RSBN1_MOUSE
ID RSBN1_MOUSE Reviewed; 795 AA.
AC Q80T69; B0V3N6; B9EI66; Q3UUB5; Q4VC18; Q7TNJ3; Q8C2Z3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lysine-specific demethylase 9 {ECO:0000303|PubMed:28867287};
DE Short=KDM9 {ECO:0000303|PubMed:28867287};
DE EC=1.14.11.- {ECO:0000269|PubMed:28867287};
DE AltName: Full=Round spermatid basic protein 1;
DE Short=Rosbin;
GN Name=Rsbn1; Synonyms=Kiaa3002, Rsbn;
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], SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14724137; DOI=10.1095/biolreprod.103.026096;
RA Takahashi T., Tanaka H., Iguchi N., Kitamura K., Chen Y., Maekawa M.,
RA Nishimura H., Ohta H., Miyagawa Y., Matsumiya K., Okuyama A., Nishimune Y.;
RT "Rosbin: a novel homeobox-like protein gene expressed exclusively in round
RT spermatids.";
RL Biol. Reprod. 70:1485-1492(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-795.
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Spinal cord;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-795.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP FUNCTION, AND COFACTOR.
RX PubMed=28867287; DOI=10.1016/j.cell.2017.07.041;
RA Brejc K., Bian Q., Uzawa S., Wheeler B.S., Anderson E.C., King D.S.,
RA Kranzusch P.J., Preston C.G., Meyer B.J.;
RT "Dynamic Control of X Chromosome Conformation and Repression by a Histone
RT H4K20 Demethylase.";
RL Cell 171:E23-E23(2017).
CC -!- FUNCTION: Histone demethylase that specifically demethylates
CC dimethylated 'Lys-20' of histone H4 (H4K20me2), thereby modulating
CC chromosome architecture. {ECO:0000269|PubMed:28867287}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:28867287};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9GRZ3};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14724137}.
CC -!- TISSUE SPECIFICITY: Testis. Expressed exclusively in haploid round
CC spermatids. {ECO:0000269|PubMed:14724137}.
CC -!- DEVELOPMENTAL STAGE: Expressed abundantly in the testis at 23 days
CC after birth and later. Expressed exclusively in the germ cells.
CC {ECO:0000269|PubMed:14724137}.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000305|PubMed:14724137}.
CC -!- SIMILARITY: Belongs to the round spermatid basic protein 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94667.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39967.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAQ12904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB101658; BAC81206.1; -; mRNA.
DR EMBL; CU210953; CAQ12178.1; -; Genomic_DNA.
DR EMBL; CU210868; CAQ12178.1; JOINED; Genomic_DNA.
DR EMBL; CU210868; CAQ12904.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU210953; CAQ12904.1; JOINED; Genomic_DNA.
DR EMBL; BC094667; AAH94667.1; ALT_INIT; mRNA.
DR EMBL; BC139213; AAI39214.1; -; mRNA.
DR EMBL; BC139215; AAI39216.1; -; mRNA.
DR EMBL; AK087685; BAC39967.1; ALT_INIT; mRNA.
DR EMBL; AK138603; BAE23712.1; ALT_INIT; mRNA.
DR EMBL; AK122577; BAC65859.1; -; mRNA.
DR CCDS; CCDS17697.1; -.
DR RefSeq; NP_766272.2; NM_172684.2.
DR RefSeq; XP_006501465.1; XM_006501402.3.
DR AlphaFoldDB; Q80T69; -.
DR SMR; Q80T69; -.
DR BioGRID; 230881; 4.
DR IntAct; Q80T69; 1.
DR STRING; 10090.ENSMUSP00000140185; -.
DR iPTMnet; Q80T69; -.
DR PhosphoSitePlus; Q80T69; -.
DR EPD; Q80T69; -.
DR jPOST; Q80T69; -.
DR MaxQB; Q80T69; -.
DR PaxDb; Q80T69; -.
DR PeptideAtlas; Q80T69; -.
DR PRIDE; Q80T69; -.
DR ProteomicsDB; 262713; -.
DR Antibodypedia; 46942; 108 antibodies from 20 providers.
DR DNASU; 229675; -.
DR Ensembl; ENSMUST00000051139; ENSMUSP00000058934; ENSMUSG00000044098.
DR Ensembl; ENSMUST00000068879; ENSMUSP00000069246; ENSMUSG00000044098.
DR GeneID; 229675; -.
DR KEGG; mmu:229675; -.
DR UCSC; uc008qtw.1; mouse.
DR CTD; 54665; -.
DR MGI; MGI:2444993; Rsbn1.
DR VEuPathDB; HostDB:ENSMUSG00000044098; -.
DR eggNOG; KOG4425; Eukaryota.
DR GeneTree; ENSGT00390000001969; -.
DR HOGENOM; CLU_009952_1_0_1; -.
DR InParanoid; Q80T69; -.
DR OMA; SNMDCDL; -.
DR OrthoDB; 930910at2759; -.
DR PhylomeDB; Q80T69; -.
DR TreeFam; TF323256; -.
DR BioGRID-ORCS; 229675; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rsbn1; mouse.
DR PRO; PR:Q80T69; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80T69; protein.
DR Bgee; ENSMUSG00000044098; Expressed in spermatid and 239 other tissues.
DR ExpressionAtlas; Q80T69; baseline and differential.
DR Genevisible; Q80T69; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0035575; F:histone H4-methyl-lysine-20 demethylase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR InterPro; IPR026306; RSBN1/Dpy-21.
DR PANTHER; PTHR13354; PTHR13354; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Isopeptide bond; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..795
FT /note="Lysine-specific demethylase 9"
FT /id="PRO_0000299413"
FT REGION 64..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 252..263
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 579
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT BINDING 582
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT BINDING 584
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT BINDING 676
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT BINDING 684
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9GRZ3"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ0"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ0"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ0"
FT CROSSLNK 734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ0"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VWQ0"
FT CONFLICT 255..256
FT /note="Missing (in Ref. 3; AAH94667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 89251 MW; A8E699F1832788B5 CRC64;
MFRSTRTTDQ WRVGERLQCP AGHARAALAR TADGGAVGPF KCVFVGEMAA QVGAVRVVRA
VAAQEEPDKE GKEKPHVGVS PRGVKRQRRA SSGGSQEKRG RPSQDPPLAP PHRRRRSRQH
PGPLPPTNAA PTVPGPVEPL LLPPPPPPSL APAGPTVAAP LPAPGTSALF TFSPLTVSAA
GPKHKGHKER HKHHHHRGSD GDPGACVPGD LKHKDKQENG ERSGGVPLIK APKRETADEN
GKTQRADDFV LKKIKKKKKK KHREDMRGRR LKMYNKEVQT VCAGLTRISK EILTQGQLNS
TSGVNKESFR YLKDEQLCRL NLGMQEYRVP QGVQTPFTTH QEHSIRRNFL KTGTKFSNFI
HEEHQSNGGA LVLHAYMDEL SFLSPMEMER FSEEFLALTF SENEKNAAYY ALAIVHGAAA
YLPDFLDYFA FNFPNTPVKM EILGKKDIET TTISNFHTQV NRTYCCGTYR AGPMRQISLV
GAVDEEVGDY FPEFLDMLEE SPFLKMTLPW GTLSSLQLQC RSQSDDGPIM WVRPGEQMIP
TADMPKSPFK RRRSMNEIKN LQYLPRTSEP REVLFEDRTR AHADHVGQGF DWQSTAAVGV
LKAVQFGEWS DQPRITKDVI CFHAEDFTDV VQRLQLDLHE PPVSQCVQWV DEAKLNQMRR
EGIRYARIQL CDNDIYFIPR NVIHQFKTVS AVCSLAWHIR LKQYHPVVET AQNTESNSNM
DCGLEVDSQC VRIKTESEER CTEMQLLTTA SPSFPPPSEL HLQDLKTQPL PVFKVESRLD
SDQQHSLQAH PSTPV
