RASF2_HUMAN
ID RASF2_HUMAN Reviewed; 326 AA.
AC P50749; A6NIX9; A8K5Z3; Q17S06; Q53HD0; Q6AHZ2; Q8IZA5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras association domain-containing protein 2;
GN Name=RASSF2; Synonyms=CENP-34 {ECO:0000303|PubMed:20813266}, KIAA0168;
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] (ISOFORMS 1 AND 2).
RA Burbee D.G., White M.A., Miller D.S., Minna J.D., Muller C.Y.;
RT "RASSF2 is inactivated by an epigenetic mechanism in ovarian cancers.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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=Brain;
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, INTERACTION WITH KRAS, AND TISSUE SPECIFICITY.
RX PubMed=12732644; DOI=10.1074/jbc.m300554200;
RA Vos M.D., Ellis C.A., Elam C., Uelkue A.S., Taylor B.J., Clark G.J.;
RT "RASSF2 is a novel K-Ras-specific effector and potential tumor
RT suppressor.";
RL J. Biol. Chem. 278:28045-28051(2003).
RN [10]
RP FUNCTION.
RX PubMed=16012945; DOI=10.1053/j.gastro.2005.03.051;
RA Akino K., Toyota M., Suzuki H., Mita H., Sasaki Y., Ohe-Toyota M.,
RA Issa J.P., Hinoda Y., Imai K., Tokino T.;
RT "The Ras effector RASSF2 is a novel tumor-suppressor gene in human
RT colorectal cancer.";
RL Gastroenterology 129:156-169(2005).
RN [11]
RP SUBCELLULAR LOCATION.
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 FUNCTION, INTERACTION WITH STK3/MST2 AND STK4/MST1, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RX PubMed=19525978; DOI=10.1038/onc.2009.152;
RA Cooper W.N., Hesson L.B., Matallanas D., Dallol A., von Kriegsheim A.,
RA Ward R., Kolch W., Latif F.;
RT "RASSF2 associates with and stabilizes the proapoptotic kinase MST2.";
RL Oncogene 28:2988-2998(2009).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
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 VARIANT [LARGE SCALE ANALYSIS] HIS-144.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Potential tumor suppressor. Acts as a KRAS-specific effector
CC protein. May promote apoptosis and cell cycle arrest. Stabilizes
CC STK3/MST2 by protecting it from proteasomal degradation.
CC {ECO:0000269|PubMed:12732644, ECO:0000269|PubMed:16012945,
CC ECO:0000269|PubMed:19525978}.
CC -!- SUBUNIT: Interacts directly with activated KRAS in a GTP-dependent
CC manner. Interacts (via SARAH domain) with STK3/MST2 AND STK4/MST1.
CC {ECO:0000269|PubMed:12732644, ECO:0000269|PubMed:19525978}.
CC -!- INTERACTION:
CC P50749; P27797: CALR; NbExp=3; IntAct=EBI-960081, EBI-1049597;
CC P50749; P36957: DLST; NbExp=3; IntAct=EBI-960081, EBI-351007;
CC P50749; P14136: GFAP; NbExp=3; IntAct=EBI-960081, EBI-744302;
CC P50749; P42858: HTT; NbExp=3; IntAct=EBI-960081, EBI-466029;
CC P50749; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-960081, EBI-1055254;
CC P50749; O60341: KDM1A; NbExp=2; IntAct=EBI-960081, EBI-710124;
CC P50749; P01116: KRAS; NbExp=2; IntAct=EBI-960081, EBI-367415;
CC P50749; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-960081, EBI-1055945;
CC P50749; Q96CV9: OPTN; NbExp=3; IntAct=EBI-960081, EBI-748974;
CC P50749; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-960081, EBI-912440;
CC P50749; Q8WWW0: RASSF5; NbExp=3; IntAct=EBI-960081, EBI-367390;
CC P50749; Q8WXG8: S100Z; NbExp=3; IntAct=EBI-960081, EBI-12198403;
CC P50749; Q13188: STK3; NbExp=19; IntAct=EBI-960081, EBI-992580;
CC P50749; Q13043: STK4; NbExp=16; IntAct=EBI-960081, EBI-367376;
CC P50749; O43463: SUV39H1; NbExp=2; IntAct=EBI-960081, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome, centromere,
CC kinetochore {ECO:0000269|PubMed:20813266}. Note=Translocates to the
CC cytoplasm in the presence of STK3/MST2 AND STK4/MST1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50749-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50749-2; Sequence=VSP_055851, VSP_055852;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC placenta, peripheral blood and lung. Frequently down-regulated in lung
CC tumor cell lines. {ECO:0000269|PubMed:12732644}.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1.
CC {ECO:0000269|PubMed:19525978}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11485.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RASSF2ID43461ch20p13.html";
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DR EMBL; AY154470; AAN59975.1; -; mRNA.
DR EMBL; AY154471; AAN59976.1; -; mRNA.
DR EMBL; AY154472; AAN59977.1; -; mRNA.
DR EMBL; D79990; BAA11485.2; ALT_INIT; mRNA.
DR EMBL; AK291458; BAF84147.1; -; mRNA.
DR EMBL; AK222650; BAD96370.1; -; mRNA.
DR EMBL; CR627436; CAH10522.1; -; mRNA.
DR EMBL; AL133354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10445.1; -; Genomic_DNA.
DR EMBL; BC110385; AAI10386.1; -; mRNA.
DR EMBL; BC117118; AAI17119.1; -; mRNA.
DR EMBL; BC117120; AAI17121.1; -; mRNA.
DR CCDS; CCDS13083.1; -. [P50749-1]
DR RefSeq; NP_055552.1; NM_014737.2. [P50749-1]
DR RefSeq; NP_739580.1; NM_170774.1. [P50749-1]
DR RefSeq; XP_005260952.1; XM_005260895.3. [P50749-1]
DR RefSeq; XP_016883639.1; XM_017028150.1. [P50749-1]
DR RefSeq; XP_016883640.1; XM_017028151.1. [P50749-1]
DR RefSeq; XP_016883641.1; XM_017028152.1. [P50749-1]
DR RefSeq; XP_016883642.1; XM_017028153.1. [P50749-1]
DR AlphaFoldDB; P50749; -.
DR BioGRID; 115115; 37.
DR IntAct; P50749; 38.
DR MINT; P50749; -.
DR STRING; 9606.ENSP00000368710; -.
DR iPTMnet; P50749; -.
DR MetOSite; P50749; -.
DR PhosphoSitePlus; P50749; -.
DR BioMuta; RASSF2; -.
DR DMDM; 1723118; -.
DR EPD; P50749; -.
DR jPOST; P50749; -.
DR MassIVE; P50749; -.
DR MaxQB; P50749; -.
DR PaxDb; P50749; -.
DR PeptideAtlas; P50749; -.
DR PRIDE; P50749; -.
DR ProteomicsDB; 56262; -. [P50749-1]
DR Antibodypedia; 42660; 176 antibodies from 33 providers.
DR DNASU; 9770; -.
DR Ensembl; ENST00000379376.2; ENSP00000368684.2; ENSG00000101265.16. [P50749-1]
DR Ensembl; ENST00000379400.8; ENSP00000368710.3; ENSG00000101265.16. [P50749-1]
DR GeneID; 9770; -.
DR KEGG; hsa:9770; -.
DR MANE-Select; ENST00000379400.8; ENSP00000368710.3; NM_014737.3; NP_055552.1.
DR UCSC; uc002wld.4; human. [P50749-1]
DR CTD; 9770; -.
DR DisGeNET; 9770; -.
DR GeneCards; RASSF2; -.
DR HGNC; HGNC:9883; RASSF2.
DR HPA; ENSG00000101265; Tissue enhanced (brain, retina).
DR MIM; 609492; gene.
DR neXtProt; NX_P50749; -.
DR OpenTargets; ENSG00000101265; -.
DR PharmGKB; PA34246; -.
DR VEuPathDB; HostDB:ENSG00000101265; -.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000158546; -.
DR HOGENOM; CLU_018893_1_0_1; -.
DR InParanoid; P50749; -.
DR OMA; RYNYLRN; -.
DR OrthoDB; 1043350at2759; -.
DR PhylomeDB; P50749; -.
DR TreeFam; TF319243; -.
DR PathwayCommons; P50749; -.
DR SignaLink; P50749; -.
DR BioGRID-ORCS; 9770; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; RASSF2; human.
DR GeneWiki; RASSF2; -.
DR GenomeRNAi; 9770; -.
DR Pharos; P50749; Tbio.
DR PRO; PR:P50749; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P50749; protein.
DR Bgee; ENSG00000101265; Expressed in inferior vagus X ganglion and 183 other tissues.
DR Genevisible; P50749; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0004672; F:protein kinase activity; IGI:MGI.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0038168; P:epidermal growth factor receptor signaling pathway via I-kappaB kinase/NF-kappaB cascade; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033614; RASSF1-6.
DR InterPro; IPR033618; RASSF2.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR PANTHER; PTHR22738:SF14; PTHR22738:SF14; 1.
DR Pfam; PF16517; Nore1-SARAH; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50951; SARAH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Centromere; Chromosome; Cytoplasm;
KW Kinetochore; Nucleus; Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..326
FT /note="Ras association domain-containing protein 2"
FT /id="PRO_0000097172"
FT DOMAIN 176..264
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 272..319
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 111..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..96
FT /note="MDYSHQTSLVPCGQDKYISKNELLLHLKTYNLYYEGQNLQLRHREEEDEFIV
FT EGLLNISWGLRRPIRLQMQDDNERIRPPPSSSSWHSGCNLGAQG -> MSLNWNLTLQN
FT EWPLLEFSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_055851"
FT VAR_SEQ 231..326
FT /note="EKQKLKATDYPLIARILQGPCEQISKVFLMEKDQVEEVTYDVAQYIKFEMPV
FT LKSFIQKLQEEEDREVKKLMRKYTVLRLMIRQRLEEIAETPATI -> GPM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_055852"
FT VARIANT 144
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs758816530)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035825"
FT CONFLICT 166
FT /note="R -> C (in Ref. 4; BAD96370)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> Q (in Ref. 4; BAD96370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37790 MW; C29D16376904249E CRC64;
MDYSHQTSLV PCGQDKYISK NELLLHLKTY NLYYEGQNLQ LRHREEEDEF IVEGLLNISW
GLRRPIRLQM QDDNERIRPP PSSSSWHSGC NLGAQGTTLK PLTVPKVQIS EVDAPPEGDQ
MPSSTDSRGL KPLQEDTPQL MRTRSDVGVR RRGNVRTPSD QRRIRRHRFS INGHFYNHKT
SVFTPAYGSV TNVRINSTMT TPQVLKLLLN KFKIENSAEE FALYVVHTSG EKQKLKATDY
PLIARILQGP CEQISKVFLM EKDQVEEVTY DVAQYIKFEM PVLKSFIQKL QEEEDREVKK
LMRKYTVLRL MIRQRLEEIA ETPATI
