RABE1_HUMAN
ID RABE1_HUMAN Reviewed; 862 AA.
AC Q15276; B2RAG7; O95369; Q8IVX3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Rab GTPase-binding effector protein 1;
DE AltName: Full=Rabaptin-4;
DE AltName: Full=Rabaptin-5;
DE AltName: Full=Rabaptin-5alpha;
DE AltName: Full=Renal carcinoma antigen NY-REN-17;
GN Name=RABEP1; Synonyms=RAB5EP, RABPT5, RABPT5A;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RAB5A.
RC TISSUE=Cervix carcinoma;
RX PubMed=8521472; DOI=10.1016/0092-8674(95)90120-5;
RA Stenmark H., Vitale G., Ulrich O., Zerial M.;
RT "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic
RT membrane fusion.";
RL Cell 83:423-432(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RAB4A AND RAB5A.
RC TISSUE=Cervix carcinoma;
RX PubMed=10698684; DOI=10.1042/bj3460593;
RA Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K.,
RA van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P.;
RT "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to
RT perinuclear recycling vesicles.";
RL Biochem. J. 346:593-601(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP PROTEIN SEQUENCE OF 807-819, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP INTERACTION WITH RABGEF1.
RX PubMed=9323142; DOI=10.1016/s0092-8674(00)80380-3;
RA Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H.,
RA Rybin V., Wilm M., Ashman K., Mann M., Zerial M.;
RT "A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
RT nucleotide exchange to effector recruitment and function.";
RL Cell 90:1149-1159(1997).
RN [7]
RP PROTEOLYTIC CLEAVAGE BY CASPASES IN APOPTOTIC CELLS.
RX PubMed=9321397; DOI=10.1093/emboj/16.20.6182;
RA Cosulich S.C., Horiuchi H., Zerial M., Clarke P.R., Woodman P.G.;
RT "Cleavage of rabaptin-5 blocks endosome fusion during apoptosis.";
RL EMBO J. 16:6182-6191(1997).
RN [8]
RP INTERACTION WITH TSC2.
RX PubMed=9045618; DOI=10.1074/jbc.272.10.6097;
RA Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S.;
RT "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase
RT activating protein (GAP) in modulating endocytosis.";
RL J. Biol. Chem. 272:6097-6100(1997).
RN [9]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH RABGEF1.
RX PubMed=11452015; DOI=10.1091/mbc.12.7.2219;
RA Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M.;
RT "Functional synergy between Rab5 effector Rabaptin-5 and exchange factor
RT Rabex-5 when physically associated in a complex.";
RL Mol. Biol. Cell 12:2219-2228(2001).
RN [11]
RP INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12505986; DOI=10.1093/emboj/cdg015;
RA Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.;
RT "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.";
RL EMBO J. 22:78-88(2003).
RN [12]
RP FUNCTION, INTERACTION WITH RAB4A AND AP1G1, AND SUBCELLULAR LOCATION.
RX PubMed=12773381; DOI=10.1093/emboj/cdg257;
RA Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V.,
RA Klumperman J., Schu P., van der Sluijs P.;
RT "Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-
RT adaptin in membrane recycling from endosomes.";
RL EMBO J. 22:2645-2657(2003).
RN [13]
RP INTERACTION WITH AP1G1; AP1G2; GGA1; GGA2 AND GGA3, AND MUTAGENESIS OF
RP PHE-439; GLY-440; PRO-441 AND LEU-442.
RX PubMed=14665628; DOI=10.1074/jbc.m311873200;
RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.;
RT "Definition of the consensus motif recognized by gamma-adaptin ear
RT domains.";
RL J. Biol. Chem. 279:8018-8028(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, AND
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-282, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [21]
RP INTERACTION WITH RAB4A.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, 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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, AND
RP 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 [25]
RP FUNCTION.
RX PubMed=22841712; DOI=10.1016/j.febslet.2012.07.055;
RA Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.;
RT "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion
RT channel trafficking.";
RL FEBS Lett. 586:3077-3084(2012).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-407 AND SER-410, AND
RP IDENTIFICATION BY MASS 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-407; THR-408 AND
RP SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [29]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 789-862 IN COMPLEX WITH RAB5A,
RP SUBUNIT, AND MUTAGENESIS OF ASP-812; GLU-815; GLN-818; ASP-820; PHE-821;
RP VAL-822; GLN-826 AND GLN-829.
RX PubMed=15378032; DOI=10.1038/nsmb832;
RA Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C.;
RT "Structural basis of Rab5-Rabaptin5 interaction in endocytosis.";
RL Nat. Struct. Mol. Biol. 11:975-983(2004).
CC -!- FUNCTION: Rab effector protein acting as linker between gamma-adaptin,
CC RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane
CC trafficking of recycling endosomes. Involved in KCNH1 channels
CC trafficking to and from the cell membrane (PubMed:22841712). Stimulates
CC RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of
CC PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to
CC the cilium (By similarity). {ECO:0000250|UniProtKB:O35551,
CC ECO:0000269|PubMed:10698684, ECO:0000269|PubMed:11452015,
CC ECO:0000269|PubMed:12773381, ECO:0000269|PubMed:22841712,
CC ECO:0000269|PubMed:8521472}.
CC -!- SUBUNIT: Homodimer when bound to RAB5A (PubMed:15378032). Heterodimer
CC with RABGEF1 (PubMed:11452015, PubMed:9323142). The heterodimer binds
CC RAB4A and RAB5A that have been activated by GTP-binding
CC (PubMed:10698684, PubMed:8521472, PubMed:20098723, PubMed:12773381).
CC Interacts with TSC2 (PubMed:9045618). Interacts with GGA1 (via GAE
CC domain), GGA2 (via GAE domain) and GGA3 (via GAE domain)
CC (PubMed:12505986, PubMed:14665628). Interacts with AP1G1 (via GAE
CC domain) (PubMed:12505986, PubMed:12773381, PubMed:14665628). Interacts
CC with AP1G2 (via GAE domain) (PubMed:12505986, PubMed:14665628).
CC Interacts with ECPAS (PubMed:20682791). Interacts with KCNH1 (By
CC similarity). Interacts with PKD1 (via C-terminal domain) and GGA1; the
CC interactions recruit PKD1:PKD2 complex to GGA1 and ARL3 at trans-Golgi
CC network (By similarity). Interacts with KCNH1 (By similarity).
CC {ECO:0000250|UniProtKB:O35550, ECO:0000250|UniProtKB:O35551,
CC ECO:0000269|PubMed:10698684, ECO:0000269|PubMed:11452015,
CC ECO:0000269|PubMed:12505986, ECO:0000269|PubMed:12773381,
CC ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15378032,
CC ECO:0000269|PubMed:20098723, ECO:0000269|PubMed:20682791,
CC ECO:0000269|PubMed:8521472, ECO:0000269|PubMed:9045618,
CC ECO:0000269|PubMed:9323142}.
CC -!- INTERACTION:
CC Q15276; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-447043, EBI-11096309;
CC Q15276; Q13155: AIMP2; NbExp=3; IntAct=EBI-447043, EBI-745226;
CC Q15276; O43747: AP1G1; NbExp=2; IntAct=EBI-447043, EBI-447609;
CC Q15276; O75843: AP1G2; NbExp=2; IntAct=EBI-447043, EBI-373637;
CC Q15276; Q99728: BARD1; NbExp=3; IntAct=EBI-447043, EBI-473181;
CC Q15276; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-447043, EBI-744556;
CC Q15276; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-447043, EBI-930143;
CC Q15276; Q07002: CDK18; NbExp=3; IntAct=EBI-447043, EBI-746238;
CC Q15276; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-447043, EBI-3919850;
CC Q15276; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-447043, EBI-11752486;
CC Q15276; Q96M91: CFAP53; NbExp=3; IntAct=EBI-447043, EBI-742422;
CC Q15276; Q14241: ELOA; NbExp=3; IntAct=EBI-447043, EBI-742350;
CC Q15276; Q56NI9: ESCO2; NbExp=3; IntAct=EBI-447043, EBI-3951849;
CC Q15276; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-447043, EBI-742802;
CC Q15276; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-447043, EBI-6658203;
CC Q15276; Q9UJY5: GGA1; NbExp=8; IntAct=EBI-447043, EBI-447141;
CC Q15276; Q9UJY4: GGA2; NbExp=7; IntAct=EBI-447043, EBI-447646;
CC Q15276; Q9NZ52: GGA3; NbExp=4; IntAct=EBI-447043, EBI-447404;
CC Q15276; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-447043, EBI-726510;
CC Q15276; Q9NZL9: MAT2B; NbExp=3; IntAct=EBI-447043, EBI-10317491;
CC Q15276; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-447043, EBI-348259;
CC Q15276; A5D8V7: ODAD3; NbExp=3; IntAct=EBI-447043, EBI-8466445;
CC Q15276; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-447043, EBI-448407;
CC Q15276; Q99959-2: PKP2; NbExp=3; IntAct=EBI-447043, EBI-10987518;
CC Q15276; O43395: PRPF3; NbExp=3; IntAct=EBI-447043, EBI-744322;
CC Q15276; P20338: RAB4A; NbExp=3; IntAct=EBI-447043, EBI-722284;
CC Q15276; P61018: RAB4B; NbExp=3; IntAct=EBI-447043, EBI-10218066;
CC Q15276; Q9UJ41-2: RABGEF1; NbExp=2; IntAct=EBI-447043, EBI-6448458;
CC Q15276; Q9H2S5: RNF39; NbExp=3; IntAct=EBI-447043, EBI-12235180;
CC Q15276; Q13573: SNW1; NbExp=3; IntAct=EBI-447043, EBI-632715;
CC Q15276; P49675: STAR; NbExp=3; IntAct=EBI-447043, EBI-722932;
CC Q15276; Q8IZW8: TNS4; NbExp=3; IntAct=EBI-447043, EBI-7543499;
CC Q15276; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-447043, EBI-11119202;
CC Q15276; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-447043, EBI-10687282;
CC Q15276; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-447043, EBI-17208936;
CC Q15276; O75604: USP2; NbExp=3; IntAct=EBI-447043, EBI-743272;
CC Q15276; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-447043, EBI-11737646;
CC Q15276; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-447043, EBI-712969;
CC Q15276; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-447043, EBI-11962468;
CC Q15276; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-447043, EBI-1049952;
CC Q15276; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-447043, EBI-10251462;
CC Q15276; P68590: yscH; Xeno; NbExp=2; IntAct=EBI-447043, EBI-2845098;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Recycling endosome.
CC Cytoplasmic vesicle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Rabaptin-5;
CC IsoId=Q15276-1; Sequence=Displayed;
CC Name=2; Synonyms=Rabaptin-4;
CC IsoId=Q15276-2; Sequence=VSP_010451;
CC -!- PTM: Proteolytic cleavage by caspases in apoptotic cells causes loss of
CC endosome fusion activity. {ECO:0000269|PubMed:9321397}.
CC -!- SIMILARITY: Belongs to the rabaptin family. {ECO:0000305}.
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DR EMBL; X91141; CAA62580.1; -; mRNA.
DR EMBL; AF098638; AAC70781.1; -; mRNA.
DR EMBL; AK314183; BAG36864.1; -; mRNA.
DR EMBL; BC041700; AAH41700.1; -; mRNA.
DR CCDS; CCDS42243.1; -. [Q15276-2]
DR CCDS; CCDS45592.1; -. [Q15276-1]
DR RefSeq; NP_001077054.1; NM_001083585.2. [Q15276-2]
DR RefSeq; NP_001278510.1; NM_001291581.1.
DR RefSeq; NP_004694.2; NM_004703.5. [Q15276-1]
DR PDB; 1P4U; X-ray; 2.20 A; B=435-447.
DR PDB; 1TU3; X-ray; 2.31 A; F/G/H/I/J=789-862.
DR PDB; 1X79; X-ray; 2.41 A; B/C=551-661.
DR PDB; 4N3Y; X-ray; 2.20 A; B/C=552-642.
DR PDB; 4N3Z; X-ray; 3.10 A; B/C=552-642.
DR PDB; 4Q9U; X-ray; 4.62 A; C/D/G/H=552-642.
DR PDBsum; 1P4U; -.
DR PDBsum; 1TU3; -.
DR PDBsum; 1X79; -.
DR PDBsum; 4N3Y; -.
DR PDBsum; 4N3Z; -.
DR PDBsum; 4Q9U; -.
DR AlphaFoldDB; Q15276; -.
DR SMR; Q15276; -.
DR BioGRID; 114583; 175.
DR CORUM; Q15276; -.
DR DIP; DIP-29350N; -.
DR IntAct; Q15276; 79.
DR MINT; Q15276; -.
DR STRING; 9606.ENSP00000445408; -.
DR iPTMnet; Q15276; -.
DR MetOSite; Q15276; -.
DR PhosphoSitePlus; Q15276; -.
DR BioMuta; RABEP1; -.
DR DMDM; 116242743; -.
DR EPD; Q15276; -.
DR jPOST; Q15276; -.
DR MassIVE; Q15276; -.
DR MaxQB; Q15276; -.
DR PaxDb; Q15276; -.
DR PeptideAtlas; Q15276; -.
DR PRIDE; Q15276; -.
DR ProteomicsDB; 60509; -. [Q15276-1]
DR ProteomicsDB; 60510; -. [Q15276-2]
DR Antibodypedia; 3875; 123 antibodies from 27 providers.
DR DNASU; 9135; -.
DR Ensembl; ENST00000341923.10; ENSP00000339569.6; ENSG00000029725.17. [Q15276-2]
DR Ensembl; ENST00000537505.6; ENSP00000445408.2; ENSG00000029725.17. [Q15276-1]
DR GeneID; 9135; -.
DR KEGG; hsa:9135; -.
DR MANE-Select; ENST00000537505.6; ENSP00000445408.2; NM_004703.6; NP_004694.2.
DR UCSC; uc032ery.2; human. [Q15276-1]
DR CTD; 9135; -.
DR DisGeNET; 9135; -.
DR GeneCards; RABEP1; -.
DR HGNC; HGNC:17677; RABEP1.
DR HPA; ENSG00000029725; Low tissue specificity.
DR MIM; 603616; gene.
DR neXtProt; NX_Q15276; -.
DR OpenTargets; ENSG00000029725; -.
DR PharmGKB; PA134884097; -.
DR VEuPathDB; HostDB:ENSG00000029725; -.
DR eggNOG; KOG0993; Eukaryota.
DR GeneTree; ENSGT00530000063743; -.
DR HOGENOM; CLU_016882_0_0_1; -.
DR InParanoid; Q15276; -.
DR OMA; MSPSGYR; -.
DR OrthoDB; 1369937at2759; -.
DR PhylomeDB; Q15276; -.
DR TreeFam; TF329365; -.
DR PathwayCommons; Q15276; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q15276; -.
DR SIGNOR; Q15276; -.
DR BioGRID-ORCS; 9135; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; RABEP1; human.
DR EvolutionaryTrace; Q15276; -.
DR GeneWiki; RABEP1; -.
DR GenomeRNAi; 9135; -.
DR Pharos; Q15276; Tbio.
DR PRO; PR:Q15276; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q15276; protein.
DR Bgee; ENSG00000029725; Expressed in skeletal muscle tissue of rectus abdominis and 188 other tissues.
DR ExpressionAtlas; Q15276; baseline and differential.
DR Genevisible; Q15276; HS.
DR GO; GO:0005769; C:early endosome; TAS:ProtInc.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:1903441; P:protein localization to ciliary membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR InterPro; IPR003914; Rabaptin.
DR InterPro; IPR029880; Rabaptin-5.
DR InterPro; IPR018514; Rabaptin_coiled-coil.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR PANTHER; PTHR31179; PTHR31179; 1.
DR PANTHER; PTHR31179:SF5; PTHR31179:SF5; 1.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF03528; Rabaptin; 1.
DR PRINTS; PR01432; RABAPTIN.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endocytosis;
KW Endosome; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..862
FT /note="Rab GTPase-binding effector protein 1"
FT /id="PRO_0000187556"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..447
FT /note="Interaction with AP1G1, AP1G2, GGA1, GGA2 and GGA3"
FT /evidence="ECO:0000269|PubMed:14665628"
FT COILED 11..345
FT /evidence="ECO:0000255"
FT COILED 534..816
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 282
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 758..790
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10698684"
FT /id="VSP_010451"
FT VARIANT 640
FT /note="E -> G (in dbSNP:rs3026099)"
FT /id="VAR_028106"
FT MUTAGEN 439
FT /note="F->A,V,I,M,L: Abolishes the interaction with AP1G1,
FT AP1G2, GGA1, GGA2 and GGA3."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 440
FT /note="G->A,E,V,S: Abolishes the interaction with AP1G1,
FT AP1G2, GGA1, GGA2 and GGA3."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 441
FT /note="P->A,D,E: Reduces the interaction with AP1G1 and
FT GGA3."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 441
FT /note="P->A: Abolishes the interaction with AP1G2, GGA1 and
FT GGA2."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 441
FT /note="P->D,E: Reduces the interaction with AP1G2, GGA1,
FT GGA2."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 441
FT /note="P->K,F,G,V: Abolishes the interaction with AP1G1,
FT AP1G2, GGA1, GGA2 and GGA3."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 442
FT /note="L->A,V,I: Abolishes the interaction with AP1G1,
FT AP1G2, GGA1, GGA2 and GGA3."
FT /evidence="ECO:0000269|PubMed:14665628"
FT MUTAGEN 812
FT /note="D->K: No effect on RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 815
FT /note="E->K: No effect on RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 818
FT /note="Q->W: Strongly decreases RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 820
FT /note="D->K: Strongly decreases RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 821
FT /note="F->R: Strongly decreases RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 822
FT /note="V->D: Strongly decreases RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 826
FT /note="Q->A: Strongly decreases RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT MUTAGEN 829
FT /note="Q->A: Strongly decreases RAB5A binding affinity."
FT /evidence="ECO:0000269|PubMed:15378032"
FT CONFLICT 149
FT /note="S -> Y (in Ref. 1; CAA62580 and 2; AAC70781)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="M -> I (in Ref. 3; BAG36864)"
FT /evidence="ECO:0000305"
FT HELIX 553..633
FT /evidence="ECO:0007829|PDB:4N3Y"
FT HELIX 805..836
FT /evidence="ECO:0007829|PDB:1TU3"
FT HELIX 841..847
FT /evidence="ECO:0007829|PDB:1TU3"
SQ SEQUENCE 862 AA; 99290 MW; CAAF91638B8ED516 CRC64;
MAQPGPASQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ
NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAV
MKETVRDYEH QFHLRLEQER TQWAQYRESA EREIADLRRR LSEGQEEENL ENEMKKAQED
AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV
LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
MEIVLTSEQL RQVEELKKKD QEDDEQQRLN KRKDHKKADV EEEIKIPVVC ALTQEESSAQ
LSNEEEHLDS TRGSVHSLDA GLLLPSGDPF SKSDNDMFKD GLRRAQSTDS LGTSGSLQSK
ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTASLGSL QMPSGFMLTK DQERAIKAMT
PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE
KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKDKQE LEDFIKQSSE DSSHQISALV
LRAQASEILL EELQQGLSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV
SLQQAEDFIL PDTTEALREL VLKYREDIIN VRTAADHVEE KLKAEILFLK EQIQAEQCLK
ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQLES TLREKSQQLE SLQEIKISLE
EQLKKETAAK ATVEQLMFEE KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS
LERIRAILND TKLTDINQLP ET
