S30BP_MOUSE
ID S30BP_MOUSE Reviewed; 308 AA.
AC Q02614; Q8VDJ5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=SAP30-binding protein;
DE AltName: Full=Transcriptional regulator protein HCNGP;
GN Name=Sap30bp; Synonyms=Hcngp;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Spleen;
RX PubMed=1459361; DOI=10.1111/j.1432-0436.1992.tb00697.x;
RA Palmer D.B., McVey J.H., Robinson P.J., Dyson P.J.;
RT "The chromatin structure of the mouse beta-2-microglobulin locus.";
RL Differentiation 51:201-207(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Melanocyte;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in transcriptional repression by promoting
CC histone deacetylase activity, leading to deacetylation of histone H3
CC (By similarity). May be involved in the regulation of beta-2-
CC microglobulin genes (PubMed:1459361). {ECO:0000250|UniProtKB:Q9UHR5,
CC ECO:0000269|PubMed:1459361}.
CC -!- SUBUNIT: Interacts with histone deacetylase complex subunit SAP30.
CC {ECO:0000250|UniProtKB:Q9UHR5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1459361}.
CC -!- SIMILARITY: Belongs to the HCNGP family. {ECO:0000305}.
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DR EMBL; X68061; CAA48198.1; -; mRNA.
DR EMBL; AK147869; BAE28192.1; -; mRNA.
DR EMBL; BC021757; AAH21757.1; -; mRNA.
DR CCDS; CCDS25651.1; -.
DR PIR; S26660; S26660.
DR RefSeq; NP_065229.2; NM_020483.3.
DR AlphaFoldDB; Q02614; -.
DR BioGRID; 208215; 2.
DR IntAct; Q02614; 3.
DR MINT; Q02614; -.
DR STRING; 10090.ENSMUSP00000114844; -.
DR iPTMnet; Q02614; -.
DR PhosphoSitePlus; Q02614; -.
DR EPD; Q02614; -.
DR jPOST; Q02614; -.
DR MaxQB; Q02614; -.
DR PaxDb; Q02614; -.
DR PeptideAtlas; Q02614; -.
DR PRIDE; Q02614; -.
DR ProteomicsDB; 253381; -.
DR Antibodypedia; 19600; 285 antibodies from 27 providers.
DR DNASU; 57230; -.
DR Ensembl; ENSMUST00000140991; ENSMUSP00000114844; ENSMUSG00000020755.
DR GeneID; 57230; -.
DR KEGG; mmu:57230; -.
DR UCSC; uc007mjd.1; mouse.
DR CTD; 29115; -.
DR MGI; MGI:1927479; Sap30bp.
DR VEuPathDB; HostDB:ENSMUSG00000020755; -.
DR eggNOG; KOG2959; Eukaryota.
DR GeneTree; ENSGT00390000007870; -.
DR HOGENOM; CLU_053268_0_1_1; -.
DR InParanoid; Q02614; -.
DR OMA; ENSKQSX; -.
DR OrthoDB; 1557444at2759; -.
DR PhylomeDB; Q02614; -.
DR TreeFam; TF323387; -.
DR BioGRID-ORCS; 57230; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Sap30bp; mouse.
DR PRO; PR:Q02614; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q02614; protein.
DR Bgee; ENSMUSG00000020755; Expressed in embryonic brain and 245 other tissues.
DR Genevisible; Q02614; MM.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0052472; P:modulation by host of symbiont transcription; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR InterPro; IPR012479; SAP30BP.
DR PANTHER; PTHR13464; PTHR13464; 1.
DR Pfam; PF07818; HCNGP; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..308
FT /note="SAP30-binding protein"
FT /id="PRO_0000083924"
FT REGION 15..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHR5"
FT CONFLICT 34
FT /note="A -> R (in Ref. 1; CAA48198)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="A -> T (in Ref. 1; CAA48198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33832 MW; 4E36A6A4B58098FB CRC64;
MAGKKNVLSS LAIYAEYSDP ESDGETGVDA VGGATEEKGG LVSDAYGEDD FSRPGGDEDG
YEEEEDENSK QSEDDDSETE KPEADDPKDN TEAEKRDPQE LVASFSERVR NMSPDEIKIP
PEPPGRCSNH LQDKIQKLYE RKIKEGMDMN YIIQRKKEFR NPSIYEKLIQ FCAIDELGTN
YPKDMFDPHG WSEDSYYEAL AKAQKIEMDK LEKAKKERTK IEFVTGTKKG TTTNATATST
STASTAVADA QKRKSKWDSA IPVTTIAQPT ILTTTATLPA VVTVTTSASG SKTTVISAVG
TIVKKAKQ
