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O75695

- XRP2_HUMAN

UniProt

O75695 - XRP2_HUMAN

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Protein

Protein XRP2

Gene

RP2

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

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. 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
Complete GO annotation...

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. centriole Source: Ensembl
  2. ciliary basal body Source: MGI
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle Source: MGI
  5. extracellular vesicular exosome Source: UniProtKB
  6. Golgi apparatus Source: Ensembl
  7. periciliary membrane compartment Source: Ensembl
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

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. 38 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 – 446Combined sources
Beta strandi49 – 524Combined sources
Beta strandi62 – 665Combined sources
Beta strandi71 – 744Combined sources
Beta strandi81 – 855Combined sources
Beta strandi90 – 10415Combined sources
Beta strandi106 – 12116Combined sources
Beta strandi123 – 13311Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi141 – 1477Combined sources
Helixi155 – 1617Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi185 – 1884Combined sources
Helixi195 – 1973Combined sources
Helixi205 – 2073Combined sources
Turni216 – 2183Combined sources
Beta strandi235 – 2406Combined sources
Helixi246 – 25914Combined sources
Beta strandi263 – 2708Combined sources
Helixi274 – 2818Combined sources
Helixi282 – 2876Combined sources
Helixi289 – 2946Combined sources
Beta strandi297 – 3048Combined sources
Helixi307 – 31812Combined sources
Beta strandi324 – 3263Combined sources
Helixi330 – 34819Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063741.
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

« Hide

        10         20         30         40         50
MGCFFSKRRK ADKESRPENE EERPKQYSWD QREKVDPKDY MFSGLKDETV
60 70 80 90 100
GRLPGTVAGQ QFLIQDCENC NIYIFDHSAT VTIDDCTNCI IFLGPVKGSV
110 120 130 140 150
FFRNCRDCKC TLACQQFRVR DCRKLEVFLC CATQPIIESS SNIKFGCFQW
160 170 180 190 200
YYPELAFQFK DAGLSIFNNT WSNIHDFTPV SGELNWSLLP EDAVVQDYVP
210 220 230 240 250
IPTTEELKAV RVSTEANRSI VPISRGQRQK SSDESCLVVL FAGDYTIANA
260 270 280 290 300
RKLIDEMVGK GFFLVQTKEV SMKAEDAQRV FREKAPDFLP LLNKGPVIAL
310 320 330 340 350
EFNGDGAVEV CQLIVNEIFN GTKMFVSESK ETASGDVDSF YNFADIQMGI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 38 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.
GeneTreei ENSGT00530000063741.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 136 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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