RAB4A_HUMAN
ID RAB4A_HUMAN Reviewed; 218 AA.
AC P20338; Q5T7P7; Q9BQ44;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Ras-related protein Rab-4A;
DE EC=3.6.5.2 {ECO:0000269|PubMed:15907487, ECO:0000269|PubMed:16034420};
GN Name=RAB4A; Synonyms=RAB4;
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].
RX PubMed=2501306; DOI=10.1016/s0021-9258(18)63872-4;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "The human Rab genes encode a family of GTP-binding proteins related to
RT yeast YPT1 and SEC4 products involved in secretion.";
RL J. Biol. Chem. 264:12394-12401(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16935861; DOI=10.1074/jbc.m606301200;
RA Nagy G., Ward J., Mosser D.D., Koncz A., Gergely P. Jr., Stancato C.,
RA Qian Y., Fernandez D., Niland B., Grossman C.E., Telarico T., Banki K.,
RA Perl A.;
RT "Regulation of CD4 expression via recycling by HRES-1/RAB4 controls
RT susceptibility to HIV infection.";
RL J. Biol. Chem. 281:34574-34591(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 PHOSPHORYLATION BY CDK1.
RX PubMed=1902553; DOI=10.1038/350715a0;
RA Bailly E., McCaffrey M., Touchot N., Zahraoui A., Goud B., Bornens M.;
RT "Phosphorylation of two small GTP-binding proteins of the Rab family by
RT p34cdc2.";
RL Nature 350:715-718(1991).
RN [9]
RP PHOSPHORYLATION AT SER-204 BY CDK1, AND SUBCELLULAR LOCATION.
RX PubMed=1425574;
RA van der Sluijs P., Hull M., Huber L.A., Male P., Goud B., Mellman I.;
RT "Reversible phosphorylation-dephosphorylation determines the localization
RT of rab4 during the cell cycle.";
RL EMBO J. 11:4379-4389(1992).
RN [10]
RP INTERACTION WITH RABEP1.
RX PubMed=10698684; DOI=10.1042/bj3460593;
RA Nagelkerken B., van Anken E., van Raak M., Gerez L., Mohrmann K.,
RA van Uden N., Holthuizen J., Pelkmans L., van der Sluijs P.;
RT "Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to
RT perinuclear recycling vesicles.";
RL Biochem. J. 346:593-601(2000).
RN [11]
RP INTERACTION WITH RAB11FIP1.
RC TISSUE=Cervix carcinoma;
RX PubMed=11786538; DOI=10.1074/jbc.m108665200;
RA Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B.,
RA Bucci C., McCaffrey M.W.;
RT "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein.";
RL J. Biol. Chem. 277:12190-12199(2002).
RN [12]
RP INTERACTION WITH ZFYVE20.
RX PubMed=11788822; DOI=10.1038/ncb744;
RA de Renzis S., Soennichsen B., Zerial M.;
RT "Divalent Rab effectors regulate the sub-compartmental organization and
RT sorting of early endosomes.";
RL Nat. Cell Biol. 4:124-133(2002).
RN [13]
RP INTERACTION WITH RAB11FIP1.
RX PubMed=15280022; DOI=10.1016/j.febslet.2004.06.068;
RA Lindsay A.J., McCaffrey M.W.;
RT "Characterisation of the Rab binding properties of Rab coupling protein
RT (RCP) by site-directed mutagenesis.";
RL FEBS Lett. 571:86-92(2004).
RN [14]
RP INTERACTION WITH RUFY1.
RX PubMed=14617813; DOI=10.1091/mbc.e03-05-0343;
RA Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
RA van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
RT "Rabip4' is an effector of rab5 and rab4 and regulates transport through
RT early endosomes.";
RL Mol. Biol. Cell 15:611-624(2004).
RN [15]
RP INTERACTION WITH NDRG1.
RX PubMed=17786215; DOI=10.1371/journal.pone.0000844;
RA Kachhap S.K., Faith D., Qian D.Z., Shabbeer S., Galloway N.L., Pili R.,
RA Denmeade S.R., DeMarzo A.M., Carducci M.A.;
RT "The N-Myc down regulated Gene1 (NDRG1) is a Rab4a effector involved in
RT vesicular recycling of E-cadherin.";
RL PLoS ONE 2:E844-E844(2007).
RN [16]
RP INTERACTION WITH GRIPAP1; RABEP1 AND RBSN.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [19]
RP FUNCTION, AND INTERACTION WITH RABEP2.
RX PubMed=29425100; DOI=10.1074/jbc.m117.812172;
RA Kofler N., Corti F., Rivera-Molina F., Deng Y., Toomre D., Simons M.;
RT "The Rab-effector protein RABEP2 regulates endosomal trafficking to mediate
RT vascular endothelial growth factor receptor-2 (VEGFR2)-dependent
RT signaling.";
RL J. Biol. Chem. 293:4805-4817(2018).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 6-189 IN COMPLEX WITH GTP ANALOG
RP AND GDP, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15907487; DOI=10.1016/j.febslet.2005.04.020;
RA Huber S.K., Scheidig A.J.;
RT "High resolution crystal structures of human Rab4a in its active and
RT inactive conformations.";
RL FEBS Lett. 579:2821-2829(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 7-177 IN COMPLEX WITH GTP,
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ZFYVE20, AND MUTAGENESIS OF
RP GLY-51.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
CC -!- FUNCTION: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state (PubMed:15907487, PubMed:16034420). Involved
CC in protein transport (PubMed:29425100). Plays a role in vesicular
CC traffic. Mediates VEGFR2 endosomal trafficking to enhance VEGFR2
CC signaling (PubMed:29425100). Acts as a regulator of platelet alpha-
CC granule release during activation and aggregation of platelets (By
CC similarity). {ECO:0000250|UniProtKB:P56371,
CC ECO:0000269|PubMed:15907487, ECO:0000269|PubMed:16034420,
CC ECO:0000269|PubMed:29425100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:15907487, ECO:0000269|PubMed:16034420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:15907487, ECO:0000269|PubMed:16034420};
CC -!- SUBUNIT: Interacts with SGSM1, SGSM2 and SGSM3 (By similarity).
CC Interacts with RAB11FIP1, RABEP1, ZFYVE20 and RUFY1 (PubMed:10698684,
CC PubMed:11786538, PubMed:11788822, PubMed:14617813, PubMed:15280022,
CC PubMed:16034420). Interacts (membrane-bound form) with NDRG1; the
CC interaction involves NDRG1 in vesicular recycling of E-cadherin
CC (PubMed:17786215). Interacts (in GTP-bound form) with GRIPAP1 (via N-
CC terminus) (PubMed:20098723). Interacts with RABEP1 and RBSN
CC (PubMed:20098723). Does not interact with HPS4 (By similarity).
CC Interacts with RABEP2; this interaction may mediate VEGFR2 cell surface
CC expression (PubMed:29425100). {ECO:0000250|UniProtKB:P56371,
CC ECO:0000269|PubMed:10698684, ECO:0000269|PubMed:11786538,
CC ECO:0000269|PubMed:11788822, ECO:0000269|PubMed:14617813,
CC ECO:0000269|PubMed:15280022, ECO:0000269|PubMed:15907487,
CC ECO:0000269|PubMed:16034420, ECO:0000269|PubMed:17786215,
CC ECO:0000269|PubMed:20098723, ECO:0000269|PubMed:29425100}.
CC -!- INTERACTION:
CC P20338; O00471: EXOC5; NbExp=6; IntAct=EBI-722284, EBI-949824;
CC P20338; Q8NEG0: FAM71C; NbExp=3; IntAct=EBI-722284, EBI-752049;
CC P20338; P31150: GDI1; NbExp=4; IntAct=EBI-722284, EBI-946999;
CC P20338; Q4V328: GRIPAP1; NbExp=4; IntAct=EBI-722284, EBI-717919;
CC P20338; Q8IYU2: HACE1; NbExp=3; IntAct=EBI-722284, EBI-308277;
CC P20338; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-722284, EBI-11954971;
CC P20338; Q15276: RABEP1; NbExp=3; IntAct=EBI-722284, EBI-447043;
CC P20338; Q9H1K0: RBSN; NbExp=4; IntAct=EBI-722284, EBI-1105310;
CC P20338; Q8N1B4: VPS52; NbExp=4; IntAct=EBI-722284, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:1425574}. Cytoplasm {ECO:0000269|PubMed:1425574}.
CC Early endosome membrane {ECO:0000250|UniProtKB:P05714}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P05714}. Recycling endosome
CC membrane {ECO:0000250|UniProtKB:P05714}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P05714}. Note=Generally associated with
CC membranes. Cytoplasmic when phosphorylated by CDK1.
CC {ECO:0000269|PubMed:1425574}.
CC -!- PTM: Phosphorylated by CDK1 kinase during mitosis.
CC {ECO:0000269|PubMed:1425574, ECO:0000269|PubMed:1902553}.
CC -!- PTM: Serotonylation of Gln-72 by TGM2 during activation and aggregation
CC of platelets leads to constitutive activation of GTPase activity.
CC {ECO:0000250|UniProtKB:P56371}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60244.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M28211; AAA60244.1; ALT_FRAME; mRNA.
DR EMBL; AY585832; AAT91347.1; -; mRNA.
DR EMBL; AF498934; AAM21082.1; -; mRNA.
DR EMBL; AK313807; BAG36543.1; -; mRNA.
DR EMBL; AL162595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69890.1; -; Genomic_DNA.
DR EMBL; BC002438; AAH02438.1; -; mRNA.
DR EMBL; BC004309; AAH04309.1; -; mRNA.
DR CCDS; CCDS31050.1; -.
DR PIR; E34323; E34323.
DR RefSeq; NP_001258927.1; NM_001271998.1.
DR RefSeq; NP_004569.2; NM_004578.3.
DR PDB; 1YU9; X-ray; 2.07 A; A=7-177.
DR PDB; 1Z0K; X-ray; 1.92 A; A/C=7-177.
DR PDB; 2BMD; X-ray; 1.80 A; A=6-189.
DR PDB; 2BME; X-ray; 1.57 A; A/B/C/D=6-189.
DR PDBsum; 1YU9; -.
DR PDBsum; 1Z0K; -.
DR PDBsum; 2BMD; -.
DR PDBsum; 2BME; -.
DR AlphaFoldDB; P20338; -.
DR SMR; P20338; -.
DR BioGRID; 111805; 382.
DR DIP; DIP-372N; -.
DR IntAct; P20338; 31.
DR MINT; P20338; -.
DR STRING; 9606.ENSP00000355651; -.
DR MoonDB; P20338; Predicted.
DR iPTMnet; P20338; -.
DR PhosphoSitePlus; P20338; -.
DR BioMuta; RAB4A; -.
DR DMDM; 460018296; -.
DR EPD; P20338; -.
DR jPOST; P20338; -.
DR MassIVE; P20338; -.
DR MaxQB; P20338; -.
DR PaxDb; P20338; -.
DR PeptideAtlas; P20338; -.
DR PRIDE; P20338; -.
DR ProteomicsDB; 53750; -.
DR Antibodypedia; 34673; 339 antibodies from 35 providers.
DR DNASU; 5867; -.
DR Ensembl; ENST00000366690.5; ENSP00000355651.4; ENSG00000168118.12.
DR GeneID; 5867; -.
DR KEGG; hsa:5867; -.
DR MANE-Select; ENST00000366690.5; ENSP00000355651.4; NM_004578.4; NP_004569.2.
DR UCSC; uc001hth.5; human.
DR CTD; 5867; -.
DR DisGeNET; 5867; -.
DR GeneCards; RAB4A; -.
DR HGNC; HGNC:9781; RAB4A.
DR HPA; ENSG00000168118; Low tissue specificity.
DR MIM; 179511; gene.
DR neXtProt; NX_P20338; -.
DR OpenTargets; ENSG00000168118; -.
DR PharmGKB; PA34141; -.
DR VEuPathDB; HostDB:ENSG00000168118; -.
DR eggNOG; KOG0086; Eukaryota.
DR GeneTree; ENSGT00940000157464; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P20338; -.
DR OMA; STQECGC; -.
DR OrthoDB; 1146851at2759; -.
DR PhylomeDB; P20338; -.
DR TreeFam; TF300032; -.
DR PathwayCommons; P20338; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8875656; MET receptor recycling.
DR SignaLink; P20338; -.
DR SIGNOR; P20338; -.
DR BioGRID-ORCS; 5867; 48 hits in 1081 CRISPR screens.
DR ChiTaRS; RAB4A; human.
DR EvolutionaryTrace; P20338; -.
DR GeneWiki; RAB4A; -.
DR GenomeRNAi; 5867; -.
DR Pharos; P20338; Tbio.
DR PRO; PR:P20338; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P20338; protein.
DR Bgee; ENSG00000168118; Expressed in lateral nuclear group of thalamus and 212 other tissues.
DR ExpressionAtlas; P20338; baseline and differential.
DR Genevisible; P20338; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04113; Rab4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041819; Rab4.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..218
FT /note="Ras-related protein Rab-4A"
FT /id="PRO_0000121093"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16034420"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16034420"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16034420"
FT BINDING 156..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16034420"
FT MOD_RES 72
FT /note="5-glutamyl serotonin"
FT /evidence="ECO:0000250|UniProtKB:P56371"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:1425574"
FT MOD_RES 218
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 216
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 51
FT /note="G->A: 10-fold decrease in ZFYVE20 binding affinity."
FT /evidence="ECO:0000269|PubMed:16034420"
FT MUTAGEN 51
FT /note="G->L: 10-fold decrease in ZFYVE20 binding affinity."
FT /evidence="ECO:0000269|PubMed:16034420"
FT CONFLICT 162
FT /note="N -> D (in Ref. 1; AAA60244)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> T (in Ref. 1; AAA60244)"
FT /evidence="ECO:0000305"
FT STRAND 11..21
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2BME"
FT STRAND 46..57
FT /evidence="ECO:0007829|PDB:2BME"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:2BME"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:2BME"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:2BME"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2BME"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2BME"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:2BME"
SQ SEQUENCE 218 AA; 24390 MW; 983D65E1162741B0 CRC64;
MSQTAMSETY DFLFKFLVIG NAGTGKSCLL HQFIEKKFKD DSNHTIGVEF GSKIINVGGK
YVKLQIWDTA GQERFRSVTR SYYRGAAGAL LVYDITSRET YNALTNWLTD ARMLASQNIV
IILCGNKKDL DADREVTFLE ASRFAQENEL MFLETSALTG ENVEEAFVQC ARKILNKIES
GELDPERMGS GIQYGDAALR QLRSPRRAQA PNAQECGC
