RASF5_HUMAN
ID RASF5_HUMAN Reviewed; 418 AA.
AC Q8WWW0; A8K1E6; Q5SY32; Q8WWV9; Q8WXF4; Q9BT99;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras association domain-containing protein 5;
DE AltName: Full=New ras effector 1;
DE AltName: Full=Regulator for cell adhesion and polarization enriched in lymphoid tissues;
DE Short=RAPL;
GN Name=RASSF5; Synonyms=NORE1, RAPL;
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 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=11965544; DOI=10.1038/sj.onc.1205365;
RA Tommasi S., Dammann R., Jin S.-G., Zhang X.-F., Avruch J., Pfeifer G.P.;
RT "RASSF3 and NORE1: identification and cloning of two human homologues of
RT the putative tumor suppressor gene RASSF1.";
RL Oncogene 21:2713-2720(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INTEGRIN ACTIVATION,
RP INTERACTION WITH RAP1A AND ITGAL, AND SUBCELLULAR LOCATION.
RX PubMed=12845325; DOI=10.1038/ni950;
RA Katagiri K., Maeda A., Shimonaka M., Kinashi T.;
RT "RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through
RT spatial regulation of LFA-1.";
RL Nat. Immunol. 4:741-748(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA Burbee D.G., White M.A., Minna J.D.;
RT "RASSF3 is regulated by methylation in lung and breast tumor cell lines.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin;
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 AS A TUMOR SUPPRESSOR, AND TISSUE SPECIFICITY.
RX PubMed=12676952; DOI=10.1074/jbc.m211019200;
RA Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J.;
RT "The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor
RT suppressor in the lung.";
RL J. Biol. Chem. 278:21938-21943(2003).
RN [10]
RP INTERACTION WITH STK4/MST1.
RX PubMed=15109305; DOI=10.1042/bj20040025;
RA Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.;
RT "Regulation of the MST1 kinase by autophosphorylation, by the growth
RT inhibitory proteins, RASSF1 and NORE1, and by Ras.";
RL Biochem. J. 381:453-462(2004).
RN [11]
RP FUNCTION IN MICROTUBULE GROWTH REGULATION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RAP1A.
RX PubMed=15569673; DOI=10.1074/jbc.m409701200;
RA Fujita H., Fukuhara S., Sakurai A., Yamagishi A., Kamioka Y., Nakaoka Y.,
RA Masuda M., Mochizuki N.;
RT "Local activation of Rap1 contributes to directional vascular endothelial
RT cell migration accompanied by extension of microtubules on which RAPL, a
RT Rap1-associating molecule, localizes.";
RL J. Biol. Chem. 280:5022-5031(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT THR-352, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, 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 [16]
RP INTERACTION WITH RRAS2.
RX PubMed=31130282; DOI=10.1016/j.ajhg.2019.04.013;
RA Capri Y., Flex E., Krumbach O.H.F., Carpentieri G., Cecchetti S.,
RA Lissewski C., Rezaei Adariani S., Schanze D., Brinkmann J., Piard J.,
RA Pantaleoni F., Lepri F.R., Goh E.S., Chong K., Stieglitz E., Meyer J.,
RA Kuechler A., Bramswig N.C., Sacharow S., Strullu M., Vial Y., Vignal C.,
RA Kensah G., Cuturilo G., Kazemein Jasemi N.S., Dvorsky R., Monaghan K.G.,
RA Vincent L.M., Cave H., Verloes A., Ahmadian M.R., Tartaglia M., Zenker M.;
RT "Activating Mutations of RRAS2 Are a Rare Cause of Noonan Syndrome.";
RL Am. J. Hum. Genet. 104:1223-1232(2019).
CC -!- FUNCTION: Potential tumor suppressor. Seems to be involved in
CC lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or
CC chemokine stimulation to integrin activation. Isoform 2 stimulates
CC lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1,
CC resulting in an enhanced adhesion to ICAM1. Together with RAP1A may
CC participate in regulation of microtubule growth. The association of
CC isoform 2 with activated RAP1A is required for directional movement of
CC endothelial cells during wound healing. May be involved in regulation
CC of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate
CC HRAS and KRAS induced apoptosis. {ECO:0000269|PubMed:12676952,
CC ECO:0000269|PubMed:12845325, ECO:0000269|PubMed:15569673}.
CC -!- SUBUNIT: Interacts directly with activated HRAS; a RASSF5-STK4/MST1
CC complex probably associates with activated HRAS (By similarity).
CC Interacts with KRAS (By similarity). Probably interacts with Ras-like
CC GTPases RRAS, MRAS, RAP1B, RAP2A and RALA (By similarity). Interacts
CC with RRAS2 (PubMed:31130282). Can self-associate (By similarity).
CC Interacts with RSSF1 isoform A (By similarity). The RSSF1 isoform A-
CC RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS
CC (By similarity). Isoform 2 interacts with activated RAP1A and
CC ITGAL/LFA-1 (PubMed:12845325, PubMed:15569673). Binds STK4/MST1,
CC inhibiting STK4/MST1 autoactivation (PubMed:15109305).
CC {ECO:0000250|UniProtKB:Q5EBH1, ECO:0000269|PubMed:12845325,
CC ECO:0000269|PubMed:15109305, ECO:0000269|PubMed:15569673,
CC ECO:0000269|PubMed:31130282}.
CC -!- INTERACTION:
CC Q8WWW0; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-367390, EBI-10187270;
CC Q8WWW0; Q9Y297: BTRC; NbExp=4; IntAct=EBI-367390, EBI-307461;
CC Q8WWW0; O95166: GABARAP; NbExp=2; IntAct=EBI-367390, EBI-712001;
CC Q8WWW0; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-367390, EBI-746969;
CC Q8WWW0; P60520: GABARAPL2; NbExp=2; IntAct=EBI-367390, EBI-720116;
CC Q8WWW0; P01112: HRAS; NbExp=2; IntAct=EBI-367390, EBI-350145;
CC Q8WWW0; Q6A162: KRT40; NbExp=3; IntAct=EBI-367390, EBI-10171697;
CC Q8WWW0; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-367390, EBI-10172511;
CC Q8WWW0; Q9GZQ8: MAP1LC3B; NbExp=5; IntAct=EBI-367390, EBI-373144;
CC Q8WWW0; Q9BXW4: MAP1LC3C; NbExp=2; IntAct=EBI-367390, EBI-2603996;
CC Q8WWW0; Q8WY64: MYLIP; NbExp=4; IntAct=EBI-367390, EBI-6952711;
CC Q8WWW0; P47224: RABIF; NbExp=3; IntAct=EBI-367390, EBI-713992;
CC Q8WWW0; P61224: RAP1B; NbExp=3; IntAct=EBI-367390, EBI-358143;
CC Q8WWW0; P61225: RAP2B; NbExp=3; IntAct=EBI-367390, EBI-750871;
CC Q8WWW0; P50749: RASSF2; NbExp=3; IntAct=EBI-367390, EBI-960081;
CC Q8WWW0; Q04864: REL; NbExp=3; IntAct=EBI-367390, EBI-307352;
CC Q8WWW0; Q13485: SMAD4; NbExp=5; IntAct=EBI-367390, EBI-347263;
CC Q8WWW0; Q13188: STK3; NbExp=9; IntAct=EBI-367390, EBI-992580;
CC Q8WWW0; Q13043: STK4; NbExp=8; IntAct=EBI-367390, EBI-367376;
CC Q8WWW0; Q13077: TRAF1; NbExp=3; IntAct=EBI-367390, EBI-359224;
CC Q8WWW0; Q12933: TRAF2; NbExp=3; IntAct=EBI-367390, EBI-355744;
CC Q8WWW0; Q548N1: VPS28; NbExp=3; IntAct=EBI-367390, EBI-10243107;
CC Q8WWW0; A8K940; NbExp=3; IntAct=EBI-367390, EBI-10174788;
CC Q8WWW0-1; Q8WWW0-1: RASSF5; NbExp=2; IntAct=EBI-960496, EBI-960496;
CC Q8WWW0-1; Q13188: STK3; NbExp=6; IntAct=EBI-960496, EBI-992580;
CC Q8WWW0-1; Q13043-1: STK4; NbExp=3; IntAct=EBI-960496, EBI-15638366;
CC Q8WWW0-2; A0A0S2Z507: BTRC; NbExp=3; IntAct=EBI-960502, EBI-16429247;
CC Q8WWW0-2; Q9Y297: BTRC; NbExp=3; IntAct=EBI-960502, EBI-307461;
CC Q8WWW0-2; P14136: GFAP; NbExp=3; IntAct=EBI-960502, EBI-744302;
CC Q8WWW0-2; P42858: HTT; NbExp=3; IntAct=EBI-960502, EBI-466029;
CC Q8WWW0-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-960502, EBI-1055254;
CC Q8WWW0-2; P51608: MECP2; NbExp=3; IntAct=EBI-960502, EBI-1189067;
CC Q8WWW0-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-960502, EBI-713665;
CC Q8WWW0-2; P62834: RAP1A; NbExp=3; IntAct=EBI-960502, EBI-491414;
CC Q8WWW0-2; Q13043: STK4; NbExp=4; IntAct=EBI-960502, EBI-367376;
CC Q8WWW0-2; Q9UK41: VPS28; NbExp=3; IntAct=EBI-960502, EBI-727424;
CC Q8WWW0-3; Q13043: STK4; NbExp=2; IntAct=EBI-960507, EBI-367376;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Note=Isoform
CC 2 is mainly located in the perinuclear region of unstimulated primary
CC T-cells. Upon stimulation translocates to the leading edge and
CC colocalizes with ITGAL/LFA-1 in the peripheral zone of the
CC immunological synapse. Isoform 2 is localized to growing microtubules
CC in vascular endothelial cells and is dissociated from microtubules by
CC activated RAP1A.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A, NORE1A;
CC IsoId=Q8WWW0-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q8WWW0-2; Sequence=VSP_019363, VSP_019364;
CC Name=3; Synonyms=C, NORE1B;
CC IsoId=Q8WWW0-3; Sequence=VSP_019365, VSP_019366;
CC -!- TISSUE SPECIFICITY: Widely expressed. Frequently down-regulated in lung
CC tumor cell lines and primary lung tumors. {ECO:0000269|PubMed:11965544,
CC ECO:0000269|PubMed:12676952}.
CC -!- CAUTION: Was termed (Ref.3) RASSF3. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH04270.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAH07203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH07203.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RASSF5ID42059ch1q32.html";
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DR EMBL; AF445801; AAL38592.1; -; mRNA.
DR EMBL; AY261332; AAP83360.1; -; mRNA.
DR EMBL; AY062002; AAL40388.1; -; mRNA.
DR EMBL; AY062003; AAL40389.1; -; mRNA.
DR EMBL; AY216268; AAO61668.1; -; mRNA.
DR EMBL; AK289861; BAF82550.1; -; mRNA.
DR EMBL; AL832784; CAI46164.1; -; mRNA.
DR EMBL; AL591846; CAI13536.1; -; Genomic_DNA.
DR EMBL; AL354681; CAI13536.1; JOINED; Genomic_DNA.
DR EMBL; AL591846; CAI13538.1; -; Genomic_DNA.
DR EMBL; AL354681; CAI13538.1; JOINED; Genomic_DNA.
DR EMBL; AL354681; CAI15252.1; -; Genomic_DNA.
DR EMBL; AL591846; CAI15252.1; JOINED; Genomic_DNA.
DR EMBL; AL591846; CAI13537.1; -; Genomic_DNA.
DR EMBL; AL354681; CAI13537.1; JOINED; Genomic_DNA.
DR EMBL; AL591846; CAI13542.1; -; Genomic_DNA.
DR EMBL; AL354681; CAI13542.1; JOINED; Genomic_DNA.
DR EMBL; AL354681; CAI15253.1; -; Genomic_DNA.
DR EMBL; AL591846; CAI15253.1; JOINED; Genomic_DNA.
DR EMBL; AL354681; CAI15254.1; -; Genomic_DNA.
DR EMBL; AL591846; CAI15254.1; JOINED; Genomic_DNA.
DR EMBL; AL354681; CAI15256.1; -; Genomic_DNA.
DR EMBL; AL591846; CAI15256.1; JOINED; Genomic_DNA.
DR EMBL; CH471100; EAW93544.1; -; Genomic_DNA.
DR EMBL; BC004270; AAH04270.1; ALT_SEQ; mRNA.
DR EMBL; BC007203; AAH07203.1; ALT_SEQ; mRNA.
DR EMBL; BC042651; AAH42651.1; -; mRNA.
DR CCDS; CCDS1463.1; -. [Q8WWW0-3]
DR CCDS; CCDS1464.1; -. [Q8WWW0-2]
DR CCDS; CCDS30998.1; -. [Q8WWW0-1]
DR RefSeq; NP_872604.1; NM_182663.3. [Q8WWW0-1]
DR RefSeq; NP_872605.1; NM_182664.3. [Q8WWW0-3]
DR RefSeq; NP_872606.1; NM_182665.3. [Q8WWW0-2]
DR PDB; 4LGD; X-ray; 3.05 A; E/F/G/H=365-413.
DR PDB; 4OH8; X-ray; 2.28 A; B=366-418.
DR PDBsum; 4LGD; -.
DR PDBsum; 4OH8; -.
DR AlphaFoldDB; Q8WWW0; -.
DR SMR; Q8WWW0; -.
DR BioGRID; 123689; 46.
DR DIP; DIP-32490N; -.
DR IntAct; Q8WWW0; 51.
DR MINT; Q8WWW0; -.
DR STRING; 9606.ENSP00000462099; -.
DR iPTMnet; Q8WWW0; -.
DR PhosphoSitePlus; Q8WWW0; -.
DR BioMuta; RASSF5; -.
DR DMDM; 74751587; -.
DR EPD; Q8WWW0; -.
DR jPOST; Q8WWW0; -.
DR MassIVE; Q8WWW0; -.
DR MaxQB; Q8WWW0; -.
DR PaxDb; Q8WWW0; -.
DR PeptideAtlas; Q8WWW0; -.
DR PRIDE; Q8WWW0; -.
DR ProteomicsDB; 74944; -. [Q8WWW0-1]
DR ProteomicsDB; 74945; -. [Q8WWW0-2]
DR ProteomicsDB; 74946; -. [Q8WWW0-3]
DR Antibodypedia; 73646; 282 antibodies from 29 providers.
DR DNASU; 83593; -.
DR Ensembl; ENST00000577571.5; ENSP00000462576.1; ENSG00000266094.8. [Q8WWW0-2]
DR Ensembl; ENST00000579436.7; ENSP00000462099.1; ENSG00000266094.8. [Q8WWW0-1]
DR Ensembl; ENST00000580449.5; ENSP00000462544.1; ENSG00000266094.8. [Q8WWW0-3]
DR GeneID; 83593; -.
DR KEGG; hsa:83593; -.
DR MANE-Select; ENST00000579436.7; ENSP00000462099.1; NM_182663.4; NP_872604.1.
DR UCSC; uc031vlp.2; human. [Q8WWW0-1]
DR CTD; 83593; -.
DR DisGeNET; 83593; -.
DR GeneCards; RASSF5; -.
DR HGNC; HGNC:17609; RASSF5.
DR HPA; ENSG00000266094; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 607020; gene.
DR neXtProt; NX_Q8WWW0; -.
DR OpenTargets; ENSG00000266094; -.
DR PharmGKB; PA134958571; -.
DR VEuPathDB; HostDB:ENSG00000266094; -.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000159288; -.
DR HOGENOM; CLU_045544_0_0_1; -.
DR InParanoid; Q8WWW0; -.
DR OrthoDB; 1120975at2759; -.
DR PhylomeDB; Q8WWW0; -.
DR TreeFam; TF319243; -.
DR PathwayCommons; Q8WWW0; -.
DR SignaLink; Q8WWW0; -.
DR SIGNOR; Q8WWW0; -.
DR BioGRID-ORCS; 83593; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; RASSF5; human.
DR GeneWiki; RASSF5; -.
DR GenomeRNAi; 83593; -.
DR Pharos; Q8WWW0; Tbio.
DR PRO; PR:Q8WWW0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WWW0; protein.
DR Bgee; ENSG00000266094; Expressed in upper arm skin and 180 other tissues.
DR ExpressionAtlas; Q8WWW0; baseline and differential.
DR Genevisible; Q8WWW0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046651; P:lymphocyte proliferation; IEA:Ensembl.
DR GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR IDEAL; IID00631; -.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033614; RASSF1-6.
DR InterPro; IPR033623; RASSF5.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR PANTHER; PTHR22738:SF9; PTHR22738:SF9; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF16517; Nore1-SARAH; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50951; SARAH; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Cytoskeleton; Metal-binding; Microtubule; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..418
FT /note="Ras association domain-containing protein 5"
FT /id="PRO_0000240401"
FT DOMAIN 274..364
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 366..413
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT ZN_FING 122..170
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBH1"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11965544,
FT ECO:0000303|PubMed:12845325, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT /id="VSP_019363"
FT VAR_SEQ 154..193
FT /note="CKFTCHPECRSLIQLDCSQQEGLSRDRPSPESTLTVTFSQ -> MTVDSSMS
FT SGYCSLDEELEDCFFTAKTTFFRNAQSKHLSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11965544,
FT ECO:0000303|PubMed:12845325, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT /id="VSP_019364"
FT VAR_SEQ 331..336
FT /note="LFQKLS -> GCLLHP (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019365"
FT VAR_SEQ 337..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019366"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:4OH8"
FT HELIX 374..411
FT /evidence="ECO:0007829|PDB:4OH8"
FT INIT_MET Q8WWW0-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES Q8WWW0-2:2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19369195"
SQ SEQUENCE 418 AA; 47090 MW; 4AFBC69B1325CC9E CRC64;
MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL STAPGAREGR
SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP RDVRSIFEQP QDPRVPAERG
EGHCFAELVL PGGPGWCDLC GREVLRQALR CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR
PSPESTLTVT FSQNVCKPVE ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI
KVHLKLRRPV TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE
VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV LFQKLSIADR PLYLRLLAGP DTEVLSFVLK
ENETGEVEWD AFSIPELQNF LTILEKEEQD KIQQVQKKYD KFRQKLEEAL RESQGKPG
