REPS1_HUMAN
ID REPS1_HUMAN Reviewed; 796 AA.
AC Q96D71; B7ZBZ8; B7ZBZ9; B7ZC00; J3KP76; Q5JWJ5; Q5JWJ6; Q5JWJ7; Q8NDR7;
AC Q8WU62; Q9BXY9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=RalBP1-associated Eps domain-containing protein 1;
DE AltName: Full=RalBP1-interacting protein 1;
GN Name=REPS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-159 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R.,
RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T.,
RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K.,
RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T.,
RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T.,
RA Sugano S.;
RT "Diversification of transcriptional modulation: large-scale identification
RT and characterization of putative alternative promoters of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-796 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11750063; DOI=10.1016/s0167-4781(01)00310-4;
RA Xu J., Zhou Z., Zeng L., Huang Y., Zhao W., Cheng C., Xu M., Xie Y.,
RA Mao Y.;
RT "Cloning, expression and characterization of a novel human REPS1 gene.";
RL Biochim. Biophys. Acta 1522:118-121(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-796 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-796 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP INTERACTION WITH RAB11FIP2.
RX PubMed=12364336; DOI=10.1074/jbc.m206316200;
RA Cullis D.N., Philip B., Baleja J.D., Feig L.A.;
RT "Rab11-FIP2, an adaptor protein connecting cellular components involved in
RT internalization and recycling of epidermal growth factor receptors.";
RL J. Biol. Chem. 277:49158-49166(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-166; SER-170 AND
RP SER-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-170; THR-173 AND
RP SER-540, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP INTERACTION WITH AMPH; ITSN1 AND SGIP1, AND SUBCELLULAR LOCATION.
RX PubMed=20946875; DOI=10.1016/j.bbrc.2010.10.045;
RA Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J.,
RA Rynditch A.;
RT "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated
RT pits.";
RL Biochem. Biophys. Res. Commun. 402:408-413(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-562 AND SER-740, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-170; SER-562 AND
RP SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-272; SER-273;
RP SER-307; SER-475; SER-482 AND SER-709, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-170; THR-173;
RP SER-272 AND SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP INVOLVEMENT IN NBIA7, VARIANTS NBIA7 LEU-78 AND GLU-113, AND
RP CHARACTERIZATION OF VARIANTS NBIA7 LEU-78 AND GLU-113.
RX PubMed=29395073; DOI=10.1016/j.ajhg.2018.01.003;
RA Drecourt A., Babdor J., Dussiot M., Petit F., Goudin N., Garfa-Traore M.,
RA Habarou F., Bole-Feysot C., Nitschke P., Ottolenghi C., Metodiev M.D.,
RA Serre V., Desguerre I., Boddaert N., Hermine O., Munnich A., Roetig A.;
RT "Impaired Transferrin Receptor Palmitoylation and Recycling in
RT Neurodegeneration with Brain Iron Accumulation.";
RL Am. J. Hum. Genet. 102:266-277(2018).
CC -!- FUNCTION: May coordinate the cellular actions of activated EGF
CC receptors and Ral-GTPases. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Potential). Interacts with RAB11FIP2. Interacts
CC with RALBP1, CRK and GRB2. Binding to RALBP1 does not affect its Ral-
CC binding activity. Forms a complex with the SH3 domains of CRK and GRB2
CC which may link it to an EGF-responsive tyrosine kinase (By similarity).
CC Interacts with AMPH, ITSN1 (via SH3 domains) and SGIP1; may be involved
CC in clathrin-mediated endocytosis. {ECO:0000250,
CC ECO:0000269|PubMed:12364336, ECO:0000269|PubMed:20946875, ECO:0000305}.
CC -!- INTERACTION:
CC Q96D71; P49757: NUMB; NbExp=3; IntAct=EBI-1171195, EBI-915016;
CC Q96D71; Q15311: RALBP1; NbExp=4; IntAct=EBI-1171195, EBI-749285;
CC Q96D71; Q9QZS3-1: Numb; Xeno; NbExp=3; IntAct=EBI-1171195, EBI-9547433;
CC Q96D71; Q9QZS3-2: Numb; Xeno; NbExp=2; IntAct=EBI-1171195, EBI-3896014;
CC Q96D71-2; Q9UL33: TRAPPC2L; NbExp=3; IntAct=EBI-10284498, EBI-747601;
CC Q96D71-3; Q9UL33: TRAPPC2L; NbExp=3; IntAct=EBI-10284512, EBI-747601;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:20946875}. Note=Colocalize with ITSN1 at the plasma
CC membrane in structures that are most probably clathrin-coated pits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96D71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96D71-2; Sequence=VSP_007953, VSP_007954;
CC Name=3;
CC IsoId=Q96D71-3; Sequence=VSP_007955;
CC Name=4;
CC IsoId=Q96D71-4; Sequence=VSP_007953;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart and
CC testis. {ECO:0000269|PubMed:11750063}.
CC -!- PTM: EGF stimulates phosphorylation on Tyr-residues. {ECO:0000250}.
CC -!- DISEASE: Neurodegeneration with brain iron accumulation 7 (NBIA7)
CC [MIM:617916]: A neurodegenerative disorder associated with iron
CC accumulation, primarily in the basal ganglia. Clinical features include
CC speech and motor delay, truncal hypotonia, progressive cerebellar
CC ataxia, and loss of ambulation. NBIA7 transmission pattern is
CC consistent with autosomal recessive inheritance.
CC {ECO:0000269|PubMed:29395073}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12764.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21211.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK34942.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL121834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47904.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47906.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47907.1; -; Genomic_DNA.
DR EMBL; BC012764; AAH12764.1; ALT_INIT; mRNA.
DR EMBL; BC021211; AAH21211.1; ALT_INIT; mRNA.
DR EMBL; DB263697; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF251052; AAK34942.1; ALT_INIT; mRNA.
DR EMBL; AL832307; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL831900; CAD38569.1; -; mRNA.
DR CCDS; CCDS47488.1; -. [Q96D71-4]
DR CCDS; CCDS5193.2; -. [Q96D71-3]
DR CCDS; CCDS69212.1; -. [Q96D71-2]
DR CCDS; CCDS69213.1; -. [Q96D71-1]
DR RefSeq; NP_001122089.1; NM_001128617.2. [Q96D71-4]
DR RefSeq; NP_001273540.1; NM_001286611.1. [Q96D71-1]
DR RefSeq; NP_001273541.1; NM_001286612.1. [Q96D71-2]
DR RefSeq; NP_114128.3; NM_031922.4. [Q96D71-3]
DR AlphaFoldDB; Q96D71; -.
DR BMRB; Q96D71; -.
DR SMR; Q96D71; -.
DR BioGRID; 124433; 68.
DR IntAct; Q96D71; 44.
DR MINT; Q96D71; -.
DR STRING; 9606.ENSP00000392065; -.
DR GlyGen; Q96D71; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q96D71; -.
DR PhosphoSitePlus; Q96D71; -.
DR BioMuta; REPS1; -.
DR DMDM; 262527572; -.
DR EPD; Q96D71; -.
DR jPOST; Q96D71; -.
DR MassIVE; Q96D71; -.
DR MaxQB; Q96D71; -.
DR PaxDb; Q96D71; -.
DR PeptideAtlas; Q96D71; -.
DR PRIDE; Q96D71; -.
DR ProteomicsDB; 76256; -. [Q96D71-1]
DR ProteomicsDB; 76257; -. [Q96D71-2]
DR ProteomicsDB; 76258; -. [Q96D71-3]
DR Antibodypedia; 33064; 119 antibodies from 25 providers.
DR DNASU; 85021; -.
DR Ensembl; ENST00000258062.9; ENSP00000258062.5; ENSG00000135597.19. [Q96D71-3]
DR Ensembl; ENST00000367663.8; ENSP00000356635.4; ENSG00000135597.19. [Q96D71-4]
DR Ensembl; ENST00000409812.6; ENSP00000386699.2; ENSG00000135597.19. [Q96D71-2]
DR Ensembl; ENST00000450536.7; ENSP00000392065.2; ENSG00000135597.19. [Q96D71-1]
DR GeneID; 85021; -.
DR KEGG; hsa:85021; -.
DR MANE-Select; ENST00000450536.7; ENSP00000392065.2; NM_001286611.2; NP_001273540.1.
DR UCSC; uc003qig.6; human. [Q96D71-1]
DR CTD; 85021; -.
DR DisGeNET; 85021; -.
DR GeneCards; REPS1; -.
DR HGNC; HGNC:15578; REPS1.
DR HPA; ENSG00000135597; Low tissue specificity.
DR MalaCards; REPS1; -.
DR MIM; 614825; gene.
DR MIM; 617916; phenotype.
DR neXtProt; NX_Q96D71; -.
DR OpenTargets; ENSG00000135597; -.
DR PharmGKB; PA34329; -.
DR VEuPathDB; HostDB:ENSG00000135597; -.
DR eggNOG; KOG1955; Eukaryota.
DR GeneTree; ENSGT00940000158749; -.
DR InParanoid; Q96D71; -.
DR OMA; QCCDVEN; -.
DR PhylomeDB; Q96D71; -.
DR TreeFam; TF316546; -.
DR PathwayCommons; Q96D71; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q96D71; -.
DR BioGRID-ORCS; 85021; 26 hits in 1074 CRISPR screens.
DR ChiTaRS; REPS1; human.
DR GeneWiki; REPS1; -.
DR GenomeRNAi; 85021; -.
DR Pharos; Q96D71; Tbio.
DR PRO; PR:Q96D71; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96D71; protein.
DR Bgee; ENSG00000135597; Expressed in ventricular zone and 172 other tissues.
DR ExpressionAtlas; Q96D71; baseline and differential.
DR Genevisible; Q96D71; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR026814; Reps1.
DR PANTHER; PTHR11216:SF63; PTHR11216:SF63; 1.
DR Pfam; PF12763; EF-hand_4; 1.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coated pit; Coiled coil; Disease variant;
KW Membrane; Metal-binding; Neurodegeneration; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..796
FT /note="RalBP1-associated Eps domain-containing protein 1"
FT /id="PRO_0000073829"
FT DOMAIN 10..113
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 285..374
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 318..353
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 105..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..796
FT /note="Interaction with RALBP1"
FT /evidence="ECO:0000250"
FT COILED 751..791
FT /evidence="ECO:0000255"
FT COMPBIAS 108..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 544
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O54916"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 420..446
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_007953"
FT VAR_SEQ 510..573
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007954"
FT VAR_SEQ 510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007955"
FT VARIANT 78
FT /note="V -> L (in NBIA7; primary fibroblasts from patients,
FT who are compound heterozygous with E-113, show much higher
FT intracellular iron content than fibroblasts from control
FT individuals and abnormally elevated levels of transferrin
FT receptor 1/TFRC at the cell surface; dbSNP:rs1554292444)"
FT /evidence="ECO:0000269|PubMed:29395073"
FT /id="VAR_080634"
FT VARIANT 113
FT /note="A -> E (in NBIA7; primary fibroblasts from patients,
FT who are compound heterozygous with L-78, show much higher
FT intracellular iron content than fibroblasts from control
FT individuals and abnormally elevated levels of transferrin
FT receptor 1/TFRC at the cell surface; dbSNP:rs201191394)"
FT /evidence="ECO:0000269|PubMed:29395073"
FT /id="VAR_080635"
FT CONFLICT 628
FT /note="A -> V (in Ref. 5; AAK34942)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="V -> I (in Ref. 6; CAD38569)"
FT /evidence="ECO:0000305"
FT CONFLICT 794..795
FT /note="SH -> FP (in Ref. 3; AAH12764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 86662 MW; FAD7A57ED6206922 CRC64;
MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL QIMELCGATR
LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR FVASKNEQES RHAASYSSDS
ENQGSYSGVI PPPPGRGQVK KGSVSHDTVQ PRTSADAQEP ASPVVSPQQS PPTSPHTWRK
HSRHPSGGNS ERPLAGPGPF WSPFGEAQSG SSAGDAVWSG HSPPPPQENW VSFADTPPTS
TLLTMHPASV QDQTTVRTVA SATTAIEIRR QSSSYDDPWK ITDEQRQYYV NQFKTIQPDL
NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV VARKNGYDLP
EKLPESLMPK LIDLEDSADV GDQPGEVGYS GSPAEAPPSK SPSMPSLNQT WPELNQSSEQ
WETFSERSSS SQTLTQFDSN IAPADPDTAI VHPVPIRMTP SKIHMQEMEL KRTGSDHTNP
TSPLLVKPSD LLEENKINSS VKFASGNTVA DGYSSSDSFT SDPEQIGSNV TRQRSHSGTS
PDNTAPPPPP PRPQPSHSRS SSLDMNRTFT VTTGQQQAGV VAHPPAVPPR PQPSQAPGPA
VHRPVDADGL ITHTSTSPQQ IPEQPNFADF SQFEVFAASN VNDEQDDEAE KHPEVLPAEK
ASDPASSLRV AKTDSKTEEK TAASAPANVS KGTTPLAPPP KPVRRRLKSE DELRPEVDEH
TQKTGVLAAV LASQPSIPRS VGKDKKAIQA SIRRNKETNT VLARLNSELQ QQLKDVLEER
ISLEVQLEQL RPFSHL
