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Q92834

- RPGR_HUMAN

UniProt

Q92834 - RPGR_HUMAN

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Protein

X-linked retinitis pigmentosa GTPase regulator

Gene
RPGR, RP3, XLRP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 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
Complete GO annotation...

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
Isoform 6 : Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletoncilium basal body. Cytoplasmcytoskeletoncilium axoneme 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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.14 Publications
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. 3 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. 2 Publications
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. 3 Publications
VAR_008505
Natural varianti235 – 2351P → S in RP3; reduces interaction with PDE6D. 2 Publications
VAR_006851
Natural varianti250 – 2501C → R in RP3; reduces interaction with PDE6D. 3 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. 2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.1 Publication

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 form Reviewed predictionPRO_0000370844

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1017 – 10171Cysteine methyl ester Reviewed prediction
Lipidationi1017 – 10171S-geranylgeranyl cysteine Reviewed prediction

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.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112030. 6 interactions.
IntActiQ92834. 4 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.

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.

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

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. 3 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. 2 Publications
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. 3 Publications
VAR_008505
Natural varianti235 – 2351P → S in RP3; reduces interaction with PDE6D. 2 Publications
VAR_006851
Natural varianti250 – 2501C → R in RP3; reduces interaction with PDE6D. 3 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. 2 Publications
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. VSP_005547Add
BLAST
Alternative sequencei473 – 4808YLLDEMTK → THHEPEFQ in isoform 5. VSP_009183
Alternative sequencei481 – 1020540Missing in isoform 5. VSP_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. VSP_044559Add
BLAST
Alternative sequencei585 – 789205Missing in isoform 2, isoform 3 and isoform 4. VSP_005548Add
BLAST
Alternative sequencei841 – 85111DHEFSKTEELK → YSASHSQIVSV in isoform 3. VSP_005549Add
BLAST
Alternative sequencei852 – 1020169Missing in isoform 3. VSP_005550Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 33MRE → MAKLRRSTTTAL in CAB54002. 1 Publication
Sequence conflicti190 – 1901K → N in CAC86116. 1 Publication
Isoform 6 (identifier: Q92834-6)
Sequence conflicti1144 – 11441V → I in DAA05713. 1 Publication

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

EnsembliENST00000309513; 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]
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. 6 interactions.
IntActi Q92834. 4 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 ENST00000309513 ; 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 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 153 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

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