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Ras-related protein Rab-5A

 RAB5A_HUMAN             Reviewed;         215 AA.
P20339; B4DJA5; Q6FI44;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
05-DEC-2018, entry version 210.
RecName: Full=Ras-related protein Rab-5A;
Name=RAB5A; Synonyms=RAB5;
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 1).
PubMed=2501306;
Zahraoui A., Touchot N., Chardin P., Tavitian A.;
"The human Rab genes encode a family of GTP-binding proteins related
to yeast YPT1 and SEC4 products involved in secretion.";
J. Biol. Chem. 264:12394-12401(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-212 AND
CYS-213, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=7991565; DOI=10.1073/pnas.91.25.11963;
Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.;
"Rab geranylgeranyl transferase catalyzes the geranylgeranylation of
adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.";
Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kim J.W.;
"Identification of a new oncogene in human cancers.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Subthalamic nucleus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix, and Placenta;
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).
[10]
INTERACTION WITH EEA1.
PubMed=10491193; DOI=10.1046/j.1432-1327.1999.00743.x;
Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.;
"Direct interaction of EEA1 with Rab5b.";
Eur. J. Biochem. 265:361-366(1999).
[11]
INTERACTION WITH SUN2, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10818110; DOI=10.1074/jbc.M909600199;
Hoffenberg S., Liu X., Nikolova L., Hall H.S., Dai W., Baughn R.E.,
Dickey B.F., Barbieri M.A., Aballay A., Stahl P.D., Knoll B.J.;
"A novel membrane-anchored Rab5 interacting protein required for
homotypic endosome fusion.";
J. Biol. Chem. 275:24661-24669(2000).
[12]
INTERACTION WITH ZFYVE20.
TISSUE=Cervix carcinoma;
PubMed=11062261; DOI=10.1083/jcb.151.3.601;
Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M.,
Dewitte F., Wilm M., Hoflack B., Zerial M.;
"Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and
recruited to endosomes through a FYVE finger domain.";
J. Cell Biol. 151:601-612(2000).
[13]
ACTIVATION BY RIN1.
PubMed=11703925; DOI=10.1016/S1534-5807(01)00008-9;
Tall G.G., Barbieri M.A., Stahl P.D., Horazdovsky B.F.;
"Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide
exchange activity of RIN1.";
Dev. Cell 1:73-82(2001).
[14]
INTERACTION WITH ALS2CL.
PubMed=15388334; DOI=10.1016/j.febslet.2004.07.092;
Hadano S., Otomo A., Suzuki-Utsunomiya K., Kunita R., Yanagisawa Y.,
Showguchi-Miyata J., Mizumura H., Ikeda J.-E.;
"ALS2CL, the novel protein highly homologous to the carboxy-terminal
half of ALS2, binds to Rab5 and modulates endosome dynamics.";
FEBS Lett. 575:64-70(2004).
[15]
FUNCTION, AND INTERACTION WITH RUFY1.
PubMed=14617813; DOI=10.1091/mbc.E03-05-0343;
Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
"Rabip4' is an effector of rab5 and rab4 and regulates transport
through early endosomes.";
Mol. Biol. Cell 15:611-624(2004).
[16]
FUNCTION, AND MUTAGENESIS OF GLN-79.
PubMed=14978216; DOI=10.1091/mbc.E03-07-0493;
Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
"Regulation of dendritic branching and filopodia formation in
hippocampal neurons by specific acylated protein motifs.";
Mol. Biol. Cell 15:2205-2217(2004).
[17]
INTERACTION WITH ZFYVE20, AND MUTAGENESIS OF GLY-54; ALA-56 AND
PHE-57.
PubMed=16034420; DOI=10.1038/nature03798;
Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
"Structural basis of family-wide Rab GTPase recognition by rabenosyn-
5.";
Nature 436:415-419(2005).
[18]
FUNCTION, AND INTERACTION WITH GAPVD1.
PubMed=16410077; DOI=10.1016/j.bbrc.2005.12.099;
Hunker C.M., Galvis A., Kruk I., Giambini H., Veisaga M.L.,
Barbieri M.A.;
"Rab5-activating protein 6, a novel endosomal protein with a role in
endocytosis.";
Biochem. Biophys. Res. Commun. 340:967-975(2006).
[19]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[20]
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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
INTERACTION WITH CLN5, AND SUBCELLULAR LOCATION.
PubMed=22431521; DOI=10.1128/MCB.06726-11;
Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
"The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in
endosomal sorting.";
Mol. Cell. Biol. 32:1855-1866(2012).
[23]
FUNCTION.
PubMed=22660413; DOI=10.1038/ncb2502;
Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G.,
Geeraerts A., Ivarsson Y., Depoortere F., Coomans C., Vermeiren E.,
Zimmermann P., David G.;
"Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
Nat. Cell Biol. 14:677-685(2012).
[24]
INTERACTION WITH GDI1, AND SUBCELLULAR LOCATION.
PubMed=23815289; DOI=10.3109/09687688.2013.818725;
Kirsten M.L., Baron R.A., Seabra M.C., Ces O.;
"Rab1a and Rab5a preferentially bind to binary lipid compositions with
higher stored curvature elastic energy.";
Mol. Membr. Biol. 30:303-314(2013).
[25]
SUBCELLULAR LOCATION, AND INTERACTION WITH OCRL.
PubMed=25869668; DOI=10.1083/jcb.201409064;
Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
De Camilli P.;
"Sac2/INPP5F is an inositol 4-phosphatase that functions in the
endocytic pathway.";
J. Cell Biol. 209:85-95(2015).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=12433916; DOI=10.1074/jbc.M211042200;
Zhu G., Liu J., Terzyan S., Zhai P., Li G., Zhang X.C.;
"High resolution crystal structures of human Rab5a and five mutants
with substitutions in the catalytically important phosphate-binding
loop.";
J. Biol. Chem. 278:2452-2460(2003).
[28]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP
ANALOG.
PubMed=14684892;
Terzyan S., Zhu G., Li G., Zhang X.C.;
"Refinement of the structure of human Rab5a GTPase domain at 1.05 A
resolution.";
Acta Crystallogr. D 60:54-60(2004).
[29]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-184 IN COMPLEX WITH GTP
ANALOG; GDP AND RABEP1, FUNCTION, INTERACTION WITH RABEP1, AND
MUTAGENESIS OF PHE-57; TRP-74; GLN-79; TYR-82; TYR-89; LYS-116 AND
ARG-120.
PubMed=15378032; DOI=10.1038/nsmb832;
Zhu G., Zhai P., Liu J., Terzyan S., Li G., Zhang X.C.;
"Structural basis of Rab5-Rabaptin5 interaction in endocytosis.";
Nat. Struct. Mol. Biol. 11:975-983(2004).
[30]
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 16-183 OF MUTANT LEU-79 IN
COMPLEX WITH EEA1, AND INTERACTION WITH EEA1.
PubMed=20534488; DOI=10.1073/pnas.1000843107;
Mishra A., Eathiraj S., Corvera S., Lambright D.G.;
"Structural basis for Rab GTPase recognition and endosome tethering by
the C2H2 zinc finger of early endosomal autoantigen 1 (EEA1).";
Proc. Natl. Acad. Sci. U.S.A. 107:10866-10871(2010).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different sets of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion. RAB5A is required for the fusion of plasma
membranes and early endosomes (PubMed:10818110, PubMed:14617813,
PubMed:16410077, PubMed:15378032). Contributes to the regulation
of filopodia extension (PubMed:14978216). Required for the
exosomal release of SDCBP, CD63, PDCD6IP and syndecan
(PubMed:22660413). Regulates maturation of apoptotic cell-
containing phagosomes, probably downstream of DYN2 and PIK3C3 (By
similarity). {ECO:0000250|UniProtKB:Q9CQD1,
ECO:0000269|PubMed:10818110, ECO:0000269|PubMed:14617813,
ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:16410077, ECO:0000269|PubMed:22660413}.
-!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange
factors (GEFs) which promote the exchange of bound GDP for free
GTP.
-!- SUBUNIT: Interacts with SGSM1 and SGSM3 (By similarity). Interacts
with PIK3CB (By similarity). Interacts with GDI1; this promotes
dissociation from membranes (PubMed:23815289). Interacts with EEA1
(PubMed:10491193, PubMed:20534488). Interacts with RIN1 and
GAPVD1, which regulate its pathway, probably by acting as a GEF
(PubMed:11703925, PubMed:16410077). Interacts with RINL. Interacts
with ALS2CL, SUN2, ZFYVE20 and RUFY1 (PubMed:10818110,
PubMed:11062261, PubMed:15388334, PubMed:14617813,
PubMed:16034420). Interacts with RABEP1; one RABEP1 homodimer
binds two RAB5A chains, but at opposite sides of the dimer
(PubMed:15378032). Interacts with OCRL (PubMed:25869668).
Interacts with INPP5F. May be a component of a complex composed of
RAB5A, DYN2 and PIK3C3 (By similarity). Does not interact with
BLOC-3 complex (heterodimer of HPS1 and HPS4) (By similarity).
Interacts with CLN5 (PubMed:22431521).
{ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:Q9CQD1,
ECO:0000269|PubMed:10491193, ECO:0000269|PubMed:10818110,
ECO:0000269|PubMed:11062261, ECO:0000269|PubMed:11703925,
ECO:0000269|PubMed:14617813, ECO:0000269|PubMed:14684892,
ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:15388334,
ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:16410077,
ECO:0000269|PubMed:20534488, ECO:0000269|PubMed:22431521,
ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:25869668}.
-!- INTERACTION:
Q96Q42:ALS2; NbExp=2; IntAct=EBI-399437, EBI-1044902;
Q9P2R3:ANKFY1; NbExp=2; IntAct=EBI-399437, EBI-2513908;
Q9UKG1:APPL1; NbExp=20; IntAct=EBI-399437, EBI-741243;
Q15075:EEA1; NbExp=4; IntAct=EBI-399437, EBI-298113;
Q01968:OCRL; NbExp=11; IntAct=EBI-399437, EBI-6148898;
P23727:PIK3R1 (xeno); NbExp=5; IntAct=EBI-399437, EBI-520244;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23815289};
Lipid-anchor {ECO:0000305|PubMed:7991565}; Cytoplasmic side
{ECO:0000250|UniProtKB:P18066}. Early endosome membrane
{ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:25869668}; Lipid-
anchor {ECO:0000305|PubMed:7991565}. Melanosome
{ECO:0000269|PubMed:17081065}. Cytoplasmic vesicle
{ECO:0000269|PubMed:10818110}. Cell projection, ruffle
{ECO:0000250|UniProtKB:P18066}. Membrane
{ECO:0000269|PubMed:23815289}. Cytoplasm, cytosol. Cytoplasmic
vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9CQD1}.
Endosome membrane {ECO:0000269|PubMed:22431521}. Note=Enriched in
stage I melanosomes (PubMed:17081065). Alternates between
membrane-bound and cytosolic forms (Probable).
{ECO:0000269|PubMed:17081065, ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P20339-1; Sequence=Displayed;
Name=2;
IsoId=P20339-2; Sequence=VSP_055830;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; M28215; AAA60245.1; -; mRNA.
EMBL; AF464088; AAO15677.1; -; mRNA.
EMBL; AF498936; AAM21084.1; -; mRNA.
EMBL; AK295992; BAG58767.1; -; mRNA.
EMBL; AK312618; BAG35504.1; -; mRNA.
EMBL; CR536492; CAG38731.1; -; mRNA.
EMBL; AC097635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64301.1; -; Genomic_DNA.
EMBL; BC001267; AAH01267.1; -; mRNA.
EMBL; BC018288; AAH18288.1; -; mRNA.
CCDS; CCDS2633.1; -. [P20339-1]
CCDS; CCDS77710.1; -. [P20339-2]
PIR; F34323; F34323.
RefSeq; NP_001278977.1; NM_001292048.1. [P20339-2]
RefSeq; NP_004153.2; NM_004162.4. [P20339-1]
UniGene; Hs.475663; -.
PDB; 1N6H; X-ray; 1.51 A; A=15-184.
PDB; 1N6I; X-ray; 1.60 A; A=15-184.
PDB; 1N6K; X-ray; 1.55 A; A=15-184.
PDB; 1N6L; X-ray; 1.60 A; A=15-184.
PDB; 1N6N; X-ray; 1.60 A; A=15-184.
PDB; 1N6O; X-ray; 1.80 A; A=15-184.
PDB; 1N6P; X-ray; 1.54 A; A=15-184.
PDB; 1N6R; X-ray; 1.55 A; A=15-184.
PDB; 1R2Q; X-ray; 1.05 A; A=15-184.
PDB; 1TU3; X-ray; 2.31 A; A/B/C/D/E=15-184.
PDB; 1TU4; X-ray; 2.20 A; A/B/C/D=15-184.
PDB; 3MJH; X-ray; 2.03 A; A/C=16-183.
PDB; 4Q9U; X-ray; 4.62 A; B/F=15-184.
PDBsum; 1N6H; -.
PDBsum; 1N6I; -.
PDBsum; 1N6K; -.
PDBsum; 1N6L; -.
PDBsum; 1N6N; -.
PDBsum; 1N6O; -.
PDBsum; 1N6P; -.
PDBsum; 1N6R; -.
PDBsum; 1R2Q; -.
PDBsum; 1TU3; -.
PDBsum; 1TU4; -.
PDBsum; 3MJH; -.
PDBsum; 4Q9U; -.
ProteinModelPortal; P20339; -.
SMR; P20339; -.
BioGrid; 111806; 121.
CORUM; P20339; -.
DIP; DIP-380N; -.
IntAct; P20339; 77.
MINT; P20339; -.
STRING; 9606.ENSP00000273047; -.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
DrugBank; DB02467; L-methionine (S)-S-oxide.
iPTMnet; P20339; -.
PhosphoSitePlus; P20339; -.
SwissPalm; P20339; -.
BioMuta; RAB5A; -.
DMDM; 1346958; -.
EPD; P20339; -.
PaxDb; P20339; -.
PeptideAtlas; P20339; -.
PRIDE; P20339; -.
ProteomicsDB; 53751; -.
TopDownProteomics; P20339-1; -. [P20339-1]
DNASU; 5868; -.
Ensembl; ENST00000273047; ENSP00000273047; ENSG00000144566. [P20339-1]
Ensembl; ENST00000422242; ENSP00000411941; ENSG00000144566. [P20339-2]
GeneID; 5868; -.
KEGG; hsa:5868; -.
UCSC; uc003cbn.4; human. [P20339-1]
CTD; 5868; -.
DisGeNET; 5868; -.
EuPathDB; HostDB:ENSG00000144566.10; -.
GeneCards; RAB5A; -.
HGNC; HGNC:9783; RAB5A.
HPA; CAB004567; -.
HPA; HPA049354; -.
MIM; 179512; gene.
neXtProt; NX_P20339; -.
OpenTargets; ENSG00000144566; -.
PharmGKB; PA34143; -.
eggNOG; KOG0092; Eukaryota.
eggNOG; ENOG410YCCP; LUCA.
GeneTree; ENSGT00940000154337; -.
HOGENOM; HOG000233968; -.
HOVERGEN; HBG009351; -.
InParanoid; P20339; -.
KO; K07887; -.
OMA; GKDACNC; -.
OrthoDB; EOG091G0HKN; -.
PhylomeDB; P20339; -.
TreeFam; TF300199; -.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8873719; RAB geranylgeranylation.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; P20339; -.
ChiTaRS; RAB5A; human.
EvolutionaryTrace; P20339; -.
GeneWiki; RAB5A; -.
GenomeRNAi; 5868; -.
PRO; PR:P20339; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144566; Expressed in 236 organ(s), highest expression level in substantia nigra.
CleanEx; HS_RAB5A; -.
ExpressionAtlas; P20339; baseline and differential.
Genevisible; P20339; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IBA:GO_Central.
GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
GO; GO:0043679; C:axon terminus; ISS:ParkinsonsUK-UCL.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0098559; C:cytoplasmic side of early endosome membrane; IMP:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
GO; GO:0005768; C:endosome; ISS:ParkinsonsUK-UCL.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0098842; C:postsynaptic early endosome; IBA:GO_Central.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0036477; C:somatodendritic compartment; IDA:ParkinsonsUK-UCL.
GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0032482; P:Rab protein signal transduction; IBA:GO_Central.
GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:2000785; P:regulation of autophagosome assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
GO; GO:0051036; P:regulation of endosome size; IMP:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IBA:GO_Central.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:ParkinsonsUK-UCL.
GO; GO:0036465; P:synaptic vesicle recycling; IDA:ParkinsonsUK-UCL.
GO; GO:0045056; P:transcytosis; IMP:ARUK-UCL.
GO; GO:0039694; P:viral RNA genome replication; IMP:ParkinsonsUK-UCL.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51419; RAB; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
Endosome; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
Phagocytosis; Prenylation; Protein transport; Reference proteome;
Transport.
CHAIN 1 215 Ras-related protein Rab-5A.
/FTId=PRO_0000121104.
NP_BIND 27 35 GTP. {ECO:0000244|PDB:1N6H,
ECO:0000244|PDB:1N6L,
ECO:0000244|PDB:1N6N,
ECO:0000244|PDB:1N6O,
ECO:0000244|PDB:1N6P,
ECO:0000244|PDB:1N6R,
ECO:0000244|PDB:1R2Q,
ECO:0000244|PDB:1TU3,
ECO:0000244|PDB:3MJH,
ECO:0000269|PubMed:12433916,
ECO:0000269|PubMed:14684892,
ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:20534488}.
NP_BIND 46 52 GTP. {ECO:0000244|PDB:1N6H,
ECO:0000244|PDB:1N6L,
ECO:0000244|PDB:1N6N,
ECO:0000244|PDB:1N6O,
ECO:0000244|PDB:1N6P,
ECO:0000244|PDB:1N6R,
ECO:0000244|PDB:1R2Q,
ECO:0000244|PDB:1TU3,
ECO:0000244|PDB:3MJH,
ECO:0000269|PubMed:12433916,
ECO:0000269|PubMed:14684892,
ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:20534488}.
NP_BIND 75 79 GTP. {ECO:0000244|PDB:1N6H,
ECO:0000244|PDB:1N6L,
ECO:0000244|PDB:1N6N,
ECO:0000244|PDB:1N6O,
ECO:0000244|PDB:1N6P,
ECO:0000244|PDB:1N6R,
ECO:0000244|PDB:1R2Q,
ECO:0000244|PDB:1TU3,
ECO:0000244|PDB:3MJH,
ECO:0000269|PubMed:12433916,
ECO:0000269|PubMed:14684892,
ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:20534488}.
NP_BIND 133 136 GTP. {ECO:0000244|PDB:1N6H,
ECO:0000244|PDB:1N6L,
ECO:0000244|PDB:1N6N,
ECO:0000244|PDB:1N6O,
ECO:0000244|PDB:1N6P,
ECO:0000244|PDB:1N6R,
ECO:0000244|PDB:1R2Q,
ECO:0000244|PDB:1TU3,
ECO:0000244|PDB:3MJH,
ECO:0000269|PubMed:12433916,
ECO:0000269|PubMed:14684892,
ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:20534488}.
NP_BIND 163 165 GTP. {ECO:0000244|PDB:1N6H,
ECO:0000244|PDB:1N6L,
ECO:0000244|PDB:1N6N,
ECO:0000244|PDB:1N6O,
ECO:0000244|PDB:1N6P,
ECO:0000244|PDB:1N6R,
ECO:0000244|PDB:1R2Q,
ECO:0000244|PDB:1TU3,
ECO:0000244|PDB:3MJH,
ECO:0000269|PubMed:12433916,
ECO:0000269|PubMed:14684892,
ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:20534488}.
MOTIF 49 57 Effector region. {ECO:0000250}.
LIPID 212 212 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:7991565}.
LIPID 213 213 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:7991565}.
VAR_SEQ 55 68 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055830.
MUTAGEN 54 54 G->Q: Strongly decreases ZFYVE20 binding
affinity. {ECO:0000269|PubMed:16034420}.
MUTAGEN 56 56 A->E: Strongly decreases ZFYVE20 binding
affinity. {ECO:0000269|PubMed:16034420}.
MUTAGEN 57 57 F->A: Strongly decreases RABEP1 and
ZFYVE20 binding affinity.
{ECO:0000269|PubMed:15378032,
ECO:0000269|PubMed:16034420}.
MUTAGEN 74 74 W->A: Strongly decreases RABEP1 binding
affinity. {ECO:0000269|PubMed:15378032}.
MUTAGEN 79 79 Q->L: Loss of GTPase activity. Does not
inhibit filopodia formation.
{ECO:0000269|PubMed:14978216,
ECO:0000269|PubMed:15378032}.
MUTAGEN 82 82 Y->A: Strongly decreases RABEP1 binding
affinity. Impairs endosome fusion.
{ECO:0000269|PubMed:15378032}.
MUTAGEN 89 89 Y->A: Strongly decreases RABEP1 binding
affinity. {ECO:0000269|PubMed:15378032}.
MUTAGEN 116 116 K->E: No effect on RABEP1 binding
affinity. {ECO:0000269|PubMed:15378032}.
MUTAGEN 120 120 R->E: No effect on RABEP1 binding
affinity. {ECO:0000269|PubMed:15378032}.
CONFLICT 81 81 R -> G (in Ref. 1; AAA60245).
{ECO:0000305}.
CONFLICT 197 197 R -> G (in Ref. 1; AAA60245).
{ECO:0000305}.
STRAND 17 26 {ECO:0000244|PDB:1R2Q}.
STRAND 28 32 {ECO:0000244|PDB:1N6K}.
HELIX 33 42 {ECO:0000244|PDB:1R2Q}.
STRAND 53 64 {ECO:0000244|PDB:1R2Q}.
STRAND 67 76 {ECO:0000244|PDB:1R2Q}.
HELIX 80 85 {ECO:0000244|PDB:1R2Q}.
HELIX 86 90 {ECO:0000244|PDB:1R2Q}.
STRAND 94 101 {ECO:0000244|PDB:1R2Q}.
HELIX 105 121 {ECO:0000244|PDB:1R2Q}.
STRAND 127 133 {ECO:0000244|PDB:1R2Q}.
HELIX 135 140 {ECO:0000244|PDB:1R2Q}.
HELIX 145 154 {ECO:0000244|PDB:1R2Q}.
STRAND 158 161 {ECO:0000244|PDB:1R2Q}.
TURN 164 166 {ECO:0000244|PDB:1R2Q}.
HELIX 170 179 {ECO:0000244|PDB:1R2Q}.
SEQUENCE 215 AA; 23659 MW; EC03DDF96BBEF821 CRC64;
MASRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ
TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR
QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK
LPKNEPQNPG ANSARGRGVD LTEPTQPTRN QCCSN


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