RASFA_HUMAN
ID RASFA_HUMAN Reviewed; 507 AA.
AC A6NK89;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ras association domain-containing protein 10;
GN Name=RASSF10;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP IDENTIFICATION.
RX PubMed=18272789; DOI=10.1091/mbc.e07-07-0652;
RA Sherwood V., Manbodh R., Sheppard C., Chalmers A.D.;
RT "RASSF7 is a member of a new family of RAS association domain-containing
RT proteins and is required for completing mitosis.";
RL Mol. Biol. Cell 19:1772-1782(2008).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOWN-REGULATION IN ASTROCYTIC
RP GLIOMAS.
RX PubMed=20956940; DOI=10.1038/onc.2010.471;
RA Hill V.K., Underhill-Day N., Krex D., Robel K., Sangan C.B.,
RA Summersgill H.R., Morris M., Gentle D., Chalmers A.D., Maher E.R.,
RA Latif F.;
RT "Epigenetic inactivation of the RASSF10 candidate tumor suppressor gene is
RT a frequent and an early event in gliomagenesis.";
RL Oncogene 30:978-989(2011).
CC -!- FUNCTION: Plays an important role in regulating embryonic neurogenesis.
CC {ECO:0000250|UniProtKB:Q8BL43}.
CC -!- INTERACTION:
CC A6NK89; Q96A05: ATP6V1E2; NbExp=3; IntAct=EBI-6912267, EBI-8650380;
CC A6NK89; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-6912267, EBI-947308;
CC A6NK89; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-6912267, EBI-744311;
CC A6NK89; G5E9W6: CCDC183; NbExp=3; IntAct=EBI-6912267, EBI-17212717;
CC A6NK89; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-6912267, EBI-11752486;
CC A6NK89; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-6912267, EBI-739624;
CC A6NK89; Q9UHF1: EGFL7; NbExp=3; IntAct=EBI-6912267, EBI-949532;
CC A6NK89; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-6912267, EBI-750700;
CC A6NK89; Q9BQ89: FAM110A; NbExp=5; IntAct=EBI-6912267, EBI-1752811;
CC A6NK89; Q5VUB5: FAM171A1; NbExp=3; IntAct=EBI-6912267, EBI-2682893;
CC A6NK89; O95257: GADD45G; NbExp=3; IntAct=EBI-6912267, EBI-448202;
CC A6NK89; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-6912267, EBI-11427343;
CC A6NK89; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-6912267, EBI-5916454;
CC A6NK89; O95751: LDOC1; NbExp=3; IntAct=EBI-6912267, EBI-740738;
CC A6NK89; P43360: MAGEA6; NbExp=3; IntAct=EBI-6912267, EBI-1045155;
CC A6NK89; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-6912267, EBI-10698339;
CC A6NK89; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-6912267, EBI-2872322;
CC A6NK89; Q2TAY7: SMU1; NbExp=3; IntAct=EBI-6912267, EBI-298027;
CC A6NK89; Q15561: TEAD4; NbExp=3; IntAct=EBI-6912267, EBI-747736;
CC A6NK89; P19429: TNNI3; NbExp=3; IntAct=EBI-6912267, EBI-704146;
CC A6NK89; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-6912267, EBI-11952721;
CC A6NK89; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-6912267, EBI-2130429;
CC A6NK89; O96014: WNT11; NbExp=3; IntAct=EBI-6912267, EBI-8058160;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20956940}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:20956940}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:20956940}. Note=During interphase, predominantly
CC cytoplasmic, although some nuclear staining in several tumor cell
CC contexts. During prophase, observed at developing centrosomes. Displays
CC persistent localization with centrosomally radiating microtubule
CC bundles until late telophase. Associates with spindle poles
CC particularly during metaphase and anaphase before relocating back to
CC the cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Tends to be down-regulated in
CC astrocytic gliomas due to promoter methylation. Methylation occurs
CC early in gliomagenesis and the extent of methylation parallels with
CC higher glioma grades, so that methylation is observed in close to 70%
CC WHO grade IV primary glioblastomas, but not in grade I astrocytomas.
CC {ECO:0000269|PubMed:20956940}.
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DR EMBL; AC084859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44542.2; -.
DR RefSeq; NP_001073990.2; NM_001080521.2.
DR AlphaFoldDB; A6NK89; -.
DR SMR; A6NK89; -.
DR BioGRID; 570026; 61.
DR IntAct; A6NK89; 63.
DR STRING; 9606.ENSP00000485526; -.
DR iPTMnet; A6NK89; -.
DR PhosphoSitePlus; A6NK89; -.
DR BioMuta; RASSF10; -.
DR jPOST; A6NK89; -.
DR MassIVE; A6NK89; -.
DR PeptideAtlas; A6NK89; -.
DR PRIDE; A6NK89; -.
DR ProteomicsDB; 1387; -.
DR Antibodypedia; 74573; 83 antibodies from 20 providers.
DR DNASU; 644943; -.
DR Ensembl; ENST00000529419.3; ENSP00000485526.1; ENSG00000189431.8.
DR GeneID; 644943; -.
DR KEGG; hsa:644943; -.
DR MANE-Select; ENST00000529419.3; ENSP00000485526.1; NM_001080521.3; NP_001073990.2.
DR UCSC; uc021qdz.2; human.
DR CTD; 644943; -.
DR DisGeNET; 644943; -.
DR GeneCards; RASSF10; -.
DR HGNC; HGNC:33984; RASSF10.
DR HPA; ENSG00000189431; Tissue enhanced (esophagus, salivary gland, skin).
DR MIM; 614713; gene.
DR neXtProt; NX_A6NK89; -.
DR OpenTargets; ENSG00000189431; -.
DR VEuPathDB; HostDB:ENSG00000189431; -.
DR eggNOG; KOG1574; Eukaryota.
DR GeneTree; ENSGT00950000182839; -.
DR HOGENOM; CLU_036954_0_0_1; -.
DR InParanoid; A6NK89; -.
DR OMA; KADLDYS; -.
DR OrthoDB; 592471at2759; -.
DR PhylomeDB; A6NK89; -.
DR PathwayCommons; A6NK89; -.
DR SignaLink; A6NK89; -.
DR BioGRID-ORCS; 644943; 5 hits in 133 CRISPR screens.
DR GenomeRNAi; 644943; -.
DR Pharos; A6NK89; Tbio.
DR PRO; PR:A6NK89; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; A6NK89; protein.
DR Bgee; ENSG00000189431; Expressed in esophagus squamous epithelium and 110 other tissues.
DR Genevisible; A6NK89; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR033593; N-RASSF.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033634; RASSF10.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15286; PTHR15286; 1.
DR PANTHER; PTHR15286:SF13; PTHR15286:SF13; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Neurogenesis; Reference proteome.
FT CHAIN 1..507
FT /note="Ras association domain-containing protein 10"
FT /id="PRO_0000332284"
FT DOMAIN 4..133
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 46..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..264
FT /evidence="ECO:0000255"
FT COILED 319..358
FT /evidence="ECO:0000255"
FT COMPBIAS 190..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 194
FT /note="Q -> H (in dbSNP:rs4323847)"
FT /id="VAR_042999"
SQ SEQUENCE 507 AA; 56900 MW; A9A5D0A546F61518 CRC64;
MDPSEKKISV WICQEEKLVS GLSRRTTCSD VVRVLLEDGC RRRRRQRRSR RLGSAGDPHG
PGELPEPPNE DDEDDDEALP QGMLCGPPQC YCIVEKWRGF ERILPNKTRI LRLWAAWGEE
QENVRFVLVR SEASLPNAGP RSAEARVVLS RERPCPARGA PARPSLAMTQ EKQRRVVRKA
FRKLAKLNRR RQQQTPSSCS STSSSTASSC SSSPRTHESA SVERMETLVH LVLSQDHTIR
QQVQRLHELD REIDHYEAKV HLDRMRRHGV NYVQDTYLVG AGIELDGSRP GEEPEEVAAE
AEEAAAAPPL AGEAQAAALE ELARRCDDLL RLQEQRVQQE ELLERLSAEI QEELNQRWMR
RRQEELAARE EPLEPDGGPD GELLLEQERV RTQLSTSLYI GLRLNTDLEA VKSDLDYSQQ
QWDSKKRELQ GLLQTLHTLE LTVAPDGAPG SGSPSREPGP QACADMWVDQ ARGLAKSGPG
NDEDSDTGLS SMHSQDSDSL PMCESLV
