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O75695 (XRP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein XRP2
Gene names
Name:RP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. Ref.6 Ref.9 Ref.10 Ref.12

Subunit structure

Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119 (or UNC119B). Interacts with ARL3; interaction is direct and stimulated with the activated GTP-bound form of ARL3. Ref.6 Ref.8 Ref.11 Ref.12

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projectioncilium. Note: Detected predominantly to the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. Ref.5 Ref.7 Ref.9

Tissue specificity

Ubiquitous. Expressed in the rod and cone photoreceptors, extending from the tips of the outer segment (OS) through the inner segment (IS) and outer nuclear layer (ONL) and into the synaptic terminals of the outer plexiform layer (ONL). Also detected in the bipolar, horizontal and amacrine cells in the inner nuclear layer (INL), extending to the inner plexiform layer (IPL) and though the ganglion cell layer (GCL) and into the nerve fiber layer (NFL) (at protein level). Ref.5 Ref.7 Ref.12

Post-translational modification

Myristoylated on Gly-2; which may be required for membrane targeting Probable.

Palmitoylated on Cys-3; which may be required for plasma membrane targeting Probable. Mutation of Cys-3 targets the protein to internal membranes. Ref.5

Involvement in disease

Retinitis pigmentosa 2 (RP2) [MIM:312600]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Sequence similarities

Belongs to the TBCC family.

Contains 1 C-CAP/cofactor C-like domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cell projection
Cilium
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   LigandGTP-binding
Nucleotide-binding
   Molecular functionGTPase activation
   PTMLipoprotein
Myristate
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCTP biosynthetic process

Inferred from electronic annotation. Source: InterPro

GTP biosynthetic process

Inferred from electronic annotation. Source: InterPro

UTP biosynthetic process

Inferred from electronic annotation. Source: InterPro

cell morphogenesis

Inferred from electronic annotation. Source: InterPro

cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

positive regulation of GTPase activity

Inferred from direct assay Ref.6Ref.12. Source: GOC

post-Golgi vesicle-mediated transport

Inferred from mutant phenotype Ref.9. Source: MGI

protein folding

Traceable author statement Ref.1. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentciliary basal body

Inferred from direct assay Ref.9. Source: MGI

cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasmic vesicle

Inferred from genetic interaction Ref.9. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activator activity

Inferred from direct assay Ref.6Ref.12. Source: UniProtKB

nucleoside diphosphate kinase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.6Ref.12. Source: UniProtKB

unfolded protein binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 350349Protein XRP2
PRO_0000080047

Regions

Domain24 – 179156C-CAP/cofactor C-like
Nucleotide binding98 – 992GTP
Nucleotide binding115 – 1184GTP

Amino acid modifications

Lipidation21N-myristoyl glycine Probable
Lipidation31S-palmitoyl cysteine Probable

Natural variations

Natural variant61Missing in RP2; loss of membrane association; enhances interaction with ARL3. Ref.1 Ref.5 Ref.6 Ref.14
VAR_008497
Natural variant671C → Y in RP2. Ref.19
VAR_018069
Natural variant861C → Y in RP2. Ref.17 Ref.20
VAR_018070
Natural variant951P → L in RP2; uncertain pathological significance. Ref.17 Ref.20
VAR_018071
Natural variant1081C → G in RP2.
VAR_008498
Natural variant1081C → Y in RP2. Ref.22
VAR_068353
Natural variant1181R → C in RP2. Ref.21
VAR_026058
Natural variant1181R → H in RP2; reduces affinity for ARL3 800-fold; loss of stimulation of tubulin GTPase activity; no effect on subcellular location. Ref.1 Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21
VAR_008499
Natural variant1181R → L in RP2. Ref.12 Ref.18
Corresponds to variant rs28933687 [ dbSNP | Ensembl ].
VAR_018072
Natural variant1371Missing in RP2. Ref.17 Ref.19 Ref.20
VAR_018073
Natural variant1381E → G in RP2; reduces affinity for ARL3 150-fold and inhibits the GTP-hydrolysis rate of ARL3. Ref.11 Ref.12 Ref.18
VAR_018074
Natural variant1441K → R.
Corresponds to variant rs3126141 [ dbSNP | Ensembl ].
VAR_053961
Natural variant1881L → P in RP2. Ref.19
VAR_018075
Natural variant2531L → R in RP2. Ref.16
VAR_008500
Natural variant2821R → W Might play a role in retinitis pigmentosa 2; reduces affinity for ARL3 3-fold. Ref.11 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20
Corresponds to variant rs1805147 [ dbSNP | Ensembl ].
VAR_014535
Natural variant3381D → Y. Ref.15
Corresponds to variant rs1805148 [ dbSNP | Ensembl ].
VAR_014536

Experimental info

Mutagenesis21G → A: Loss of membrane association. Ref.5
Mutagenesis31C → S: Targeting to internal membranes. Loss of targeting to the plasma membrane. Ref.5
Mutagenesis281S → A: Reduces affinity for mouse ARL3; when associated with A-29. Ref.12
Mutagenesis291W → A: Reduces affinity for mouse ARL3; when associated with A-28. Ref.12
Mutagenesis311Q → A: Does not reduce affinity for mouse ARL3; when associated with A-32. Ref.12
Mutagenesis321R → A: Does not reduce affinity for mouse ARL3; when associated with A-31. Ref.12
Mutagenesis1011F → A: Reduces affinity for mouse ARL3. Ref.12
Mutagenesis1151Q → A: Reduces affinity for mouse ARL3. Ref.12
Mutagenesis1161Q → A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3. Ref.12
Mutagenesis1181R → A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3. Ref.12
Mutagenesis1201R → H: Reduces affinity for mouse ARL3; when associated with S-121. Ref.12
Mutagenesis1211D → S: Reduces affinity for mouse ARL3; when associated with H-120.
Mutagenesis1771F → A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3. Ref.12
Sequence conflict1681N → D in CAA07577. Ref.1

Secondary structure

.................................................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75695 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3C912B52C53A817E

FASTA35039,641
        10         20         30         40         50         60 
MGCFFSKRRK ADKESRPENE EERPKQYSWD QREKVDPKDY MFSGLKDETV GRLPGTVAGQ 

        70         80         90        100        110        120 
QFLIQDCENC NIYIFDHSAT VTIDDCTNCI IFLGPVKGSV FFRNCRDCKC TLACQQFRVR 

       130        140        150        160        170        180 
DCRKLEVFLC CATQPIIESS SNIKFGCFQW YYPELAFQFK DAGLSIFNNT WSNIHDFTPV 

       190        200        210        220        230        240 
SGELNWSLLP EDAVVQDYVP IPTTEELKAV RVSTEANRSI VPISRGQRQK SSDESCLVVL 

       250        260        270        280        290        300 
FAGDYTIANA RKLIDEMVGK GFFLVQTKEV SMKAEDAQRV FREKAPDFLP LLNKGPVIAL 

       310        320        330        340        350 
EFNGDGAVEV CQLIVNEIFN GTKMFVSESK ETASGDVDSF YNFADIQMGI 

« Hide

References

« Hide 'large scale' references
[1]"Positional cloning of the gene for X-linked retinitis pigmentosa 2."
Schwahn U., Lenzner S., Dong J., Feil S., Hinzmann B., van Duijnhoven G., Kirschner R., Hemberger M., Bergen A.A.B., Rosenberg T., Pinckers A.J.L.G., Fundele R., Rosenthal A., Cremers F.P.M., Ropers H.-H., Berger W.
Nat. Genet. 19:327-332(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS RP2 SER-6 DEL AND HIS-118.
Tissue: Brain.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Eye and Uterus.
[4]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane."
Chapple J.P., Hardcastle A.J., Grayson C., Spackman L.A., Willison K.R., Cheetham M.E.
Hum. Mol. Genet. 9:1919-1926(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS RP2 SER-6 DEL AND HIS-118, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, MUTAGENESIS OF GLY-2 AND CYS-3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[6]"Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C."
Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., Cowan N.J.
J. Biol. Chem. 277:14629-14634(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS RP2 SER-6 DEL AND HIS-118, INTERACTION WITH ARL3.
[7]"Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3."
Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A., Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., Cheetham M.E.
Hum. Mol. Genet. 11:3065-3074(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex."
Veltel S., Kravchenko A., Ismail S., Wittinghofer A.
FEBS Lett. 582:2501-2507(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ARL3 AND UNC119.
[9]"The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium."
Evans R.J., Schwarz N., Nagel-Wolfrum K., Wolfrum U., Hardcastle A.J., Cheetham M.E.
Hum. Mol. Genet. 19:1358-1367(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium."
Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L., Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P., Slusarski D.C., Jackson P.K.
Genes Dev. 25:2347-2360(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3."
Kuehnel K., Veltel S., Schlichting I., Wittinghofer A.
Structure 14:367-378(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), INTERACTION WITH ARL3, CHARACTERIZATION OF VARIANTS RP2 HIS-118 AND GLY-138, CHARACTERIZATION OF VARIANT TRP-282.
[12]"The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3."
Veltel S., Gasper R., Eisenacher E., Wittinghofer A.
Nat. Struct. Mol. Biol. 15:373-380(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-350 OF COMPLEX WITH MOUSE ARL3 AND GTP, FUNCTION, INTERACTION WITH ARL3, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANTS LEU-118 AND GLY-138, MUTAGENESIS OF SER-28; TRP-29; GLN-31; ARG-32; PHE-101; GLN-115; GLN-116; ARG-118; ARG-120 AND PHE-177.
[13]"Mutations in the RP2 gene cause disease in 10% of families with familial X-Linked retinitis pigmentosa assessed in this study."
Hardcastle A.J., Thiselton D.L., Van Maldergem L., Saha B.K., Jay M., Plant C., Taylor R., Bird A.C., Bhattacharya S.
Am. J. Hum. Genet. 64:1210-1215(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP2 HIS-118.
[14]"Genotype-phenotype correlation in X-linked retinitis pigmentosa 2 (RP2)."
Rosenberg T., Schwahn U., Feil S., Berger W.
Ophthalmic Genet. 20:161-172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP2 SER-6 DEL AND HIS-118.
[15]"Novel frameshift mutations in the RP2 gene and polymorphic variants."
Thiselton D.L., Zito I., Plant C., Jay M., Hodgson S.V., Bird A.C., Bhattacharya S.S., Hardcastle A.J.
Hum. Mutat. 15:580-580(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TRP-282 AND TYR-338.
[16]"A new Leu253Arg mutation in the RP2 gene in a Japanese family with X-linked retinitis pigmentosa."
Wada Y., Nakazawa M., Abe T., Tamai M.
Invest. Ophthalmol. Vis. Sci. 41:290-293(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP2 ARG-253.
[17]"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 RP2 TYR-86; LEU-95; HIS-118 AND ILE-137 DEL, VARIANT TRP-282.
[18]"Identification of novel RP2 mutations in a subset of X-linked retinitis pigmentosa families and prediction of new domains."
Miano M.G., Testa F., Filippini F., Trujillo M., Conte I., Lanzara C., Millan J.M., De Bernardo C., Grammatico B., Mangino M., Torrente I., Carrozzo R., Simonelli F., Rinaldi E., Ventruto V., D'Urso M., Ayuso C., Ciccodicola A.
Hum. Mutat. 18:109-119(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP2 LEU-118 AND GLY-138, VARIANT TRP-282.
[19]"A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa."
Breuer D.K., Yashar B.M., Filippova E., Hiriyanna S., Lyons R.H., Mears A.J., Asaye B., Acar C., Vervoort R., Wright A.F., Musarella M.A., Wheeler P., MacDonald I., Iannaccone A., Birch D., Hoffman D.R., Fishman G.A., Heckenlively J.R. expand/collapse author list , Jacobson S.G., Sieving P.A., Swaroop A.
Am. J. Hum. Genet. 70:1545-1554(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP2 TYR-67; HIS-118; ILE-137 DEL AND PRO-188, VARIANT TRP-282.
[20]"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 RP2 TYR-86; LEU-95; HIS-118 AND ILE-137 DEL, VARIANT TRP-282.
[21]"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 RP2 HIS-118 AND CYS-118.
[22]"Next-generation genetic testing for retinitis pigmentosa."
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. expand/collapse author list , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.
Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP2 TYR-108.
+Additional computationally mapped references.

Web resources

Mutations of the RP2 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007590 mRNA. Translation: CAA07577.1.
AL050307, AL627143 Genomic DNA. Translation: CAB82030.2.
BC043348 mRNA. Translation: AAH43348.1.
BC053530 mRNA. Translation: AAH53530.1.
CCDSCCDS14270.1.
RefSeqNP_008846.2. NM_006915.2.
UniGeneHs.44766.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BX6X-ray2.10A1-350[»]
3BH6X-ray2.60B1-350[»]
3BH7X-ray1.90B1-350[»]
ProteinModelPortalO75695.
SMRO75695. Positions 37-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112029. 2 interactions.
DIPDIP-29024N.
IntActO75695. 1 interaction.
MINTMINT-5003911.
STRING9606.ENSP00000218340.

PTM databases

PhosphoSiteO75695.

Proteomic databases

MaxQBO75695.
PaxDbO75695.
PeptideAtlasO75695.
PRIDEO75695.

Protocols and materials databases

DNASU6102.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218340; ENSP00000218340; ENSG00000102218.
ENST00000603075; ENSP00000474087; ENSG00000271091.
GeneID6102.
KEGGhsa:6102.
UCSCuc004dgw.4. human.

Organism-specific databases

CTD6102.
GeneCardsGC0XP046696.
GeneReviewsRP2.
H-InvDBHIX0016754.
HGNCHGNC:10274. RP2.
HPAHPA000234.
MIM300757. gene.
312600. phenotype.
neXtProtNX_O75695.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA34641.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326369.
HOGENOMHOG000007790.
HOVERGENHBG054784.
InParanoidO75695.
KOK18272.
OMAQWYYPEL.
OrthoDBEOG7ZPNKQ.
PhylomeDBO75695.
TreeFamTF105832.

Gene expression databases

BgeeO75695.
CleanExHS_RP2.
GenevestigatorO75695.

Family and domain databases

Gene3D2.160.20.70. 1 hit.
InterProIPR013912. Adenylate_cyclase-assoc_CAP_C.
IPR017901. C-CAP_CF_C-like.
IPR016098. CAP/MinC_C.
IPR006599. CARP_motif.
IPR001564. Nucleoside_diP_kinase.
IPR017332. Protein_XRP2.
IPR012945. Tubulin-bd_cofactor_C_dom.
[Graphical view]
PANTHERPTHR15440:SF0. PTHR15440:SF0. 1 hit.
PfamPF07986. TBCC. 1 hit.
[Graphical view]
PIRSFPIRSF037947. Protein_XRP2_. 1 hit.
SMARTSM00673. CARP. 2 hits.
[Graphical view]
SUPFAMSSF54919. SSF54919. 1 hit.
SSF69340. SSF69340. 1 hit.
PROSITEPS51329. C_CAP_COFACTOR_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75695.
GeneWikiRP2_(gene).
GenomeRNAi6102.
NextBio23737.
PROO75695.
SOURCESearch...

Entry information

Entry nameXRP2_HUMAN
AccessionPrimary (citable) accession number: O75695
Secondary accession number(s): Q86XJ7, Q9NU67
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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