SAS10_HUMAN
ID SAS10_HUMAN Reviewed; 479 AA.
AC Q9NQZ2; Q6FI82;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Something about silencing protein 10;
DE AltName: Full=Charged amino acid-rich leucine zipper 1;
DE Short=CRL1;
DE AltName: Full=Disrupter of silencing SAS10;
DE AltName: Full=UTP3 homolog;
GN Name=UTP3; Synonyms=CRLZ1, SAS10 {ECO:0000312|EMBL:AAF91408.1};
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] {ECO:0000312|EMBL:AAF91408.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAF91408.1};
RA Frye R.A.;
RT "Human and mouse homologs of yeast SAS10 disrupter of silencing gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAB66525.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala {ECO:0000312|EMBL:CAB66525.1};
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3] {ECO:0000312|EMBL:AAF91408.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB15588.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon {ECO:0000312|EMBL:BAB15588.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAH04546.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH04546.1};
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-365 AND SER-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; THR-362; SER-365 AND
RP SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-365 AND SER-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-365 AND SER-368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Essential for gene silencing: has a role in the structure of
CC silenced chromatin. Plays a role in the developing brain (By
CC similarity). {ECO:0000250|UniProtKB:Q12136,
CC ECO:0000250|UniProtKB:Q9JI13}.
CC -!- INTERACTION:
CC Q9NQZ2; Q8NDD1-6: C1orf131; NbExp=3; IntAct=EBI-714067, EBI-17761821;
CC Q9NQZ2; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-714067, EBI-5278764;
CC Q9NQZ2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-714067, EBI-739624;
CC Q9NQZ2; Q92997: DVL3; NbExp=3; IntAct=EBI-714067, EBI-739789;
CC Q9NQZ2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-714067, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
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DR EMBL; AF271212; AAF91408.1; -; mRNA.
DR EMBL; AL136590; CAB66525.1; -; mRNA.
DR EMBL; CR533544; CAG38575.1; -; mRNA.
DR EMBL; AK026909; BAB15588.1; -; mRNA.
DR EMBL; BC004546; AAH04546.1; -; mRNA.
DR CCDS; CCDS3546.1; -.
DR RefSeq; NP_065101.1; NM_020368.2.
DR PDB; 7MQ8; EM; 3.60 A; NB=1-479.
DR PDB; 7MQ9; EM; 3.87 A; NB=1-479.
DR PDB; 7MQA; EM; 2.70 A; NB=1-479.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9NQZ2; -.
DR BioGRID; 121342; 146.
DR IntAct; Q9NQZ2; 50.
DR MINT; Q9NQZ2; -.
DR STRING; 9606.ENSP00000254803; -.
DR iPTMnet; Q9NQZ2; -.
DR PhosphoSitePlus; Q9NQZ2; -.
DR BioMuta; UTP3; -.
DR DMDM; 76364208; -.
DR EPD; Q9NQZ2; -.
DR jPOST; Q9NQZ2; -.
DR MassIVE; Q9NQZ2; -.
DR MaxQB; Q9NQZ2; -.
DR PaxDb; Q9NQZ2; -.
DR PeptideAtlas; Q9NQZ2; -.
DR PRIDE; Q9NQZ2; -.
DR ProteomicsDB; 82231; -.
DR Antibodypedia; 24355; 127 antibodies from 23 providers.
DR DNASU; 57050; -.
DR Ensembl; ENST00000254803.4; ENSP00000254803.2; ENSG00000132467.4.
DR GeneID; 57050; -.
DR KEGG; hsa:57050; -.
DR MANE-Select; ENST00000254803.4; ENSP00000254803.2; NM_020368.3; NP_065101.1.
DR UCSC; uc003hfo.3; human.
DR CTD; 57050; -.
DR DisGeNET; 57050; -.
DR GeneCards; UTP3; -.
DR HGNC; HGNC:24477; UTP3.
DR HPA; ENSG00000132467; Low tissue specificity.
DR MIM; 611614; gene.
DR neXtProt; NX_Q9NQZ2; -.
DR OpenTargets; ENSG00000132467; -.
DR PharmGKB; PA162408779; -.
DR VEuPathDB; HostDB:ENSG00000132467; -.
DR eggNOG; KOG3118; Eukaryota.
DR GeneTree; ENSGT00500000044947; -.
DR HOGENOM; CLU_025161_1_0_1; -.
DR InParanoid; Q9NQZ2; -.
DR OMA; EEYIRPQ; -.
DR OrthoDB; 1451774at2759; -.
DR PhylomeDB; Q9NQZ2; -.
DR TreeFam; TF315177; -.
DR PathwayCommons; Q9NQZ2; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9NQZ2; -.
DR SIGNOR; Q9NQZ2; -.
DR BioGRID-ORCS; 57050; 475 hits in 1085 CRISPR screens.
DR ChiTaRS; UTP3; human.
DR GeneWiki; UTP3; -.
DR GenomeRNAi; 57050; -.
DR Pharos; Q9NQZ2; Tbio.
DR PRO; PR:Q9NQZ2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NQZ2; protein.
DR Bgee; ENSG00000132467; Expressed in parietal pleura and 205 other tissues.
DR Genevisible; Q9NQZ2; HS.
DR GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR InterPro; IPR018972; Sas10_C_dom.
DR PANTHER; PTHR13237; PTHR13237; 2.
DR Pfam; PF09368; Sas10; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Citrullination;
KW Developmental protein; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..479
FT /note="Something about silencing protein 10"
FT /id="PRO_0000114326"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..449
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JI13"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9JI13"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 385
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 23
FT /note="T -> M (in dbSNP:rs16845385)"
FT /id="VAR_051897"
FT CONFLICT 109
FT /note="D -> G (in Ref. 3; CAG38575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 54558 MW; B4A842785342766D CRC64;
MVGRSRRRGA AKWAAVRAKA GPTLTDENGD DLGLPPSPGD TSYYQDQVDD FHEARSRAAL
AKGWNEVQSG DEEDGEEEEE EVLALDMDDE DDEDGGNAGE EEEEENADDD GGSSVQSEAE
ASVDPSLSWG QRKKLYYDTD YGSKSRGRQS QQEAEEEERE EEEEAQIIQR RLAQALQEDD
FGVAWVEAFA KPVPQVDEAE TRVVKDLAKV SVKEKLKMLR KESPELLELI EDLKVKLTEV
KDELEPLLEL VEQGIIPPGK GSQYLRTKYN LYLNYCSNIS FYLILKARRV PAHGHPVIER
LVTYRNLINK LSVVDQKLSS EIRHLLTLKD DAVKKELIPK AKSTKPKPKS VSKTSAAACA
VTDLSDDSDF DEKAKLKYYK EIEDRQKLKR KKEENSTEEQ ALEDQNAKRA ITYQIAKNRG
LTPRRKKIDR NPRVKHREKF RRAKIRRRGQ VREVRKEEQR YSGELSGIRA GVKKSIKLK
