RABX5_MOUSE
ID RABX5_MOUSE Reviewed; 491 AA.
AC Q9JM13; Q3UIW0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Rab5 GDP/GTP exchange factor;
DE AltName: Full=Rabex-5;
GN Name=Rabgef1; Synonyms=Rabex5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Tam S.-Y., Tsai M., Galli S.J.;
RT "Rabex-5 is a negative regulator of Fc-epsilon-RI-dependent and Ras-
RT mediated mast cell activation.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [4]
RP INTERACTION WITH RGS14, AND TISSUE SPECIFICITY.
RX PubMed=10926822; DOI=10.1042/bj3500019;
RA Traver S., Bidot C., Spassky N., Baltauss T., De Tand M.F., Thomas J.L.,
RA Zalc B., Janoueix-Lerosey I., Gunzburg J.D.;
RT "RGS14 is a novel Rap effector that preferentially regulates the GTPase
RT activity of galphao.";
RL Biochem. J. 350:19-29(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Can act as a ubiquitin ligase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with RABEP1. The heterodimer binds RAB4A and RAB5A
CC that have been activated by GTP-binding. Binds TSC2, GGA1, GGA2, GGA3,
CC AP1G1 and AP1G2 (By similarity). Interacts with RAB21, and with 100-
CC fold lower affinity also with RAB22 (By similarity). Interacts with
CC ubiquitinated EGFR (By similarity). Interacts with RGS14; the
CC interaction is GTP-dependent. {ECO:0000250,
CC ECO:0000269|PubMed:10926822}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC {ECO:0000250}. Recycling endosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the white matter tracts of the
CC cerebellum, the fimbria hippocampi and the corpus callosum.
CC {ECO:0000269|PubMed:10926822}.
CC -!- PTM: Monoubiquitinated. {ECO:0000250}.
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DR EMBL; AF093590; AAF28738.1; -; mRNA.
DR EMBL; AK044568; BAC31984.1; -; mRNA.
DR EMBL; AK146734; BAE27396.1; -; mRNA.
DR EMBL; BC018229; AAH18229.1; -; mRNA.
DR CCDS; CCDS19708.1; -.
DR RefSeq; NP_001185988.1; NM_001199059.1.
DR RefSeq; NP_064367.1; NM_019983.2.
DR AlphaFoldDB; Q9JM13; -.
DR SMR; Q9JM13; -.
DR BioGRID; 208140; 19.
DR IntAct; Q9JM13; 2.
DR STRING; 10090.ENSMUSP00000026390; -.
DR iPTMnet; Q9JM13; -.
DR PhosphoSitePlus; Q9JM13; -.
DR EPD; Q9JM13; -.
DR jPOST; Q9JM13; -.
DR MaxQB; Q9JM13; -.
DR PaxDb; Q9JM13; -.
DR PeptideAtlas; Q9JM13; -.
DR PRIDE; Q9JM13; -.
DR ProteomicsDB; 255071; -.
DR DNASU; 56715; -.
DR Ensembl; ENSMUST00000026390; ENSMUSP00000026390; ENSMUSG00000025340.
DR Ensembl; ENSMUST00000119797; ENSMUSP00000114103; ENSMUSG00000025340.
DR GeneID; 56715; -.
DR KEGG; mmu:56715; -.
DR UCSC; uc008zuf.2; mouse.
DR CTD; 27342; -.
DR MGI; MGI:1929459; Rabgef1.
DR VEuPathDB; HostDB:ENSMUSG00000025340; -.
DR eggNOG; KOG2319; Eukaryota.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000154540; -.
DR HOGENOM; CLU_018416_1_1_1; -.
DR InParanoid; Q9JM13; -.
DR OMA; EFERHMS; -.
DR OrthoDB; 944088at2759; -.
DR PhylomeDB; Q9JM13; -.
DR TreeFam; TF321331; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 56715; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Rabgef1; mouse.
DR PRO; PR:Q9JM13; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JM13; protein.
DR Bgee; ENSMUSG00000025340; Expressed in retinal neural layer and 249 other tissues.
DR ExpressionAtlas; Q9JM13; baseline and differential.
DR Genevisible; Q9JM13; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0038109; P:Kit signaling pathway; IMP:MGI.
DR GO; GO:0043303; P:mast cell degranulation; IMP:MGI.
DR GO; GO:0097531; P:mast cell migration; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:1900235; P:negative regulation of Kit signaling pathway; IMP:MGI.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; IMP:MGI.
DR GO; GO:0033004; P:negative regulation of mast cell activation; IMP:MGI.
DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; IMP:MGI.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:MGI.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; IDA:MGI.
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 Acetylation; Coiled coil; Cytoplasm; Endocytosis; Endosome; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..491
FT /note="Rab5 GDP/GTP exchange factor"
FT /id="PRO_0000191316"
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 /evidence="ECO:0000250"
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 COILED 407..448
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:Q9UJ41"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ41"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ41"
FT MOD_RES 170
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ41"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ41"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ41"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 491 AA; 56869 MW; 4CC795C192D235F0 CRC64;
MSLKSERRGI HVDQSELLCK KGCGYYGNPA WQGFCSKCWR EEYHKARQRQ IQEDWELAER
LQREEEEAFA SSQSSQGAQS LTFSKFEEKK TNEKTRKVTT VKKFFSASSR AGSKKEIQEA
KAPSPSINRQ TSIETDRVTK EFIDFLKTFH KTGQEVYKQT KMFLEAMPYK RDLSIEEQSE
CTQDFYQNVA ERMQTRGKVP PEKVEKIMDQ IEKHIMTRLY KFVFCPETTD DEKKDLAIQK
RIRALHWVTP QMLCVPVNEE IPEVSDMVVK AITDIIEMDS KRVPRDKLAC ITRCSKHIFN
AIKITKNEPA SADDFLPTLI YIVLKGNPPR LQSNIQYITR FCNPSRLMTG EDGYYFTNLC
CAVAFIEKLD AQSLNLSQED FDRYMSGQTS PRKQESESWP PEACLGVKQM YKNLDLLSQL
NERQERIMNE AKKLEKDLID WTDGIAKEVQ DIVEKYPLEI KPPNQPLAAI DSENVENDKL
PPPLQPQVYA G
