Full text data of RAB35
RAB35
(RAB1C, RAY)
[Confidence: high (present in two of the MS resources)]
Ras-related protein Rab-35 (GTP-binding protein RAY; Ras-related protein Rab-1C)
Ras-related protein Rab-35 (GTP-binding protein RAY; Ras-related protein Rab-1C)
hRBCD
IPI00300096
IPI00300096 Ras-related protein Rab-35 Ras-related protein Rab-35 membrane 1 n/a n/a n/a 1 1 n/a n/a n/a n/a 7 5 n/a 5 n/a 2 2 4 n/a n/a cytoplasmic and membrane associated n/a found at its expected molecular weight found at molecular weight
IPI00300096 Ras-related protein Rab-35 Ras-related protein Rab-35 membrane 1 n/a n/a n/a 1 1 n/a n/a n/a n/a 7 5 n/a 5 n/a 2 2 4 n/a n/a cytoplasmic and membrane associated n/a found at its expected molecular weight found at molecular weight
UniProt
Q15286
ID RAB35_HUMAN Reviewed; 201 AA.
AC Q15286; B2R6E0; B4E390;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 131.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT skeletal 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
RT sequenced by 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
RT 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT terminal steps of cytokinesis.";
RL Curr. Biol. 16:1719-1725(2006).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 ENZYME 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.,
RA Buerckstuemmer T., 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,
RP AND CHOLINEPHOSPHORYLATION 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 CHOLINEPHOSPHORYLATION.
RX PubMed=22307087; DOI=10.1038/emboj.2012.16;
RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A.,
RA Goody R.S.;
RT "Reversible phosphocholination of Rab proteins by Legionella
RT pneumophila 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
RT Arf6 with Rab8a.";
RL Traffic 13:82-93(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-180 IN COMPLEX WITH
RP 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
RT a 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
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different sets of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab is involved in the process of
CC endocytosis and is an essential rate-limiting regulator of the
CC fast recycling pathway back to the plasma membrane. During
CC cytokinesis, required for the postfurrowing terminal steps, namely
CC for intercellular bridge stability and abscission, possibly by
CC controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and
CC SEPT2 localization at the intercellular bridge. May indirectly
CC regulate neurite outgrowth.
CC -!- ENZYME REGULATION: Rab activation is generally mediated by a
CC guanine exchange factor (GEF), while inactivation through
CC hydrolysis of bound GTP is catalyzed by a GTPase activating
CC protein (GAP). That Rab is activated by the guanine exchange
CC factors DENND1A, DENND1B and DENND1C.
CC -!- SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-
CC dependent manner. Interacts with DENND1C; weak interaction which
CC is nucleotide-independent. Interacts (GTP-bound form) with ACAP2
CC and MICALL1; the interaction is direct and probably recruits ACAP2
CC and MICALL1 to membranes. Interacts with EHD1; the interaction is
CC indirect through MICALL1 and probably recruits EHD1 to membranes.
CC -!- INTERACTION:
CC Q8N3F8:MICALL1; NbExp=2; IntAct=EBI-722275, EBI-1056885;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential). Membrane, clathrin-coated pit. Cytoplasmic
CC vesicle, clathrin-coated vesicle. Endosome. Melanosome.
CC Note=Present on sorting endosomes and recycling endosome tubules.
CC Tends to be enriched in PIP2-positive cell membrane domains.
CC During mitosis, associated with the plasma membrane and present at
CC the ingressing furrow during early cytokinesis as well as at the
CC intercellular bridge later during cytokinesis. Identified in stage
CC I to stage IV melanosomes.
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 Note=No experimental confirmation available;
CC -!- PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the
CC switch 2 region and leads to moderate inactivation of the GTPase
CC activity. It appears to prolong the lifetime of the GTP state of
CC RAB1B by restricting access of GTPase effectors to switch 2 and
CC blocking effector-stimulated GTP hydrolysis, thereby rendering
CC RAB35 constitutively active.
CC -!- PTM: Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and
CC GTP-bound forms can be phosphocholinated. Phosphocholination
CC inhibits the GEF activity of DENND1A.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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 PIR; JC2488; JC2488.
DR RefSeq; NP_001161078.1; NM_001167606.1.
DR RefSeq; NP_006852.1; NM_006861.6.
DR UniGene; Hs.524788; -.
DR PDB; 3TW8; X-ray; 2.10 A; B/D=1-180.
DR PDBsum; 3TW8; -.
DR ProteinModelPortal; Q15286; -.
DR SMR; Q15286; 4-177.
DR IntAct; Q15286; 16.
DR MINT; MINT-1370578; -.
DR STRING; 9606.ENSP00000229340; -.
DR PhosphoSite; Q15286; -.
DR DMDM; 3024525; -.
DR PaxDb; Q15286; -.
DR PRIDE; Q15286; -.
DR DNASU; 11021; -.
DR Ensembl; ENST00000229340; ENSP00000229340; ENSG00000111737.
DR Ensembl; ENST00000534951; ENSP00000441883; ENSG00000111737.
DR GeneID; 11021; -.
DR KEGG; hsa:11021; -.
DR UCSC; uc001txm.2; human.
DR CTD; 11021; -.
DR GeneCards; GC12M120532; -.
DR HGNC; HGNC:9774; RAB35.
DR HPA; HPA054146; -.
DR MIM; 604199; gene.
DR neXtProt; NX_Q15286; -.
DR PharmGKB; PA34127; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q15286; -.
DR KO; K07876; -.
DR OMA; NRILVGN; -.
DR OrthoDB; EOG7VB2H4; -.
DR GeneWiki; RAB35; -.
DR GenomeRNAi; 11021; -.
DR NextBio; 41874; -.
DR PRO; PR:Q15286; -.
DR ArrayExpress; Q15286; -.
DR Bgee; Q15286; -.
DR CleanEx; HS_RAB35; -.
DR Genevestigator; Q15286; -.
DR GO; GO:0031253; C:cell projection membrane; IDA:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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; TAS:ProtInc.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS: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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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 Complete proteome; Cytoplasmic vesicle; Endosome; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1 201 Ras-related protein Rab-35.
FT /FTId=PRO_0000121245.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 120 123 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 75 75 O-(2-cholinephosphoryl)serine; by
FT Legionella AnkX (Probable).
FT MOD_RES 77 77 O-AMP-tyrosine; by Legionella DrrA
FT (Probable).
FT LIPID 200 200 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 201 201 S-geranylgeranyl cysteine (By
FT similarity).
FT VAR_SEQ 118 201 VGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVE
FT EMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKR
FT CC -> DVQLHHGAGPPSKERQPGKTAAATTERCGEAHEEQ
FT (in isoform 2).
FT /FTId=VSP_042918.
FT MUTAGEN 22 22 S->N: Destabilization of the
FT intercellular bridge during cytokinesis.
FT Strong reduction in fast recycling.
FT MUTAGEN 67 67 Q->L: Loss of GTPase activity. Increased
FT fast recycling.
FT STRAND 7 14
FT HELIX 21 28
FT TURN 38 40
FT STRAND 41 52
FT STRAND 55 64
FT HELIX 67 69
FT HELIX 75 78
FT STRAND 82 89
FT HELIX 93 109
FT STRAND 113 120
FT HELIX 125 127
FT HELIX 132 142
FT STRAND 146 148
FT TURN 151 154
FT HELIX 157 175
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
//
ID RAB35_HUMAN Reviewed; 201 AA.
AC Q15286; B2R6E0; B4E390;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 131.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT skeletal 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
RT sequenced by 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
RT 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT terminal steps of cytokinesis.";
RL Curr. Biol. 16:1719-1725(2006).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 ENZYME 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.,
RA Buerckstuemmer T., 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,
RP AND CHOLINEPHOSPHORYLATION 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 CHOLINEPHOSPHORYLATION.
RX PubMed=22307087; DOI=10.1038/emboj.2012.16;
RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A.,
RA Goody R.S.;
RT "Reversible phosphocholination of Rab proteins by Legionella
RT pneumophila 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
RT Arf6 with Rab8a.";
RL Traffic 13:82-93(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-180 IN COMPLEX WITH
RP 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
RT a 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
CC intracellular membrane trafficking, from the formation of
CC transport vesicles to their fusion with membranes. Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form
CC that is able to recruit to membranes different sets of downstream
CC effectors directly responsible for vesicle formation, movement,
CC tethering and fusion. That Rab is involved in the process of
CC endocytosis and is an essential rate-limiting regulator of the
CC fast recycling pathway back to the plasma membrane. During
CC cytokinesis, required for the postfurrowing terminal steps, namely
CC for intercellular bridge stability and abscission, possibly by
CC controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and
CC SEPT2 localization at the intercellular bridge. May indirectly
CC regulate neurite outgrowth.
CC -!- ENZYME REGULATION: Rab activation is generally mediated by a
CC guanine exchange factor (GEF), while inactivation through
CC hydrolysis of bound GTP is catalyzed by a GTPase activating
CC protein (GAP). That Rab is activated by the guanine exchange
CC factors DENND1A, DENND1B and DENND1C.
CC -!- SUBUNIT: Interacts with DENND1A and DENND1B; in a nucleotide-
CC dependent manner. Interacts with DENND1C; weak interaction which
CC is nucleotide-independent. Interacts (GTP-bound form) with ACAP2
CC and MICALL1; the interaction is direct and probably recruits ACAP2
CC and MICALL1 to membranes. Interacts with EHD1; the interaction is
CC indirect through MICALL1 and probably recruits EHD1 to membranes.
CC -!- INTERACTION:
CC Q8N3F8:MICALL1; NbExp=2; IntAct=EBI-722275, EBI-1056885;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential). Membrane, clathrin-coated pit. Cytoplasmic
CC vesicle, clathrin-coated vesicle. Endosome. Melanosome.
CC Note=Present on sorting endosomes and recycling endosome tubules.
CC Tends to be enriched in PIP2-positive cell membrane domains.
CC During mitosis, associated with the plasma membrane and present at
CC the ingressing furrow during early cytokinesis as well as at the
CC intercellular bridge later during cytokinesis. Identified in stage
CC I to stage IV melanosomes.
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 Note=No experimental confirmation available;
CC -!- PTM: AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the
CC switch 2 region and leads to moderate inactivation of the GTPase
CC activity. It appears to prolong the lifetime of the GTP state of
CC RAB1B by restricting access of GTPase effectors to switch 2 and
CC blocking effector-stimulated GTP hydrolysis, thereby rendering
CC RAB35 constitutively active.
CC -!- PTM: Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and
CC GTP-bound forms can be phosphocholinated. Phosphocholination
CC inhibits the GEF activity of DENND1A.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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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 PIR; JC2488; JC2488.
DR RefSeq; NP_001161078.1; NM_001167606.1.
DR RefSeq; NP_006852.1; NM_006861.6.
DR UniGene; Hs.524788; -.
DR PDB; 3TW8; X-ray; 2.10 A; B/D=1-180.
DR PDBsum; 3TW8; -.
DR ProteinModelPortal; Q15286; -.
DR SMR; Q15286; 4-177.
DR IntAct; Q15286; 16.
DR MINT; MINT-1370578; -.
DR STRING; 9606.ENSP00000229340; -.
DR PhosphoSite; Q15286; -.
DR DMDM; 3024525; -.
DR PaxDb; Q15286; -.
DR PRIDE; Q15286; -.
DR DNASU; 11021; -.
DR Ensembl; ENST00000229340; ENSP00000229340; ENSG00000111737.
DR Ensembl; ENST00000534951; ENSP00000441883; ENSG00000111737.
DR GeneID; 11021; -.
DR KEGG; hsa:11021; -.
DR UCSC; uc001txm.2; human.
DR CTD; 11021; -.
DR GeneCards; GC12M120532; -.
DR HGNC; HGNC:9774; RAB35.
DR HPA; HPA054146; -.
DR MIM; 604199; gene.
DR neXtProt; NX_Q15286; -.
DR PharmGKB; PA34127; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233968; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; Q15286; -.
DR KO; K07876; -.
DR OMA; NRILVGN; -.
DR OrthoDB; EOG7VB2H4; -.
DR GeneWiki; RAB35; -.
DR GenomeRNAi; 11021; -.
DR NextBio; 41874; -.
DR PRO; PR:Q15286; -.
DR ArrayExpress; Q15286; -.
DR Bgee; Q15286; -.
DR CleanEx; HS_RAB35; -.
DR Genevestigator; Q15286; -.
DR GO; GO:0031253; C:cell projection membrane; IDA:UniProtKB.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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; TAS:ProtInc.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS: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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003579; Small_GTPase_Rab_type.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 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 Complete proteome; Cytoplasmic vesicle; Endosome; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1 201 Ras-related protein Rab-35.
FT /FTId=PRO_0000121245.
FT NP_BIND 15 22 GTP (By similarity).
FT NP_BIND 63 67 GTP (By similarity).
FT NP_BIND 120 123 GTP (By similarity).
FT MOTIF 37 45 Effector region (By similarity).
FT MOD_RES 75 75 O-(2-cholinephosphoryl)serine; by
FT Legionella AnkX (Probable).
FT MOD_RES 77 77 O-AMP-tyrosine; by Legionella DrrA
FT (Probable).
FT LIPID 200 200 S-geranylgeranyl cysteine (By
FT similarity).
FT LIPID 201 201 S-geranylgeranyl cysteine (By
FT similarity).
FT VAR_SEQ 118 201 VGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVE
FT EMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKR
FT CC -> DVQLHHGAGPPSKERQPGKTAAATTERCGEAHEEQ
FT (in isoform 2).
FT /FTId=VSP_042918.
FT MUTAGEN 22 22 S->N: Destabilization of the
FT intercellular bridge during cytokinesis.
FT Strong reduction in fast recycling.
FT MUTAGEN 67 67 Q->L: Loss of GTPase activity. Increased
FT fast recycling.
FT STRAND 7 14
FT HELIX 21 28
FT TURN 38 40
FT STRAND 41 52
FT STRAND 55 64
FT HELIX 67 69
FT HELIX 75 78
FT STRAND 82 89
FT HELIX 93 109
FT STRAND 113 120
FT HELIX 125 127
FT HELIX 132 142
FT STRAND 146 148
FT TURN 151 154
FT HELIX 157 175
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
//
MIM
604199
*RECORD*
*FIELD* NO
604199
*FIELD* TI
*604199 RAS-ASSOCIATED PROTEIN RAB35; RAB35
*FIELD* TX
CLONING
The Ras superfamily of small GTP-binding proteins, which includes the
read moreRas, Ral, Rho, Rap, and Rab families, is involved in controlling a
diverse set of essential cellular functions. The Rab family appears to
play a critical role in regulating exocytotic and endocytotic pathways.
By PCR using degenerate oligonucleotides based on the RAB3D (604350)
amino acid sequence, followed by screening of a human fetal skeletal
muscle cDNA library with the PCR product, Zhu et al. (1994) isolated
cDNAs encoding RAB11B (604198) and RAB35, which they named RAY. The
deduced 201-amino acid RAB35 protein contains the 4 conserved domains
important for GTP binding. RAB35 is similar to human RAB1A (RAB1;
179508), rat Rab1b (612565), and yeast YPT1 in the N-terminal region,
but is different from these Rab family members in the C-terminal region.
However, like these other Rab proteins, RAB35 has 2 consecutive cysteine
residues at its C terminus; in Rab proteins, this region is thought to
be involved in membrane association. Recombinant RAB35 expressed in
bacteria had GTP-binding activity. Northern blot analysis detected a
3.6-kb RAB35 transcript in all human tissues examined.
GENE FUNCTION
Zhang et al. (2009) found that RAB35 regulates the assembly of actin
filaments during bristle development in Drosophila and filopodia
formation in cultured cells. These effects were mediated by the
actin-bundling protein fascin (602689), which directly associated with
active Rab35. Targeting Rab35 to the outer mitochondrial membrane
triggered actin recruitment, demonstrating a role for an intracellular
trafficking protein in localized actin assembly.
*FIELD* RF
1. Zhang, J.; Fonovic, M.; Suyama, K.; Bogyo, M.; Scott, M. P.: Rab35
controls actin bundling by recruiting fascin as an effector protein. Science 325:
1250-1254, 2009.
2. Zhu, A. X.; Zhao, Y.; Flier, J. S.: Molecular cloning of two small
GTP-binding proteins from human skeletal muscle. Biochem. Biophys.
Res. Commun. 205: 1875-1882, 1994.
*FIELD* CN
Ada Hamosh - updated: 10/13/2009
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
alopez: 10/23/2009
terry: 10/13/2009
mgross: 1/29/2009
carol: 3/14/2006
alopez: 12/13/1999
mgross: 9/29/1999
psherman: 9/29/1999
*RECORD*
*FIELD* NO
604199
*FIELD* TI
*604199 RAS-ASSOCIATED PROTEIN RAB35; RAB35
*FIELD* TX
CLONING
The Ras superfamily of small GTP-binding proteins, which includes the
read moreRas, Ral, Rho, Rap, and Rab families, is involved in controlling a
diverse set of essential cellular functions. The Rab family appears to
play a critical role in regulating exocytotic and endocytotic pathways.
By PCR using degenerate oligonucleotides based on the RAB3D (604350)
amino acid sequence, followed by screening of a human fetal skeletal
muscle cDNA library with the PCR product, Zhu et al. (1994) isolated
cDNAs encoding RAB11B (604198) and RAB35, which they named RAY. The
deduced 201-amino acid RAB35 protein contains the 4 conserved domains
important for GTP binding. RAB35 is similar to human RAB1A (RAB1;
179508), rat Rab1b (612565), and yeast YPT1 in the N-terminal region,
but is different from these Rab family members in the C-terminal region.
However, like these other Rab proteins, RAB35 has 2 consecutive cysteine
residues at its C terminus; in Rab proteins, this region is thought to
be involved in membrane association. Recombinant RAB35 expressed in
bacteria had GTP-binding activity. Northern blot analysis detected a
3.6-kb RAB35 transcript in all human tissues examined.
GENE FUNCTION
Zhang et al. (2009) found that RAB35 regulates the assembly of actin
filaments during bristle development in Drosophila and filopodia
formation in cultured cells. These effects were mediated by the
actin-bundling protein fascin (602689), which directly associated with
active Rab35. Targeting Rab35 to the outer mitochondrial membrane
triggered actin recruitment, demonstrating a role for an intracellular
trafficking protein in localized actin assembly.
*FIELD* RF
1. Zhang, J.; Fonovic, M.; Suyama, K.; Bogyo, M.; Scott, M. P.: Rab35
controls actin bundling by recruiting fascin as an effector protein. Science 325:
1250-1254, 2009.
2. Zhu, A. X.; Zhao, Y.; Flier, J. S.: Molecular cloning of two small
GTP-binding proteins from human skeletal muscle. Biochem. Biophys.
Res. Commun. 205: 1875-1882, 1994.
*FIELD* CN
Ada Hamosh - updated: 10/13/2009
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
alopez: 10/23/2009
terry: 10/13/2009
mgross: 1/29/2009
carol: 3/14/2006
alopez: 12/13/1999
mgross: 9/29/1999
psherman: 9/29/1999