CJ090_HUMAN
ID CJ090_HUMAN Reviewed; 699 AA.
AC Q96M02; B9EIQ9; Q5JRP6; Q5T023; Q8NCV5; Q8WU75;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=(E2-independent) E3 ubiquitin-conjugating enzyme FATS {ECO:0000305};
DE EC=2.3.2.- {ECO:0000250|UniProtKB:D2J0Y4};
DE AltName: Full=Centrosomal protein C10orf90 {ECO:0000305};
DE AltName: Full=E2/E3 hybrid ubiquitin-protein ligase FATS {ECO:0000305};
DE AltName: Full=Fragile-site associated tumor suppressor homolog {ECO:0000250|UniProtKB:D2J0Y4};
DE Short=FATS {ECO:0000250|UniProtKB:D2J0Y4};
GN Name=C10orf90 {ECO:0000312|HGNC:HGNC:26563};
GN Synonyms=FATS {ECO:0000250|UniProtKB:D2J0Y4};
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-262.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-662 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-699 (ISOFORM 2).
RA Guo J.H., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION.
RX PubMed=20844083; DOI=10.1091/mbc.e10-03-0246;
RA Knorz V.J., Spalluto C., Lessard M., Purvis T.L., Adigun F.F., Collin G.B.,
RA Hanley N.A., Wilson D.I., Hearn T.;
RT "Centriolar association of ALMS1 and likely centrosomal functions of the
RT ALMS motif-containing proteins C10orf90 and KIAA1731.";
RL Mol. Biol. Cell 21:3617-3629(2010).
CC -!- FUNCTION: Tumor suppressor that is required to sustain G2/M checkpoint
CC after DNA damage. Acts as a p53/TP53 activator by inhibiting MDM2
CC binding to p53/TP53 and stimulating non-proteolytic polyubiquitination
CC of p53/TP53. Exhibits ubiquitin ligase (E3) activity and assemble
CC ubiquitin polymers through 'Lys-11'- (K11-), 'Lys-29'- (K29-) and 'Lys-
CC 63'- (K63)-linkages, independently of the ubiquitin-conjugating enzyme
CC (E2). Promotes p53/TP53-dependent transcription of CDKN1A/p21, leading
CC to robust checkpoint response. Mediates CDKN1A/p21 protein stability in
CC a ubiquitin-independent manner. Interacts with HDAC1 and prevents
CC binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and
CC stabilization of CDKN1A/p21 (By similarity). May have a role in the
CC assembly of primary cilia (Probable). {ECO:0000250|UniProtKB:D2J0Y4,
CC ECO:0000305|PubMed:20844083}.
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. Interacts with p53/TP53; the interaction inhibits
CC binding of p53/TP53 and MDM2. {ECO:0000250|UniProtKB:D2J0Y4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20844083}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:20844083}. Note=Localizes to the actin cytoskeleton
CC in a proportion of cells. Colocalizes with centriolar acetylated
CC tubulin. {ECO:0000269|PubMed:20844083}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96M02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96M02-2; Sequence=VSP_023458;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20911.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL583860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021140; AAH21140.1; -; mRNA.
DR EMBL; BC140898; AAI40899.1; -; mRNA.
DR EMBL; BC146869; AAI46870.1; -; mRNA.
DR EMBL; AK057500; BAB71512.1; -; mRNA.
DR EMBL; AF435960; AAM20911.1; ALT_INIT; mRNA.
DR CCDS; CCDS31310.1; -. [Q96M02-1]
DR RefSeq; NP_001004298.2; NM_001004298.2. [Q96M02-1]
DR AlphaFoldDB; Q96M02; -.
DR SMR; Q96M02; -.
DR BioGRID; 125615; 9.
DR IntAct; Q96M02; 3.
DR STRING; 9606.ENSP00000284694; -.
DR iPTMnet; Q96M02; -.
DR PhosphoSitePlus; Q96M02; -.
DR BioMuta; C10orf90; -.
DR DMDM; 143377520; -.
DR EPD; Q96M02; -.
DR MassIVE; Q96M02; -.
DR PaxDb; Q96M02; -.
DR PeptideAtlas; Q96M02; -.
DR PRIDE; Q96M02; -.
DR ProteomicsDB; 77276; -. [Q96M02-1]
DR ProteomicsDB; 77277; -. [Q96M02-2]
DR Antibodypedia; 48773; 24 antibodies from 10 providers.
DR DNASU; 118611; -.
DR Ensembl; ENST00000284694.11; ENSP00000284694.7; ENSG00000154493.20. [Q96M02-1]
DR GeneID; 118611; -.
DR KEGG; hsa:118611; -.
DR UCSC; uc001ljq.4; human. [Q96M02-1]
DR CTD; 118611; -.
DR DisGeNET; 118611; -.
DR GeneCards; C10orf90; -.
DR HGNC; HGNC:26563; C10orf90.
DR HPA; ENSG00000154493; Tissue enriched (brain).
DR MIM; 617735; gene.
DR neXtProt; NX_Q96M02; -.
DR OpenTargets; ENSG00000154493; -.
DR PharmGKB; PA134895930; -.
DR VEuPathDB; HostDB:ENSG00000154493; -.
DR eggNOG; ENOG502S6G8; Eukaryota.
DR GeneTree; ENSGT00940000153123; -.
DR HOGENOM; CLU_026504_0_0_1; -.
DR InParanoid; Q96M02; -.
DR OMA; HEYWVTH; -.
DR OrthoDB; 460739at2759; -.
DR PhylomeDB; Q96M02; -.
DR PathwayCommons; Q96M02; -.
DR SignaLink; Q96M02; -.
DR BioGRID-ORCS; 118611; 9 hits in 1011 CRISPR screens.
DR ChiTaRS; C10orf90; human.
DR GenomeRNAi; 118611; -.
DR Pharos; Q96M02; Tbio.
DR PRO; PR:Q96M02; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96M02; protein.
DR Bgee; ENSG00000154493; Expressed in C1 segment of cervical spinal cord and 102 other tissues.
DR ExpressionAtlas; Q96M02; baseline and differential.
DR Genevisible; Q96M02; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Reference proteome;
KW Transferase; Tumor suppressor; Ubl conjugation pathway.
FT CHAIN 1..699
FT /note="(E2-independent) E3 ubiquitin-conjugating enzyme
FT FATS"
FT /id="PRO_0000279492"
FT REGION 48..116
FT /note="Required for interaction with p53/TP53"
FT /evidence="ECO:0000250|UniProtKB:D2J0Y4"
FT REGION 107..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..224
FT /note="Required for interaction with HDAC1"
FT /evidence="ECO:0000250"
FT REGION 443..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..699
FT /note="ALMS motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 415..511
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_023458"
FT VARIANT 57
FT /note="M -> I (in dbSNP:rs11558415)"
FT /id="VAR_050855"
FT VARIANT 134
FT /note="R -> H (in dbSNP:rs11245008)"
FT /id="VAR_030908"
FT VARIANT 262
FT /note="D -> N (in dbSNP:rs11245007)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030909"
FT VARIANT 531
FT /note="D -> E (in dbSNP:rs12412320)"
FT /id="VAR_050856"
FT CONFLICT 654
FT /note="R -> G (in Ref. 3; BAB71512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 77910 MW; 099E8CEF3C910F1E CRC64;
MLKLSGEGLR DSYHSRRDQI ALKNLQSDVT EAKSDFTKET LASQNTKMIS SIVISQMIDE
NKSRENRASL PLPCAIAQSR AHHAKQSLAN RSGVNIHRAF ALLPGRLGIP APSDERGPEA
ELPPKEERPC GGPRRGFASI TITARRVGPP ARALVWGTAG DSLCPKCRAE DTLFQAPPAL
ANGAHPGRHQ RSFACTEFSR NSSVVRLKVP EAHTGLCERR KYWVTHADDK ETSFSPDTPL
SGKSPLVFSS CVHLRVSQQC PDSIYYVDKS LSVPIEPPQI ASPKMHRSVL SLNLNCSSHR
LTADGVDGLV NREPISEALK QELLEGDQDL VGQRWNPGLQ ESHLKETPSL RRVHLGTGAC
PWSGSFPLEN TELANVGANQ VTVRKGEKDH TTHCHASDHA NQLSIHIPGW SYRAVHTKVF
SGSSKRQQGE VCMTVSAPPV EQKPTRHFLP IGDSSPSDDC LSRDLSEPTE RRHQSFLKPR
ILFPGFLCPL QDVCASLQED NGVQIESKFP KGDYTCCDLV VKIKECKKSE DPTTPEPSPA
APSPAPRDGA GSPGLSEDCS ESQQTPARSL TLQEALEVRK PQFISRSQER LKKLEHMVQQ
RKAQRKEDLR QKQSLLPIRT SKKQFTIPHP LSDNLFKPKE RCISEKEMHM RSKRIYDNLP
EVKKKKEEQR KRVILQSNRL RAEVFKKQLL DQLLQRNAV
