Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q92834

- RPGR_HUMAN

UniProt

Q92834 - RPGR_HUMAN

Protein

X-linked retinitis pigmentosa GTPase regulator

Gene

RPGR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity1 Publication

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cilium assembly Source: UniProtKB
    2. eye photoreceptor cell development Source: Ensembl
    3. intracellular protein transport Source: ProtInc
    4. intraciliary transport Source: UniProtKB
    5. response to stimulus Source: UniProtKB-KW
    6. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Cilium biogenesis/degradation, Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    X-linked retinitis pigmentosa GTPase regulator
    Gene namesi
    Name:RPGR
    Synonyms:RP3, XLRP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10295. RPGR.

    Subcellular locationi

    Cytoplasmcytoskeletonflagellum axoneme By similarity. Golgi apparatus 1 Publication

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. ciliary basal body Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB
    4. photoreceptor outer segment Source: UniProtKB
    5. sperm flagellum Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton, Golgi apparatus

    Pathology & Biotechi

    Involvement in diseasei

    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.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431G → E in RP3. 1 Publication
    VAR_018057
    Natural varianti43 – 431G → R in RP3. 1 Publication
    VAR_018058
    Natural varianti60 – 601G → V in RP3. 3 Publications
    VAR_008501
    Natural varianti75 – 751I → V in RP3; unknown pathological significance. 1 Publication
    Corresponds to variant rs111631988 [ dbSNP | Ensembl ].
    VAR_008503
    Natural varianti98 – 981H → Q in RP3; reduces interaction with PDE6D. 2 Publications
    VAR_008504
    Natural varianti99 – 991T → N in RP3. 1 Publication
    VAR_013625
    Natural varianti127 – 1271R → G in RP3. 2 Publications
    VAR_018059
    Natural varianti130 – 1301F → C in RP3; reduces interaction with PDE6D. 1 Publication
    VAR_006850
    Natural varianti152 – 1521S → L in RP3. 1 Publication
    VAR_025949
    Natural varianti173 – 1731G → R in RP3 and RPDSI. 2 Publications
    VAR_018060
    Natural varianti215 – 2151G → V in RP3; reduces interaction with PDE6D. 2 Publications
    VAR_008505
    Natural varianti235 – 2351P → S in RP3; reduces interaction with PDE6D. 1 Publication
    VAR_006851
    Natural varianti250 – 2501C → R in RP3; reduces interaction with PDE6D. 2 Publications
    VAR_008506
    Natural varianti250 – 2501C → Y in RP3. 1 Publication
    VAR_018061
    Natural varianti258 – 2581Missing in RP3. 1 Publication
    VAR_018062
    Natural varianti262 – 2621A → G in RP3; unknown pathological significance. 1 Publication
    Corresponds to variant rs138018739 [ dbSNP | Ensembl ].
    VAR_008507
    Natural varianti267 – 2671G → E in RP3.
    VAR_018063
    Natural varianti267 – 2671G → R in RP3. 1 Publication
    VAR_026127
    Natural varianti275 – 2751G → S in RP3; reduces interaction with PDE6D. 1 Publication
    VAR_006852
    Natural varianti285 – 2851E → G in RP3. 1 Publication
    VAR_026128
    Natural varianti289 – 2891I → V in RP3. 1 Publication
    VAR_013626
    Natural varianti296 – 3005Missing in RP3.
    VAR_013627
    Natural varianti302 – 3021C → R in RP3. 1 Publication
    VAR_011561
    Natural varianti302 – 3021C → Y in RP3. 1 Publication
    Corresponds to variant rs62640590 [ dbSNP | Ensembl ].
    VAR_018064
    Natural varianti312 – 3121D → N in RP3. 1 Publication
    VAR_018065
    Natural varianti312 – 3121D → Y in RP3. 1 Publication
    VAR_018066
    Natural varianti320 – 3201G → R in RP3. 1 Publication
    VAR_018067
    Natural varianti436 – 4361G → D in RP3. 3 Publications
    VAR_008510
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731G → R in RP3 and RPDSI. 2 Publications
    VAR_018060
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361V → F: Does not reduce interaction with PDE6D. 1 Publication

    Keywords - Diseasei

    Ciliopathy, Cone-rod dystrophy, Deafness, Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi300029. phenotype.
    300455. phenotype.
    300834. phenotype.
    304020. phenotype.
    Orphaneti49382. Achromatopsia.
    1872. Cone rod dystrophy.
    244. Primary ciliary dyskinesia.
    247522. Primary ciliary dyskinesia - retinitis pigmentosa.
    791. Retinitis pigmentosa.
    PharmGKBiPA34656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10171017X-linked retinitis pigmentosa GTPase regulatorPRO_0000206638Add
    BLAST
    Propeptidei1018 – 10203Removed in mature formSequence AnalysisPRO_0000370844

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1017 – 10171Cysteine methyl esterSequence Analysis
    Lipidationi1017 – 10171S-geranylgeranyl cysteineSequence Analysis

    Post-translational modificationi

    Prenylated.By similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ92834.
    PaxDbiQ92834.
    PRIDEiQ92834.

    PTM databases

    PhosphoSiteiQ92834.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    BgeeiQ92834.
    CleanExiHS_RPGR.
    GenevestigatoriQ92834.

    Organism-specific databases

    HPAiHPA001593.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDE6DO439249EBI-6558417,EBI-712685
    Pde6dO550573EBI-6558417,EBI-6558402From a different organism.

    Protein-protein interaction databases

    BioGridi112030. 7 interactions.
    IntActiQ92834. 5 interactions.
    STRINGi9606.ENSP00000367766.

    Structurei

    Secondary structure

    1
    1020
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 208
    Beta strandi26 – 305
    Beta strandi37 – 426
    Beta strandi44 – 518
    Beta strandi56 – 616
    Beta strandi69 – 713
    Beta strandi73 – 808
    Helixi82 – 843
    Beta strandi89 – 946
    Beta strandi96 – 1038
    Beta strandi108 – 1125
    Beta strandi121 – 1233
    Beta strandi127 – 1326
    Beta strandi142 – 1476
    Beta strandi149 – 1568
    Beta strandi161 – 1666
    Beta strandi179 – 1857
    Beta strandi188 – 1903
    Beta strandi192 – 1976
    Beta strandi199 – 2068
    Beta strandi211 – 2155
    Turni219 – 2224
    Helixi226 – 2316
    Beta strandi245 – 2506
    Beta strandi252 – 26110
    Beta strandi263 – 2686
    Beta strandi282 – 2887
    Turni291 – 2944
    Beta strandi297 – 3026
    Beta strandi304 – 3118
    Beta strandi316 – 3205
    Helixi323 – 3253
    Beta strandi337 – 3426
    Helixi344 – 3463
    Beta strandi349 – 3568
    Beta strandi358 – 36710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JHNX-ray1.70A/B/C/D1-392[»]
    4JHPX-ray1.90C7-368[»]
    ProteinModelPortaliQ92834.
    SMRiQ92834. Positions 7-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati54 – 10552RCC1 1Add
    BLAST
    Repeati106 – 15853RCC1 2Add
    BLAST
    Repeati159 – 20850RCC1 3Add
    BLAST
    Repeati209 – 26153RCC1 4Add
    BLAST
    Repeati262 – 31352RCC1 5Add
    BLAST
    Repeati314 – 36754RCC1 6Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi530 – 903374Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 6 RCC1 repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5184.
    HOVERGENiHBG026899.
    OMAiESENNYF.
    OrthoDBiEOG7N8ZVG.
    PhylomeDBiQ92834.
    TreeFamiTF331400.

    Family and domain databases

    Gene3Di2.130.10.30. 1 hit.
    InterProiIPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    [Graphical view]
    PfamiPF00415. RCC1. 6 hits.
    [Graphical view]
    PRINTSiPR00633. RCCNDNSATION.
    SUPFAMiSSF50985. SSF50985. 1 hit.
    PROSITEiPS00626. RCC1_2. 4 hits.
    PS50012. RCC1_3. 6 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q92834-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MREPEELMPD SGAVFTFGKS KFAENNPGKF WFKNDVPVHL SCGDEHSAVV     50
    TGNNKLYMFG SNNWGQLGLG SKSAISKPTC VKALKPEKVK LAACGRNHTL 100
    VSTEGGNVYA TGGNNEGQLG LGDTEERNTF HVISFFTSEH KIKQLSAGSN 150
    TSAALTEDGR LFMWGDNSEG QIGLKNVSNV CVPQQVTIGK PVSWISCGYY 200
    HSAFVTTDGE LYVFGEPENG KLGLPNQLLG NHRTPQLVSE IPEKVIQVAC 250
    GGEHTVVLTE NAVYTFGLGQ FGQLGLGTFL FETSEPKVIE NIRDQTISYI 300
    SCGENHTALI TDIGLMYTFG DGRHGKLGLG LENFTNHFIP TLCSNFLRFI 350
    VKLVACGGCH MVVFAAPHRG VAKEIEFDEI NDTCLSVATF LPYSSLTSGN 400
    VLQRTLSARM RRRERERSPD SFSMRRTLPP IEGTLGLSAC FLPNSVFPRC 450
    SERNLQESVL SEQDLMQPEE PDYLLDEMTK EAEIDNSSTV ESLGETTDIL 500
    NMTHIMSLNS NEKSLKLSPV QKQKKQQTIG ELTQDTALTE NDDSDEYEEM 550
    SEMKEGKACK QHVSQGIFMT QPATTIEAFS DEEVGNDTGQ VGPQADTDGE 600
    GLQKEVYRHE NNNGVDQLDA KEIEKESDGG HSQKESEAEE IDSEKETKLA 650
    EIAGMKDLRE REKSTKKMSP FFGNLPDRGM NTESEENKDF VKKRESCKQD 700
    VIFDSERESV EKPDSYMEGA SESQQGIADG FQQPEAIEFS SGEKEDDEVE 750
    TDQNIRYGRK LIEQGNEKET KPIISKSMAK YDFKCDRLSE IPEEKEGAED 800
    SKGNGIEEQE VEANEENVKV HGGRKEKTEI LSDDLTDKAE DHEFSKTEEL 850
    KLEDVDEEIN AENVESKKKT VGDDESVPTG YHSKTEGAER TNDDSSAETI 900
    EKKEKANLEE RAICEYNENP KGYMLDDADS SSLEILENSE TTPSKDMKKT 950
    KKIFLFKRVP SINQKIVKNN NEPLPEIKSI GDQIILKSDN KDADQNHMSQ 1000
    NHQNIPPTNT ERRSKSCTIL 1020
    Length:1,020
    Mass (Da):113,387
    Last modified:September 19, 2002 - v2
    Checksum:iEAB16275A9A436C3
    GO
    Isoform 2 (identifier: Q92834-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         585-789: Missing.

    Show »
    Length:815
    Mass (Da):90,245
    Checksum:i70D84EAD988348D1
    GO
    Isoform 3 (identifier: Q92834-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         585-789: Missing.
         841-851: DHEFSKTEELK → YSASHSQIVSV
         852-1020: Missing.

    Show »
    Length:646
    Mass (Da):70,981
    Checksum:iBE8E98184F0404A6
    GO
    Isoform 4 (identifier: Q92834-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         354-415: Missing.
         585-789: Missing.

    Show »
    Length:753
    Mass (Da):83,394
    Checksum:iA84202BD00B84930
    GO
    Isoform 5 (identifier: Q92834-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         473-480: YLLDEMTK → THHEPEFQ
         481-1020: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:480
    Mass (Da):52,628
    Checksum:i6766EA259A232631
    GO
    Isoform 6 (identifier: Q92834-6) [UniParc]FASTAAdd to Basket

    Also known as: ORF15

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

    Show »
    Length:1,152
    Mass (Da):127,042
    Checksum:i9A07A64016D8C01A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 33MRE → MAKLRRSTTTAL in CAB54002. (PubMed:10401007)Curated
    Sequence conflicti190 – 1901K → N in CAC86116. (PubMed:10401007)Curated
    Isoform 6 (identifier: Q92834-6)
    Sequence conflicti1144 – 11441V → I in DAA05713. (PubMed:15772089)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431G → E in RP3. 1 Publication
    VAR_018057
    Natural varianti43 – 431G → R in RP3. 1 Publication
    VAR_018058
    Natural varianti60 – 601G → V in RP3. 3 Publications
    VAR_008501
    Natural varianti75 – 751I → V in RP3; unknown pathological significance. 1 Publication
    Corresponds to variant rs111631988 [ dbSNP | Ensembl ].
    VAR_008503
    Natural varianti76 – 761S → I.1 Publication
    Corresponds to variant rs1801685 [ dbSNP | Ensembl ].
    VAR_013624
    Natural varianti98 – 981H → Q in RP3; reduces interaction with PDE6D. 2 Publications
    VAR_008504
    Natural varianti99 – 991T → N in RP3. 1 Publication
    VAR_013625
    Natural varianti127 – 1271R → G in RP3. 2 Publications
    VAR_018059
    Natural varianti130 – 1301F → C in RP3; reduces interaction with PDE6D. 1 Publication
    VAR_006850
    Natural varianti152 – 1521S → L in RP3. 1 Publication
    VAR_025949
    Natural varianti173 – 1731G → R in RP3 and RPDSI. 2 Publications
    VAR_018060
    Natural varianti184 – 1841Q → H.
    Corresponds to variant rs5963403 [ dbSNP | Ensembl ].
    VAR_033259
    Natural varianti215 – 2151G → V in RP3; reduces interaction with PDE6D. 2 Publications
    VAR_008505
    Natural varianti235 – 2351P → S in RP3; reduces interaction with PDE6D. 1 Publication
    VAR_006851
    Natural varianti250 – 2501C → R in RP3; reduces interaction with PDE6D. 2 Publications
    VAR_008506
    Natural varianti250 – 2501C → Y in RP3. 1 Publication
    VAR_018061
    Natural varianti258 – 2581Missing in RP3. 1 Publication
    VAR_018062
    Natural varianti262 – 2621A → G in RP3; unknown pathological significance. 1 Publication
    Corresponds to variant rs138018739 [ dbSNP | Ensembl ].
    VAR_008507
    Natural varianti267 – 2671G → E in RP3.
    VAR_018063
    Natural varianti267 – 2671G → R in RP3. 1 Publication
    VAR_026127
    Natural varianti275 – 2751G → S in RP3; reduces interaction with PDE6D. 1 Publication
    VAR_006852
    Natural varianti285 – 2851E → G in RP3. 1 Publication
    VAR_026128
    Natural varianti289 – 2891I → V in RP3. 1 Publication
    VAR_013626
    Natural varianti296 – 3005Missing in RP3.
    VAR_013627
    Natural varianti302 – 3021C → R in RP3. 1 Publication
    VAR_011561
    Natural varianti302 – 3021C → Y in RP3. 1 Publication
    Corresponds to variant rs62640590 [ dbSNP | Ensembl ].
    VAR_018064
    Natural varianti312 – 3121D → N in RP3. 1 Publication
    VAR_018065
    Natural varianti312 – 3121D → Y in RP3. 1 Publication
    VAR_018066
    Natural varianti320 – 3201G → R in RP3. 1 Publication
    VAR_018067
    Natural varianti345 – 3451N → D Rare polymorphism. 2 Publications
    Corresponds to variant rs41305223 [ dbSNP | Ensembl ].
    VAR_018068
    Natural varianti425 – 4251R → K.4 Publications
    Corresponds to variant rs1801687 [ dbSNP | Ensembl ].
    VAR_008508
    Natural varianti431 – 4311I → V.2 Publications
    Corresponds to variant rs62635003 [ dbSNP | Ensembl ].
    VAR_008509
    Natural varianti436 – 4361G → D in RP3. 3 Publications
    VAR_008510
    Natural varianti526 – 5261Missing.1 Publication
    VAR_011562
    Natural varianti533 – 5331T → M.1 Publication
    Corresponds to variant rs41312104 [ dbSNP | Ensembl ].
    VAR_011563
    Natural varianti566 – 5661G → E.4 Publications
    Corresponds to variant rs1801688 [ dbSNP | Ensembl ].
    VAR_008511

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei354 – 41562Missing in isoform 4. 1 PublicationVSP_005547Add
    BLAST
    Alternative sequencei473 – 4808YLLDEMTK → THHEPEFQ in isoform 5. 1 PublicationVSP_009183
    Alternative sequencei481 – 1020540Missing in isoform 5. 1 PublicationVSP_009184Add
    BLAST
    Alternative sequencei585 – 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. CuratedVSP_044559Add
    BLAST
    Alternative sequencei585 – 789205Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_005548Add
    BLAST
    Alternative sequencei841 – 85111DHEFSKTEELK → YSASHSQIVSV in isoform 3. 1 PublicationVSP_005549Add
    BLAST
    Alternative sequencei852 – 1020169Missing in isoform 3. 1 PublicationVSP_005550Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14246.1. [Q92834-2]
    CCDS35229.1. [Q92834-6]
    RefSeqiNP_000319.1. NM_000328.2. [Q92834-2]
    NP_001030025.1. NM_001034853.1. [Q92834-6]
    XP_006724601.1. XM_006724538.1. [Q92834-1]
    UniGeneiHs.61438.

    Genome annotation databases

    EnsembliENST00000318842; ENSP00000322219; ENSG00000156313. [Q92834-2]
    ENST00000339363; ENSP00000343671; ENSG00000156313. [Q92834-1]
    ENST00000378505; ENSP00000367766; ENSG00000156313. [Q92834-6]
    ENST00000474584; ENSP00000418926; ENSG00000156313. [Q92834-5]
    ENST00000482855; ENSP00000419276; ENSG00000156313. [Q92834-3]
    GeneIDi6103.
    KEGGihsa:6103.
    UCSCiuc004deb.3. human. [Q92834-2]

    Polymorphism databases

    DMDMi23503098.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Mutations of the RPGR gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14246.1. [Q92834-2 ]
    CCDS35229.1. [Q92834-6 ]
    RefSeqi NP_000319.1. NM_000328.2. [Q92834-2 ]
    NP_001030025.1. NM_001034853.1. [Q92834-6 ]
    XP_006724601.1. XM_006724538.1. [Q92834-1 ]
    UniGenei Hs.61438.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JHN X-ray 1.70 A/B/C/D 1-392 [» ]
    4JHP X-ray 1.90 C 7-368 [» ]
    ProteinModelPortali Q92834.
    SMRi Q92834. Positions 7-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112030. 7 interactions.
    IntActi Q92834. 5 interactions.
    STRINGi 9606.ENSP00000367766.

    PTM databases

    PhosphoSitei Q92834.

    Polymorphism databases

    DMDMi 23503098.

    Proteomic databases

    MaxQBi Q92834.
    PaxDbi Q92834.
    PRIDEi Q92834.

    Protocols and materials databases

    DNASUi 6103.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318842 ; ENSP00000322219 ; ENSG00000156313 . [Q92834-2 ]
    ENST00000339363 ; ENSP00000343671 ; ENSG00000156313 . [Q92834-1 ]
    ENST00000378505 ; ENSP00000367766 ; ENSG00000156313 . [Q92834-6 ]
    ENST00000474584 ; ENSP00000418926 ; ENSG00000156313 . [Q92834-5 ]
    ENST00000482855 ; ENSP00000419276 ; ENSG00000156313 . [Q92834-3 ]
    GeneIDi 6103.
    KEGGi hsa:6103.
    UCSCi uc004deb.3. human. [Q92834-2 ]

    Organism-specific databases

    CTDi 6103.
    GeneCardsi GC0XM038128.
    GeneReviewsi RPGR.
    HGNCi HGNC:10295. RPGR.
    HPAi HPA001593.
    MIMi 300029. phenotype.
    300455. phenotype.
    300834. phenotype.
    304020. phenotype.
    312610. gene.
    neXtProti NX_Q92834.
    Orphaneti 49382. Achromatopsia.
    1872. Cone rod dystrophy.
    244. Primary ciliary dyskinesia.
    247522. Primary ciliary dyskinesia - retinitis pigmentosa.
    791. Retinitis pigmentosa.
    PharmGKBi PA34656.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5184.
    HOVERGENi HBG026899.
    OMAi ESENNYF.
    OrthoDBi EOG7N8ZVG.
    PhylomeDBi Q92834.
    TreeFami TF331400.

    Miscellaneous databases

    ChiTaRSi RPGR. human.
    GeneWikii Retinitis_pigmentosa_GTPase_regulator.
    GenomeRNAii 6103.
    NextBioi 23741.
    PROi Q92834.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q92834.
    CleanExi HS_RPGR.
    Genevestigatori Q92834.

    Family and domain databases

    Gene3Di 2.130.10.30. 1 hit.
    InterProi IPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    [Graphical view ]
    Pfami PF00415. RCC1. 6 hits.
    [Graphical view ]
    PRINTSi PR00633. RCCNDNSATION.
    SUPFAMi SSF50985. SSF50985. 1 hit.
    PROSITEi PS00626. RCC1_2. 4 hits.
    PS50012. RCC1_3. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: INTERACTION WITH RPGRIP1L.
    21. 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. 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. 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. Cited for: VARIANT RP3 ASP-436.
    30. 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.

    Entry informationi

    Entry nameiRPGR_HUMAN
    AccessioniPrimary (citable) accession number: Q92834
    Secondary accession number(s): B1ARN3
    , E9PE28, O00702, O00737, Q3KN84, Q8N5T6, Q93039, Q9HD29, Q9UMR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3