RP2
entrez
6102
canonical
uniprot
O75695
canonical
ensembl
ENSG00000102218
resolver
ensp
ENSP00000218340
resolver
ensp
ENSP00000561171
resolver
enst
ENST00000218340
resolver
enst
ENST00000891112
resolver
genesymbol
RP2
resolver
hgnc
HGNC:10274
resolver
uniprot
Q86XJ7
resolver
uniprot
Q9NU67
resolver
uniprot_entry
XRP2_HUMAN
resolver
uniprot_sec
Q86XJ7
resolver
uniprot_sec
Q9NU67
resolver
amino_acid_sequence
MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
uniprot
proteins
disease_involvement
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. {ECO:0000269|PubMed:10053026, ECO:0000269|PubMed:10090907, ECO:0000269|PubMed:10520237, ECO:0000269|PubMed:10634633, ECO:0000269|PubMed:10937588, ECO:0000269|PubMed:10942419, ECO:0000269|PubMed:11462235, ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:11992260, ECO:0000269|PubMed:12657579, ECO:0000269|PubMed:14564670, ECO:0000269|PubMed:16472755, ECO:0000269|PubMed:22334370, ECO:0000269|PubMed:9697692}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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 a guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. {ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:20106869, ECO:0000269|PubMed:22085962}.
uniprot
proteins
mass_dalton
39641
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Loss of membrane association."; /evidence="ECO:0000269|PubMed:10942419"; MUTAGEN 3; /note="C->S: Targeting to internal membranes. Loss of targeting to the plasma membrane."; /evidence="ECO:0000269|PubMed:10942419"; MUTAGEN 28; /note="S->A: Reduces affinity for mouse ARL3; when associated with A-29."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 29; /note="W->A: Reduces affinity for mouse ARL3; when associated with A-28."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 31; /note="Q->A: Does not reduce affinity for mouse ARL3; when associated with A-32."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 32; /note="R->A: Does not reduce affinity for mouse ARL3; when associated with A-31."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 101; /note="F->A: Reduces affinity for mouse ARL3."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 115; /note="Q->A: Reduces affinity for mouse ARL3."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 116; /note="Q->A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 118; /note="R->A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 120; /note="R->H: Reduces affinity for mouse ARL3; when associated with S-121."; /evidence="ECO:0000269|PubMed:18376416"; MUTAGEN 121; /note="D->S: Reduces affinity for mouse ARL3; when associated with H-120."; MUTAGEN 177; /note="F->A: Reduces affinity and GTP-hydrolysis rate for mouse ARL3."; /evidence="ECO:0000269|PubMed:18376416
uniprot
proteins
post_translational_modification
PTM: Myristoylated on Gly-2; which may be required for membrane targeting. {ECO:0000305|PubMed:10942419}.; PTM: Palmitoylated on Cys-3; which may be required for plasma membrane targeting (Probable). Mutation of Cys-3 targets the protein to internal membranes. {ECO:0000269|PubMed:10942419, ECO:0000305}.
uniprot
proteins
protein_family
TBCC family
uniprot
proteins
pubmed
10053026
uniprot
proteins
pubmed
10090907
uniprot
proteins
pubmed
10520237
uniprot
proteins
pubmed
10634633
uniprot
proteins
pubmed
10862093
uniprot
proteins
pubmed
10937588
uniprot
proteins
pubmed
10942419
uniprot
proteins
pubmed
11462235
uniprot
proteins
pubmed
11847227
uniprot
proteins
pubmed
11992260
uniprot
proteins
pubmed
12417528
uniprot
proteins
pubmed
12657579
uniprot
proteins
pubmed
14564670
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16472755
uniprot
proteins
pubmed
18376416
uniprot
proteins
pubmed
18588884
uniprot
proteins
pubmed
20106869
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22085962
uniprot
proteins
pubmed
22334370
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27535533
uniprot
proteins
pubmed
9697692
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10942419, ECO:0000269|PubMed:12417528}; Lipid-anchor {ECO:0000269|PubMed:10942419}; Cytoplasmic side {ECO:0000269|PubMed:10942419}. Cell projection, cilium {ECO:0000269|PubMed:20106869}. Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. {ECO:0000269|PubMed:12417528}.
uniprot
proteins