IN80B_MOUSE
ID IN80B_MOUSE Reviewed; 375 AA.
AC Q99PT3; Q9CY38;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=INO80 complex subunit B;
DE AltName: Full=High mobility group AT-hook 1-like 4;
DE AltName: Full=PAP-1-associated protein 1;
DE Short=PAPA-1;
DE AltName: Full=Zinc finger HIT domain-containing protein 4;
GN Name=Ino80b; Synonyms=Hmga1l4, Papa1, Znhit4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-375, SUBCELLULAR LOCATION, INTERACTION WITH
RP RP9, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15556297; DOI=10.1016/j.gene.2004.05.025;
RA Kuroda T.S., Maita H., Tabata T., Taira T., Kitaura H., Ariga H.,
RA Iguchi-Ariga S.M.M.;
RT "A novel nucleolar protein, PAPA-1, induces growth arrest as a result of
RT cell cycle arrest at the G1 phase.";
RL Gene 340:83-98(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-375.
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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-114; SER-116; SER-144;
RP SER-147 AND SER-149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {ECO:0000250,
CC ECO:0000269|PubMed:15556297}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the helicase ATP-
CC binding and the helicase C-terminal domain of INO80 (By similarity).
CC Interacts with RP9. {ECO:0000250, ECO:0000269|PubMed:15556297}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C086}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15556297}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in the testis and moderately in
CC the kidney, skeletal muscle, liver and lung.
CC {ECO:0000269|PubMed:15556297}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19383.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH58788.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21110.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK010946; BAB27284.1; -; mRNA.
DR EMBL; AB054537; BAB21110.1; ALT_SEQ; mRNA.
DR EMBL; BC019383; AAH19383.1; ALT_INIT; mRNA.
DR EMBL; BC058788; AAH58788.1; ALT_INIT; mRNA.
DR RefSeq; NP_076036.1; NM_023547.1.
DR AlphaFoldDB; Q99PT3; -.
DR SMR; Q99PT3; -.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR IntAct; Q99PT3; 3.
DR MINT; Q99PT3; -.
DR STRING; 10090.ENSMUSP00000109568; -.
DR iPTMnet; Q99PT3; -.
DR PhosphoSitePlus; Q99PT3; -.
DR EPD; Q99PT3; -.
DR jPOST; Q99PT3; -.
DR MaxQB; Q99PT3; -.
DR PaxDb; Q99PT3; -.
DR PRIDE; Q99PT3; -.
DR ProteomicsDB; 267132; -.
DR DNASU; 70020; -.
DR GeneID; 70020; -.
DR KEGG; mmu:70020; -.
DR UCSC; uc009cmr.1; mouse.
DR CTD; 83444; -.
DR MGI; MGI:1917270; Ino80b.
DR VEuPathDB; HostDB:ENSMUSG00000030034; -.
DR eggNOG; ENOG502QUQX; Eukaryota.
DR InParanoid; Q99PT3; -.
DR OrthoDB; 1111317at2759; -.
DR PhylomeDB; Q99PT3; -.
DR TreeFam; TF105373; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR BioGRID-ORCS; 70020; 8 hits in 111 CRISPR screens.
DR PRO; PR:Q99PT3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99PT3; protein.
DR Genevisible; Q99PT3; MM.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR InterPro; IPR029523; INO80B/Ies2.
DR InterPro; IPR006880; INO80B_C.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR21561; PTHR21561; 1.
DR Pfam; PF04795; PAPA-1; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR SMART; SM01406; PAPA-1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA damage; DNA recombination; DNA repair; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..375
FT /note="INO80 complex subunit B"
FT /id="PRO_0000173555"
FT ZN_FING 324..355
FT /note="HIT-type"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..262
FT /evidence="ECO:0000255"
FT COMPBIAS 49..68
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 375 AA; 40565 MW; 20A66F7189EA4A7F CRC64;
MSACVPTVSS PLPLQDPMSK LWRRGSTSGA MEAPEPGETL ELSLAGAHGH GVHKKKHKKH
KKKHKKKHHQ EEEAGPTLQT PAKPQLKLKI KLGGQVLGTK SVPTFTVIPE GPRSPSPLMV
VDNEEEPMEG VPLEQYRAWL DEDSNLSPSP LRDLPGDLEG QEEEEEQRWL DALEKGELDD
NGDLKKEINE RLLTARQRAL LQKARSQPSP TLPLPVGGGC PAPALTEEML LKREERARKR
RLQAARRAEE HKNQTIERLT KTAAPSGRGG RGAARGERRG GRAAAPAPAP MVRYCSGAQG
STLSFPPGVP TPTAVAQRPA PSGPAPRCSV PGCPHPRRYA CSRTGQALCS LQCYRINLQL
RLGGPEGPGS PLLAT
