LOCUS       NP_001273540             796 aa            linear   PRI 21-SEP-2024
DEFINITION  ralBP1-associated Eps domain-containing protein 1 isoform c [Homo
            sapiens].
ACCESSION   NP_001273540 XP_005267233
VERSION     NP_001273540.1
DBSOURCE    REFSEQ: accession NM_001286611.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Kim,S.H., Cho,J.H., Park,B.O., Park,B.C., Kim,J.H., Park,S.G. and
            Kim,S.
  TITLE     Phosphorylation of REPS1 at Ser709 by RSK attenuates the recycling
            of transferrin receptor
  JOURNAL   BMB Rep 54 (5), 272-277 (2021)
   PUBMED   33407999
  REMARK    GeneRIF: Phosphorylation of REPS1 at Ser709 by RSK attenuates the
            recycling of transferrin receptor.
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Muller,P.M., Rademacher,J., Bagshaw,R.D., Wortmann,C., Barth,C.,
            van Unen,J., Alp,K.M., Giudice,G., Eccles,R.L., Heinrich,L.E.,
            Pascual-Vargas,P., Sanchez-Castro,M., Brandenburg,L., Mbamalu,G.,
            Tucholska,M., Spatt,L., Czajkowski,M.T., Welke,R.W., Zhang,S.,
            Nguyen,V., Rrustemi,T., Trnka,P., Freitag,K., Larsen,B., Popp,O.,
            Mertins,P., Gingras,A.C., Roth,F.P., Colwill,K., Bakal,C.,
            Pertz,O., Pawson,T., Petsalaki,E. and Rocks,O.
  TITLE     Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals
            spatially organized RAC1 signalling from integrin adhesions
  JOURNAL   Nat Cell Biol 22 (4), 498-511 (2020)
   PUBMED   32203420
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Cullis,D.N., Philip,B., Baleja,J.D. and Feig,L.A.
  TITLE     Rab11-FIP2, an adaptor protein connecting cellular components
            involved in internalization and recycling of epidermal growth
            factor receptors
  JOURNAL   J Biol Chem 277 (51), 49158-49166 (2002)
   PUBMED   12364336
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Xu,J., Zhou,Z., Zeng,L., Huang,Y., Zhao,W., Cheng,C., Xu,M., Xie,Y.
            and Mao,Y.
  TITLE     Cloning, expression and characterization of a novel human REPS1
            gene
  JOURNAL   Biochim Biophys Acta 1522 (2), 118-121 (2001)
   PUBMED   11750063
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Ikeda,M., Ishida,O., Hinoi,T., Kishida,S. and Kikuchi,A.
  TITLE     Identification and characterization of a novel protein interacting
            with Ral-binding protein 1, a putative effector protein of Ral
  JOURNAL   J Biol Chem 273 (2), 814-821 (1998)
   PUBMED   9422736
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Yamaguchi,A., Urano,T., Goi,T. and Feig,L.A.
  TITLE     An Eps homology (EH) domain protein that binds to the Ral-GTPase
            target, RalBP1
  JOURNAL   J Biol Chem 272 (50), 31230-31234 (1997)
   PUBMED   9395447
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Cantor,S.B., Urano,T. and Feig,L.A.
  TITLE     Identification and characterization of Ral-binding protein 1, a
            potential downstream target of Ral GTPases
  JOURNAL   Mol Cell Biol 15 (8), 4578-4584 (1995)
   PUBMED   7623849
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012764.2, AF251052.1,
            AK312938.1, CA424106.1, AA025663.1, AA653442.1, R51073.1 and
            AL121834.20.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 8, 2013 this sequence version replaced XP_005267233.1.
            
            SUMMARY: This gene encodes a signaling adaptor protein with two EH
            domains that interacts with proteins that participate in signaling,
            endocytosis and cytoskeletal changes. The encoded protein has been
            found in association with intersectin 1 and Src homology 3-domain
            growth factor receptor-bound 2-like (endophilin) interacting
            protein 1 when intersectin 1 was isolated from clathrin-coated
            pits. The encoded protein has also been shown to interact with
            amphiphysin, a cytoplasmic protein at the surface of synaptic
            vesicles. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Mar
            2014].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2257912.1, AF251052.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000450536.7/ ENSP00000392065.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.1"
     Protein         1..796
                     /product="ralBP1-associated Eps domain-containing protein
                     1 isoform c"
                     /note="ralBP1-interacting protein 1"
                     /calculated_mol_wt=86531
     Region          6..85
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <97..228
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          105..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Region          278..369
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Region          377..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Region          506..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O54916; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Region          638..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D71.3)"
     Region          652..796
                     /region_name="Interaction with RALBP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96D71.3)"
     CDS             1..796
                     /gene="REPS1"
                     /gene_synonym="NBIA7; RALBP1"
                     /coded_by="NM_001286611.2:572..2962"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS69213.1"
                     /db_xref="GeneID:85021"
                     /db_xref="HGNC:HGNC:15578"
                     /db_xref="MIM:614825"
ORIGIN      
        1 megltlsdae qkyysdlfsy cdiestkkvv vngrvlelfr aaqlpndvvl qimelcgatr
       61 lgyfgrsqfy ialklvavaq sgfplrvesi ntvkdlplpr fvaskneqes rhaasyssds
      121 enqgsysgvi ppppgrgqvk kgsvshdtvq prtsadaqep aspvvspqqs pptsphtwrk
      181 hsrhpsggns erplagpgpf wspfgeaqsg ssagdavwsg hsppppqenw vsfadtppts
      241 tlltmhpasv qdqttvrtva sattaieirr qsssyddpwk itdeqrqyyv nqfktiqpdl
      301 ngfipgsaak efftksklpi lelshiwels dfdkdgaltl defcaafhlv varkngydlp
      361 eklpeslmpk lidledsadv gdqpgevgys gspaeappsk spsmpslnqt wpelnqsseq
      421 wetfsersss sqtltqfdsn iapadpdtai vhpvpirmtp skihmqemel krtgsdhtnp
      481 tspllvkpsd lleenkinss vkfasgntva dgysssdsft sdpeqigsnv trqrshsgts
      541 pdntappppp prpqpshsrs ssldmnrtft vttgqqqagv vahppavppr pqpsqapgpa
      601 vhrpvdadgl ithtstspqq ipeqpnfadf sqfevfaasn vndeqddeae khpevlpaek
      661 asdpasslrv aktdskteek taasapanvs kgttplappp kpvrrrlkse delrpevdeh
      721 tqktgvlaav lasqpsiprs vgkdkkaiqa sirrnketnt vlarlnselq qqlkdvleer
      781 islevqleql rpfshl
//
