CJ090_MOUSE
ID CJ090_MOUSE Reviewed; 644 AA.
AC D2J0Y4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=(E2-independent) E3 ubiquitin-conjugating enzyme FATS {ECO:0000305};
DE EC=2.3.2.- {ECO:0000269|PubMed:24240685};
DE AltName: Full=Centrosomal protein C10orf90 homolog {ECO:0000305};
DE AltName: Full=E2/E3 hybrid ubiquitin-protein ligase FATS {ECO:0000305};
DE AltName: Full=Fragile-site associated tumor suppressor homolog {ECO:0000303|PubMed:20843368, ECO:0000303|PubMed:24240685};
DE Short=FATS {ECO:0000303|PubMed:20843368, ECO:0000303|PubMed:24240685};
GN Name=D7Ertd443e {ECO:0000312|MGI:MGI:1196431};
GN Synonyms=Fats {ECO:0000303|PubMed:20843368, ECO:0000303|PubMed:24240685};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=20843368; DOI=10.1186/1476-4598-9-244;
RA Zhang X., Zhang Q., Zhang J., Qiu L., Yan S.S., Feng J., Sun Y., Huang X.,
RA Lu K.H., Li Z.;
RT "FATS is a transcriptional target of p53 and associated with antitumor
RT activity.";
RL Mol. Cancer 9:244-244(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH HDAC1, AND FUNCTION.
RX PubMed=20154723; DOI=10.1038/onc.2010.19;
RA Li Z., Zhang Q., Mao J.H., Weise A., Mrasek K., Fan X., Zhang X., Liehr T.,
RA Lu K.H., Balmain A., Cai W.W.;
RT "An HDAC1-binding domain within FATS bridges p21 turnover to radiation-
RT induced tumorigenesis.";
RL Oncogene 29:2659-2671(2010).
RN [5]
RP FUNCTION, INTERACTION WITH TP53, DOMAIN, AND MUTAGENESIS OF CYS-118;
RP CYS-202; CYS-211 AND CYS-247.
RX PubMed=24240685; DOI=10.1038/onc.2013.494;
RA Yan S., Qiu L., Ma K., Zhang X., Zhao Y., Zhang J., Li X., Hao X., Li Z.;
RT "FATS is an E2-independent ubiquitin ligase that stabilizes p53 and
RT promotes its activation in response to DNA damage.";
RL Oncogene 33:5424-5433(2014).
CC -!- FUNCTION: Tumor suppressor that is required to sustain G2/M checkpoint
CC after DNA damage (PubMed:20843368, PubMed:20154723, PubMed:24240685).
CC Acts as a p53/TP53 activator by inhibiting MDM2 binding to p53/TP53 and
CC stimulating non-proteolytic polyubiquitination of p53/TP53. Exhibits
CC ubiquitin ligase (E3) activity and assemble ubiquitin polymers through
CC 'Lys-11'- (K11-), 'Lys-29'- (K29-) and 'Lys-63'- (K63)-linkages,
CC independently of the ubiquitin-conjugating enzyme (E2). Promotes
CC p53/TP53-dependent transcription of CDKN1A/p21, leading to robust
CC checkpoint response (PubMed:24240685). Mediates CDKN1A/p21 protein
CC stability in a ubiquitin-independent manner. Interacts with HDAC1 and
CC prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation
CC and stabilization of CDKN1A/p21 (PubMed:20154723). May have a role in
CC the assembly of primary cilia (By similarity).
CC {ECO:0000250|UniProtKB:Q96M02, ECO:0000269|PubMed:20154723,
CC ECO:0000269|PubMed:20843368, ECO:0000269|PubMed:24240685}.
CC -!- SUBUNIT: Interacts with HDAC1; the interaction prevents binding of
CC HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization
CC of CDKN1A/p21 (PubMed:20154723). Interacts with p53/TP53; the
CC interaction inhibits binding of p53/TP53 and MDM2 (PubMed:24240685).
CC {ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:24240685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96M02}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q96M02}. Note=Localizes to the actin
CC cytoskeleton in a proportion of cells. Colocalizes with centriolar
CC acetylated tubulin (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q96M02}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Weak expression found
CC in brain, lung, heart, ovary, thymus, spleen and kidney.
CC {ECO:0000269|PubMed:20843368}.
CC -!- INDUCTION: Upon DNA damage by agents such as ionizing radiation, UV and
CC actinomycin D. Activated by p53/TP53. {ECO:0000269|PubMed:20843368}.
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DR EMBL; GQ499374; ACZ64206.1; -; mRNA.
DR EMBL; AC124369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL17791.1; -; Genomic_DNA.
DR CCDS; CCDS57590.1; -.
DR RefSeq; NP_001074800.1; NM_001081331.1.
DR RefSeq; NP_001186870.1; NM_001199941.1.
DR RefSeq; XP_011240206.1; XM_011241904.2.
DR RefSeq; XP_011240207.1; XM_011241905.2.
DR AlphaFoldDB; D2J0Y4; -.
DR SMR; D2J0Y4; -.
DR STRING; 10090.ENSMUSP00000134479; -.
DR iPTMnet; D2J0Y4; -.
DR PhosphoSitePlus; D2J0Y4; -.
DR PaxDb; D2J0Y4; -.
DR PeptideAtlas; D2J0Y4; -.
DR PRIDE; D2J0Y4; -.
DR ProteomicsDB; 285449; -.
DR Antibodypedia; 48773; 24 antibodies from 10 providers.
DR Ensembl; ENSMUST00000094002; ENSMUSP00000091539; ENSMUSG00000030994.
DR GeneID; 71007; -.
DR KEGG; mmu:71007; -.
DR UCSC; uc009kds.1; mouse.
DR CTD; 71007; -.
DR MGI; MGI:1196431; D7Ertd443e.
DR VEuPathDB; HostDB:ENSMUSG00000030994; -.
DR eggNOG; ENOG502S6G8; Eukaryota.
DR GeneTree; ENSGT00940000153123; -.
DR InParanoid; D2J0Y4; -.
DR OMA; HEYWVTH; -.
DR OrthoDB; 460739at2759; -.
DR PhylomeDB; D2J0Y4; -.
DR BioGRID-ORCS; 71007; 0 hits in 71 CRISPR screens.
DR ChiTaRS; D7Ertd443e; mouse.
DR PRO; PR:D2J0Y4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; D2J0Y4; protein.
DR Bgee; ENSMUSG00000030994; Expressed in animal zygote and 77 other tissues.
DR ExpressionAtlas; D2J0Y4; baseline and differential.
DR Genevisible; D2J0Y4; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR InterPro; IPR029299; ALMS_motif.
DR InterPro; IPR041179; C10orf90_N.
DR InterPro; IPR029561; FATS.
DR PANTHER; PTHR21553:SF24; PTHR21553:SF24; 1.
DR Pfam; PF15309; ALMS_motif; 1.
DR Pfam; PF17730; Centro_C10orf90; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Transferase;
KW Tumor suppressor; Ubl conjugation pathway.
FT CHAIN 1..644
FT /note="(E2-independent) E3 ubiquitin-conjugating enzyme
FT FATS"
FT /id="PRO_0000413487"
FT REGION 1..67
FT /note="Required for interaction with p53/TP53"
FT /evidence="ECO:0000269|PubMed:24240685"
FT REGION 62..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..175
FT /note="Required for interaction with HDAC1"
FT /evidence="ECO:0000269|PubMed:20154723"
FT REGION 305..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..644
FT /note="ALMS motif"
FT COILED 598..629
FT /evidence="ECO:0000255"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 118
FT /note="C->G: No effect on p53/TP53 polyubiquitination."
FT /evidence="ECO:0000269|PubMed:24240685"
FT MUTAGEN 202
FT /note="C->G: No effect on p53/TP53 polyubiquitination."
FT /evidence="ECO:0000269|PubMed:24240685"
FT MUTAGEN 211
FT /note="C->G: Abolishes p53/TP53 polyubiquitination. No
FT effect on interaction with p53/TP53."
FT /evidence="ECO:0000269|PubMed:24240685"
FT MUTAGEN 247
FT /note="C->G: No effect on p53/TP53 polyubiquitination."
FT /evidence="ECO:0000269|PubMed:24240685"
SQ SEQUENCE 644 AA; 71521 MW; 343EDBF0C61A0577 CRC64;
MISPVVISRL IDEKKSMENG AILPQAIAQP QLCPTKPALA RRDGVSMHRR FALSPDRLGI
LTPSDDQGLE TEPLSTGDNL GKGSHSGFSS ITITARRVGP PASSLVWDTF RDPLCPKCKA
KDALFQEPPV LAGDAHLCQH NRPFTCTESP SNGSVEGMKV FQAHSRLSAR QDYWVTHTND
NEDSFSSDNS PSRKVPLVFS SCVHFRVSQQ CPNAIYYLDK SLSVPLERPQ IASPKMHRSV
LSLSLRCSSH QLTADGVDSS ANGEPISTAL SQELSEGKQD LLGPQWGQPQ GGHWKESPAL
VPVHLGSGTC PRTGSPPLEN VKFADVGRNQ VPVRKEKEDH ATCTSSSHTN QLSIHIPGWS
YRAETKVLSG SKKQQQEAQR TLPAFPVGQK TIKHFPPEGD SSPSSDGQPS ILSESNERQH
PYFMIPRVPL PGFYCPLQTG CASLQEDGAV QIETHFPKDY TCCDLVVKLK ECEKNEDPTV
TPEPSPATPS PSTPEGAQSS DPSEDSYEPL LASSMTLQEA LEVHRPQFIS RSQERLQKLK
RMVQQRKTQQ KESLGQKQSL LPVRANKKQF TIPHPLSDNL FKPKERCISE KEMHMRSKRI
YNNLPEVKKK KEEQKKRMIL QSNRLRAEVF KKQLLDQLLQ RNAV
