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Rab5 GDP/GTP exchange factor (Rabex-5)

 RABX5_MOUSE             Reviewed;         491 AA.
Q9JM13; Q3UIW0;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-MAR-2018, entry version 120.
RecName: Full=Rab5 GDP/GTP exchange factor;
AltName: Full=Rabex-5;
Name=Rabgef1; Synonyms=Rabex5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
Tam S.-Y., Tsai M., Galli S.J.;
"Rabex-5 is a negative regulator of Fc-epsilon-RI-dependent and Ras-
mediated mast cell activation.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Amnion, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
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).
[4]
INTERACTION WITH RGS14, AND TISSUE SPECIFICITY.
PubMed=10926822; DOI=10.1042/bj3500019;
Traver S., Bidot C., Spassky N., Baltauss T., De Tand M.F.,
Thomas J.L., Zalc B., Janoueix-Lerosey I., Gunzburg J.D.;
"RGS14 is a novel Rap effector that preferentially regulates the
GTPase activity of galphao.";
Biochem. J. 350:19-29(2000).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity). Can act as a ubiquitin ligase
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer with RABEP1. The heterodimer binds RAB4A and
RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1,
GGA2, GGA3, AP1G1 and AP1G2 (By similarity). Interacts with RAB21,
and with 100-fold lower affinity also with RAB22 (By similarity).
Interacts with ubiquitinated EGFR (By similarity). Interacts with
RGS14; the interaction is GTP-dependent. {ECO:0000250,
ECO:0000269|PubMed:10926822}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
{ECO:0000250}. Recycling endosome {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the white matter tracts of the
cerebellum, the fimbria hippocampi and the corpus callosum.
{ECO:0000269|PubMed:10926822}.
-!- PTM: Monoubiquitinated. {ECO:0000250}.
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EMBL; AF093590; AAF28738.1; -; mRNA.
EMBL; AK044568; BAC31984.1; -; mRNA.
EMBL; AK146734; BAE27396.1; -; mRNA.
EMBL; BC018229; AAH18229.1; -; mRNA.
CCDS; CCDS19708.1; -.
RefSeq; NP_001185988.1; NM_001199059.1.
RefSeq; NP_064367.1; NM_019983.2.
UniGene; Mm.288639; -.
ProteinModelPortal; Q9JM13; -.
SMR; Q9JM13; -.
BioGrid; 208140; 6.
CORUM; Q9JM13; -.
IntAct; Q9JM13; 2.
STRING; 10090.ENSMUSP00000026390; -.
iPTMnet; Q9JM13; -.
PhosphoSitePlus; Q9JM13; -.
EPD; Q9JM13; -.
MaxQB; Q9JM13; -.
PaxDb; Q9JM13; -.
PeptideAtlas; Q9JM13; -.
PRIDE; Q9JM13; -.
Ensembl; ENSMUST00000026390; ENSMUSP00000026390; ENSMUSG00000025340.
Ensembl; ENSMUST00000119797; ENSMUSP00000114103; ENSMUSG00000025340.
GeneID; 56715; -.
KEGG; mmu:56715; -.
UCSC; uc008zuf.2; mouse.
CTD; 27342; -.
MGI; MGI:1929459; Rabgef1.
eggNOG; KOG2319; Eukaryota.
eggNOG; KOG3173; Eukaryota.
eggNOG; ENOG410YGAZ; LUCA.
GeneTree; ENSGT00530000063341; -.
HOGENOM; HOG000070180; -.
HOVERGEN; HBG062584; -.
InParanoid; Q9JM13; -.
KO; K20131; -.
OMA; RCCRHIF; -.
OrthoDB; EOG091G059N; -.
PhylomeDB; Q9JM13; -.
TreeFam; TF321331; -.
Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; Rabgef1; mouse.
PRO; PR:Q9JM13; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000025340; -.
CleanEx; MM_RABGEF1; -.
ExpressionAtlas; Q9JM13; baseline and differential.
Genevisible; Q9JM13; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
GO; GO:1900165; P:negative regulation of interleukin-6 secretion; IMP:MGI.
GO; GO:1900235; P:negative regulation of Kit signaling pathway; IMP:MGI.
GO; GO:0002686; P:negative regulation of leukocyte migration; IMP:MGI.
GO; GO:0033004; P:negative regulation of mast cell activation; IMP:MGI.
GO; GO:0043305; P:negative regulation of mast cell degranulation; IMP:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:MGI.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IMP:MGI.
GO; GO:0006612; P:protein targeting to membrane; ISO:MGI.
GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; IDA:MGI.
Gene3D; 1.20.1050.80; -; 1.
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; 1.
PROSITE; PS51205; VPS9; 1.
PROSITE; PS51036; ZF_A20; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Endocytosis;
Endosome; Metal-binding; Phosphoprotein; Protein transport;
Reference proteome; Transport; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 491 Rab5 GDP/GTP exchange factor.
/FTId=PRO_0000191316.
DOMAIN 232 375 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
ZN_FING 13 47 A20-type. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
REGION 1 74 Interaction with ubiquitinated proteins.
{ECO:0000250}.
COILED 407 448 {ECO:0000255}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UJ41}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UJ41}.
MOD_RES 151 151 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UJ41}.
MOD_RES 170 170 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UJ41}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UJ41}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UJ41}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
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


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