RAB35_HUMAN
ID RAB35_HUMAN Reviewed; 201 AA.
AC Q15286; B2R6E0; B4E390;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Ras-related protein Rab-35;
DE AltName: Full=GTP-binding protein RAY;
DE AltName: Full=Ras-related protein Rab-1C;
GN Name=RAB35; Synonyms=RAB1C, RAY;
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] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=7811277; DOI=10.1006/bbrc.1994.2889;
RA Zhu A.X., Zhao Y., Flier J.S.;
RT "Molecular cloning of two small GTP-binding proteins from human skeletal
RT muscle.";
RL Biochem. Biophys. Res. Commun. 205:1875-1882(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Tongue, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-22 AND GLN-67.
RX PubMed=16950109; DOI=10.1016/j.cub.2006.07.020;
RA Kouranti I., Sachse M., Arouche N., Goud B., Echard A.;
RT "Rab35 regulates an endocytic recycling pathway essential for the terminal
RT steps of cytokinesis.";
RL Curr. Biol. 16:1719-1725(2006).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [11]
RP ACTIVITY REGULATION, AND INTERACTION WITH DENND1A; DENND1B AND DENND1C.
RX PubMed=20154091; DOI=10.1074/jbc.m109.050930;
RA Marat A.L., McPherson P.S.;
RT "The connecdenn family, Rab35 guanine nucleotide exchange factors
RT interfacing with the clathrin machinery.";
RL J. Biol. Chem. 285:10627-10637(2010).
RN [12]
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 [13]
RP INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION AT TYR-77, AND
RP PHOSPHORYLATION AT SER-75.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [14]
RP INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION, AND
RP PHOSPHORYLATION AT SER-75.
RX PubMed=22307087; DOI=10.1038/emboj.2012.16;
RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S.;
RT "Reversible phosphocholination of Rab proteins by Legionella pneumophila
RT effector proteins.";
RL EMBO J. 31:1774-1784(2012).
RN [15]
RP FUNCTION IN ENDOCYTOSIS, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP MICALL1.
RX PubMed=21951725; DOI=10.1111/j.1600-0854.2011.01294.x;
RA Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.;
RT "MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6
RT with Rab8a.";
RL Traffic 13:82-93(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP INTERACTION WITH GDI1; GDI2; CHM AND CHML, PHOSPHORYLATION AT THR-72, AND
RP MUTAGENESIS OF THR-72.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-180 IN COMPLEX WITH DENND1B.
RX PubMed=22065758; DOI=10.1073/pnas.1110415108;
RA Wu X., Bradley M.J., Cai Y., Kummel D., De La Cruz E.M., Barr F.A.,
RA Reinisch K.M.;
RT "Insights regarding guanine nucleotide exchange from the structure of a
RT DENN-domain protein complexed with its Rab GTPase substrate.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18672-18677(2011).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in the
CC process of endocytosis and is an essential rate-limiting regulator of
CC the fast recycling pathway back to the plasma membrane. During
CC cytokinesis, required for the postfurrowing terminal steps, namely for
CC intercellular bridge stability and abscission, possibly by controlling
CC phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at
CC the intercellular bridge. May indirectly regulate neurite outgrowth.
CC Together with TBC1D13 may be involved in regulation of insulin-induced
CC glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane
CC in adipocytes. {ECO:0000250|UniProtKB:Q6PHN9,
CC ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP)
CC (PubMed:20154091). That Rab is activated by the guanine exchange
CC factors DENND1A, DENND1B and DENND1C (PubMed:20154091).
CC {ECO:0000269|PubMed:20154091}.
CC -!- SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-dependent
CC manner (PubMed:20154091, PubMed:22065758). Interacts with DENND1C; weak
CC interaction which is nucleotide-independent (PubMed:20154091).
CC Interacts (GTP-bound form) with ACAP2 and MICALL1; the interaction is
CC direct and probably recruits ACAP2 and MICALL1 to membranes
CC (PubMed:21951725). Interacts with EHD1; the interaction is indirect
CC through MICALL1 and probably recruits EHD1 to membranes (By
CC similarity). Interacts with GDI1, GDI2, CHM and CHML; phosphorylation
CC at Thr-72 disrupts these interactions (PubMed:29125462).
CC {ECO:0000250|UniProtKB:Q6PHN9, ECO:0000269|PubMed:20154091,
CC ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:22065758,
CC ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC Q15286; P50570-2: DNM2; NbExp=3; IntAct=EBI-722275, EBI-10968534;
CC Q15286; P42858: HTT; NbExp=3; IntAct=EBI-722275, EBI-466029;
CC Q15286; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-722275, EBI-1055254;
CC Q15286; Q8N3F8: MICALL1; NbExp=2; IntAct=EBI-722275, EBI-1056885;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16950109,
CC ECO:0000269|PubMed:21951725}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:16950109}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:16950109}. Endosome
CC {ECO:0000269|PubMed:16950109, ECO:0000269|PubMed:21951725}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=Present on sorting endosomes and
CC recycling endosome tubules (PubMed:16950109). Tends to be enriched in
CC PIP2-positive cell membrane domains (PubMed:16950109). During mitosis,
CC associated with the plasma membrane and present at the ingressing
CC furrow during early cytokinesis as well as at the intercellular bridge
CC later during cytokinesis (PubMed:16950109). Identified in stage I to
CC stage IV melanosomes (PubMed:17081065). {ECO:0000269|PubMed:16950109,
CC ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15286-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15286-2; Sequence=VSP_042918;
CC -!- PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2
CC region and leads to moderate inactivation of the GTPase activity. It
CC appears to prolong the lifetime of the GTP state of RAB1B by
CC restricting access of GTPase effectors to switch 2 and blocking
CC effector-stimulated GTP hydrolysis, thereby rendering RAB35
CC constitutively active. {ECO:0000269|PubMed:21822290,
CC ECO:0000269|PubMed:22307087}.
CC -!- PTM: Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and GTP-
CC bound forms can be phosphocholinated. Phosphocholination inhibits the
CC GEF activity of DENND1A.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X79781; CAA56177.1; -; mRNA.
DR EMBL; AF498960; AAM21108.1; -; mRNA.
DR EMBL; BT020024; AAV38827.1; -; mRNA.
DR EMBL; CR536486; CAG38725.1; -; mRNA.
DR EMBL; CR541683; CAG46484.1; -; mRNA.
DR EMBL; AK304620; BAG65402.1; -; mRNA.
DR EMBL; AK312538; BAG35437.1; -; mRNA.
DR EMBL; AC004812; AAC83182.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW98163.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW98164.1; -; Genomic_DNA.
DR EMBL; BC015931; AAH15931.1; -; mRNA.
DR CCDS; CCDS41846.1; -. [Q15286-1]
DR CCDS; CCDS53836.1; -. [Q15286-2]
DR PIR; JC2488; JC2488.
DR RefSeq; NP_001161078.1; NM_001167606.1. [Q15286-2]
DR RefSeq; NP_006852.1; NM_006861.6. [Q15286-1]
DR PDB; 3TW8; X-ray; 2.10 A; B/D=1-180.
DR PDB; 6EKK; X-ray; 1.82 A; C/D=3-178.
DR PDB; 6IF2; X-ray; 2.40 A; B=1-180.
DR PDB; 6IF3; X-ray; 1.50 A; B=1-180.
DR PDBsum; 3TW8; -.
DR PDBsum; 6EKK; -.
DR PDBsum; 6IF2; -.
DR PDBsum; 6IF3; -.
DR AlphaFoldDB; Q15286; -.
DR SMR; Q15286; -.
DR BioGRID; 116211; 554.
DR IntAct; Q15286; 44.
DR MINT; Q15286; -.
DR STRING; 9606.ENSP00000229340; -.
DR GlyGen; Q15286; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15286; -.
DR MetOSite; Q15286; -.
DR PhosphoSitePlus; Q15286; -.
DR SwissPalm; Q15286; -.
DR BioMuta; RAB35; -.
DR DMDM; 3024525; -.
DR EPD; Q15286; -.
DR jPOST; Q15286; -.
DR MassIVE; Q15286; -.
DR MaxQB; Q15286; -.
DR PaxDb; Q15286; -.
DR PeptideAtlas; Q15286; -.
DR PRIDE; Q15286; -.
DR ProteomicsDB; 60512; -. [Q15286-1]
DR ProteomicsDB; 60513; -. [Q15286-2]
DR TopDownProteomics; Q15286-1; -. [Q15286-1]
DR TopDownProteomics; Q15286-2; -. [Q15286-2]
DR Antibodypedia; 45490; 308 antibodies from 32 providers.
DR DNASU; 11021; -.
DR Ensembl; ENST00000229340.10; ENSP00000229340.5; ENSG00000111737.12. [Q15286-1]
DR Ensembl; ENST00000534951.5; ENSP00000441883.1; ENSG00000111737.12. [Q15286-2]
DR GeneID; 11021; -.
DR KEGG; hsa:11021; -.
DR MANE-Select; ENST00000229340.10; ENSP00000229340.5; NM_006861.7; NP_006852.1.
DR UCSC; uc001txm.2; human. [Q15286-1]
DR CTD; 11021; -.
DR DisGeNET; 11021; -.
DR GeneCards; RAB35; -.
DR HGNC; HGNC:9774; RAB35.
DR HPA; ENSG00000111737; Low tissue specificity.
DR MIM; 604199; gene.
DR neXtProt; NX_Q15286; -.
DR OpenTargets; ENSG00000111737; -.
DR PharmGKB; PA34127; -.
DR VEuPathDB; HostDB:ENSG00000111737; -.
DR eggNOG; KOG0079; Eukaryota.
DR GeneTree; ENSGT00940000158557; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q15286; -.
DR OMA; FMAITRQ; -.
DR OrthoDB; 1173342at2759; -.
DR PhylomeDB; Q15286; -.
DR TreeFam; TF105954; -.
DR PathwayCommons; Q15286; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SABIO-RK; Q15286; -.
DR SignaLink; Q15286; -.
DR BioGRID-ORCS; 11021; 67 hits in 1091 CRISPR screens.
DR ChiTaRS; RAB35; human.
DR GeneWiki; RAB35; -.
DR GenomeRNAi; 11021; -.
DR Pharos; Q15286; Tbio.
DR PRO; PR:Q15286; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15286; protein.
DR Bgee; ENSG00000111737; Expressed in cortical plate and 182 other tissues.
DR ExpressionAtlas; Q15286; baseline and differential.
DR Genevisible; Q15286; HS.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0031253; C:cell projection membrane; IDA:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
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:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0048227; P:plasma membrane to endosome transport; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; 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:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04110; Rab35; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041815; Rab35.
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; Alternative splicing; Cell membrane; Coated pit;
KW Cytoplasmic vesicle; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-35"
FT /id="PRO_0000121245"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 150..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 72
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="O-(2-cholinephosphoryl)serine"
FT /evidence="ECO:0000305|PubMed:21822290,
FT ECO:0000305|PubMed:22307087"
FT MOD_RES 77
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000305|PubMed:21822290"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 118..201
FT /note="VGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVL
FT RAKKDNLAKQQQQQQNDVVKLTKNSKRKKRCC -> DVQLHHGAGPPSKERQPGKTAAA
FT TTERCGEAHEEQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042918"
FT MUTAGEN 22
FT /note="S->N: Destabilization of the intercellular bridge
FT during cytokinesis. Strong reduction in fast recycling."
FT /evidence="ECO:0000269|PubMed:16950109"
FT MUTAGEN 67
FT /note="Q->L: Loss of GTPase activity. Increased fast
FT recycling."
FT /evidence="ECO:0000269|PubMed:16950109"
FT MUTAGEN 72
FT /note="T->A: Loss of phosphorylation. No effect on binding
FT to GDI1 and GDI2."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 72
FT /note="T->E: Phosphomimetic mutant. Loss of binding to
FT GDI1, GDI2, CHM and CHML."
FT /evidence="ECO:0000269|PubMed:29125462"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6EKK"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:6IF3"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:6IF3"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:6IF3"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:6IF3"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6IF3"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:6IF3"
SQ SEQUENCE 201 AA; 23025 MW; 31EB15D6D42E076E CRC64;
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ
IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN
KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ
QQQQNDVVKL TKNSKRKKRC C
