Q92834 (RPGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
X-linked retinitis pigmentosa GTPase regulator

Gene names

Name:	RPGR
Synonyms:	RP3, XLRP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1020 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20
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.19
Subcellular location	Cytoplasm › cytoskeleton › flagellum axoneme By similarity. Golgi apparatus Ref.17. Isoform 6: Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › cilium basal body. Cytoplasm › cytoskeleton › cilium 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.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 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.32 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 process	Cilium biogenesis/degradation Sensory transduction Vision
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Golgi apparatus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ciliopathy Cone-rod dystrophy Deafness Disease mutation Retinitis pigmentosa
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cilium assembly Inferred from mutant phenotype Ref.20. Source: UniProtKB intracellular protein transport Traceable author statement Ref.10. Source: ProtInc intraflagellar 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.21. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB centrosome Inferred from direct assay Ref.17. Source: UniProtKB cilium axoneme Inferred from electronic annotation. Source: UniProtKB-SubCell cilium 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_function	guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1017	1017	X-linked retinitis pigmentosa GTPase regulator		PRO_0000206638
	Propeptide	1018 – 1020	3	Removed in mature form Potential		PRO_0000370844
Regions
	Repeat	54 – 105	52	RCC1 1
	Repeat	106 – 158	53	RCC1 2
	Repeat	159 – 208	50	RCC1 3
	Repeat	209 – 261	53	RCC1 4
	Repeat	262 – 313	52	RCC1 5
	Repeat	314 – 367	54	RCC1 6
	Compositional bias	530 – 903	374	Glu-rich
Amino acid modifications
	Modified residue	1017	1	Cysteine methyl ester Potential
	Lipidation	1017	1	S-geranylgeranyl cysteine Potential
Natural variations
	Alternative sequence	354 – 415	62	Missing in isoform 4.		VSP_005547
	Alternative sequence	473 – 480	8	YLLDEMTK → THHEPEFQ in isoform 5.		VSP_009183
	Alternative sequence	481 – 1020	540	Missing in isoform 5.		VSP_009184
	Alternative sequence	585 – 1020	436	GNDTG…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 sequence	585 – 789	205	Missing in isoform 2, isoform 3 and isoform 4.		VSP_005548
	Alternative sequence	841 – 851	11	DHEFSKTEELK → YSASHSQIVSV in isoform 3.		VSP_005549
	Alternative sequence	852 – 1020	169	Missing in isoform 3.		VSP_005550
	Natural variant	43	1	G → E in RP3. Ref.27		VAR_018057
	Natural variant	43	1	G → R in RP3. Ref.27		VAR_018058
	Natural variant	60	1	G → V in RP3. Ref.21 Ref.22 Ref.27		VAR_008501
	Natural variant	75	1	I → V in RP3; unknown pathological significance. Ref.21		VAR_008503
	Natural variant	76	1	S → I. Ref.24 Corresponds to variant rs1801685 [ dbSNP | Ensembl ].		VAR_013624
	Natural variant	98	1	H → Q in RP3; reduces interaction with PDE6D. Ref.1 Ref.9 Ref.10		VAR_008504
	Natural variant	99	1	T → N in RP3. Ref.23		VAR_013625
	Natural variant	127	1	R → G in RP3. Ref.27 Ref.29		VAR_018059
	Natural variant	130	1	F → C in RP3; reduces interaction with PDE6D. Ref.2 Ref.10		VAR_006850
	Natural variant	152	1	S → L in RP3. Ref.31		VAR_025949
	Natural variant	173	1	G → R in RP3 and RPDSI. Ref.29 Ref.32		VAR_018060
	Natural variant	184	1	Q → H. Corresponds to variant rs5963403 [ dbSNP | Ensembl ].		VAR_033259
	Natural variant	215	1	G → V in RP3; reduces interaction with PDE6D. Ref.1 Ref.10 Ref.31		VAR_008505
	Natural variant	235	1	P → S in RP3; reduces interaction with PDE6D. Ref.2 Ref.10		VAR_006851
	Natural variant	250	1	C → R in RP3; reduces interaction with PDE6D. Ref.1 Ref.9 Ref.10		VAR_008506
	Natural variant	250	1	C → Y in RP3. Ref.29		VAR_018061
	Natural variant	258	1	Missing in RP3. Ref.29		VAR_018062
	Natural variant	262	1	A → G in RP3; unknown pathological significance. Ref.21		VAR_008507
	Natural variant	267	1	G → E in RP3.		VAR_018063
	Natural variant	267	1	G → R in RP3. Ref.29		VAR_026127
	Natural variant	275	1	G → S in RP3; reduces interaction with PDE6D. Ref.2 Ref.10		VAR_006852
	Natural variant	285	1	E → G in RP3. Ref.29		VAR_026128
	Natural variant	289	1	I → V in RP3. Ref.23		VAR_013626
	Natural variant	296 – 300	5	Missing in RP3.		VAR_013627
	Natural variant	302	1	C → R in RP3. Ref.25		VAR_011561
	Natural variant	302	1	C → Y in RP3. Ref.27		VAR_018064
	Natural variant	312	1	D → N in RP3. Ref.30		VAR_018065
	Natural variant	312	1	D → Y in RP3. Ref.30		VAR_018066
	Natural variant	320	1	G → R in RP3. Ref.30		VAR_018067
	Natural variant	345	1	N → D Rare polymorphism. Ref.13 Ref.27 Corresponds to variant rs41305223 [ dbSNP | Ensembl ].		VAR_018068
	Natural variant	425	1	R → K. Ref.21 Ref.24 Ref.26 Ref.27 Corresponds to variant rs1801687 [ dbSNP | Ensembl ].		VAR_008508
	Natural variant	431	1	I → V. Ref.21 Ref.27		VAR_008509
	Natural variant	436	1	G → D in RP3. Ref.27 Ref.28 Ref.29		VAR_008510
	Natural variant	526	1	Missing. Ref.26		VAR_011562
	Natural variant	533	1	T → M. Ref.26 Corresponds to variant rs41312104 [ dbSNP | Ensembl ].		VAR_011563
	Natural variant	566	1	G → E. Ref.21 Ref.24 Ref.26 Ref.27 Corresponds to variant rs1801688 [ dbSNP | Ensembl ].		VAR_008511
Experimental info
	Mutagenesis	36	1	V → F: Does not reduce interaction with PDE6D. Ref.10
	Sequence conflict	1 – 3	3	MRE → MAKLRRSTTTAL in CAB54002. Ref.4
	Sequence conflict	190	1	K → N in CAC86116. Ref.4
Isoform 6:
	Sequence conflict	1144	1	V → I in DAA05713. Ref.17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: EAB16275A9A436C3	FASTA	1,020	113,387
	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
	Isoform 2 [UniParc]. Checksum: 70D84EAD988348D1	FASTA	815	90,245
	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 DEEVEIPEEK EGAEDSKGNG 610 620 630 640 650 660 IEEQEVEANE ENVKVHGGRK EKTEILSDDL TDKAEDHEFS KTEELKLEDV DEEINAENVE 670 680 690 700 710 720 SKKKTVGDDE SVPTGYHSKT EGAERTNDDS SAETIEKKEK ANLEERAICE YNENPKGYML 730 740 750 760 770 780 DDADSSSLEI LENSETTPSK DMKKTKKIFL FKRVPSINQK IVKNNNEPLP EIKSIGDQII 790 800 810 LKSDNKDADQ NHMSQNHQNI PPTNTERRSK SCTIL
	Isoform 3 [UniParc]. Checksum: BE8E98184F0404A6	FASTA	646	70,981
	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 DEEVEIPEEK EGAEDSKGNG 610 620 630 640 IEEQEVEANE ENVKVHGGRK EKTEILSDDL TDKAEYSASH SQIVSV
	Isoform 4 [UniParc]. Checksum: A84202BD00B84930	FASTA	753	83,394
	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 VKLERSPDSF 370 380 390 400 410 420 SMRRTLPPIE GTLGLSACFL PNSVFPRCSE RNLQESVLSE QDLMQPEEPD YLLDEMTKEA 430 440 450 460 470 480 EIDNSSTVES LGETTDILNM THIMSLNSNE KSLKLSPVQK QKKQQTIGEL TQDTALTEND 490 500 510 520 530 540 DSDEYEEMSE MKEGKACKQH VSQGIFMTQP ATTIEAFSDE EVEIPEEKEG AEDSKGNGIE 550 560 570 580 590 600 EQEVEANEEN VKVHGGRKEK TEILSDDLTD KAEDHEFSKT EELKLEDVDE EINAENVESK 610 620 630 640 650 660 KKTVGDDESV PTGYHSKTEG AERTNDDSSA ETIEKKEKAN LEERAICEYN ENPKGYMLDD 670 680 690 700 710 720 ADSSSLEILE NSETTPSKDM KKTKKIFLFK RVPSINQKIV KNNNEPLPEI KSIGDQIILK 730 740 750 SDNKDADQNH MSQNHQNIPP TNTERRSKSC TIL
	Isoform 5 [UniParc]. Checksum: 6766EA259A232631	FASTA	480	52,628
	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 PDTHHEPEFQ
	Isoform 6 (ORF15) [UniParc]. Checksum: 9A07A64016D8C01A	FASTA	1,152	127,042
	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 DEEVEIPEEK EGAEDSKGNG 610 620 630 640 650 660 IEEQEVEANE ENVKVHGGRK EKTEILSDDL TDKAEVSEGK AKSVGEAEDG PEGRGDGTCE 670 680 690 700 710 720 EGSSGAEHWQ DEEREKGEKD KGRGEMERPG EGEKELAEKE EWKKRDGEEQ EQKEREQGHQ 730 740 750 760 770 780 KERNQEMEEG GEEEHGEGEE EEGDREEEEE KEGEGKEEGE GEEVEGEREK EEGERKKEER 790 800 810 820 830 840 AGKEEKGEEE GDQGEGEEEE TEGRGEEKEE GGEVEGGEVE EGKGEREEEE EEGEGEEEEG 850 860 870 880 890 900 EGEEEEGEGE EEEGEGKGEE EGEEGEGEEE GEEGEGEGEE EEGEGEGEEE GEGEGEEEEG 910 920 930 940 950 960 EGEGEEEGEG EGEEEEGEGK GEEEGEEGEG EGEEEEGEGE GEDGEGEGEE EEGEWEGEEE 970 980 990 1000 1010 1020 EGEGEGEEEG EGEGEEGEGE GEEEEGEGEG EEEEGEEEGE EEGEGEEEGE GEGEEEEEGE 1030 1040 1050 1060 1070 1080 VEGEVEGEEG EGEGEEEEGE EEGEEREKEG EGEENRRNRE EEEEEEGKYQ ETGEEENERQ 1090 1100 1110 1120 1130 1140 DGEEYKKVSK IKGSVKYGKH KTYQKKSVTN TQGNGKEQRS KMPVQSKRLL KNGPSGSKKF 1150 WNNVLPHYLE LK

References

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[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]	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. , 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]	"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. , 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.
[20]	"The role of RPGR in cilia formation and actin stability." Gakovic M., Shu X., Kasioulis I., Carpanini S., Moraga I., Wright A.F. Hum. Mol. Genet. 20:4840-4850(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"Spectrum of mutations in the RPGR gene that are identified in 20% of families with X-linked retinitis pigmentosa." Buraczynska M., Wu W., Fujita R., Buraczynska K., Phelps E., Andreasson S., Bennett J., Birch D.G., Fishman G.A., Hoffman D.R., Inana G., Jacobson S.G., Musarella M.A., Sieving P.A., Swaroop A. Am. J. Hum. Genet. 61:1287-1292(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP3 VAL-60; VAL-75 AND GLY-262, VARIANTS LYS-425; VAL-431 AND GLU-566.
[22]	"X-linked retinitis pigmentosa in two families with a missense mutation in the RPGR gene and putative change of glycine to valine at codon 60." Fishman G.A., Grover S., Jacobson S.G., Alexander K.R., Derlacki D.J., Wu W., Buraczynska M., Swaroop A. Ophthalmology 105:2286-2296(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP3 VAL-60.
[23]	"Mutation analysis of the RPGR gene reveals novel mutations in south European patients with X-linked retinitis pigmentosa." Miano M.G., Testa F., Strazzullo M., Trujillo M., De Bernardo C., Grammatico B., Simonelli F., Mangino M., Torrente I., Ruberto G., Beneyto M., Antinolo G., Rinaldi E., Danesino C., Ventruto V., D'Urso M., Ayuso C., Baiget M., Ciccodicola A. Eur. J. Hum. Genet. 7:687-694(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP3 ASN-99 AND VAL-289.
[24]	"Identification of novel RPGR (retinitis pigmentosa GTPase regulator) mutations in a subset of X-linked retinitis pigmentosa families segregating with the RP3 locus." Zito I., Thiselton D.L., Gorin M.B., Stout J.T., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J. Hum. Genet. 105:57-62(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ILE-76; LYS-425 AND GLU-566.
[25]	"Novel mutations of the RPGR gene in RP3 families." Zito I., Gorin M.B., Plant C., Bird A.C., Bhattacharya S.S., Hardcastle A.J. Hum. Mutat. 15:386-386(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP3 ARG-302.
[26]	"Sequence variation within the RPGR gene: evidence for a founder complex allele." Zito I., Morris A., Tyson P., Winship I., Sharp D., Gilbert D., Thiselton D.L., Bhattacharya S.S., Hardcastle A.J. Hum. Mutat. 16:273-274(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LYS-425; GLN-526 DEL; MET-533 AND GLU-566.
[27]	"X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function." Sharon D., Bruns G.A.P., McGee T.L., Sandberg M.A., Berson E.L., Dryja T.P. Invest. Ophthalmol. Vis. Sci. 41:2712-2721(2000) [PubMed] [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.
[28]	"Five novel RPGR mutations in families with X-linked retinitis pigmentosa." Guevara-Fujita M., Fahrner S., Buraczynska K., Cook J., Wheaton D., Cortes F., Vicencio C., Pena M., Fishman G.A., Mintz-Hittner H., Birch D.G., Hoffman D.R., Mears A.J., Fujita R., Swaroop A. Hum. Mutat. 17:151-151(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP3 ASP-436.
[29]	"A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa." Breuer D.K., Yashar B.M., Filippova E., Hiriyanna S., Lyons R.H., Mears A.J., Asaye B., Acar C., Vervoort R., Wright A.F., Musarella M.A., Wheeler P., MacDonald I., Iannaccone A., Birch D., Hoffman D.R., Fishman G.A., Heckenlively J.R. , 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.
[30]	"RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa." Sharon D., Sandberg M.A., Rabe V.W., Stillberger M., Dryja T.P., Berson E.L. Am. J. Hum. Genet. 73:1131-1146(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP3 ASN-312; TYR-312 AND ARG-320.
[31]	"X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15." Bader I., Brandau O., Achatz H., Apfelstedt-Sylla E., Hergersberg M., Lorenz B., Wissinger B., Wittwer B., Rudolph G., Meindl A., Meitinger T. Invest. Ophthalmol. Vis. Sci. 44:1458-1463(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP3 LEU-152 AND VAL-215.
[32]	"Clinical and immunohistochemical evidence for an X linked retinitis pigmentosa syndrome with recurrent infections and hearing loss in association with an RPGR mutation." Iannaccone A., Breuer D.K., Wang X.F., Kuo S.F., Normando E.M., Filippova E., Baldi A., Hiriyanna S., MacDonald C.B., Baldi F., Cosgrove D., Morton C.C., Swaroop A., Jablonski M.M. J. Med. Genet. 40:E118-E118(2003) [PubMed] [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

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U57629 mRNA. Translation: AAC50481.1. X97668 mRNA. Translation: CAA66258.1. AJ238395 mRNA. Translation: CAB54002.1. AJ318463 Genomic DNA. Translation: CAC86116.1. AL606748 Genomic DNA. Translation: CAI95407.1. CH471141 Genomic DNA. Translation: EAW59441.1. BC031624 mRNA. Translation: AAH31624.1. AF286471 Genomic DNA. Translation: AAG00550.1. BK005711 mRNA. Translation: DAA05713.1.
IPI	IPI00023757. IPI00215806. IPI00215807. IPI00215808. IPI00382445. IPI00397031.
RefSeq	NP_000319.1. NM_000328.2. NP_001030025.1. NM_001034853.1.
UniGene	Hs.61438.
3D structure databases
ProteinModelPortal	Q92834.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000367766.
PTM databases
PhosphoSite	Q92834.
Polymorphism databases
DMDM	23503098.
Proteomic databases
PaxDb	Q92834.
PRIDE	Q92834.
Protocols and materials databases
DNASU	6103.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309513; ENSP00000308783; ENSG00000156313. ENST00000318842; ENSP00000322219; ENSG00000156313. ENST00000338898; ENSP00000340208; ENSG00000156313. ENST00000339363; ENSP00000343671; ENSG00000156313. ENST00000342811; ENSP00000339531; ENSG00000156313. ENST00000378505; ENSP00000367766; ENSG00000156313. ENST00000474584; ENSP00000418926; ENSG00000156313. ENST00000482855; ENSP00000419276; ENSG00000156313.
GeneID	6103.
KEGG	hsa:6103.
UCSC	uc004deb.3. human.
Organism-specific databases
CTD	6103.
GeneCards	GC0XM038128.
HGNC	HGNC:10295. RPGR.
HPA	HPA001593.
MIM	300029. phenotype. 300455. phenotype. 300834. phenotype. 304020. phenotype. 312610. gene.
neXtProt	NX_Q92834.
Orphanet	49382. Achromatopsia. 1872. Cone rod dystrophy. 244. Primary ciliary dyskinesia. 247522. Primary ciliary dyskinesia - retinitis pigmentosa. 791. Retinitis pigmentosa.
PharmGKB	PA34656.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5184.
HOVERGEN	HBG026899.
OMA	NNVLPHY.
PhylomeDB	Q92834.
Gene expression databases
ArrayExpress	Q92834.
Bgee	Q92834.
CleanEx	HS_RPGR.
Genevestigator	Q92834.
GermOnline	ENSG00000156313. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.30. 1 hit.
InterPro	IPR009091. RCC1/BLIP-II. IPR000408. Reg_chr_condens. [Graphical view]
Pfam	PF00415. RCC1. 6 hits. [Graphical view]
PRINTS	PR00633. RCCNDNSATION.
SUPFAM	SSF50985. RCC1/BLIP-II. 1 hit.
PROSITE	PS00625. RCC1_1. False negative. PS00626. RCC1_2. 4 hits. PS50012. RCC1_3. 6 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPGR. human.
GenomeRNAi	6103.
NextBio	23741.
SOURCE	Search...

Entry information

Entry name

RPGR_HUMAN

Accession

Primary (citable) accession number: Q92834
Secondary accession number(s): B1ARN3 , 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:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.