RASF2_MOUSE
ID RASF2_MOUSE Reviewed; 326 AA.
AC Q8BMS9; Q6A0B2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ras association domain-containing protein 2;
GN Name=Rassf2; Synonyms=Kiaa0168;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P50749}. Cytoplasm
CC {ECO:0000250|UniProtKB:P50749}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P50749}. Note=Translocates to the cytoplasm in
CC the presence of STK3/MST2 AND STK4/MST1.
CC {ECO:0000250|UniProtKB:P50749}.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32184.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172906; BAD32184.1; ALT_INIT; mRNA.
DR EMBL; AK028384; BAC25921.1; -; mRNA.
DR EMBL; BC057402; AAH57402.1; -; mRNA.
DR CCDS; CCDS16768.1; -.
DR RefSeq; NP_780654.1; NM_175445.4.
DR RefSeq; XP_006499202.1; XM_006499139.3.
DR RefSeq; XP_006499203.1; XM_006499140.3.
DR RefSeq; XP_006499204.1; XM_006499141.2.
DR RefSeq; XP_006499205.1; XM_006499142.2.
DR RefSeq; XP_006499206.1; XM_006499143.3.
DR RefSeq; XP_006499207.1; XM_006499144.3.
DR AlphaFoldDB; Q8BMS9; -.
DR SMR; Q8BMS9; -.
DR STRING; 10090.ENSMUSP00000028814; -.
DR iPTMnet; Q8BMS9; -.
DR PhosphoSitePlus; Q8BMS9; -.
DR EPD; Q8BMS9; -.
DR MaxQB; Q8BMS9; -.
DR PaxDb; Q8BMS9; -.
DR PeptideAtlas; Q8BMS9; -.
DR PRIDE; Q8BMS9; -.
DR ProteomicsDB; 255106; -.
DR Antibodypedia; 42660; 176 antibodies from 33 providers.
DR DNASU; 215653; -.
DR Ensembl; ENSMUST00000028814; ENSMUSP00000028814; ENSMUSG00000027339.
DR Ensembl; ENSMUST00000103182; ENSMUSP00000099471; ENSMUSG00000027339.
DR GeneID; 215653; -.
DR KEGG; mmu:215653; -.
DR UCSC; uc008mmf.2; mouse.
DR CTD; 9770; -.
DR MGI; MGI:2442060; Rassf2.
DR VEuPathDB; HostDB:ENSMUSG00000027339; -.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000158546; -.
DR HOGENOM; CLU_018893_1_0_1; -.
DR InParanoid; Q8BMS9; -.
DR OMA; RYNYLRN; -.
DR OrthoDB; 1043350at2759; -.
DR PhylomeDB; Q8BMS9; -.
DR TreeFam; TF319243; -.
DR BioGRID-ORCS; 215653; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Rassf2; mouse.
DR PRO; PR:Q8BMS9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BMS9; protein.
DR Bgee; ENSMUSG00000027339; Expressed in meninx and 194 other tissues.
DR ExpressionAtlas; Q8BMS9; baseline and differential.
DR Genevisible; Q8BMS9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0046849; P:bone remodeling; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
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 Cell cycle; Centromere; Chromosome; Cytoplasm; Kinetochore; Nucleus;
KW Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..326
FT /note="Ras association domain-containing protein 2"
FT /id="PRO_0000233038"
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"
SQ SEQUENCE 326 AA; 37973 MW; 5CEFDFC1BEA0F473 CRC64;
MDYTHQPALI PCGQDKYMPK SELLLHLKTY NLYYEGQNLQ LRHREEEDEF IVEGLLNISW
GLRRPIRLQM QDDHERIRPP PSSSSWHSGC NLGAQGTTLK PLTMPTVQIS EVDMPVEGLE
THSPTDSRGL KPVQEDTPQL MRTRSDVGVR RRGNVRTSSD QRRIRRHRFS INGHFYNHKT
SVFTPAYGSV TNVRINSTMT TPQVLKLLLN KFKIENSAEE FALYVVHTSG EKQRLKSSDY
PLIARILQGP CEQISKVFLM EKDQVEEVTY DVAQYIKFEM PVLKSFIQKL QEEEDREVEK
LMRKYTVLRL MIRQRLEEIA ETPETI
