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P56715

- RP1_HUMAN

UniProt

P56715 - RP1_HUMAN

Protein

Oxygen-regulated protein 1

Gene

RP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (30 May 2000)
      Previous versions | rss
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    Functioni

    Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme By similarity.By similarity

    GO - Molecular functioni

    1. microtubule binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. axoneme assembly Source: UniProtKB
    2. cellular response to light stimulus Source: Ensembl
    3. intracellular signal transduction Source: InterPro
    4. photoreceptor cell development Source: UniProtKB
    5. photoreceptor cell maintenance Source: UniProtKB
    6. photoreceptor cell outer segment organization Source: UniProtKB
    7. phototransduction, visible light Source: ProtInc
    8. retinal cone cell development Source: UniProtKB
    9. retinal rod cell development Source: UniProtKB
    10. visual perception Source: ProtInc

    Keywords - Biological processi

    Cilium biogenesis/degradation, Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxygen-regulated protein 1
    Alternative name(s):
    Retinitis pigmentosa 1 protein
    Retinitis pigmentosa RP1 protein
    Gene namesi
    Name:RP1
    Synonyms:ORP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:10263. RP1.

    Subcellular locationi

    Cytoplasmcytoskeletoncilium axoneme By similarity. Cell projectionciliumphotoreceptor outer segment 1 Publication
    Note: Specifically localized in the connecting cilia of rod and cone photoreceptors.

    GO - Cellular componenti

    1. axoneme Source: Ensembl
    2. microtubule Source: UniProtKB-KW
    3. microtubule associated complex Source: UniProtKB
    4. photoreceptor connecting cilium Source: MGI
    5. photoreceptor inner segment Source: UniProtKB
    6. photoreceptor outer segment Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 1 (RP1) [MIM:180100]: 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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721L → R in RP1. 1 Publication
    Corresponds to variant rs180729424 [ dbSNP | Ensembl ].
    VAR_068351
    Natural varianti202 – 2021D → E in RP1. 1 Publication
    VAR_064182
    Natural varianti373 – 3731T → I in RP1. 3 Publications
    Corresponds to variant rs77775126 [ dbSNP | Ensembl ].
    VAR_064183
    Natural varianti663 – 6631K → N in RP1; unknown pathological significance. 2 Publications
    VAR_064467
    Natural varianti669 – 6691A → T in RP1. 1 Publication
    VAR_064468
    Natural varianti900 – 9001K → N in RP1. 1 Publication
    VAR_066951
    Natural varianti984 – 9841D → G in RP1. 1 Publication
    VAR_064471
    Natural varianti1370 – 13701K → E in RP1; unknown pathological significance. 1 Publication
    Corresponds to variant rs186594858 [ dbSNP | Ensembl ].
    VAR_064472
    Natural varianti1652 – 16521R → L in RP1; unknown pathological significance. 1 Publication
    VAR_064473
    Natural varianti1808 – 18081L → P in RP1; unknown pathological significance. 1 Publication
    VAR_064474
    Natural varianti2113 – 21131T → N in RP1. 1 Publication
    Corresponds to variant rs137887415 [ dbSNP | Ensembl ].
    VAR_066959

    Keywords - Diseasei

    Disease mutation, Retinitis pigmentosa

    Organism-specific databases

    MIMi145750. phenotype.
    180100. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA34635.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21562156Oxygen-regulated protein 1PRO_0000097410Add
    BLAST

    Proteomic databases

    MaxQBiP56715.
    PaxDbiP56715.
    PeptideAtlasiP56715.
    PRIDEiP56715.

    PTM databases

    PhosphoSiteiP56715.

    Expressioni

    Tissue specificityi

    Expressed in retina. Not expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, spleen and pancreas.

    Gene expression databases

    BgeeiP56715.
    CleanExiHS_RP1.
    GenevestigatoriP56715.

    Organism-specific databases

    HPAiHPA042257.

    Interactioni

    Subunit structurei

    Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1 By similarity. Interacts with MAK By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000220676.

    Structurei

    3D structure databases

    ProteinModelPortaliP56715.
    SMRiP56715. Positions 35-107.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 11883Doublecortin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini154 – 23380Doublecortin 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi268 – 2736Poly-Ser
    Compositional biasi671 – 6755Poly-Lys
    Compositional biasi1687 – 16915Poly-Ser

    Domaini

    The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation.By similarity

    Sequence similaritiesi

    Contains 2 doublecortin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG313727.
    HOGENOMiHOG000136857.
    HOVERGENiHBG018173.
    InParanoidiP56715.
    OMAiEYHMFTH.
    OrthoDBiEOG7N37DH.
    PhylomeDBiP56715.
    TreeFamiTF318770.

    Family and domain databases

    Gene3Di3.10.20.230. 2 hits.
    InterProiIPR003533. Doublecortin_dom.
    [Graphical view]
    PfamiPF03607. DCX. 2 hits.
    [Graphical view]
    SMARTiSM00537. DCX. 2 hits.
    [Graphical view]
    PROSITEiPS50309. DC. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56715-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDTPSTGFS IIHPTSSEGQ VPPPRHLSLT HPVVAKRISF YKSGDPQFGG     50
    VRVVVNPRSF KSFDALLDNL SRKVPLPFGV RNISTPRGRH SITRLEELED 100
    GESYLCSHGR KVQPVDLDKA RRRPRPWLSS RAISAHSPPH PVAVAAPGMP 150
    RPPRSLVVFR NGDPKTRRAV LLSRRVTQSF EAFLQHLTEV MQRPVVKLYA 200
    TDGRRVPSLQ AVILSSGAVV AAGREPFKPG NYDIQKYLLP ARLPGISQRV 250
    YPKGNAKSES RKISTHMSSS SRSQIYSVSS EKTHNNDCYL DYSFVPEKYL 300
    ALEKNDSQNL PIYPSEDDIE KSIIFNQDGT MTVEMKVRFR IKEEETIKWT 350
    TTVSKTGPSN NDEKSEMSFP GRTESRSSGL KLAACSFSAD VSPMERSSNQ 400
    EGSLAEEINI QMTDQVAETC SSASWENATV DTDIIQGTQD QAKHRFYRPP 450
    TPGLRRVRQK KSVIGSVTLV SETEVQEKMI GQFSYSEERE SGENKSEYHM 500
    FTHSCSKMSS VSNKPVLVQI NNNDQMEESS LERKKENSLL KSSAISAGVI 550
    EITSQKMLEM SHNNGLPSTI SNNSIVEEDV VDCVVLDNKT GIKNFKTYGN 600
    TNDRFSPISA DATHFSSNNS GTDKNISEAP ASEASSTVTA RIDRLINEFA 650
    QCGLTKLPKN EKKILSSVAS KKKKKSRQQA INSRYQDGQL ATKGILNKNE 700
    RINTKGRITK EMIVQDSDSP LKGGILCEED LQKSDTVIES NTFCSKSNLN 750
    STISKNFHRN KLNTTQNSKV QGLLTKRKSR SLNKISLGAP KKREIGQRDK 800
    VFPHNESKYC KSTFENKSLF HVFNILEQKP KDFYAPQSQA EVASGYLRGM 850
    AKKSLVSKVT DSHITLKSQK KRKGDKVKAS AILSKQHATT RANSLASLKK 900
    PDFPEAIAHH SIQNYIQSWL QNINPYPTLK PIKSAPVCRN ETSVVNCSNN 950
    SFSGNDPHTN SGKISNFVME SNKHITKIAG LTGDNLCKEG DKSFIANDTG 1000
    EEDLHETQVG SLNDAYLVPL HEHCTLSQSA INDHNTKSHI AAEKSGPEKK 1050
    LVYQEINLAR KRQSVEAAIQ VDPIEEETPK DLLPVLMLHQ LQASVPGIHK 1100
    TQNGVVQMPG SLAGVPFHSA ICNSSTNLLL AWLLVLNLKG SMNSFCQVDA 1150
    HKATNKSSET LALLEILKHI AITEEADDLK AAVANLVEST TSHFGLSEKE 1200
    QDMVPIDLSA NCSTVNIQSV PKCSENERTQ GISSLDGGCS ASEACAPEVC 1250
    VLEVTCSPCE MCTVNKAYSP KETCNPSDTF FPSDGYGVDQ TSMNKACFLG 1300
    EVCSLTDTVF SDKACAQKEN HTYEGACPID ETYVPVNVCN TIDFLNSKEN 1350
    TYTDNLDSTE ELERGDDIQK DLNILTDPEY KNGFNTLVSH QNVSNLSSCG 1400
    LCLSEKEAEL DKKHSSLDDF ENCSLRKFQD ENAYTSFDME EPRTSEEPGS 1450
    ITNSMTSSER NISELESFEE LENHDTDIFN TVVNGGEQAT EELIQEEVEA 1500
    SKTLELIDIS SKNIMEEKRM NGIIYEIISK RLATPPSLDF CYDSKQNSEK 1550
    ETNEGETKMV KMMVKTMETG SYSESSPDLK KCIKSPVTSD WSDYRPDSDS 1600
    EQPYKTSSDD PNDSGELTQE KEYNIGFVKR AIEKLYGKAD IIKPSFFPGS 1650
    TRKSQVCPYN SVEFQCSRKA SLYDSEGQSF GSSEQVSSSS SMLQEFQEER 1700
    QDKCDVSAVR DNYCRGDIVE PGTKQNDDSR ILTDIEEGVL IDKGKWLLKE 1750
    NHLLRMSSEN PGMCGNADTT SVDTLLDNNS SEVPYSHFGN LAPGPTMDEL 1800
    SSSELEELTQ PLELKCNYFN MPHGSDSEPF HEDLLDVRNE TCAKERIANH 1850
    HTEEKGSHQS ERVCTSVTHS FISAGNKVYP VSDDAIKNQP LPGSNMIHGT 1900
    LQEADSLDKL YALCGQHCPI LTVIIQPMNE EDRGFAYRKE SDIENFLGFY 1950
    LWMKIHPYLL QTDKNVFREE NNKASMRQNL IDNAIGDIFD QFYFSNTFDL 2000
    MGKRRKQKRI NFLGLEEEGN LKKFQPDLKE RFCMNFLHTS LLVVGNVDSN 2050
    TQDLSGQTNE IFKAVDENNN LLNNRFQGSR TNLNQVVREN INCHYFFEML 2100
    GQACLLDICQ VETSLNISNR NILELCMFEG ENLFIWEEED ILNLTDLESS 2150
    REQEDL 2156
    Length:2,156
    Mass (Da):240,661
    Last modified:May 30, 2000 - v1
    Checksum:i55AEDBEC43D6A507
    GO

    Polymorphismi

    Tyr-985 is associated with susceptibility to hypertriglyceridemia [MIMi:145750] in the homozygous state.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti168 – 1681R → G.1 Publication
    VAR_066948
    Natural varianti172 – 1721L → R in RP1. 1 Publication
    Corresponds to variant rs180729424 [ dbSNP | Ensembl ].
    VAR_068351
    Natural varianti202 – 2021D → E in RP1. 1 Publication
    VAR_064182
    Natural varianti218 – 2181A → T.1 Publication
    Corresponds to variant rs145691085 [ dbSNP | Ensembl ].
    VAR_066949
    Natural varianti251 – 2511Y → C.
    Corresponds to variant rs16920614 [ dbSNP | Ensembl ].
    VAR_051323
    Natural varianti373 – 3731T → I in RP1. 3 Publications
    Corresponds to variant rs77775126 [ dbSNP | Ensembl ].
    VAR_064183
    Natural varianti376 – 3761R → L.1 Publication
    VAR_066950
    Natural varianti408 – 4081I → L.1 Publication
    VAR_064466
    Natural varianti663 – 6631K → N in RP1; unknown pathological significance. 2 Publications
    VAR_064467
    Natural varianti669 – 6691A → T in RP1. 1 Publication
    VAR_064468
    Natural varianti706 – 7061G → R.1 Publication
    Corresponds to variant rs199879316 [ dbSNP | Ensembl ].
    VAR_064469
    Natural varianti727 – 7271C → W.1 Publication
    VAR_064470
    Natural varianti752 – 7521T → M.
    Corresponds to variant rs28399531 [ dbSNP | Ensembl ].
    VAR_051324
    Natural varianti872 – 8721R → H.5 Publications
    Corresponds to variant rs444772 [ dbSNP | Ensembl ].
    VAR_007810
    Natural varianti900 – 9001K → N in RP1. 1 Publication
    VAR_066951
    Natural varianti945 – 9451V → L.
    Corresponds to variant rs16920621 [ dbSNP | Ensembl ].
    VAR_051325
    Natural varianti984 – 9841D → G in RP1. 1 Publication
    VAR_064471
    Natural varianti985 – 9851N → Y Associated with susceptibility to hypertriglyceridemia. 4 Publications
    Corresponds to variant rs2293869 [ dbSNP | Ensembl ].
    VAR_007811
    Natural varianti1072 – 10721D → G.1 Publication
    VAR_066952
    Natural varianti1356 – 13561L → S.1 Publication
    VAR_066953
    Natural varianti1370 – 13701K → E in RP1; unknown pathological significance. 1 Publication
    Corresponds to variant rs186594858 [ dbSNP | Ensembl ].
    VAR_064472
    Natural varianti1417 – 14171L → P.1 Publication
    Corresponds to variant rs139294220 [ dbSNP | Ensembl ].
    VAR_066954
    Natural varianti1425 – 14251L → P.1 Publication
    VAR_066955
    Natural varianti1595 – 15951R → Q.2 Publications
    Corresponds to variant rs35084330 [ dbSNP | Ensembl ].
    VAR_051326
    Natural varianti1652 – 16521R → L in RP1; unknown pathological significance. 1 Publication
    VAR_064473
    Natural varianti1670 – 16701A → T.4 Publications
    Corresponds to variant rs446227 [ dbSNP | Ensembl ].
    VAR_007812
    Natural varianti1691 – 16911S → P.4 Publications
    Corresponds to variant rs414352 [ dbSNP | Ensembl ].
    VAR_007813
    Natural varianti1793 – 17931P → S.2 Publications
    Corresponds to variant rs143088423 [ dbSNP | Ensembl ].
    VAR_066956
    Natural varianti1808 – 18081L → P in RP1; unknown pathological significance. 1 Publication
    VAR_064474
    Natural varianti1935 – 19351F → L.1 Publication
    Corresponds to variant rs140137224 [ dbSNP | Ensembl ].
    VAR_066957
    Natural varianti2033 – 20331C → Y.3 Publications
    Corresponds to variant rs61739567 [ dbSNP | Ensembl ].
    VAR_007814
    Natural varianti2066 – 20661D → N.1 Publication
    Corresponds to variant rs149282954 [ dbSNP | Ensembl ].
    VAR_066958
    Natural varianti2113 – 21131T → N in RP1. 1 Publication
    Corresponds to variant rs137887415 [ dbSNP | Ensembl ].
    VAR_066959

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143226, AF143224, AF143225 Genomic DNA. Translation: AAD44197.1.
    AF143222 mRNA. Translation: AAD44198.1.
    AF141021 mRNA. Translation: AAD42072.1.
    AF152242, AF152240, AF152241 Genomic DNA. Translation: AAD46774.1.
    AF146592 mRNA. Translation: AAD46769.1.
    AF128525 Genomic DNA. No translation available.
    CCDSiCCDS6160.1.
    RefSeqiNP_006260.1. NM_006269.1.
    UniGeneiHs.732820.

    Genome annotation databases

    EnsembliENST00000220676; ENSP00000220676; ENSG00000104237.
    GeneIDi6101.
    KEGGihsa:6101.
    UCSCiuc003xsd.1. human.

    Polymorphism databases

    DMDMi6225804.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    RetNet

    Retinal information network

    Mutations of the RP1 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143226 , AF143224 , AF143225 Genomic DNA. Translation: AAD44197.1 .
    AF143222 mRNA. Translation: AAD44198.1 .
    AF141021 mRNA. Translation: AAD42072.1 .
    AF152242 , AF152240 , AF152241 Genomic DNA. Translation: AAD46774.1 .
    AF146592 mRNA. Translation: AAD46769.1 .
    AF128525 Genomic DNA. No translation available.
    CCDSi CCDS6160.1.
    RefSeqi NP_006260.1. NM_006269.1.
    UniGenei Hs.732820.

    3D structure databases

    ProteinModelPortali P56715.
    SMRi P56715. Positions 35-107.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000220676.

    PTM databases

    PhosphoSitei P56715.

    Polymorphism databases

    DMDMi 6225804.

    Proteomic databases

    MaxQBi P56715.
    PaxDbi P56715.
    PeptideAtlasi P56715.
    PRIDEi P56715.

    Protocols and materials databases

    DNASUi 6101.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220676 ; ENSP00000220676 ; ENSG00000104237 .
    GeneIDi 6101.
    KEGGi hsa:6101.
    UCSCi uc003xsd.1. human.

    Organism-specific databases

    CTDi 6101.
    GeneCardsi GC08P055539.
    GeneReviewsi RP1.
    HGNCi HGNC:10263. RP1.
    HPAi HPA042257.
    MIMi 145750. phenotype.
    180100. phenotype.
    603937. gene.
    neXtProti NX_P56715.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA34635.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313727.
    HOGENOMi HOG000136857.
    HOVERGENi HBG018173.
    InParanoidi P56715.
    OMAi EYHMFTH.
    OrthoDBi EOG7N37DH.
    PhylomeDBi P56715.
    TreeFami TF318770.

    Miscellaneous databases

    GeneWikii RP1.
    GenomeRNAii 6101.
    NextBioi 23733.
    PROi P56715.
    SOURCEi Search...

    Gene expression databases

    Bgeei P56715.
    CleanExi HS_RP1.
    Genevestigatori P56715.

    Family and domain databases

    Gene3Di 3.10.20.230. 2 hits.
    InterProi IPR003533. Doublecortin_dom.
    [Graphical view ]
    Pfami PF03607. DCX. 2 hits.
    [Graphical view ]
    SMARTi SM00537. DCX. 2 hits.
    [Graphical view ]
    PROSITEi PS50309. DC. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in a novel retina-specific gene cause autosomal dominant retinitis pigmentosa."
      Sullivan L.S., Heckenlively J.R., Bowne S.J., Zuo J., Hide W.A., Gal A., Denton M., Inglehearn C.F., Blanton S.H., Daiger S.P.
      Nat. Genet. 22:255-259(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS HIS-872; TYR-985; THR-1670; PRO-1691 AND TYR-2033.
      Tissue: Retina.
    2. "Mutations in a gene encoding a new oxygen-regulated photoreceptor protein cause dominant retinitis pigmentosa."
      Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.
      Nat. Genet. 22:248-254(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN RP1.
      Tissue: Retina.
    3. "A nonsense mutation in a novel gene is associated with retinitis pigmentosa in a family linked to the RP1 locus."
      Guillonneau X., Piriev N.I., Danciger M., Kozak C.A., Cideciyan A.V., Jacobson S.G., Farber D.B.
      Hum. Mol. Genet. 8:1541-1546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Identification and subcellular localization of the RP1 protein in human and mouse photoreceptors."
      Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E., Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.
      Invest. Ophthalmol. Vis. Sci. 43:22-32(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "RP1 and autosomal dominant rod-cone dystrophy: Novel mutations, a review of published variants, and genotype-phenotype correlation."
      Audo I., Mohand-Said S., Dhaenens C.M., Germain A., Orhan E., Antonio A., Hamel C., Sahel J.A., Bhattacharya S.S., Zeitz C.
      Hum. Mutat. 33:73-80(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RP1.
    7. Cited for: VARIANTS RP1 ASN-663 AND PRO-1808, VARIANT GLN-1595.
    8. "RP1 protein truncating mutations predominate at the RP1 adRP locus."
      Payne A., Vithana E., Khaliq S., Hameed A., Deller J., Abu-Safieh L., Kermani S., Leroy B.P., Mehdi S.Q., Moore A.T., Bird A.C., Bhattacharya S.S.
      Invest. Ophthalmol. Vis. Sci. 41:4069-4073(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RP1 ILE-373; ASN-663; ASN-900 AND ASN-2113, VARIANTS HIS-872; TYR-985; GLN-1595; THR-1670; PRO-1691 AND SER-1793.
    9. "Clinical features and mutations in patients with dominant retinitis pigmentosa-1 (RP1)."
      Berson E.L., Grimsby J.L., Adams S.M., McGee T.L., Sweklo E., Pierce E.A., Sandberg M.A., Dryja T.P.
      Invest. Ophthalmol. Vis. Sci. 42:2217-2224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLY-168; THR-218; ILE-373; LEU-376; HIS-872; TYR-985; GLY-1072; SER-1356; PRO-1417; PRO-1425; THR-1670; PRO-1691; SER-1793; LEU-1935; TYR-2033 AND ASN-2066.
    10. "Hypertriglyceridemia associated with amino acid variation Asn985Tyr of the RP1 gene."
      Fujita Y., Ezura Y., Emi M., Ono S., Takada D., Takahashi K., Uemura K., Iino Y., Katayama Y., Bujo H., Saito Y.
      J. Hum. Genet. 48:305-308(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF VARIANT TYR-985 WITH HYPERTRIGLYCERIDEMIA.
    11. "Novel association of RP1 gene mutations with autosomal recessive retinitis pigmentosa."
      Khaliq S., Abid A., Ismail M., Hameed A., Mohyuddin A., Lall P., Aziz A., Anwar K., Mehdi S.Q.
      J. Med. Genet. 42:436-438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RP1 ILE-373 AND THR-669.
    12. "A novel missense RP1 mutation in retinitis pigmentosa."
      Chiang S.W., Wang D.Y., Chan W.M., Tam P.O., Chong K.K., Lam D.S., Pang C.P.
      Eye 20:602-605(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RP1 GLY-984, VARIANTS TRP-727 AND HIS-872.
    13. "Molecular characterization of retinitis pigmentosa in Saudi Arabia."
      Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H., Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.
      Mol. Vis. 15:2464-2469(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RP1 GLU-202.
    14. "Differential pattern of RP1 mutations in retinitis pigmentosa."
      Zhang X., Chen L.J., Law J.P., Lai T.Y., Chiang S.W., Tam P.O., Chu K.Y., Wang N., Zhang M., Pang C.P.
      Mol. Vis. 16:1353-1360(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RP1 GLU-1370 AND LEU-1652, VARIANTS LEU-408; ARG-706; HIS-872; TYR-985; THR-1670; PRO-1691 AND TYR-2033.
    15. Cited for: VARIANT RP1 ARG-172.

    Entry informationi

    Entry nameiRP1_HUMAN
    AccessioniPrimary (citable) accession number: P56715
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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