RABX5_HUMAN
ID RABX5_HUMAN Reviewed; 491 AA.
AC Q9UJ41; B4DZM7; Q3HKR2; Q3HKR3; Q53FG0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Rab5 GDP/GTP exchange factor;
DE AltName: Full=RAP1;
DE AltName: Full=Rabaptin-5-associated exchange factor for Rab5;
DE AltName: Full=Rabex-5;
GN Name=RABGEF1; Synonyms=RABEX5;
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).
RX PubMed=11098082; DOI=10.1016/s0304-3835(00)00553-x;
RA Nimmrich I., Erdmann S., Melchers U., Finke U., Hentsch S., Moyer M.P.,
RA Hoffmann I., Mueller O.;
RT "Seven genes that are differentially transcribed in colorectal tumor cell
RT lines.";
RL Cancer Lett. 160:37-43(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix carcinoma;
RA Barbieri M.A., Hunker C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [8]
RP FUNCTION, AND INTERACTION WITH RABEP1.
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 [9]
RP FUNCTION, AND INTERACTION WITH RABEP1.
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 [10]
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 [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP 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 [14]
RP 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151 AND LYS-170, AND
RP IDENTIFICATION BY MASS 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 AND SER-377, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-400, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP 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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 134-387, FUNCTION, INTERACTION
RP WITH RAB5; RAB21 AND RAB22, AND MUTAGENESIS OF ASP-313; PRO-317; TYR-354
RP AND THR-357.
RX PubMed=15339665; DOI=10.1016/j.cell.2004.08.009;
RA Delprato A., Merithew E., Lambright D.G.;
RT "Structure, exchange determinants, and family-wide rab specificity of the
RT tandem helical bundle and Vps9 domains of Rabex-5.";
RL Cell 118:607-617(2004).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-74 IN COMPLEX WITH UBIQUITIN,
RP UBIQUITINATION, AND MUTAGENESIS OF ALA-58.
RX PubMed=16499958; DOI=10.1016/j.cell.2006.02.020;
RA Penengo L., Mapelli M., Murachelli A.G., Confalonieri S., Magri L.,
RA Musacchio A., Di Fiore P.P., Polo S., Schneider T.R.;
RT "Crystal structure of the ubiquitin binding domains of rabex-5 reveals two
RT modes of interaction with ubiquitin.";
RL Cell 124:1183-1195(2006).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-387 IN COMPLEX WITH RAB21.
RX PubMed=17450153; DOI=10.1038/nsmb1232;
RA Delprato A., Lambright D.G.;
RT "Structural basis for Rab GTPase activation by VPS9 domain exchange
RT factors.";
RL Nat. Struct. Mol. Biol. 14:406-412(2007).
CC -!- FUNCTION: Rab effector protein acting as linker between gamma-adaptin,
CC RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane
CC trafficking of recycling endosomes. Stimulates nucleotide exchange on
CC RAB5A. Can act as a ubiquitin ligase (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11452015, ECO:0000269|PubMed:15339665,
CC ECO:0000269|PubMed:9323142}.
CC -!- SUBUNIT: Interacts with RGS14; the interaction is GTP-dependent (By
CC similarity). Heterodimer with RABEP1. The heterodimer binds RAB4A and
CC RAB5A that have been activated by GTP-binding. Interacts with RAB21,
CC and with 100-fold lower affinity also with RAB22. Binds TSC2, GGA1,
CC GGA2, GGA3, AP1G1 and AP1G2. Interacts with ubiquitinated EGFR.
CC {ECO:0000250, ECO:0000269|PubMed:11452015, ECO:0000269|PubMed:12505986,
CC ECO:0000269|PubMed:15339665, ECO:0000269|PubMed:16499958,
CC ECO:0000269|PubMed:17450153, ECO:0000269|PubMed:9323142}.
CC -!- INTERACTION:
CC Q9UJ41; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-913954, EBI-465781;
CC Q9UJ41; Q9C0C6: CIPC; NbExp=3; IntAct=EBI-913954, EBI-5654244;
CC Q9UJ41; Q15038: DAZAP2; NbExp=3; IntAct=EBI-913954, EBI-724310;
CC Q9UJ41; P00533: EGFR; NbExp=4; IntAct=EBI-913954, EBI-297353;
CC Q9UJ41; Q9BQD3: KXD1; NbExp=2; IntAct=EBI-913954, EBI-739657;
CC Q9UJ41; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-913954, EBI-10176734;
CC Q9UJ41; Q96FV9: THOC1; NbExp=3; IntAct=EBI-913954, EBI-1765605;
CC Q9UJ41; Q9C019: TRIM15; NbExp=3; IntAct=EBI-913954, EBI-2342111;
CC Q9UJ41; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-913954, EBI-2130429;
CC Q9UJ41; Q99757: TXN2; NbExp=3; IntAct=EBI-913954, EBI-2932492;
CC Q9UJ41; P0CG47: UBB; NbExp=6; IntAct=EBI-913954, EBI-413034;
CC Q9UJ41; Q96C32: UBC; NbExp=3; IntAct=EBI-913954, EBI-745483;
CC Q9UJ41; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-913954, EBI-740767;
CC Q9UJ41; P62990: UBC; Xeno; NbExp=2; IntAct=EBI-913954, EBI-413053;
CC Q9UJ41-2; Q9UL25: RAB21; NbExp=2; IntAct=EBI-6448458, EBI-1056039;
CC Q9UJ41-2; Q15276: RABEP1; NbExp=2; IntAct=EBI-6448458, EBI-447043;
CC Q9UJ41-4; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-14093916, EBI-11096309;
CC Q9UJ41-4; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-14093916, EBI-17439331;
CC Q9UJ41-4; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-14093916, EBI-2875665;
CC Q9UJ41-4; Q9UL45: BLOC1S6; NbExp=6; IntAct=EBI-14093916, EBI-465781;
CC Q9UJ41-4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-14093916, EBI-10175300;
CC Q9UJ41-4; Q16543: CDC37; NbExp=3; IntAct=EBI-14093916, EBI-295634;
CC Q9UJ41-4; Q15038: DAZAP2; NbExp=6; IntAct=EBI-14093916, EBI-724310;
CC Q9UJ41-4; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-14093916, EBI-25840379;
CC Q9UJ41-4; Q13561: DCTN2; NbExp=3; IntAct=EBI-14093916, EBI-715074;
CC Q9UJ41-4; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-14093916, EBI-11748557;
CC Q9UJ41-4; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-14093916, EBI-473189;
CC Q9UJ41-4; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-14093916, EBI-10961706;
CC Q9UJ41-4; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-14093916, EBI-8638439;
CC Q9UJ41-4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-14093916, EBI-10172526;
CC Q9UJ41-4; O43482: OIP5; NbExp=3; IntAct=EBI-14093916, EBI-536879;
CC Q9UJ41-4; P54725: RAD23A; NbExp=3; IntAct=EBI-14093916, EBI-746453;
CC Q9UJ41-4; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-14093916, EBI-3437896;
CC Q9UJ41-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-14093916, EBI-396669;
CC Q9UJ41-4; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-14093916, EBI-6117072;
CC Q9UJ41-4; O95295: SNAPIN; NbExp=3; IntAct=EBI-14093916, EBI-296723;
CC Q9UJ41-4; P37840: SNCA; NbExp=3; IntAct=EBI-14093916, EBI-985879;
CC Q9UJ41-4; Q8N0X7: SPART; NbExp=3; IntAct=EBI-14093916, EBI-2643803;
CC Q9UJ41-4; Q99909: SSX3; NbExp=3; IntAct=EBI-14093916, EBI-10295431;
CC Q9UJ41-4; Q9BT92: TCHP; NbExp=3; IntAct=EBI-14093916, EBI-740781;
CC Q9UJ41-4; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-14093916, EBI-2130429;
CC Q9UJ41-4; P62987: UBA52; NbExp=3; IntAct=EBI-14093916, EBI-357304;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12505986}. Early
CC endosome {ECO:0000269|PubMed:12505986}. Recycling endosome
CC {ECO:0000269|PubMed:12505986}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJ41-2; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q9UJ41-3; Sequence=VSP_060131;
CC Name=3;
CC IsoId=Q9UJ41-4; Sequence=VSP_060130;
CC -!- PTM: Monoubiquitinated.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87138.1; Type=Miscellaneous discrepancy; Note=Readthrough transcript KCTD7-RABGEF1.; Evidence={ECO:0000305};
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DR EMBL; AJ250042; CAB57359.1; -; mRNA.
DR EMBL; DQ230533; ABA64473.1; -; mRNA.
DR EMBL; DQ230534; ABA64474.1; -; mRNA.
DR EMBL; BT007107; AAP35771.1; -; mRNA.
DR EMBL; AK127790; BAC87138.1; ALT_SEQ; mRNA.
DR EMBL; AK303006; BAG64139.1; -; mRNA.
DR EMBL; AK223329; BAD97049.1; -; mRNA.
DR EMBL; AC027644; AAQ93362.1; -; Genomic_DNA.
DR EMBL; AC079588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015330; AAH15330.1; -; mRNA.
DR CCDS; CCDS5535.1; -. [Q9UJ41-2]
DR CCDS; CCDS69308.1; -. [Q9UJ41-4]
DR RefSeq; NP_001273989.1; NM_001287060.1.
DR RefSeq; NP_001273990.1; NM_001287061.1. [Q9UJ41-4]
DR RefSeq; NP_001273991.1; NM_001287062.1. [Q9UJ41-2]
DR RefSeq; NP_055319.1; NM_014504.2. [Q9UJ41-2]
DR PDB; 1TXU; X-ray; 2.35 A; A=134-387.
DR PDB; 2C7M; X-ray; 2.40 A; A=17-74.
DR PDB; 2C7N; X-ray; 2.10 A; A/C/E/G/I/K=17-74.
DR PDB; 2OT3; X-ray; 2.10 A; A=134-387.
DR PDB; 4N3X; X-ray; 2.00 A; A/B/C/D=409-455.
DR PDB; 4N3Y; X-ray; 2.20 A; A=413-455.
DR PDB; 4N3Z; X-ray; 3.10 A; A=134-452.
DR PDB; 4Q9U; X-ray; 4.62 A; A/E=134-452.
DR PDBsum; 1TXU; -.
DR PDBsum; 2C7M; -.
DR PDBsum; 2C7N; -.
DR PDBsum; 2OT3; -.
DR PDBsum; 4N3X; -.
DR PDBsum; 4N3Y; -.
DR PDBsum; 4N3Z; -.
DR PDBsum; 4Q9U; -.
DR AlphaFoldDB; Q9UJ41; -.
DR SMR; Q9UJ41; -.
DR BioGRID; 118154; 184.
DR CORUM; Q9UJ41; -.
DR DIP; DIP-29348N; -.
DR IntAct; Q9UJ41; 77.
DR MINT; Q9UJ41; -.
DR STRING; 9606.ENSP00000370208; -.
DR TCDB; 1.F.1.1.5; the synaptosomal vesicle fusion pore (svf-pore) family.
DR GlyGen; Q9UJ41; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJ41; -.
DR MetOSite; Q9UJ41; -.
DR PhosphoSitePlus; Q9UJ41; -.
DR BioMuta; RABGEF1; -.
DR DMDM; 56405102; -.
DR EPD; Q9UJ41; -.
DR jPOST; Q9UJ41; -.
DR MassIVE; Q9UJ41; -.
DR MaxQB; Q9UJ41; -.
DR PeptideAtlas; Q9UJ41; -.
DR PRIDE; Q9UJ41; -.
DR ProteomicsDB; 5608; -.
DR ProteomicsDB; 84585; -. [Q9UJ41-3]
DR Antibodypedia; 14115; 166 antibodies from 29 providers.
DR DNASU; 27342; -.
DR Ensembl; ENST00000284957.9; ENSP00000284957.4; ENSG00000154710.18. [Q9UJ41-2]
DR Ensembl; ENST00000450873.6; ENSP00000415815.1; ENSG00000154710.18. [Q9UJ41-2]
DR GeneID; 27342; -.
DR KEGG; hsa:27342; -.
DR MANE-Select; ENST00000284957.9; ENSP00000284957.4; NM_014504.3; NP_055319.1.
DR UCSC; uc003tvh.4; human. [Q9UJ41-2]
DR CTD; 27342; -.
DR DisGeNET; 27342; -.
DR GeneCards; RABGEF1; -.
DR HGNC; HGNC:17676; RABGEF1.
DR HPA; ENSG00000154710; Tissue enhanced (bone).
DR MIM; 609700; gene.
DR neXtProt; NX_Q9UJ41; -.
DR OpenTargets; ENSG00000154710; -.
DR PharmGKB; PA134946532; -.
DR VEuPathDB; HostDB:ENSG00000154710; -.
DR GeneTree; ENSGT00940000154540; -.
DR InParanoid; Q9UJ41; -.
DR OMA; EFERHMS; -.
DR OrthoDB; 944088at2759; -.
DR PhylomeDB; Q9UJ41; -.
DR TreeFam; TF321331; -.
DR PathwayCommons; Q9UJ41; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q9UJ41; -.
DR SIGNOR; Q9UJ41; -.
DR BioGRID-ORCS; 27342; 33 hits in 1112 CRISPR screens.
DR ChiTaRS; RABGEF1; human.
DR EvolutionaryTrace; Q9UJ41; -.
DR GeneWiki; RABGEF1; -.
DR GenomeRNAi; 27342; -.
DR Pharos; Q9UJ41; Tbio.
DR PRO; PR:Q9UJ41; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UJ41; protein.
DR Bgee; ENSG00000154710; Expressed in bone marrow and 97 other tissues.
DR ExpressionAtlas; Q9UJ41; baseline and differential.
DR Genevisible; Q9UJ41; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IMP:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
DR GO; GO:0097531; P:mast cell migration; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:1900235; P:negative regulation of Kit signaling pathway; IEA:Ensembl.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Ensembl.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; IEA:Ensembl.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR041545; DUF5601.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF02204; VPS9; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SMART; SM00167; VPS9; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR PROSITE; PS51205; VPS9; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Endocytosis;
KW Endosome; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..491
FT /note="Rab5 GDP/GTP exchange factor"
FT /id="PRO_0000191315"
FT DOMAIN 232..375
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT ZN_FING 13..47
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT REGION 1..74
FT /note="Interaction with ubiquitinated proteins"
FT REGION 66..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 170
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM13"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MMASSYHEVVSRKKM (in isoform 3)"
FT /id="VSP_060130"
FT VAR_SEQ 60
FT /note="R -> RALLCYPGWSAMVQFQLTATSASWAQVILLLQPPKWLGLQK (in
FT isoform 2)"
FT /id="VSP_060131"
FT MUTAGEN 58
FT /note="A->G: Reduces affinity for ubiquitin 3-fold."
FT /evidence="ECO:0000269|PubMed:16499958"
FT MUTAGEN 313
FT /note="D->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:15339665"
FT MUTAGEN 317
FT /note="P->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:15339665"
FT MUTAGEN 354
FT /note="Y->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:15339665"
FT MUTAGEN 357
FT /note="T->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:15339665"
FT CONFLICT 270
FT /note="K -> R (in Ref. 5; BAD97049)"
FT /evidence="ECO:0000305"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2C7N"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2C7N"
FT HELIX 36..70
FT /evidence="ECO:0007829|PDB:2C7N"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 150..168
FT /evidence="ECO:0007829|PDB:2OT3"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 175..194
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 201..223
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:2OT3"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2OT3"
FT TURN 250..254
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 284..306
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:2OT3"
FT TURN 344..348
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:2OT3"
FT HELIX 409..415
FT /evidence="ECO:0007829|PDB:4N3X"
FT HELIX 417..452
FT /evidence="ECO:0007829|PDB:4N3X"
SQ SEQUENCE 491 AA; 56891 MW; 49ACABA276E65E91 CRC64;
MSLKSERRGI HVDQSDLLCK KGCGYYGNPA WQGFCSKCWR EEYHKARQKQ IQEDWELAER
LQREEEEAFA SSQSSQGAQS LTFSKFEEKK TNEKTRKVTT VKKFFSASSR VGSKKEIQEA
KAPSPSINRQ TSIETDRVSK EFIEFLKTFH KTGQEIYKQT KLFLEGMHYK RDLSIEEQSE
CAQDFYHNVA ERMQTRGKVP PERVEKIMDQ IEKYIMTRLY KYVFCPETTD DEKKDLAIQK
RIRALRWVTP QMLCVPVNED IPEVSDMVVK AITDIIEMDS KRVPRDKLAC ITKCSKHIFN
AIKITKNEPA SADDFLPTLI YIVLKGNPPR LQSNIQYITR FCNPSRLMTG EDGYYFTNLC
CAVAFIEKLD AQSLNLSQED FDRYMSGQTS PRKQEAESWS PDACLGVKQM YKNLDLLSQL
NERQERIMNE AKKLEKDLID WTDGIAREVQ DIVEKYPLEI KPPNQPLAAI DSENVENDKL
PPPLQPQVYA G
