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Ras association domain-containing protein 5 (New ras effector 1) (Regulator for cell adhesion and polarization enriched in lymphoid tissues) (RAPL)

 RASF5_HUMAN             Reviewed;         418 AA.
Q8WWW0; A8K1E6; Q5SY32; Q8WWV9; Q8WXF4; Q9BT99;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Ras association domain-containing protein 5;
AltName: Full=New ras effector 1;
AltName: Full=Regulator for cell adhesion and polarization enriched in lymphoid tissues;
Short=RAPL;
Name=RASSF5; Synonyms=NORE1, RAPL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND
TISSUE SPECIFICITY.
PubMed=11965544; DOI=10.1038/sj.onc.1205365;
Tommasi S., Dammann R., Jin S.-G., Zhang X.-F., Avruch J.,
Pfeifer G.P.;
"RASSF3 and NORE1: identification and cloning of two human homologues
of the putative tumor suppressor gene RASSF1.";
Oncogene 21:2713-2720(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INTEGRIN
ACTIVATION, INTERACTION WITH RAP1A AND ITGAL, AND SUBCELLULAR
LOCATION.
PubMed=12845325; DOI=10.1038/ni950;
Katagiri K., Maeda A., Shimonaka M., Kinashi T.;
"RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion
through spatial regulation of LFA-1.";
Nat. Immunol. 4:741-748(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Burbee D.G., White M.A., Minna J.D.;
"RASSF3 is regulated by methylation in lung and breast tumor cell
lines.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION AS A TUMOR SUPPRESSOR, AND TISSUE SPECIFICITY.
PubMed=12676952; DOI=10.1074/jbc.M211019200;
Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J.;
"The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated
tumor suppressor in the lung.";
J. Biol. Chem. 278:21938-21943(2003).
[10]
INTERACTION WITH STK4/MST1.
PubMed=15109305; DOI=10.1042/BJ20040025;
Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.;
"Regulation of the MST1 kinase by autophosphorylation, by the growth
inhibitory proteins, RASSF1 and NORE1, and by Ras.";
Biochem. J. 381:453-462(2004).
[11]
FUNCTION IN MICROTUBULE GROWTH REGULATION, SUBCELLULAR LOCATION, AND
INTERACTION WITH RAP1A.
PubMed=15569673; DOI=10.1074/jbc.M409701200;
Fujita H., Fukuhara S., Sakurai A., Yamagishi A., Kamioka Y.,
Nakaoka Y., Masuda M., Mochizuki N.;
"Local activation of Rap1 contributes to directional vascular
endothelial cell migration accompanied by extension of microtubules on
which RAPL, a Rap1-associating molecule, localizes.";
J. Biol. Chem. 280:5022-5031(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Potential tumor suppressor. Seems to be involved in
lymphocyte adhesion by linking RAP1A activation upon T-cell
receptor or chemokine stimulation to integrin activation. Isoform
2 stimulates lymphocyte polarization and the patch-like
distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to
ICAM1. Together with RAP1A may participate in regulation of
microtubule growth. The association of isoform 2 with activated
RAP1A is required for directional movement of endothelial cells
during wound healing. May be involved in regulation of Ras
apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS
and KRAS induced apoptosis. {ECO:0000269|PubMed:12676952,
ECO:0000269|PubMed:12845325, ECO:0000269|PubMed:15569673}.
-!- SUBUNIT: Interacts directly with activated HRAS; a RASSF5-
STK4/MST1 complex probably associates with activated HRAS.
Interacts with KRAS. Probably interacts with Ras-like GTPases
RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate.
Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5
heterodimer probably mediates the association of RSSF1 with HRAS
(By similarity). Isoform 2 interacts with activated RAP1A and
ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation.
{ECO:0000250, ECO:0000269|PubMed:12845325,
ECO:0000269|PubMed:15109305, ECO:0000269|PubMed:15569673}.
-!- INTERACTION:
A8K940:-; NbExp=3; IntAct=EBI-367390, EBI-10174788;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-367390, EBI-10187270;
Q9Y297:BTRC; NbExp=3; IntAct=EBI-367390, EBI-307461;
O95166:GABARAP; NbExp=2; IntAct=EBI-367390, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-367390, EBI-746969;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-367390, EBI-720116;
P01112:HRAS; NbExp=2; IntAct=EBI-367390, EBI-350145;
Q6A162:KRT40; NbExp=3; IntAct=EBI-367390, EBI-10171697;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-367390, EBI-10172511;
Q9GZQ8:MAP1LC3B; NbExp=5; IntAct=EBI-367390, EBI-373144;
Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-367390, EBI-2603996;
Q8WY64:MYLIP; NbExp=3; IntAct=EBI-367390, EBI-6952711;
P47224:RABIF; NbExp=3; IntAct=EBI-367390, EBI-713992;
P62834:RAP1A; NbExp=3; IntAct=EBI-960502, EBI-491414;
P61224:RAP1B; NbExp=3; IntAct=EBI-367390, EBI-358143;
P61225:RAP2B; NbExp=3; IntAct=EBI-367390, EBI-750871;
P50749:RASSF2; NbExp=3; IntAct=EBI-367390, EBI-960081;
Q04864:REL; NbExp=3; IntAct=EBI-367390, EBI-307352;
Q13485:SMAD4; NbExp=3; IntAct=EBI-367390, EBI-347263;
Q13188:STK3; NbExp=7; IntAct=EBI-367390, EBI-992580;
Q13043:STK4; NbExp=7; IntAct=EBI-367390, EBI-367376;
Q13043-1:STK4; NbExp=3; IntAct=EBI-960496, EBI-15638366;
Q13077:TRAF1; NbExp=3; IntAct=EBI-367390, EBI-359224;
Q12933:TRAF2; NbExp=3; IntAct=EBI-367390, EBI-355744;
Q548N1:VPS28; NbExp=3; IntAct=EBI-367390, EBI-10243107;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
Note=Isoform 2 is mainly located in the perinuclear region of
unstimulated primary T-cells. Upon stimulation translocates to the
leading edge and colocalizes with ITGAL/LFA-1 in the peripheral
zone of the immunological synapse. Isoform 2 is localized to
growing microtubules in vascular endothelial cells and is
dissociated from microtubules by activated RAP1A.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=A, NORE1A;
IsoId=Q8WWW0-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q8WWW0-2; Sequence=VSP_019363, VSP_019364;
Note=Initiator Met-1 is removed. Contains a N-acetylthreonine at
position 2. {ECO:0000244|PubMed:19369195};
Name=3; Synonyms=C, NORE1B;
IsoId=Q8WWW0-3; Sequence=VSP_019365, VSP_019366;
-!- TISSUE SPECIFICITY: Widely expressed. Frequently down-regulated in
lung tumor cell lines and primary lung tumors.
{ECO:0000269|PubMed:11965544, ECO:0000269|PubMed:12676952}.
-!- CAUTION: Was termed (Ref.3) RASSF3. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH04270.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH04270.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
Sequence=AAH07203.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH07203.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RASSF5ID42059ch1q32.html";
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EMBL; AF445801; AAL38592.1; -; mRNA.
EMBL; AY261332; AAP83360.1; -; mRNA.
EMBL; AY062002; AAL40388.1; -; mRNA.
EMBL; AY062003; AAL40389.1; -; mRNA.
EMBL; AY216268; AAO61668.1; -; mRNA.
EMBL; AK289861; BAF82550.1; -; mRNA.
EMBL; AL832784; CAI46164.1; -; mRNA.
EMBL; AL591846; CAI13536.1; -; Genomic_DNA.
EMBL; AL354681; CAI13536.1; JOINED; Genomic_DNA.
EMBL; AL591846; CAI13538.1; -; Genomic_DNA.
EMBL; AL354681; CAI13538.1; JOINED; Genomic_DNA.
EMBL; AL354681; CAI15252.1; -; Genomic_DNA.
EMBL; AL591846; CAI15252.1; JOINED; Genomic_DNA.
EMBL; AL591846; CAI13537.1; -; Genomic_DNA.
EMBL; AL354681; CAI13537.1; JOINED; Genomic_DNA.
EMBL; AL591846; CAI13542.1; -; Genomic_DNA.
EMBL; AL354681; CAI13542.1; JOINED; Genomic_DNA.
EMBL; AL354681; CAI15253.1; -; Genomic_DNA.
EMBL; AL591846; CAI15253.1; JOINED; Genomic_DNA.
EMBL; AL354681; CAI15254.1; -; Genomic_DNA.
EMBL; AL591846; CAI15254.1; JOINED; Genomic_DNA.
EMBL; AL354681; CAI15256.1; -; Genomic_DNA.
EMBL; AL591846; CAI15256.1; JOINED; Genomic_DNA.
EMBL; CH471100; EAW93544.1; -; Genomic_DNA.
EMBL; BC004270; AAH04270.1; ALT_SEQ; mRNA.
EMBL; BC007203; AAH07203.1; ALT_SEQ; mRNA.
EMBL; BC042651; AAH42651.1; -; mRNA.
CCDS; CCDS1463.1; -. [Q8WWW0-3]
CCDS; CCDS1464.1; -. [Q8WWW0-2]
CCDS; CCDS30998.1; -. [Q8WWW0-1]
RefSeq; NP_872604.1; NM_182663.3. [Q8WWW0-1]
RefSeq; NP_872605.1; NM_182664.3. [Q8WWW0-3]
RefSeq; NP_872606.1; NM_182665.3. [Q8WWW0-2]
UniGene; Hs.497579; -.
PDB; 4LGD; X-ray; 3.05 A; E/F/G/H=365-413.
PDB; 4OH8; X-ray; 2.28 A; B=366-418.
PDBsum; 4LGD; -.
PDBsum; 4OH8; -.
ProteinModelPortal; Q8WWW0; -.
SMR; Q8WWW0; -.
BioGrid; 123689; 41.
DIP; DIP-32490N; -.
IntAct; Q8WWW0; 44.
STRING; 9606.ENSP00000347443; -.
iPTMnet; Q8WWW0; -.
PhosphoSitePlus; Q8WWW0; -.
BioMuta; RASSF5; -.
DMDM; 74751587; -.
EPD; Q8WWW0; -.
MaxQB; Q8WWW0; -.
PaxDb; Q8WWW0; -.
PeptideAtlas; Q8WWW0; -.
PRIDE; Q8WWW0; -.
DNASU; 83593; -.
Ensembl; ENST00000577571; ENSP00000462576; ENSG00000266094. [Q8WWW0-2]
Ensembl; ENST00000579436; ENSP00000462099; ENSG00000266094. [Q8WWW0-1]
Ensembl; ENST00000580449; ENSP00000462544; ENSG00000266094. [Q8WWW0-3]
GeneID; 83593; -.
KEGG; hsa:83593; -.
UCSC; uc031vlp.2; human. [Q8WWW0-1]
CTD; 83593; -.
DisGeNET; 83593; -.
EuPathDB; HostDB:ENSG00000266094.6; -.
GeneCards; RASSF5; -.
HGNC; HGNC:17609; RASSF5.
HPA; HPA070480; -.
MIM; 607020; gene.
neXtProt; NX_Q8WWW0; -.
OpenTargets; ENSG00000266094; -.
PharmGKB; PA134958571; -.
eggNOG; ENOG410IPAE; Eukaryota.
eggNOG; ENOG4111HS2; LUCA.
GeneTree; ENSGT00390000003367; -.
HOGENOM; HOG000013025; -.
HOVERGEN; HBG054362; -.
InParanoid; Q8WWW0; -.
KO; K08015; -.
OrthoDB; EOG091G0EPB; -.
PhylomeDB; Q8WWW0; -.
TreeFam; TF319243; -.
SignaLink; Q8WWW0; -.
SIGNOR; Q8WWW0; -.
ChiTaRS; RASSF5; human.
GeneWiki; RASSF5; -.
GenomeRNAi; 83593; -.
PRO; PR:Q8WWW0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000266094; -.
CleanEx; HS_RASSF5; -.
ExpressionAtlas; Q8WWW0; baseline and differential.
Genevisible; Q8WWW0; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017016; F:Ras GTPase binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
CDD; cd00029; C1; 1.
InterPro; IPR033614; C-RASSF.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000159; RA_dom.
InterPro; IPR033623; RASSF5.
InterPro; IPR011524; SARAH_dom.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR22738; PTHR22738; 1.
PANTHER; PTHR22738:SF9; PTHR22738:SF9; 1.
Pfam; PF00130; C1_1; 1.
Pfam; PF16517; Nore1-SARAH; 1.
Pfam; PF00788; RA; 1.
SMART; SM00109; C1; 1.
SMART; SM00314; RA; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50951; SARAH; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Cytoskeleton; Metal-binding;
Microtubule; Phosphoprotein; Reference proteome; Tumor suppressor;
Zinc; Zinc-finger.
CHAIN 1 418 Ras association domain-containing protein
5.
/FTId=PRO_0000240401.
DOMAIN 274 364 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 366 413 SARAH. {ECO:0000255|PROSITE-
ProRule:PRU00310}.
ZN_FING 122 170 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000250|UniProtKB:Q5EBH1}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 352 352 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
VAR_SEQ 1 153 Missing (in isoform 2).
{ECO:0000303|PubMed:11965544,
ECO:0000303|PubMed:12845325,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.3}.
/FTId=VSP_019363.
VAR_SEQ 154 193 CKFTCHPECRSLIQLDCSQQEGLSRDRPSPESTLTVTFSQ
-> MTVDSSMSSGYCSLDEELEDCFFTAKTTFFRNAQSKHL
SK (in isoform 2).
{ECO:0000303|PubMed:11965544,
ECO:0000303|PubMed:12845325,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.3}.
/FTId=VSP_019364.
VAR_SEQ 331 336 LFQKLS -> GCLLHP (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_019365.
VAR_SEQ 337 418 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_019366.
HELIX 369 371 {ECO:0000244|PDB:4OH8}.
HELIX 374 411 {ECO:0000244|PDB:4OH8}.
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


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