Interacts with CEP290 By similarity. Interacts with DFNB31 By similarity. Ref.10 Ref.12 Ref.17 Ref.18 Ref.20

Subcellular location

Cytoplasmcytoskeletonflagellum axoneme By similarity. Golgi apparatus Ref.17.

Isoform 6: Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletoncilium basal body. Cytoplasmcytoskeletoncilium axoneme 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

Retinitis pigmentosa 3 (RP3) [MIM:300029]: A X-linked retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.33

Cone-rod dystrophy, X-linked 1 (CORDX1) [MIM:304020]: An inherited retinal dystrophy 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 cone-rod dystrophy X-linked type 1 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Macular degeneration, X-linked, atrophic (MDXLA) [MIM:300834]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Contains 6 RCC1 repeats.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Sensory transduction
Vision
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCiliopathy
Cone-rod dystrophy
Deafness
Disease mutation
Retinitis pigmentosa
   DomainRepeat
   Molecular functionGuanine-nucleotide releasing factor
   PTMLipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcilium assembly

Inferred from mutant phenotype Ref.21. Source: UniProtKB

eye photoreceptor cell development

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Traceable author statement Ref.10. Source: ProtInc

intraciliary transport

Inferred from sequence or structural similarity. Source: UniProtKB

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Inferred from mutant phenotype Ref.22. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Inferred from direct assay Ref.17. Source: UniProtKB

ciliary basal body

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment

Inferred from direct assay Ref.15. Source: UniProtKB

sperm flagellum

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionguanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE6DO439249EBI-6558417,EBI-712685
Pde6dO550573EBI-6558417,EBI-6558402From a different organism.

Alternative products

This entry describes 6 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.
Isoform 6 (identifier: Q92834-6)

Also known as: ORF15;

The sequence of this isoform differs from the canonical sequence as follows:
     585-1020: GNDTGQVGPQ...ERRSKSCTIL → EIPEEKEGAE...NVLPHYLELK

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 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 – 1020436GNDTG…SCTIL → EIPEEKEGAEDSKGNGIEEQ EVEANEENVKVHGGRKEKTE ILSDDLTDKAEVSEGKAKSV GEAEDGPEGRGDGTCEEGSS GAEHWQDEEREKGEKDKGRG EMERPGEGEKELAEKEEWKK RDGEEQEQKEREQGHQKERN QEMEEGGEEEHGEGEEEEGD REEEEEKEGEGKEEGEGEEV EGEREKEEGERKKEERAGKE EKGEEEGDQGEGEEEETEGR GEEKEEGGEVEGGEVEEGKG EREEEEEEGEGEEEEGEGEE EEGEGEEEEGEGKGEEEGEE GEGEEEGEEGEGEGEEEEGE GEGEEEGEGEGEEEEGEGEG EEEGEGEGEEEEGEGKGEEE GEEGEGEGEEEEGEGEGEDG EGEGEEEEGEWEGEEEEGEG EGEEEGEGEGEEGEGEGEEE EGEGEGEEEEGEEEGEEEGE GEEEGEGEGEEEEEGEVEGE VEGEEGEGEGEEEEGEEEGE EREKEGEGEENRRNREEEEE EEGKYQETGEEENERQDGEE YKKVSKIKGSVKYGKHKTYQ KKSVTNTQGNGKEQRSKMPV QSKRLLKNGPSGSKKFWNNV LPHYLELK in isoform 6.
VSP_044559
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.28
VAR_018057
Natural variant431G → R in RP3. Ref.28
VAR_018058
Natural variant601G → V in RP3. Ref.22 Ref.23 Ref.28
VAR_008501
Natural variant751I → V in RP3; unknown pathological significance. Ref.22
Corresponds to variant rs111631988 [ dbSNP | Ensembl ].
VAR_008503
Natural variant761S → I. Ref.25
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.24
VAR_013625
Natural variant1271R → G in RP3. Ref.28 Ref.30
VAR_018059
Natural variant1301F → C in RP3; reduces interaction with PDE6D. Ref.2 Ref.10
VAR_006850
Natural variant1521S → L in RP3. Ref.32
VAR_025949
Natural variant1731G → R in RP3 and RPDSI. Ref.30 Ref.33
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.32
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.30
VAR_018061
Natural variant2581Missing in RP3. Ref.30
VAR_018062
Natural variant2621A → G in RP3; unknown pathological significance. Ref.22
Corresponds to variant rs138018739 [ dbSNP | Ensembl ].
VAR_008507
Natural variant2671G → E in RP3.
VAR_018063
Natural variant2671G → R in RP3. Ref.30
VAR_026127
Natural variant2751G → S in RP3; reduces interaction with PDE6D. Ref.2 Ref.10
VAR_006852
Natural variant2851E → G in RP3. Ref.30
VAR_026128
Natural variant2891I → V in RP3. Ref.24
VAR_013626
Natural variant296 – 3005Missing in RP3.
VAR_013627
Natural variant3021C → R in RP3. Ref.26
VAR_011561
Natural variant3021C → Y in RP3. Ref.28
Corresponds to variant rs62640590 [ dbSNP | Ensembl ].
VAR_018064
Natural variant3121D → N in RP3. Ref.31
VAR_018065
Natural variant3121D → Y in RP3. Ref.31
VAR_018066
Natural variant3201G → R in RP3. Ref.31
VAR_018067
Natural variant3451N → D Rare polymorphism. Ref.13 Ref.28
Corresponds to variant rs41305223 [ dbSNP | Ensembl ].
VAR_018068
Natural variant4251R → K. Ref.22 Ref.25 Ref.27 Ref.28
Corresponds to variant rs1801687 [ dbSNP | Ensembl ].
VAR_008508
Natural variant4311I → V. Ref.22 Ref.28
Corresponds to variant rs62635003 [ dbSNP | Ensembl ].
VAR_008509
Natural variant4361G → D in RP3. Ref.28 Ref.29 Ref.30
VAR_008510
Natural variant5261Missing. Ref.27
VAR_011562
Natural variant5331T → M. Ref.27
Corresponds to variant rs41312104 [ dbSNP | Ensembl ].
VAR_011563
Natural variant5661G → E. Ref.22 Ref.25 Ref.27 Ref.28
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
Isoform 6:
Sequence conflict11441V → I in DAA05713. Ref.17

Secondary structure

......................................................................... 1020
Helix Strand Turn

Details...

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
Isoform 6 (ORF15) [UniParc].

Checksum: 9A07A64016D8C01A
Show »

FASTA1,152127,042

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 6), SUBCELLULAR LOCATION, INTERACTION WITH NPM1.
[18]"RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins."
Khanna H., Hurd T.W., Lillo C., Shu X., Parapuram S.K., He S., Akimoto M., Wright A.F., Margolis B., Williams D.S., Swaroop A.
J. Biol. Chem. 280:33580-33587(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMCA1 AND SMC3.
[19]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPGRIP1L.
[21]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS RP3 VAL-60; VAL-75 AND GLY-262, VARIANTS LYS-425; VAL-431 AND GLU-566.
[23]"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] [Europe PMC] [Abstract]
Cited for: VARIANT RP3 VAL-60.
[24]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS RP3 ASN-99 AND VAL-289.
[25]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-76; LYS-425 AND GLU-566.
[26]"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] [Europe PMC] [Abstract]
Cited for: VARIANT RP3 ARG-302.
[27]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-425; GLN-526 DEL; MET-533 AND GLU-566.
[28]"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] [Europe PMC] [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.
[29]"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] [Europe PMC] [Abstract]
Cited for: VARIANT RP3 ASP-436.
[30]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS RP3 GLY-127; ARG-173; TYR-250; LEU-258 DEL; ARG-267; GLY-285 AND ASP-436.
[31]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS RP3 ASN-312; TYR-312 AND ARG-320.
[32]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS RP3 LEU-152 AND VAL-215.
[33]"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] [Europe PMC] [Abstract]
Cited for: VARIANT RPDSI ARG-173.
+Additional computationally mapped references.

Web resources

Mutations of the RPGR gene

Retina International's Scientific Newsletter

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.
BK005711 mRNA. Translation: DAA05713.1.
CCDSCCDS14246.1. [Q92834-2]
CCDS35229.1. [Q92834-6]
RefSeqNP_000319.1. NM_000328.2. [Q92834-2]
NP_001030025.1. NM_001034853.1. [Q92834-6]
XP_006724601.1. XM_006724538.1. [Q92834-1]
UniGeneHs.61438.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JHNX-ray1.70A/B/C/D1-392[»]
4JHPX-ray1.90C7-368[»]
ProteinModelPortalQ92834.
SMRQ92834. Positions 7-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112030. 6 interactions.
IntActQ92834. 4 interactions.
STRING9606.ENSP00000367766.

PTM databases

PhosphoSiteQ92834.

Polymorphism databases

DMDM23503098.

Proteomic databases

MaxQBQ92834.
PaxDbQ92834.
PRIDEQ92834.

Protocols and materials databases

DNASU6103.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309513; ENSP00000308783; ENSG00000156313. [Q92834-4]
ENST00000318842; ENSP00000322219; ENSG00000156313. [Q92834-2]
ENST00000338898; ENSP00000340208; ENSG00000156313. [Q92834-5]
ENST00000339363; ENSP00000343671; ENSG00000156313. [Q92834-1]
ENST00000342811; ENSP00000339531; ENSG00000156313. [Q92834-3]
ENST00000378505; ENSP00000367766; ENSG00000156313. [Q92834-6]
ENST00000474584; ENSP00000418926; ENSG00000156313. [Q92834-5]
ENST00000482855; ENSP00000419276; ENSG00000156313. [Q92834-3]
GeneID6103.
KEGGhsa:6103.
UCSCuc004deb.3. human. [Q92834-2]

Organism-specific databases

CTD6103.
GeneCardsGC0XM038128.
GeneReviewsRPGR.
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.
PharmGKBPA34656.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5184.
HOVERGENHBG026899.
OMAESENNYF.
OrthoDBEOG7N8ZVG.
PhylomeDBQ92834.
TreeFamTF331400.

Gene expression databases

BgeeQ92834.
CleanExHS_RPGR.
GenevestigatorQ92834.

Family and domain databases

Gene3D2.130.10.30. 1 hit.
InterProIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
PfamPF00415. RCC1. 6 hits.
[Graphical view]
PRINTSPR00633. RCCNDNSATION.
SUPFAMSSF50985. SSF50985. 1 hit.
PROSITEPS00626. RCC1_2. 4 hits.
PS50012. RCC1_3. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPGR. human.
GeneWikiRetinitis_pigmentosa_GTPase_regulator.
GenomeRNAi6103.
NextBio23741.
PROQ92834.
SOURCESearch...

Entry information

Entry nameRPGR_HUMAN
AccessionPrimary (citable) accession number: Q92834
Secondary accession number(s): B1ARN3 expand/collapse secondary AC list , E9PE28, O00702, O00737, Q3KN84, Q8N5T6, Q93039, Q9HD29, Q9UMR1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2002
Last modified: July 9, 2014
This is version 153 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM