RASF7_HUMAN
ID RASF7_HUMAN Reviewed; 373 AA.
AC Q02833; G5E9N9; Q3KP41; Q3KP42;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ras association domain-containing protein 7;
DE AltName: Full=HRAS1-related cluster protein 1;
GN Name=RASSF7; Synonyms=C11orf13, HRC1;
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).
RC TISSUE=Placenta;
RX PubMed=1339391; DOI=10.1016/s0888-7543(05)80221-6;
RA Weitzel J.N., Kasperczyk A., Mohan C., Krontiris T.G.;
RT "The HRAS1 gene cluster: two upstream regions recognizing transcripts and a
RT third encoding a gene with a leucine zipper domain.";
RL Genomics 14:309-319(1992).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ALA-89.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20629633; DOI=10.1042/bj20100883;
RA Recino A., Sherwood V., Flaxman A., Cooper W.N., Latif F., Ward A.,
RA Chalmers A.D.;
RT "Human RASSF7 regulates the microtubule cytoskeleton and is required for
RT spindle formation, Aurora B activation and chromosomal congression during
RT mitosis.";
RL Biochem. J. 430:207-213(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH MAP2K7 AND NRAS.
RX PubMed=21278800; DOI=10.1038/cdd.2010.137;
RA Takahashi S., Ebihara A., Kajiho H., Kontani K., Nishina H., Katada T.;
RT "RASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting the
RT activity of phosphorylated-MKK7.";
RL Cell Death Differ. 18:645-655(2011).
CC -!- FUNCTION: Negatively regulates stress-induced JNK activation and
CC apoptosis by promoting MAP2K7 phosphorylation and inhibiting its
CC ability to activate JNK. Following prolonged stress, anti-apoptotic
CC effect stops because of degradation of RASSF7 protein via the
CC ubiquitin-proteasome pathway. Required for the activation of AURKB and
CC chromosomal congression during mitosis where it stimulates microtubule
CC polymerization. {ECO:0000269|PubMed:20629633,
CC ECO:0000269|PubMed:21278800}.
CC -!- SUBUNIT: Interacts with MAP2K7 and GTP-bound NRAS.
CC {ECO:0000269|PubMed:21278800}.
CC -!- INTERACTION:
CC Q02833; O43639: NCK2; NbExp=5; IntAct=EBI-929013, EBI-713635;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:20629633}. Note=Colocalizes with
CC gamma-tubulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q02833-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02833-2; Sequence=VSP_004136, VSP_004137;
CC Name=3;
CC IsoId=Q02833-3; Sequence=VSP_045623;
CC -!- PTM: Polyubiquitinated and degraded by the proteasome upon prolonged
CC stress stimuli.
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DR EMBL; M91083; AAA58667.1; -; mRNA.
DR EMBL; AP006284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02351.1; -; Genomic_DNA.
DR EMBL; BC106921; AAI06922.1; -; mRNA.
DR EMBL; BC106922; AAI06923.1; -; mRNA.
DR CCDS; CCDS44505.1; -. [Q02833-3]
DR CCDS; CCDS44506.1; -. [Q02833-2]
DR CCDS; CCDS7702.1; -. [Q02833-1]
DR PIR; A44478; A44478.
DR PIR; B44478; B44478.
DR RefSeq; NP_001137465.1; NM_001143993.1. [Q02833-2]
DR RefSeq; NP_001137466.1; NM_001143994.1. [Q02833-3]
DR RefSeq; NP_003466.1; NM_003475.3. [Q02833-1]
DR RefSeq; XP_016873850.1; XM_017018361.1.
DR RefSeq; XP_016873851.1; XM_017018362.1.
DR AlphaFoldDB; Q02833; -.
DR SMR; Q02833; -.
DR BioGRID; 113735; 43.
DR IntAct; Q02833; 33.
DR MINT; Q02833; -.
DR STRING; 9606.ENSP00000380713; -.
DR iPTMnet; Q02833; -.
DR PhosphoSitePlus; Q02833; -.
DR BioMuta; RASSF7; -.
DR DMDM; 18202480; -.
DR EPD; Q02833; -.
DR jPOST; Q02833; -.
DR MassIVE; Q02833; -.
DR MaxQB; Q02833; -.
DR PaxDb; Q02833; -.
DR PeptideAtlas; Q02833; -.
DR PRIDE; Q02833; -.
DR ProteomicsDB; 33997; -.
DR ProteomicsDB; 58129; -. [Q02833-1]
DR ProteomicsDB; 58130; -. [Q02833-2]
DR Antibodypedia; 9750; 252 antibodies from 34 providers.
DR DNASU; 8045; -.
DR Ensembl; ENST00000397582.7; ENSP00000380712.3; ENSG00000099849.15. [Q02833-2]
DR Ensembl; ENST00000397583.8; ENSP00000380713.3; ENSG00000099849.15. [Q02833-1]
DR Ensembl; ENST00000431809.5; ENSP00000403068.1; ENSG00000099849.15. [Q02833-2]
DR Ensembl; ENST00000454668.2; ENSP00000405606.2; ENSG00000099849.15. [Q02833-3]
DR Ensembl; ENST00000622905.2; ENSP00000479652.1; ENSG00000273859.4.
DR GeneID; 8045; -.
DR KEGG; hsa:8045; -.
DR MANE-Select; ENST00000397583.8; ENSP00000380713.3; NM_003475.4; NP_003466.1.
DR UCSC; uc001lqb.4; human. [Q02833-1]
DR CTD; 8045; -.
DR DisGeNET; 8045; -.
DR GeneCards; RASSF7; -.
DR HGNC; HGNC:1166; RASSF7.
DR HPA; ENSG00000099849; Low tissue specificity.
DR MIM; 143023; gene.
DR neXtProt; NX_Q02833; -.
DR OpenTargets; ENSG00000099849; -.
DR PharmGKB; PA25480; -.
DR VEuPathDB; HostDB:ENSG00000099849; -.
DR eggNOG; KOG1574; Eukaryota.
DR GeneTree; ENSGT00950000182839; -.
DR HOGENOM; CLU_031151_0_1_1; -.
DR InParanoid; Q02833; -.
DR OMA; EREIQWE; -.
DR PhylomeDB; Q02833; -.
DR TreeFam; TF318385; -.
DR PathwayCommons; Q02833; -.
DR SignaLink; Q02833; -.
DR BioGRID-ORCS; 8045; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; RASSF7; human.
DR GenomeRNAi; 8045; -.
DR Pharos; Q02833; Tbio.
DR PRO; PR:Q02833; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q02833; protein.
DR Bgee; ENSG00000099849; Expressed in right uterine tube and 91 other tissues.
DR ExpressionAtlas; Q02833; baseline and differential.
DR Genevisible; Q02833; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR033593; N-RASSF.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033631; RASSF7.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15286; PTHR15286; 1.
DR PANTHER; PTHR15286:SF11; PTHR15286:SF11; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..373
FT /note="Ras association domain-containing protein 7"
FT /id="PRO_0000097173"
FT DOMAIN 6..89
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 122..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..227
FT /evidence="ECO:0000255"
FT COILED 248..297
FT /evidence="ECO:0000255"
FT COMPBIAS 302..320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 318..373
FT /note="GPLPPAREESLLGAPSESHAGAQPRPRGGPHDAELLEVAAAPAPEWCPLAAQ
FT PQAL -> WPP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045623"
FT VAR_SEQ 318..337
FT /note="GPLPPAREESLLGAPSESHA -> VGVVLGGGWEVRTWPSPTPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:1339391"
FT /id="VSP_004136"
FT VAR_SEQ 338..373
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1339391"
FT /id="VSP_004137"
FT VARIANT 89
FT /note="P -> A (in dbSNP:rs2242183)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_021859"
FT VARIANT 156
FT /note="R -> Q (in dbSNP:rs2242182)"
FT /id="VAR_021860"
SQ SEQUENCE 373 AA; 39945 MW; 55DF1DDB1C37CAF3 CRC64;
MLLGLAAMEL KVWVDGIQRV VCGVSEQTTC QEVVIALAQA IGQTGRFVLV QRLREKERQL
LPQECPVGAQ ATCGQFASDV QFVLRRTGPS LAGRPSSDSC PPPERCLIRA SLPVKPRAAL
GCEPRKTLTP EPAPSLSRPG PAAPVTPTPG CCTDLRGLEL RVQRNAEELG HEAFWEQELR
REQAREREGQ ARLQALSAAT AEHAARLQAL DAQARALEAE LQLAAEAPGP PSPMASATER
LHQDLAVQER QSAEVQGSLA LVSRALEAAE RALQAQAQEL EELNRELRQC NLQQFIQQTG
AALPPPPRPD RGPPGTQGPL PPAREESLLG APSESHAGAQ PRPRGGPHDA ELLEVAAAPA
PEWCPLAAQP QAL
