RASF1_MOUSE
ID RASF1_MOUSE Reviewed; 340 AA.
AC Q99MK9; Q9WUF5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ras association domain-containing protein 1;
DE AltName: Full=Protein 123F2;
GN Name=Rassf1 {ECO:0000312|EMBL:AAK21200.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAK21201.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RX PubMed=11333291; DOI=10.1093/jnci/93.9.691;
RA Burbee D.G., Forgacs E., Zochbauer-Muller S., Shivakumar L., Fong K.,
RA Gao B., Randle D., Kondo M., Virmani A., Bader S., Sekido Y., Latif F.,
RA Milchgrub S., Toyooka S., Gazdar A.F., Lerman M.I., Zabarovsky E.,
RA White M., Minna J.D.;
RT "Epigenetic inactivation of RASSF1A in lung and breast cancers and
RT malignant phenotype suppression.";
RL J. Natl. Cancer Inst. 93:691-699(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK21200.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE PROMOTER USAGE.
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAK21200.1};
RA Dammann R., Pfeifer G.P.;
RT "A mouse locus containing the ortholog of the human RASSF1 tumor suppressor
RT gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH02173.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH02173.1};
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 INTERACTION WITH ECM2.
RX PubMed=17335777; DOI=10.1016/j.bbrc.2007.02.073;
RA Dmitriev R.I., Korneenko T.V., Bessonov A.A., Shakhparonov M.I.,
RA Modyanov N.N., Pestov N.B.;
RT "Characterization of hampin/MSL1 as a node in the nuclear interactome.";
RL Biochem. Biophys. Res. Commun. 355:1051-1057(2007).
RN [5]
RP INTERACTION WITH RAB39A AND RAB39B.
RX PubMed=23294242; DOI=10.1111/gtc.12028;
RA Takenaka M., Inoue H., Takeshima A., Kakura T., Hori T.;
RT "C. elegans Rassf homolog, rasf-1, is functionally associated with rab-39
RT Rab GTPase in oxidative stress response.";
RL Genes Cells 18:203-210(2013).
CC -!- FUNCTION: Potential tumor suppressor. Required for death receptor-
CC dependent apoptosis. Mediates activation of Mediates activation of
CC STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing
CC their dephosphorylation. When associated with MOAP1, promotes BAX
CC conformational change and translocation to mitochondrial membranes in
CC response to TNF and TNFSF10 stimulation. Isoform A interacts with
CC CDC20, an activator of the anaphase-promoting complex, APC, resulting
CC in the inhibition of APC activity and mitotic progression. Inhibits
CC proliferation by negatively regulating cell cycle progression at the
CC level of G1/S-phase transition by regulating accumulation of cyclin D1
CC protein. Isoform C has been shown not to perform these roles, no
CC function has been identified for this isoform. Isoform A disrupts
CC interactions among MDM2, DAXX and USP7, thus contributing to the
CC efficient activation of TP53 by promoting MDM2 self-ubiquitination in
CC cell-cycle checkpoint control in response to DNA damage (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAP1S and XPA (By similarity). Binds to the N-
CC terminal of CDC20 during prometaphase (By similarity). Binds to
CC STK3/MST2 and STK4/MST1 (By similarity). Recruited to the TNFRSF1A and
CC TNFRSF10A complexes in response to their respective cognate ligand,
CC after internalization (By similarity). Can self-associate (By
CC similarity). Part of a complex with MDM2, DAXX, RASSF1 and USP7 (By
CC similarity). {ECO:0000250|UniProtKB:Q9NS23}.
CC -!- SUBUNIT: [Isoform A]: Interacts with MOAP1 and E4F1 (By similarity).
CC Interacts with RSSF5 and probably associates with HRAS via a RSSF1
CC isoform A-RSSF5 heterodimer (By similarity). Interacts (via C-terminus)
CC with DAXX (via N-terminus); the interaction is independent of MDM2 and
CC TP53 (By similarity). Interacts (via N-terminus) with MDM2 (via C-
CC terminus); the interaction is independent of TP53 (By similarity).
CC Interacts with RAB39A (PubMed:23294242). Interacts with RAB39B; the
CC interaction is weak (PubMed:23294242). {ECO:0000250|UniProtKB:Q9NS23,
CC ECO:0000269|PubMed:23294242}.
CC -!- SUBUNIT: [Isoform C]: Interacts with ECM2 (PubMed:17335777). Interacts
CC with RAB39B; the interaction is strong (PubMed:23294242). Does not
CC interact with RAB39A (PubMed:23294242). {ECO:0000269|PubMed:17335777,
CC ECO:0000269|PubMed:23294242}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC Note=Localizes to cytoplasmic microtubules during interphase, to
CC bipolar centrosomes associated with microtubules during prophase, to
CC spindle fibers and spindle poles at metaphase and anaphase, to the
CC midzone during early telophase, and to the midbody in late telophase in
CC cells. Colocalizes with MDM2 in the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Nucleus {ECO:0000250}.
CC Note=Predominantly nuclear. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=A;
CC IsoId=Q99MK9-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q99MK9-2; Sequence=VSP_050779, VSP_050780;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF132851; AAD30061.1; -; mRNA.
DR EMBL; AF333027; AAK21200.1; -; Genomic_DNA.
DR EMBL; AF333027; AAK21201.1; -; Genomic_DNA.
DR EMBL; BC002173; AAH02173.1; -; mRNA.
DR CCDS; CCDS23494.1; -. [Q99MK9-2]
DR CCDS; CCDS57699.1; -. [Q99MK9-1]
DR RefSeq; NP_001230677.1; NM_001243748.1. [Q99MK9-1]
DR RefSeq; NP_062687.1; NM_019713.4. [Q99MK9-2]
DR AlphaFoldDB; Q99MK9; -.
DR SMR; Q99MK9; -.
DR BioGRID; 207877; 32.
DR IntAct; Q99MK9; 31.
DR MINT; Q99MK9; -.
DR STRING; 10090.ENSMUSP00000010211; -.
DR iPTMnet; Q99MK9; -.
DR PhosphoSitePlus; Q99MK9; -.
DR EPD; Q99MK9; -.
DR MaxQB; Q99MK9; -.
DR PaxDb; Q99MK9; -.
DR PRIDE; Q99MK9; -.
DR ProteomicsDB; 255104; -. [Q99MK9-1]
DR ProteomicsDB; 255105; -. [Q99MK9-2]
DR Antibodypedia; 30900; 543 antibodies from 36 providers.
DR DNASU; 56289; -.
DR Ensembl; ENSMUST00000010211; ENSMUSP00000010211; ENSMUSG00000010067. [Q99MK9-2]
DR Ensembl; ENSMUST00000093786; ENSMUSP00000091301; ENSMUSG00000010067. [Q99MK9-1]
DR GeneID; 56289; -.
DR KEGG; mmu:56289; -.
DR UCSC; uc009rlq.2; mouse. [Q99MK9-2]
DR UCSC; uc012hag.2; mouse. [Q99MK9-1]
DR CTD; 11186; -.
DR MGI; MGI:1928386; Rassf1.
DR VEuPathDB; HostDB:ENSMUSG00000010067; -.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000155664; -.
DR HOGENOM; CLU_045544_0_1_1; -.
DR InParanoid; Q99MK9; -.
DR PhylomeDB; Q99MK9; -.
DR TreeFam; TF319243; -.
DR BioGRID-ORCS; 56289; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rassf1; mouse.
DR PRO; PR:Q99MK9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99MK9; protein.
DR Bgee; ENSMUSG00000010067; Expressed in optic fissure and 248 other tissues.
DR ExpressionAtlas; Q99MK9; baseline and differential.
DR Genevisible; Q99MK9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033600; RASSF1.
DR InterPro; IPR033614; RASSF1-6.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR PANTHER; PTHR22738:SF12; PTHR22738:SF12; 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 Acetylation; Alternative promoter usage; Cell cycle; Cytoplasm;
KW Cytoskeleton; Metal-binding; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NS23"
FT CHAIN 2..340
FT /note="Ras association domain-containing protein 1"
FT /id="PRO_0000068892"
FT DOMAIN 194..288
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 290..337
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT ZN_FING 51..101
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 2..115
FT /note="Mediates interaction with E4F1"
FT /evidence="ECO:0000250"
FT REGION 175..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..314
FT /note="MOAP1-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS23"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS23"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11333291,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050779"
FT VAR_SEQ 71..119
FT /note="FIWGVVRKGLQCAHCKFTCHYRCRALVCLDCCGPRDLGWDSALERDTNV ->
FT MGEAETPSFEMTWSSTTSSGYCSQEDSDSELEQYFTARTSLVRRPRRDQ (in
FT isoform C)"
FT /evidence="ECO:0000303|PubMed:11333291,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_050780"
SQ SEQUENCE 340 AA; 38789 MW; 7DEBA4AEE705757F CRC64;
MSAEPELIEL RELAPSGRIG PGRTRLERAN ALRIAPGTTR NPSQQHVPGR GHRFQPAGPT
THTWCDLCGD FIWGVVRKGL QCAHCKFTCH YRCRALVCLD CCGPRDLGWD SALERDTNVD
EAVERETPDL SQAETEQKIK DYNGQINSNL FMSLNKDGSY TGFIKVQLKL VRPVSVPSSK
KPPSLQDARR GTGRSTAVKR RTSFYLPKDA IKHLHVLSRT RAREVIEALL RKFMVVDDPR
KFALFERTER HGQVYLRKLS DDEQPLKLRL LAGPSEKALS FVLKENDSGE VNWDAFSMPE
LHNFLRILQR EEEEHLRQIL QKYSRCRQKI QEALHACPLG
