Full text data of REPS1
REPS1
[Confidence: low (only semi-automatic identification from reviews)]
RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1)
RalBP1-associated Eps domain-containing protein 1 (RalBP1-interacting protein 1)
UniProt
Q96D71
ID REPS1_HUMAN Reviewed; 796 AA.
AC Q96D71; B7ZBZ8; B7ZBZ9; B7ZC00; Q5JWJ5; Q5JWJ6; Q5JWJ7; Q8NDR7;
read moreAC Q8WU62; Q9BXY9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 116.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-796 (ISOFORM 1), AND TISSUE
RP 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
RT gene.";
RL Biochim. Biophys. Acta 1522:118-121(2001).
RN [6]
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT involved in internalization and recycling of epidermal growth factor
RT receptors.";
RL J. Biol. Chem. 277:49158-49166(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-170, AND
RP MASS SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient 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
RP AND SER-307, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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;
RP SER-174 AND SER-540, AND MASS SPECTROMETRY.
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.,
RA Moreau J., 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
RP SER-740, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP AND SER-709, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May coordinate the cellular actions of activated EGF
CC receptors and Ral-GTPases (By similarity).
CC -!- SUBUNIT: Homodimer (Potential). Interacts with RAB11FIP2.
CC Interacts with RALBP1, CRK and GRB2. Binding to RALBP1 does not
CC affect its Ral-binding activity. Forms a complex with the SH3
CC domains of CRK and GRB2 which may link it to an EGF-responsive
CC tyrosine kinase (By similarity). Interacts with AMPH, ITSN1 (via
CC SH3 domains) and SGIP1; may be involved in clathrin-mediated
CC endocytosis.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit.
CC Note=Colocalize with ITSN1 at the plasma membrane in structures
CC that are most probably clathrin-coated pits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart
CC and testis.
CC -!- PTM: EGF stimulates phosphorylation on Tyr-residues (By
CC similarity).
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- SIMILARITY: Contains 2 EH domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12764.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH21211.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAK34942.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AL121834; CAI42877.2; -; Genomic_DNA.
DR EMBL; AL590308; CAI42877.2; JOINED; Genomic_DNA.
DR EMBL; AL121834; CAI42878.2; -; Genomic_DNA.
DR EMBL; AL590308; CAI42878.2; JOINED; Genomic_DNA.
DR EMBL; AL121834; CAI42879.2; -; Genomic_DNA.
DR EMBL; AL590308; CAI42879.2; JOINED; Genomic_DNA.
DR EMBL; AL590308; CAX15096.1; -; Genomic_DNA.
DR EMBL; AL121834; CAX15096.1; JOINED; Genomic_DNA.
DR EMBL; AL590308; CAX15097.1; -; Genomic_DNA.
DR EMBL; AL121834; CAX15097.1; JOINED; Genomic_DNA.
DR EMBL; AL590308; CAX15098.1; -; Genomic_DNA.
DR EMBL; AL121834; CAX15098.1; JOINED; 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; AL831900; CAD38569.1; -; mRNA.
DR RefSeq; NP_001122089.1; NM_001128617.2.
DR RefSeq; NP_001273540.1; NM_001286611.1.
DR RefSeq; NP_001273541.1; NM_001286612.1.
DR RefSeq; NP_114128.3; NM_031922.4.
DR UniGene; Hs.334603; -.
DR ProteinModelPortal; Q96D71; -.
DR SMR; Q96D71; 279-370.
DR IntAct; Q96D71; 11.
DR STRING; 9606.ENSP00000258062; -.
DR PhosphoSite; Q96D71; -.
DR DMDM; 262527572; -.
DR PaxDb; Q96D71; -.
DR PRIDE; Q96D71; -.
DR DNASU; 85021; -.
DR Ensembl; ENST00000258062; ENSP00000258062; ENSG00000135597.
DR Ensembl; ENST00000409812; ENSP00000386699; ENSG00000135597.
DR Ensembl; ENST00000450536; ENSP00000392065; ENSG00000135597.
DR GeneID; 85021; -.
DR KEGG; hsa:85021; -.
DR UCSC; uc003qii.3; human.
DR CTD; 85021; -.
DR GeneCards; GC06M139267; -.
DR HGNC; HGNC:15578; REPS1.
DR HPA; HPA029961; -.
DR MIM; 614825; gene.
DR neXtProt; NX_Q96D71; -.
DR PharmGKB; PA34329; -.
DR eggNOG; NOG313227; -.
DR HOVERGEN; HBG056372; -.
DR InParanoid; Q96D71; -.
DR OMA; EQKYYSD; -.
DR OrthoDB; EOG7B31MB; -.
DR ChiTaRS; REPS1; human.
DR GeneWiki; REPS1; -.
DR GenomeRNAi; 85021; -.
DR NextBio; 75659; -.
DR PMAP-CutDB; Q96D71; -.
DR PRO; PR:Q96D71; -.
DR ArrayExpress; Q96D71; -.
DR Bgee; Q96D71; -.
DR CleanEx; HS_REPS1; -.
DR Genevestigator; Q96D71; -.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EPS15_homology.
DR InterPro; IPR026814; Reps.
DR PANTHER; PTHR11216:SF33; PTHR11216:SF33; 1.
DR SMART; SM00027; EH; 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;
KW Complete proteome; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1 796 RalBP1-associated Eps domain-containing
FT protein 1.
FT /FTId=PRO_0000073829.
FT DOMAIN 10 113 EH 1.
FT DOMAIN 285 374 EH 2.
FT DOMAIN 318 353 EF-hand.
FT CA_BIND 331 342 Potential.
FT REGION 652 796 Interaction with RALBP1 (By similarity).
FT COILED 751 791 Potential.
FT COMPBIAS 541 604 Pro-rich.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 145 145 Phosphoserine.
FT MOD_RES 162 162 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 170 170 Phosphoserine.
FT MOD_RES 173 173 Phosphothreonine.
FT MOD_RES 174 174 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine (By similarity).
FT MOD_RES 288 288 Phosphotyrosine (Potential).
FT MOD_RES 307 307 Phosphoserine.
FT MOD_RES 489 489 Phosphoserine.
FT MOD_RES 540 540 Phosphoserine.
FT MOD_RES 562 562 Phosphoserine.
FT MOD_RES 709 709 Phosphoserine.
FT MOD_RES 740 740 Phosphoserine.
FT VAR_SEQ 420 446 Missing (in isoform 2).
FT /FTId=VSP_007953.
FT VAR_SEQ 510 573 Missing (in isoform 2).
FT /FTId=VSP_007954.
FT VAR_SEQ 510 510 Missing (in isoform 3).
FT /FTId=VSP_007955.
FT CONFLICT 628 628 A -> V (in Ref. 5; AAK34942).
FT CONFLICT 717 717 V -> I (in Ref. 6; CAD38569).
FT CONFLICT 794 795 SH -> FP (in Ref. 3; AAH12764).
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
//
ID REPS1_HUMAN Reviewed; 796 AA.
AC Q96D71; B7ZBZ8; B7ZBZ9; B7ZC00; Q5JWJ5; Q5JWJ6; Q5JWJ7; Q8NDR7;
read moreAC Q8WU62; Q9BXY9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 116.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-796 (ISOFORM 1), AND TISSUE
RP 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
RT gene.";
RL Biochim. Biophys. Acta 1522:118-121(2001).
RN [6]
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT involved in internalization and recycling of epidermal growth factor
RT receptors.";
RL J. Biol. Chem. 277:49158-49166(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-170, AND
RP MASS SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient 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
RP AND SER-307, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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;
RP SER-174 AND SER-540, AND MASS SPECTROMETRY.
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.,
RA Moreau J., 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
RP SER-740, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP AND SER-709, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May coordinate the cellular actions of activated EGF
CC receptors and Ral-GTPases (By similarity).
CC -!- SUBUNIT: Homodimer (Potential). Interacts with RAB11FIP2.
CC Interacts with RALBP1, CRK and GRB2. Binding to RALBP1 does not
CC affect its Ral-binding activity. Forms a complex with the SH3
CC domains of CRK and GRB2 which may link it to an EGF-responsive
CC tyrosine kinase (By similarity). Interacts with AMPH, ITSN1 (via
CC SH3 domains) and SGIP1; may be involved in clathrin-mediated
CC endocytosis.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit.
CC Note=Colocalize with ITSN1 at the plasma membrane in structures
CC that are most probably clathrin-coated pits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart
CC and testis.
CC -!- PTM: EGF stimulates phosphorylation on Tyr-residues (By
CC similarity).
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- SIMILARITY: Contains 2 EH domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12764.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH21211.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAK34942.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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DR EMBL; AL121834; CAI42877.2; -; Genomic_DNA.
DR EMBL; AL590308; CAI42877.2; JOINED; Genomic_DNA.
DR EMBL; AL121834; CAI42878.2; -; Genomic_DNA.
DR EMBL; AL590308; CAI42878.2; JOINED; Genomic_DNA.
DR EMBL; AL121834; CAI42879.2; -; Genomic_DNA.
DR EMBL; AL590308; CAI42879.2; JOINED; Genomic_DNA.
DR EMBL; AL590308; CAX15096.1; -; Genomic_DNA.
DR EMBL; AL121834; CAX15096.1; JOINED; Genomic_DNA.
DR EMBL; AL590308; CAX15097.1; -; Genomic_DNA.
DR EMBL; AL121834; CAX15097.1; JOINED; Genomic_DNA.
DR EMBL; AL590308; CAX15098.1; -; Genomic_DNA.
DR EMBL; AL121834; CAX15098.1; JOINED; 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; AL831900; CAD38569.1; -; mRNA.
DR RefSeq; NP_001122089.1; NM_001128617.2.
DR RefSeq; NP_001273540.1; NM_001286611.1.
DR RefSeq; NP_001273541.1; NM_001286612.1.
DR RefSeq; NP_114128.3; NM_031922.4.
DR UniGene; Hs.334603; -.
DR ProteinModelPortal; Q96D71; -.
DR SMR; Q96D71; 279-370.
DR IntAct; Q96D71; 11.
DR STRING; 9606.ENSP00000258062; -.
DR PhosphoSite; Q96D71; -.
DR DMDM; 262527572; -.
DR PaxDb; Q96D71; -.
DR PRIDE; Q96D71; -.
DR DNASU; 85021; -.
DR Ensembl; ENST00000258062; ENSP00000258062; ENSG00000135597.
DR Ensembl; ENST00000409812; ENSP00000386699; ENSG00000135597.
DR Ensembl; ENST00000450536; ENSP00000392065; ENSG00000135597.
DR GeneID; 85021; -.
DR KEGG; hsa:85021; -.
DR UCSC; uc003qii.3; human.
DR CTD; 85021; -.
DR GeneCards; GC06M139267; -.
DR HGNC; HGNC:15578; REPS1.
DR HPA; HPA029961; -.
DR MIM; 614825; gene.
DR neXtProt; NX_Q96D71; -.
DR PharmGKB; PA34329; -.
DR eggNOG; NOG313227; -.
DR HOVERGEN; HBG056372; -.
DR InParanoid; Q96D71; -.
DR OMA; EQKYYSD; -.
DR OrthoDB; EOG7B31MB; -.
DR ChiTaRS; REPS1; human.
DR GeneWiki; REPS1; -.
DR GenomeRNAi; 85021; -.
DR NextBio; 75659; -.
DR PMAP-CutDB; Q96D71; -.
DR PRO; PR:Q96D71; -.
DR ArrayExpress; Q96D71; -.
DR Bgee; Q96D71; -.
DR CleanEx; HS_REPS1; -.
DR Genevestigator; Q96D71; -.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EPS15_homology.
DR InterPro; IPR026814; Reps.
DR PANTHER; PTHR11216:SF33; PTHR11216:SF33; 1.
DR SMART; SM00027; EH; 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;
KW Complete proteome; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1 796 RalBP1-associated Eps domain-containing
FT protein 1.
FT /FTId=PRO_0000073829.
FT DOMAIN 10 113 EH 1.
FT DOMAIN 285 374 EH 2.
FT DOMAIN 318 353 EF-hand.
FT CA_BIND 331 342 Potential.
FT REGION 652 796 Interaction with RALBP1 (By similarity).
FT COILED 751 791 Potential.
FT COMPBIAS 541 604 Pro-rich.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 145 145 Phosphoserine.
FT MOD_RES 162 162 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 170 170 Phosphoserine.
FT MOD_RES 173 173 Phosphothreonine.
FT MOD_RES 174 174 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine (By similarity).
FT MOD_RES 288 288 Phosphotyrosine (Potential).
FT MOD_RES 307 307 Phosphoserine.
FT MOD_RES 489 489 Phosphoserine.
FT MOD_RES 540 540 Phosphoserine.
FT MOD_RES 562 562 Phosphoserine.
FT MOD_RES 709 709 Phosphoserine.
FT MOD_RES 740 740 Phosphoserine.
FT VAR_SEQ 420 446 Missing (in isoform 2).
FT /FTId=VSP_007953.
FT VAR_SEQ 510 573 Missing (in isoform 2).
FT /FTId=VSP_007954.
FT VAR_SEQ 510 510 Missing (in isoform 3).
FT /FTId=VSP_007955.
FT CONFLICT 628 628 A -> V (in Ref. 5; AAK34942).
FT CONFLICT 717 717 V -> I (in Ref. 6; CAD38569).
FT CONFLICT 794 795 SH -> FP (in Ref. 3; AAH12764).
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
//
MIM
614825
*RECORD*
*FIELD* NO
614825
*FIELD* TI
*614825 RALBP1-ASSOCIATED EPS DOMAIN-CONTAINING PROTEIN 1; REPS1
*FIELD* TX
CLONING
read more
By large-scale sequencing of clones obtained from a human fetal brain
cDNA library, followed by database analysis, Xu et al. (2001) identified
the human ortholog of mouse Reps1. The deduced 744-amino acid REPS1
protein has a calculated molecular mass of 85 kD. It has a central EPS15
(600051) homology (EH) domain containing 2 EF hand motifs, followed by 2
proline-rich motifs. Mouse and human REPS1 share 83% amino acid
identity. Northern blot analysis detected variable expression of an
approximately 2.8-kb REPS1 transcript in all 16 human tissues examined,
with highest expression in heart and testis.
Cullis et al. (2002) showed that fluorescence-tagged mouse Reps1
colocalized with rat Rab11fip2 (608599) at recycling endosomes in the
perinuclear region of transfected NIH3T3 cells.
GENE FUNCTION
By yeast 2-hybrid and mutation analyses, Cullis et al. (2002) showed
that the isolated EH domain of mouse Reps1 interacted with the NPF
motifs of rat Rab11fip2. These 2 proteins appeared to function together
in inhibiting the recycling of Egf receptors (EGFR; 131550), but not
transferrin receptors (TFRC; 190010). Both Reps1 and Rab11fip2 also
coprecipitated with the alpha-adaptin (AP2A1; 601026) subunit of the
major clathrin adaptor complex AP2.
GENE STRUCTURE
Xu et al. (2001) determined that the REPS1 gene contains 20 exons and
spans over 44 kb.
MAPPING
By genomic sequence analysis, Xu et al. (2001) mapped the REPS1 gene to
chromosome 6q23.1-q24.1.
*FIELD* RF
1. Cullis, D. N.; Philip, B.; Baleja, J. D.; Feig, L. A.: Rab11-FIP2,
an adaptor protein connecting cellular components involved in internalization
and recycling of epidermal growth factor receptors. J. Biol. Chem. 277:
49158-49166, 2002.
2. Xu, J.; Zhou, Z.; Zeng, L.; Huang, Y.; Zhao, W.; Cheng, C.; Xu,
M.; Xie, Y.; Mao, Y.: Cloning, expression and characterization of
a novel human REPS1 gene. Biochim. Biophys. Acta 1522: 118-121,
2001.
*FIELD* CD
Patricia A. Hartz: 9/17/2012
*FIELD* ED
mgross: 09/17/2012
*RECORD*
*FIELD* NO
614825
*FIELD* TI
*614825 RALBP1-ASSOCIATED EPS DOMAIN-CONTAINING PROTEIN 1; REPS1
*FIELD* TX
CLONING
read more
By large-scale sequencing of clones obtained from a human fetal brain
cDNA library, followed by database analysis, Xu et al. (2001) identified
the human ortholog of mouse Reps1. The deduced 744-amino acid REPS1
protein has a calculated molecular mass of 85 kD. It has a central EPS15
(600051) homology (EH) domain containing 2 EF hand motifs, followed by 2
proline-rich motifs. Mouse and human REPS1 share 83% amino acid
identity. Northern blot analysis detected variable expression of an
approximately 2.8-kb REPS1 transcript in all 16 human tissues examined,
with highest expression in heart and testis.
Cullis et al. (2002) showed that fluorescence-tagged mouse Reps1
colocalized with rat Rab11fip2 (608599) at recycling endosomes in the
perinuclear region of transfected NIH3T3 cells.
GENE FUNCTION
By yeast 2-hybrid and mutation analyses, Cullis et al. (2002) showed
that the isolated EH domain of mouse Reps1 interacted with the NPF
motifs of rat Rab11fip2. These 2 proteins appeared to function together
in inhibiting the recycling of Egf receptors (EGFR; 131550), but not
transferrin receptors (TFRC; 190010). Both Reps1 and Rab11fip2 also
coprecipitated with the alpha-adaptin (AP2A1; 601026) subunit of the
major clathrin adaptor complex AP2.
GENE STRUCTURE
Xu et al. (2001) determined that the REPS1 gene contains 20 exons and
spans over 44 kb.
MAPPING
By genomic sequence analysis, Xu et al. (2001) mapped the REPS1 gene to
chromosome 6q23.1-q24.1.
*FIELD* RF
1. Cullis, D. N.; Philip, B.; Baleja, J. D.; Feig, L. A.: Rab11-FIP2,
an adaptor protein connecting cellular components involved in internalization
and recycling of epidermal growth factor receptors. J. Biol. Chem. 277:
49158-49166, 2002.
2. Xu, J.; Zhou, Z.; Zeng, L.; Huang, Y.; Zhao, W.; Cheng, C.; Xu,
M.; Xie, Y.; Mao, Y.: Cloning, expression and characterization of
a novel human REPS1 gene. Biochim. Biophys. Acta 1522: 118-121,
2001.
*FIELD* CD
Patricia A. Hartz: 9/17/2012
*FIELD* ED
mgross: 09/17/2012