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O75695

- XRP2_HUMAN

UniProt

O75695 - XRP2_HUMAN

Protein

Protein XRP2

Gene

RP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi98 – 992GTP
    Nucleotide bindingi115 – 1184GTP

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. GTPase activator activity Source: UniProtKB
    3. GTP binding Source: UniProtKB-KW
    4. nucleoside diphosphate kinase activity Source: InterPro
    5. protein binding Source: UniProtKB
    6. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. cell morphogenesis Source: InterPro
    2. CTP biosynthetic process Source: InterPro
    3. cytoskeleton organization Source: InterPro
    4. GTP biosynthetic process Source: InterPro
    5. positive regulation of GTPase activity Source: GOC
    6. post-Golgi vesicle-mediated transport Source: MGI
    7. protein folding Source: UniProtKB
    8. protein transport Source: UniProtKB-KW
    9. UTP biosynthetic process Source: InterPro
    10. visual perception Source: ProtInc

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein XRP2
    Gene namesi
    Name:RP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10274. RP2.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. ciliary basal body Source: MGI
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic vesicle Source: MGI
    4. extracellular vesicular exosome Source: UniProt
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61Missing in RP2; loss of membrane association; enhances interaction with ARL3. 2 Publications
    VAR_008497
    Natural varianti67 – 671C → Y in RP2. 1 Publication
    VAR_018069
    Natural varianti86 – 861C → Y in RP2. 2 Publications
    VAR_018070
    Natural varianti95 – 951P → L in RP2; uncertain pathological significance. 2 Publications
    VAR_018071
    Natural varianti108 – 1081C → G in RP2.
    VAR_008498
    Natural varianti108 – 1081C → Y in RP2. 1 Publication
    VAR_068353
    Natural varianti118 – 1181R → C in RP2. 1 Publication
    VAR_026058
    Natural varianti118 – 1181R → H in RP2; reduces affinity for ARL3 800-fold; loss of stimulation of tubulin GTPase activity; no effect on subcellular location. 7 Publications
    VAR_008499
    Natural varianti118 – 1181R → L in RP2. 1 Publication
    Corresponds to variant rs28933687 [ dbSNP | Ensembl ].
    VAR_018072
    Natural varianti137 – 1371Missing in RP2. 3 Publications
    VAR_018073
    Natural varianti138 – 1381E → G in RP2; reduces affinity for ARL3 150-fold and inhibits the GTP-hydrolysis rate of ARL3. 1 Publication
    VAR_018074
    Natural varianti188 – 1881L → P in RP2. 1 Publication
    VAR_018075
    Natural varianti253 – 2531L → R in RP2. 1 Publication
    VAR_008500

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Loss of membrane association. 1 Publication
    Mutagenesisi3 – 31C → S: Targeting to internal membranes. Loss of targeting to the plasma membrane. 1 Publication
    Mutagenesisi28 – 281S → A: Reduces affinity for mouse ARL3; when associated with A-29. 1 Publication
    Mutagenesisi29 – 291W → A: Reduces affinity for mouse ARL3; when associated with A-28. 1 Publication
    Mutagenesisi31 – 311Q → A: Does not reduce affinity for mouse ARL3; when associated with A-32. 1 Publication
    Mutagenesisi32 – 321R → A: Does not reduce affinity for mouse ARL3; when associated with A-31. 1 Publication
    Mutagenesisi101 – 1011F → A: Reduces affinity for mouse ARL3. 1 Publication
    Mutagenesisi115 – 1151Q → A: Reduces affinity for mouse ARL3. 1 Publication
    Mutagenesisi116 – 1161Q → A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3. 1 Publication
    Mutagenesisi118 – 1181R → A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3. 1 Publication
    Mutagenesisi120 – 1201R → H: Reduces affinity for mouse ARL3; when associated with S-121. 1 Publication
    Mutagenesisi121 – 1211D → S: Reduces affinity for mouse ARL3; when associated with H-120.
    Mutagenesisi177 – 1771F → A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3. 1 Publication

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi312600. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA34641.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 350349Protein XRP2PRO_0000080047Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi3 – 31S-palmitoyl cysteine1 Publication

    Post-translational modificationi

    Myristoylated on Gly-2; which may be required for membrane targeting.1 Publication
    Palmitoylated on Cys-3; which may be required for plasma membrane targeting Probable. Mutation of Cys-3 targets the protein to internal membranes.1 PublicationCurated

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate

    Proteomic databases

    MaxQBiO75695.
    PaxDbiO75695.
    PeptideAtlasiO75695.
    PRIDEiO75695.

    PTM databases

    PhosphoSiteiO75695.

    Expressioni

    Tissue specificityi

    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).3 Publications

    Gene expression databases

    BgeeiO75695.
    CleanExiHS_RP2.
    GenevestigatoriO75695.

    Organism-specific databases

    HPAiHPA000234.

    Interactioni

    Subunit structurei

    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 ARL3.4 Publications

    Protein-protein interaction databases

    BioGridi112029. 2 interactions.
    DIPiDIP-29024N.
    IntActiO75695. 1 interaction.
    MINTiMINT-5003911.
    STRINGi9606.ENSP00000218340.

    Structurei

    Secondary structure

    1
    350
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 446
    Beta strandi49 – 524
    Beta strandi62 – 665
    Beta strandi71 – 744
    Beta strandi81 – 855
    Beta strandi90 – 10415
    Beta strandi106 – 12116
    Beta strandi123 – 13311
    Beta strandi136 – 1394
    Beta strandi141 – 1477
    Helixi155 – 1617
    Beta strandi175 – 1784
    Beta strandi185 – 1884
    Helixi195 – 1973
    Helixi205 – 2073
    Turni216 – 2183
    Beta strandi235 – 2406
    Helixi246 – 25914
    Beta strandi263 – 2708
    Helixi274 – 2818
    Helixi282 – 2876
    Helixi289 – 2946
    Beta strandi297 – 3048
    Helixi307 – 31812
    Beta strandi324 – 3263
    Helixi330 – 34819

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BX6X-ray2.10A1-350[»]
    3BH6X-ray2.60B1-350[»]
    3BH7X-ray1.90B1-350[»]
    ProteinModelPortaliO75695.
    SMRiO75695. Positions 37-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75695.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 179156C-CAP/cofactor C-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TBCC family.Curated
    Contains 1 C-CAP/cofactor C-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG326369.
    HOGENOMiHOG000007790.
    HOVERGENiHBG054784.
    InParanoidiO75695.
    KOiK18272.
    OMAiQWYYPEL.
    OrthoDBiEOG7ZPNKQ.
    PhylomeDBiO75695.
    TreeFamiTF105832.

    Family and domain databases

    Gene3Di2.160.20.70. 1 hit.
    InterProiIPR013912. 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]
    PANTHERiPTHR15440:SF0. PTHR15440:SF0. 1 hit.
    PfamiPF07986. TBCC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037947. Protein_XRP2_. 1 hit.
    SMARTiSM00673. CARP. 2 hits.
    [Graphical view]
    SUPFAMiSSF54919. SSF54919. 1 hit.
    SSF69340. SSF69340. 1 hit.
    PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O75695-1 [UniParc]FASTAAdd to Basket

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    MGCFFSKRRK ADKESRPENE EERPKQYSWD QREKVDPKDY MFSGLKDETV    50
    GRLPGTVAGQ QFLIQDCENC NIYIFDHSAT VTIDDCTNCI IFLGPVKGSV 100
    FFRNCRDCKC TLACQQFRVR DCRKLEVFLC CATQPIIESS SNIKFGCFQW 150
    YYPELAFQFK DAGLSIFNNT WSNIHDFTPV SGELNWSLLP EDAVVQDYVP 200
    IPTTEELKAV RVSTEANRSI VPISRGQRQK SSDESCLVVL FAGDYTIANA 250
    RKLIDEMVGK GFFLVQTKEV SMKAEDAQRV FREKAPDFLP LLNKGPVIAL 300
    EFNGDGAVEV CQLIVNEIFN GTKMFVSESK ETASGDVDSF YNFADIQMGI 350
    Length:350
    Mass (Da):39,641
    Last modified:January 23, 2007 - v4
    Checksum:i3C912B52C53A817E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti168 – 1681N → D in CAA07577. (PubMed:9697692)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61Missing in RP2; loss of membrane association; enhances interaction with ARL3. 2 Publications
    VAR_008497
    Natural varianti67 – 671C → Y in RP2. 1 Publication
    VAR_018069
    Natural varianti86 – 861C → Y in RP2. 2 Publications
    VAR_018070
    Natural varianti95 – 951P → L in RP2; uncertain pathological significance. 2 Publications
    VAR_018071
    Natural varianti108 – 1081C → G in RP2.
    VAR_008498
    Natural varianti108 – 1081C → Y in RP2. 1 Publication
    VAR_068353
    Natural varianti118 – 1181R → C in RP2. 1 Publication
    VAR_026058
    Natural varianti118 – 1181R → H in RP2; reduces affinity for ARL3 800-fold; loss of stimulation of tubulin GTPase activity; no effect on subcellular location. 7 Publications
    VAR_008499
    Natural varianti118 – 1181R → L in RP2. 1 Publication
    Corresponds to variant rs28933687 [ dbSNP | Ensembl ].
    VAR_018072
    Natural varianti137 – 1371Missing in RP2. 3 Publications
    VAR_018073
    Natural varianti138 – 1381E → G in RP2; reduces affinity for ARL3 150-fold and inhibits the GTP-hydrolysis rate of ARL3. 1 Publication
    VAR_018074
    Natural varianti144 – 1441K → R.
    Corresponds to variant rs3126141 [ dbSNP | Ensembl ].
    VAR_053961
    Natural varianti188 – 1881L → P in RP2. 1 Publication
    VAR_018075
    Natural varianti253 – 2531L → R in RP2. 1 Publication
    VAR_008500
    Natural varianti282 – 2821R → W Might play a role in retinitis pigmentosa 2; reduces affinity for ARL3 3-fold. 5 Publications
    Corresponds to variant rs1805147 [ dbSNP | Ensembl ].
    VAR_014535
    Natural varianti338 – 3381D → Y.1 Publication
    Corresponds to variant rs1805148 [ dbSNP | Ensembl ].
    VAR_014536

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007590 mRNA. Translation: CAA07577.1.
    AL050307, AL627143 Genomic DNA. Translation: CAB82030.2.
    BC043348 mRNA. Translation: AAH43348.1.
    BC053530 mRNA. Translation: AAH53530.1.
    CCDSiCCDS14270.1.
    RefSeqiNP_008846.2. NM_006915.2.
    UniGeneiHs.44766.

    Genome annotation databases

    EnsembliENST00000218340; ENSP00000218340; ENSG00000102218.
    GeneIDi6102.
    KEGGihsa:6102.
    UCSCiuc004dgw.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Mutations of the RP2 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007590 mRNA. Translation: CAA07577.1 .
    AL050307 , AL627143 Genomic DNA. Translation: CAB82030.2 .
    BC043348 mRNA. Translation: AAH43348.1 .
    BC053530 mRNA. Translation: AAH53530.1 .
    CCDSi CCDS14270.1.
    RefSeqi NP_008846.2. NM_006915.2.
    UniGenei Hs.44766.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BX6 X-ray 2.10 A 1-350 [» ]
    3BH6 X-ray 2.60 B 1-350 [» ]
    3BH7 X-ray 1.90 B 1-350 [» ]
    ProteinModelPortali O75695.
    SMRi O75695. Positions 37-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112029. 2 interactions.
    DIPi DIP-29024N.
    IntActi O75695. 1 interaction.
    MINTi MINT-5003911.
    STRINGi 9606.ENSP00000218340.

    PTM databases

    PhosphoSitei O75695.

    Proteomic databases

    MaxQBi O75695.
    PaxDbi O75695.
    PeptideAtlasi O75695.
    PRIDEi O75695.

    Protocols and materials databases

    DNASUi 6102.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000218340 ; ENSP00000218340 ; ENSG00000102218 .
    GeneIDi 6102.
    KEGGi hsa:6102.
    UCSCi uc004dgw.4. human.

    Organism-specific databases

    CTDi 6102.
    GeneCardsi GC0XP046696.
    GeneReviewsi RP2.
    H-InvDB HIX0016754.
    HGNCi HGNC:10274. RP2.
    HPAi HPA000234.
    MIMi 300757. gene.
    312600. phenotype.
    neXtProti NX_O75695.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA34641.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326369.
    HOGENOMi HOG000007790.
    HOVERGENi HBG054784.
    InParanoidi O75695.
    KOi K18272.
    OMAi QWYYPEL.
    OrthoDBi EOG7ZPNKQ.
    PhylomeDBi O75695.
    TreeFami TF105832.

    Miscellaneous databases

    EvolutionaryTracei O75695.
    GeneWikii RP2_(gene).
    GenomeRNAii 6102.
    NextBioi 23737.
    PROi O75695.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75695.
    CleanExi HS_RP2.
    Genevestigatori O75695.

    Family and domain databases

    Gene3Di 2.160.20.70. 1 hit.
    InterProi IPR013912. 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 ]
    PANTHERi PTHR15440:SF0. PTHR15440:SF0. 1 hit.
    Pfami PF07986. TBCC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037947. Protein_XRP2_. 1 hit.
    SMARTi SM00673. CARP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54919. SSF54919. 1 hit.
    SSF69340. SSF69340. 1 hit.
    PROSITEi PS51329. C_CAP_COFACTOR_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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. 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. 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. 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. 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. Cited for: VARIANT RP2 TYR-108.

    Entry informationi

    Entry nameiXRP2_HUMAN
    AccessioniPrimary (citable) accession number: O75695
    Secondary accession number(s): Q86XJ7, Q9NU67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 4 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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