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Rab5 GDP/GTP exchange factor (RAP1) (Rabaptin-5-associated exchange factor for Rab5) (Rabex-5)

 RABX5_HUMAN             Reviewed;         708 AA.
Q9UJ41; B4DZM7; Q3HKR2; Q3HKR3; Q53FG0;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=Rab5 GDP/GTP exchange factor;
AltName: Full=RAP1;
AltName: Full=Rabaptin-5-associated exchange factor for Rab5;
AltName: Full=Rabex-5;
Name=RABGEF1; Synonyms=RABEX5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11098082; DOI=10.1016/S0304-3835(00)00553-X;
Nimmrich I., Erdmann S., Melchers U., Finke U., Hentsch S.,
Moyer M.P., Hoffmann I., Mueller O.;
"Seven genes that are differentially transcribed in colorectal tumor
cell lines.";
Cancer Lett. 160:37-43(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Cervix carcinoma;
Barbieri M.A., Hunker C.M.;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Brain, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND INTERACTION WITH RABEP1.
PubMed=9323142; DOI=10.1016/S0092-8674(00)80380-3;
Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P.,
Stenmark H., Rybin V., Wilm M., Ashman K., Mann M., Zerial M.;
"A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
nucleotide exchange to effector recruitment and function.";
Cell 90:1149-1159(1997).
[9]
FUNCTION, AND INTERACTION WITH RABEP1.
PubMed=11452015; DOI=10.1091/mbc.12.7.2219;
Lippe R., Miaczynska M., Rybin V., Runge A., Zerial M.;
"Functional synergy between Rab5 effector Rabaptin-5 and exchange
factor Rabex-5 when physically associated in a complex.";
Mol. Biol. Cell 12:2219-2228(2001).
[10]
INTERACTION WITH GGA1; GGA2; GGA3; AP1G1 AND AP1G2, AND SUBCELLULAR
LOCATION.
PubMed=12505986; DOI=10.1093/emboj/cdg015;
Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.;
"Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
complex.";
EMBO J. 22:78-88(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-329 AND LYS-348, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590 AND SER-594, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-617, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 310-611, FUNCTION,
INTERACTION WITH RAB5; RAB21 AND RAB22, AND MUTAGENESIS OF ASP-530;
PRO-534; TYR-571 AND THR-574.
PubMed=15339665; DOI=10.1016/j.cell.2004.08.009;
Delprato A., Merithew E., Lambright D.G.;
"Structure, exchange determinants, and family-wide rab specificity of
the tandem helical bundle and Vps9 domains of Rabex-5.";
Cell 118:607-617(2004).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 139-252 IN COMPLEX WITH
UBIQUITIN, UBIQUITINATION, AND MUTAGENESIS OF ALA-196.
PubMed=16499958; DOI=10.1016/j.cell.2006.02.020;
Penengo L., Mapelli M., Murachelli A.G., Confalonieri S., Magri L.,
Musacchio A., Di Fiore P.P., Polo S., Schneider T.R.;
"Crystal structure of the ubiquitin binding domains of rabex-5 reveals
two modes of interaction with ubiquitin.";
Cell 124:1183-1195(2006).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 310-614 IN COMPLEX WITH
RAB21.
PubMed=17450153; DOI=10.1038/nsmb1232;
Delprato A., Lambright D.G.;
"Structural basis for Rab GTPase activation by VPS9 domain exchange
factors.";
Nat. Struct. Mol. Biol. 14:406-412(2007).
-!- FUNCTION: Rab effector protein acting as linker between gamma-
adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and
membrane trafficking of recycling endosomes. Stimulates nucleotide
exchange on RAB5A. Can act as a ubiquitin ligase (By similarity).
{ECO:0000250, ECO:0000269|PubMed:11452015,
ECO:0000269|PubMed:15339665, ECO:0000269|PubMed:9323142}.
-!- SUBUNIT: Interacts with RGS14; the interaction is GTP-dependent
(By similarity). Heterodimer with RABEP1. The heterodimer binds
RAB4A and RAB5A that have been activated by GTP-binding. Interacts
with RAB21, and with 100-fold lower affinity also with RAB22.
Binds TSC2, GGA1, GGA2, GGA3, AP1G1 and AP1G2. Interacts with
ubiquitinated EGFR. {ECO:0000250, ECO:0000269|PubMed:11452015,
ECO:0000269|PubMed:12505986, ECO:0000269|PubMed:15339665,
ECO:0000269|PubMed:16499958, ECO:0000269|PubMed:17450153,
ECO:0000269|PubMed:9323142}.
-!- INTERACTION:
Q9UL45:BLOC1S6; NbExp=4; IntAct=EBI-14093916, EBI-465781;
Q9C0C6:CIPC; NbExp=3; IntAct=EBI-913954, EBI-5654244;
Q15038:DAZAP2; NbExp=3; IntAct=EBI-913954, EBI-724310;
P00533:EGFR; NbExp=4; IntAct=EBI-913954, EBI-297353;
Q9Y6C2-2:EMILIN1; NbExp=4; IntAct=EBI-14093916, EBI-11748557;
Q96D09:GPRASP2; NbExp=4; IntAct=EBI-14093916, EBI-473189;
Q9BQD3:KXD1; NbExp=2; IntAct=EBI-913954, EBI-739657;
D3DUQ6:TEAD4; NbExp=3; IntAct=EBI-913954, EBI-10176734;
Q96FV9:THOC1; NbExp=3; IntAct=EBI-913954, EBI-1765605;
Q9C019:TRIM15; NbExp=3; IntAct=EBI-913954, EBI-2342111;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-913954, EBI-2130429;
Q99757:TXN2; NbExp=3; IntAct=EBI-913954, EBI-2932492;
P0CG47:UBB; NbExp=6; IntAct=EBI-913954, EBI-413034;
P62990:UBC (xeno); NbExp=2; IntAct=EBI-913954, EBI-413053;
Q96C32:UBC; NbExp=3; IntAct=EBI-913954, EBI-745483;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-913954, EBI-740767;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12505986}.
Early endosome {ECO:0000269|PubMed:12505986}. Recycling endosome
{ECO:0000269|PubMed:12505986}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9UJ41-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q9UJ41-2; Sequence=VSP_010690, VSP_010691, VSP_010692;
Name=3; Synonyms=Long;
IsoId=Q9UJ41-3; Sequence=VSP_010690, VSP_010692;
Name=4;
IsoId=Q9UJ41-4; Sequence=VSP_054643, VSP_054644, VSP_010691,
VSP_010692;
Note=No experimental confirmation available.;
-!- PTM: Monoubiquitinated.
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EMBL; AJ250042; CAB57359.1; -; mRNA.
EMBL; DQ230533; ABA64473.1; -; mRNA.
EMBL; DQ230534; ABA64474.1; -; mRNA.
EMBL; BT007107; AAP35771.1; -; mRNA.
EMBL; AK127790; BAC87138.1; -; mRNA.
EMBL; AK303006; BAG64139.1; -; mRNA.
EMBL; AK223329; BAD97049.1; -; mRNA.
EMBL; AC027644; AAQ93362.1; -; Genomic_DNA.
EMBL; AC079588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015330; AAH15330.1; -; mRNA.
CCDS; CCDS5535.1; -. [Q9UJ41-2]
CCDS; CCDS69308.1; -. [Q9UJ41-4]
RefSeq; NP_001273989.1; NM_001287060.1.
RefSeq; NP_001273990.1; NM_001287061.1. [Q9UJ41-4]
RefSeq; NP_001273991.1; NM_001287062.1. [Q9UJ41-2]
RefSeq; NP_055319.1; NM_014504.2. [Q9UJ41-2]
UniGene; Hs.530053; -.
UniGene; Hs.662268; -.
UniGene; Hs.733181; -.
PDB; 1TXU; X-ray; 2.35 A; A=311-611.
PDB; 2C7M; X-ray; 2.40 A; A=139-252.
PDB; 2C7N; X-ray; 2.10 A; A/C/E/G/I/K=139-252.
PDB; 2OT3; X-ray; 2.10 A; A=310-614.
PDB; 4N3X; X-ray; 2.00 A; A/B/C/D=626-672.
PDB; 4N3Y; X-ray; 2.20 A; A=630-672.
PDB; 4N3Z; X-ray; 3.10 A; A=310-672.
PDB; 4Q9U; X-ray; 4.62 A; A/E=310-672.
PDBsum; 1TXU; -.
PDBsum; 2C7M; -.
PDBsum; 2C7N; -.
PDBsum; 2OT3; -.
PDBsum; 4N3X; -.
PDBsum; 4N3Y; -.
PDBsum; 4N3Z; -.
PDBsum; 4Q9U; -.
ProteinModelPortal; Q9UJ41; -.
SMR; Q9UJ41; -.
BioGrid; 118154; 90.
DIP; DIP-29348N; -.
IntAct; Q9UJ41; 40.
MINT; MINT-1189235; -.
iPTMnet; Q9UJ41; -.
PhosphoSitePlus; Q9UJ41; -.
BioMuta; RABGEF1; -.
DMDM; 56405102; -.
EPD; Q9UJ41; -.
PeptideAtlas; Q9UJ41; -.
PRIDE; Q9UJ41; -.
DNASU; 27342; -.
Ensembl; ENST00000284957; ENSP00000284957; ENSG00000154710. [Q9UJ41-2]
Ensembl; ENST00000380828; ENSP00000370208; ENSG00000154710. [Q9UJ41-4]
Ensembl; ENST00000450873; ENSP00000415815; ENSG00000154710. [Q9UJ41-2]
GeneID; 27342; -.
KEGG; hsa:27342; -.
UCSC; uc003tvh.4; human. [Q9UJ41-1]
CTD; 27342; -.
DisGeNET; 27342; -.
EuPathDB; HostDB:ENSG00000154710.15; -.
GeneCards; RABGEF1; -.
HGNC; HGNC:17676; RABGEF1.
HPA; HPA001407; -.
MIM; 609700; gene.
neXtProt; NX_Q9UJ41; -.
OpenTargets; ENSG00000154710; -.
PharmGKB; PA134946532; -.
GeneTree; ENSGT00530000063341; -.
HOGENOM; HOG000070180; -.
HOVERGEN; HBG062584; -.
InParanoid; Q9UJ41; -.
KO; K20131; -.
OMA; RCCRHIF; -.
OrthoDB; EOG091G059N; -.
PhylomeDB; Q9UJ41; -.
TreeFam; TF321331; -.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
SIGNOR; Q9UJ41; -.
ChiTaRS; RABGEF1; human.
EvolutionaryTrace; Q9UJ41; -.
GeneWiki; RABGEF1; -.
GenomeRNAi; 27342; -.
PRO; PR:Q9UJ41; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000154710; -.
CleanEx; HS_RABGEF1; -.
ExpressionAtlas; Q9UJ41; baseline and differential.
Genevisible; Q9UJ41; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IMP:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
InterPro; IPR003123; VPS9.
InterPro; IPR037191; VPS9_dom_sf.
InterPro; IPR002653; Znf_A20.
Pfam; PF02204; VPS9; 1.
Pfam; PF01754; zf-A20; 1.
SMART; SM00167; VPS9; 1.
SMART; SM00259; ZnF_A20; 1.
SUPFAM; SSF109993; SSF109993; 2.
PROSITE; PS51205; VPS9; 1.
PROSITE; PS51036; ZF_A20; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Endocytosis; Endosome; Metal-binding;
Phosphoprotein; Protein transport; Reference proteome; Transport;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 708 Rab5 GDP/GTP exchange factor.
/FTId=PRO_0000191315.
DOMAIN 449 592 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
ZN_FING 151 185 A20-type. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
REGION 139 252 Interaction with ubiquitinated proteins.
COILED 624 665 {ECO:0000255}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 329 329 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 348 348 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JM13}.
MOD_RES 617 617 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 138 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11098082,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2, ECO:0000303|Ref.3,
ECO:0000303|Ref.5}.
/FTId=VSP_010690.
VAR_SEQ 1 8 MVVVTGRE -> MMASSYHE (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054643.
VAR_SEQ 9 132 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054644.
VAR_SEQ 199 238 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11098082,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2, ECO:0000303|Ref.3,
ECO:0000303|Ref.5}.
/FTId=VSP_010691.
VAR_SEQ 377 415 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:11098082,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2, ECO:0000303|Ref.3,
ECO:0000303|Ref.5}.
/FTId=VSP_010692.
MUTAGEN 196 196 A->G: Reduces affinity for ubiquitin 3-
fold. {ECO:0000269|PubMed:16499958}.
MUTAGEN 530 530 D->A: Strongly reduced activity.
{ECO:0000269|PubMed:15339665}.
MUTAGEN 534 534 P->A: Strongly reduced activity.
{ECO:0000269|PubMed:15339665}.
MUTAGEN 571 571 Y->A: Strongly reduced activity.
{ECO:0000269|PubMed:15339665}.
MUTAGEN 574 574 T->A: Strongly reduced activity.
{ECO:0000269|PubMed:15339665}.
CONFLICT 199 199 V -> A (in Ref. 2; ABA64474).
{ECO:0000305}.
CONFLICT 203 203 C -> Y (in Ref. 2; ABA64474).
{ECO:0000305}.
CONFLICT 476 476 E -> D (in Ref. 4; BAC87138).
{ECO:0000305}.
CONFLICT 487 487 K -> R (in Ref. 5; BAD97049).
{ECO:0000305}.
STRAND 161 163 {ECO:0000244|PDB:2C7N}.
HELIX 167 169 {ECO:0000244|PDB:2C7N}.
HELIX 174 199 {ECO:0000244|PDB:2C7N}.
HELIX 318 325 {ECO:0000244|PDB:2OT3}.
HELIX 328 346 {ECO:0000244|PDB:2OT3}.
TURN 347 350 {ECO:0000244|PDB:2OT3}.
HELIX 353 372 {ECO:0000244|PDB:2OT3}.
HELIX 418 440 {ECO:0000244|PDB:2OT3}.
HELIX 448 461 {ECO:0000244|PDB:2OT3}.
TURN 462 464 {ECO:0000244|PDB:2OT3}.
TURN 467 471 {ECO:0000244|PDB:2OT3}.
HELIX 479 494 {ECO:0000244|PDB:2OT3}.
HELIX 495 497 {ECO:0000244|PDB:2OT3}.
HELIX 501 523 {ECO:0000244|PDB:2OT3}.
HELIX 529 543 {ECO:0000244|PDB:2OT3}.
HELIX 548 558 {ECO:0000244|PDB:2OT3}.
TURN 561 565 {ECO:0000244|PDB:2OT3}.
HELIX 568 585 {ECO:0000244|PDB:2OT3}.
HELIX 589 591 {ECO:0000244|PDB:2OT3}.
HELIX 595 602 {ECO:0000244|PDB:2OT3}.
HELIX 626 632 {ECO:0000244|PDB:4N3X}.
HELIX 634 669 {ECO:0000244|PDB:4N3X}.
SEQUENCE 708 AA; 79371 MW; 007E404F13AC91D8 CRC64;
MVVVTGREPD SRRQDGAMSS SDAEDDFLEP ATPTATQAGH ALPLLPQERC AEFPALRGPP
TQGACSSCVQ RGPVLCHRAP PGAAGEHAAT EGREGAPSVS GTHALLQRPL GADCGDRPAA
CGPAEGPLCQ AQVVSRKKMS LKSERRGIHV DQSDLLCKKG CGYYGNPAWQ GFCSKCWREE
YHKARQKQIQ EDWELAERVL LCCPGWSAMV QFQLTATSAS WAQVILLLQP PKWLGLQKLQ
REEEEAFASS QSSQGAQSLT FSKFEEKKTN EKTRKVTTVK KFFSASSRVG SKKEIQEAKA
PSPSINRQTS IETDRVSKEF IEFLKTFHKT GQEIYKQTKL FLEGMHYKRD LSIEEQSECA
QDFYHNVAER MQTRGKERRF HHVGQAGLEL LTSGDPPASA SQSAGNTGVE PPHPAVPPER
VEKIMDQIEK YIMTRLYKYV FCPETTDDEK KDLAIQKRIR ALRWVTPQML CVPVNEDIPE
VSDMVVKAIT DIIEMDSKRV PRDKLACITK CSKHIFNAIK ITKNEPASAD DFLPTLIYIV
LKGNPPRLQS NIQYITRFCN PSRLMTGEDG YYFTNLCCAV AFIEKLDAQS LNLSQEDFDR
YMSGQTSPRK QEAESWSPDA CLGVKQMYKN LDLLSQLNER QERIMNEAKK LEKDLIDWTD
GIAREVQDIV EKYPLEIKPP NQPLAAIDSE NVENDKLPPP LQPQVYAG


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