SAS10_RAT
ID SAS10_RAT Reviewed; 470 AA.
AC Q6AXX4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Something about silencing protein 10;
DE AltName: Full=Charged amino acid-rich leucine zipper 1;
DE AltName: Full=Disrupter of silencing SAS10;
DE AltName: Full=UTP3 homolog;
GN Name=Utp3; Synonyms=Crlz1, Sas10 {ECO:0000250|UniProtKB:Q9JI13};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079277; AAH79277.1; -; mRNA.
DR RefSeq; NP_001012036.1; NM_001012036.1.
DR AlphaFoldDB; Q6AXX4; -.
DR STRING; 10116.ENSRNOP00000004787; -.
DR iPTMnet; Q6AXX4; -.
DR PhosphoSitePlus; Q6AXX4; -.
DR jPOST; Q6AXX4; -.
DR PaxDb; Q6AXX4; -.
DR PRIDE; Q6AXX4; -.
DR Ensembl; ENSRNOT00000004787; ENSRNOP00000004787; ENSRNOG00000003599.
DR GeneID; 305258; -.
DR KEGG; rno:305258; -.
DR UCSC; RGD:1308540; rat.
DR CTD; 57050; -.
DR RGD; 1308540; Utp3.
DR eggNOG; KOG3118; Eukaryota.
DR GeneTree; ENSGT00500000044947; -.
DR HOGENOM; CLU_025161_1_0_1; -.
DR InParanoid; Q6AXX4; -.
DR OMA; EEYIRPQ; -.
DR OrthoDB; 1451774at2759; -.
DR PhylomeDB; Q6AXX4; -.
DR TreeFam; TF315177; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q6AXX4; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003599; Expressed in thymus and 20 other tissues.
DR Genevisible; Q6AXX4; RN.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
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 Acetylation; Chromatin regulator; Citrullination; Developmental protein;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..470
FT /note="Something about silencing protein 10"
FT /id="PRO_0000114328"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..440
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:22673903"
FT MOD_RES 140
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9JI13"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQZ2"
FT MOD_RES 376
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQZ2"
SQ SEQUENCE 470 AA; 53924 MW; 4EA29E47B0220919 CRC64;
MVKRSRRRGA AQWATVRAKA GRTATDENED DLGSPPSPGD SSYYQDQVDE FHEARSRAVL
AKGWNEVESG EEDDDEEEEV LPLNIDDEND EDGESSEEEE DGEDDDGGSS VQSEAEASVD
PSLSWGQRKR LYYDTDYGSK SRGRQSQQEV EEEEREEEEE AQVIQRRLTQ ALQEDDFGVA
WVEAFAKPVP QVDEAETRVV KDLAKVSVKE KLKMLRKESP ELLELIEDLK VKLTEVKDEL
EPLIQLVEKG VIPPGKGSQY LKTKYNLYLN YCANISFYLI LKARRVPAHG HPVIERLVTY
RNLINKLSVV DQKLSSEIRH LLTAKEGAGK KDLNPKAKLT KTKPKSAKQT DVNADLTEEP
EFDEAALEFY KEMEDRPELK RKKEENSAEE QALEEQNAKR AITYQIAKNR GLTPRRKKID
RNPRVKHREK FRRAKIRRRG QVREVRREEQ RYSGELSGIR AGVKKSIKLK
