ARI4B_RAT
ID ARI4B_RAT Reviewed; 1228 AA.
AC Q9JKB5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=AT-rich interactive domain-containing protein 4B;
DE Short=ARID domain-containing protein 4B;
DE AltName: Full=180 kDa Sin3-associated polypeptide;
DE Short=Sin3-associated polypeptide p180;
DE AltName: Full=Histone deacetylase complex subunit SAP180;
DE AltName: Full=Retinoblastoma-binding protein 1-like 1;
GN Name=Arid4b; Synonyms=Rbbp1l1, Sap180;
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 [MRNA].
RA Kholodilov N.G., Neystat M., Burke R.E.;
RT "Upregulation of rat homolog of human retinoblastoma-binding protein
RT (RBBP1) in substantia nigra following developmental striatal target
RT injury.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-296; SER-581;
RP SER-588; SER-703 AND THR-706, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Acts as a transcriptional repressor. May function in the
CC assembly and/or enzymatic activity of the Sin3A corepressor complex or
CC in mediating interactions between the complex and other regulatory
CC complexes.Plays a role in the regulation of epigenetic modifications at
CC the PWS/AS imprinting center near the SNRPN promoter, where it might
CC function as part of a complex with RB1 and ARID4A. Involved in
CC spermatogenesis, together with ARID4A, where it functions as a
CC transcriptional coactivator for AR (androgen receptor) and enhances
CC expression of genes required for sperm maturation. Regulates expression
CC of the tight junction protein CLDN3 in the testis, which is important
CC for integrity of the blood-testis barrier. Plays a role in myeloid
CC homeostasis where it regulates the histone methylation state of bone
CC marrow cells and expression of various genes involved in hematopoiesis.
CC May function as a leukemia suppressor. {ECO:0000250|UniProtKB:A2CG63,
CC ECO:0000250|UniProtKB:Q4LE39}.
CC -!- SUBUNIT: Component of a Sin3A corepressor complex consisting of SIN3A,
CC SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2. Interacts with ARID4A (By
CC similarity). Interacts with AR (By similarity).
CC {ECO:0000250|UniProtKB:A2CG63, ECO:0000250|UniProtKB:Q4LE39}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- DOMAIN: The C-terminus mediates interaction with mSin3A corepressor
CC complex. {ECO:0000250|UniProtKB:Q4LE39}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional repression by
CC HDAC-independent mechanisms. {ECO:0000250|UniProtKB:Q4LE39}.
CC -!- DOMAIN: The ARID domain is involved in stabilizing the mSin3A
CC corepressor complex on DNA. {ECO:0000250|UniProtKB:Q4LE39}.
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DR EMBL; AF245512; AAF61271.1; -; mRNA.
DR RefSeq; NP_445873.1; NM_053421.1.
DR AlphaFoldDB; Q9JKB5; -.
DR SMR; Q9JKB5; -.
DR STRING; 10116.ENSRNOP00000010836; -.
DR iPTMnet; Q9JKB5; -.
DR PhosphoSitePlus; Q9JKB5; -.
DR PaxDb; Q9JKB5; -.
DR PRIDE; Q9JKB5; -.
DR GeneID; 84481; -.
DR KEGG; rno:84481; -.
DR UCSC; RGD:619919; rat.
DR CTD; 51742; -.
DR RGD; 619919; Arid4b.
DR eggNOG; KOG2744; Eukaryota.
DR eggNOG; KOG3001; Eukaryota.
DR InParanoid; Q9JKB5; -.
DR OrthoDB; 329541at2759; -.
DR PhylomeDB; Q9JKB5; -.
DR Reactome; R-RNO-3214815; HDACs deacetylate histones.
DR PRO; PR:Q9JKB5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISO:RGD.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; ISO:RGD.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR028853; ARID4B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR012603; RBB1NT.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR13964:SF24; PTHR13964:SF24; 2.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF08169; RBB1NT; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1228
FT /note="AT-rich interactive domain-containing protein 4B"
FT /id="PRO_0000282865"
FT DOMAIN 306..398
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 123..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1141..1186
FT /evidence="ECO:0000255"
FT COMPBIAS 144..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 942
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1066
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1075
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
SQ SEQUENCE 1228 AA; 137080 MW; DE50F198D9E46C6C CRC64;
MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE VQDDHIKGPL
KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT LRRSSLCLKG ERHFAESETL
DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP EEESSSSSSD DDEDDRKQTD ELLGKVVCVD
YISLDKKKAL WFPALVVCPD CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK
PDAVLKQAFD QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE
EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL GGFDNIESGA
VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA NIDFQMALPE KVLNKPCKDC
ENKEIKVKEE SDAEIKEVNV EDSKNMIPKE ETPAEDESER KENIKPSLGS KKGLLECIPA
QSDQEKEANI TKLEEKESLE DKDGATARAE EALSTEVDAE EEQARSGYDE WIKADKIVRP
ADKNVPKIKH RKKIKNKLDK EKDRDEKYSP KNCKLRRLSK SPFQSNPSPE MVSKLDLADA
KNSDTGHIKS IEITSILNGL QASESSAEDS EQEEERCAQD PESSSKDESK VEHSAHSRSE
LISKEELSSP SLLEENKVHP DLVIAKTVSK SPERLRKDVE AISEDTDFEE EDEITKKRKD
VKKDTTDKAL KPQTKTWGKD RYCIQTNCLQ SGSPGKKEDR TKSKEPLCTG NSSNSSSDED
EEEKSKAKMT PTKKYNGLEE KRKSLRTTSF YSGFSEVAEK RIKLLNNSDE RLQNNRAKDR
KDVWSSIQGQ WPKKTLKELF SDSDTEAAAS PPHAAPDEGT VEESLQTVAE EESCSPNMEL
EKPLPTSVDS KPVEEKPLEV SDRKTEFPSS GSNSVLNTPP TTPESPSSVT VTETSQQQSS
VTVSVPLPPN QEEVRSIKSE TDSTIEVDSV VGELQDLQSE GNSSPAGFNA SVSSSSSNQP
EPEHPEKACT GQKRVKDTQG VGSSSKKQKR SHKATVVNNK KKGKGTNSSD SEDLSAGESV
TKTQAIKSVP TGMKTHNSKS PARIQSPGKC GKNGDKDPDL KEPSNRLPKV YKWSFQMSDL
ENMTSAERIS ILQEKLQEIR KHYLSLKSEV ASIDRRRKRL KKKERESAAT SSSSSSPSSS
SITAAVMLTL AEPSMSSASQ NGMSVECR
