RASF4_HUMAN
ID RASF4_HUMAN Reviewed; 321 AA.
AC Q9H2L5; Q86WH5; Q86WH6; Q86WH7; Q8N5A9; Q8TCK6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ras association domain-containing protein 4;
GN Name=RASSF4; ORFNames=AD037;
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; 2; 3 AND 4).
RA Burbee D.G., White M.A., Miller D.S., Muller C.Y., Minna J.D.;
RT "RASSF4 (AD037) is transcriptionally repressed by an epigenetic mechanism
RT in ovarian cancer cell lines.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-321.
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 FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH KRAS.
RX PubMed=15574778; DOI=10.1158/0008-5472.can-04-2065;
RA Eckfeld K., Hesson L., Vos M.D., Bieche I., Latif F., Clark G.J.;
RT "RASSF4/AD037 is a potential ras effector/tumor suppressor of the RASSF
RT family.";
RL Cancer Res. 64:8688-8693(2004).
CC -!- FUNCTION: Potential tumor suppressor. May act as a KRAS effector
CC protein. May promote apoptosis and cell cycle arrest.
CC {ECO:0000269|PubMed:15574778}.
CC -!- SUBUNIT: Interacts directly with activated KRAS in a GTP-dependent
CC manner. {ECO:0000269|PubMed:15574778}.
CC -!- INTERACTION:
CC Q9H2L5; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-2933362, EBI-1003700;
CC Q9H2L5; O14964: HGS; NbExp=3; IntAct=EBI-2933362, EBI-740220;
CC Q9H2L5; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-2933362, EBI-9091197;
CC Q9H2L5; P43360: MAGEA6; NbExp=6; IntAct=EBI-2933362, EBI-1045155;
CC Q9H2L5; Q13188: STK3; NbExp=11; IntAct=EBI-2933362, EBI-992580;
CC Q9H2L5; Q13043: STK4; NbExp=6; IntAct=EBI-2933362, EBI-367376;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q9H2L5-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=Q9H2L5-2; Sequence=VSP_019356, VSP_019357;
CC Name=3; Synonyms=B;
CC IsoId=Q9H2L5-3; Sequence=VSP_019355;
CC Name=4; Synonyms=D;
CC IsoId=Q9H2L5-4; Sequence=VSP_019358, VSP_019359;
CC -!- TISSUE SPECIFICITY: Widely expressed. Frequently down-regulated in
CC tumor cell lines. {ECO:0000269|PubMed:15574778}.
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DR EMBL; AY216713; AAO61138.1; -; mRNA.
DR EMBL; AY216714; AAO61139.1; -; mRNA.
DR EMBL; AY216715; AAO61140.1; -; mRNA.
DR EMBL; AY216716; AAO61141.1; -; mRNA.
DR EMBL; AF260335; AAG44666.1; -; mRNA.
DR EMBL; AL353801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032593; AAH32593.1; -; mRNA.
DR EMBL; AL713716; CAD28511.1; -; mRNA.
DR CCDS; CCDS7208.1; -. [Q9H2L5-1]
DR RefSeq; NP_114412.2; NM_032023.3. [Q9H2L5-1]
DR AlphaFoldDB; Q9H2L5; -.
DR BioGRID; 123820; 7.
DR IntAct; Q9H2L5; 10.
DR MINT; Q9H2L5; -.
DR STRING; 9606.ENSP00000339692; -.
DR iPTMnet; Q9H2L5; -.
DR PhosphoSitePlus; Q9H2L5; -.
DR BioMuta; RASSF4; -.
DR DMDM; 109892952; -.
DR EPD; Q9H2L5; -.
DR jPOST; Q9H2L5; -.
DR MassIVE; Q9H2L5; -.
DR MaxQB; Q9H2L5; -.
DR PaxDb; Q9H2L5; -.
DR PeptideAtlas; Q9H2L5; -.
DR PRIDE; Q9H2L5; -.
DR ProteomicsDB; 80562; -. [Q9H2L5-1]
DR ProteomicsDB; 80563; -. [Q9H2L5-2]
DR ProteomicsDB; 80564; -. [Q9H2L5-3]
DR ProteomicsDB; 80565; -. [Q9H2L5-4]
DR Antibodypedia; 26967; 184 antibodies from 28 providers.
DR DNASU; 83937; -.
DR Ensembl; ENST00000340258.10; ENSP00000339692.4; ENSG00000107551.21. [Q9H2L5-1]
DR GeneID; 83937; -.
DR KEGG; hsa:83937; -.
DR MANE-Select; ENST00000340258.10; ENSP00000339692.4; NM_032023.4; NP_114412.2.
DR UCSC; uc001jbo.4; human. [Q9H2L5-1]
DR CTD; 83937; -.
DR DisGeNET; 83937; -.
DR GeneCards; RASSF4; -.
DR HGNC; HGNC:20793; RASSF4.
DR HPA; ENSG00000107551; Tissue enhanced (brain).
DR MIM; 610559; gene.
DR neXtProt; NX_Q9H2L5; -.
DR OpenTargets; ENSG00000107551; -.
DR PharmGKB; PA134951366; -.
DR VEuPathDB; HostDB:ENSG00000107551; -.
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000160176; -.
DR HOGENOM; CLU_018893_1_0_1; -.
DR InParanoid; Q9H2L5; -.
DR OMA; HAPGEAQ; -.
DR PhylomeDB; Q9H2L5; -.
DR TreeFam; TF319243; -.
DR PathwayCommons; Q9H2L5; -.
DR SignaLink; Q9H2L5; -.
DR BioGRID-ORCS; 83937; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; RASSF4; human.
DR GenomeRNAi; 83937; -.
DR Pharos; Q9H2L5; Tbio.
DR PRO; PR:Q9H2L5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H2L5; protein.
DR Bgee; ENSG00000107551; Expressed in right lobe of thyroid gland and 178 other tissues.
DR ExpressionAtlas; Q9H2L5; baseline and differential.
DR Genevisible; Q9H2L5; HS.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033614; RASSF1-6.
DR InterPro; IPR033622; RASSF4.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR PANTHER; PTHR22738:SF4; PTHR22738:SF4; 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; Phosphoprotein; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..321
FT /note="Ras association domain-containing protein 4"
FT /id="PRO_0000240398"
FT DOMAIN 174..262
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 270..317
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 79..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CB96"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019355"
FT VAR_SEQ 29..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019356"
FT VAR_SEQ 94
FT /note="L -> LGCWSLLLGLSSLSLPAAISALQLSVFR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019357"
FT VAR_SEQ 95..126
FT /note="KEPSPQNGNITAQGPSIQPVHKAESSTDSSGP -> APGGGRGGPPADADQE
FT RRQLHEPEEAQ (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019358"
FT VAR_SEQ 127..321
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019359"
FT VARIANT 10
FT /note="H -> Y (in dbSNP:rs34692238)"
FT /id="VAR_034438"
FT VARIANT 88
FT /note="R -> G (in dbSNP:rs870957)"
FT /id="VAR_034439"
FT CONFLICT 107
FT /note="Q -> K (in Ref. 1; AAG44666 and 2; AAO61138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 36748 MW; 8EB5990165886D99 CRC64;
MKEDCLPSSH VPISDSKSIQ KSELLGLLKT YNCYHEGKSF QLRHREEEGT LIIEGLLNIA
WGLRRPIRLQ MQDDREQVHL PSTSWMPRRP SCPLKEPSPQ NGNITAQGPS IQPVHKAESS
TDSSGPLEEA EEAPQLMRTK SDASCMSQRR PKCRAPGEAQ RIRRHRFSIN GHFYNHKTSV
FTPAYGSVTN VRVNSTMTTL QVLTLLLNKF RVEDGPSEFA LYIVHESGER TKLKDCEYPL
ISRILHGPCE KIARIFLMEA DLGVEVPHEV AQYIKFEMPV LDSFVEKLKE EEEREIIKLT
MKFQALRLTM LQRLEQLVEA K
