ID   MBB1A_RAT               Reviewed;        1344 AA.
AC   O35821;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Myb-binding protein 1A;
DE   AltName: Full=PAR-interacting protein;
DE            Short=PIP;
GN   Name=Mybbp1a;
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 GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 68-1344.
RA   Comte P.A., Ossipow V., Schibler U.;
RT   "Isolation of PIP, a 160 kDa nucleolar protein that interacts with the
RT   activation domain of PAR transcription factors.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-1166; SER-1255;
RP   SER-1283; SER-1323 AND SER-1325, 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: May activate or repress transcription via interactions with
CC       sequence specific DNA-binding proteins (By similarity). Repression may
CC       be mediated at least in part by histone deacetylase activity (HDAC
CC       activity) (By similarity). Acts as a corepressor and in concert with
CC       CRY1, represses the transcription of the core circadian clock component
CC       PER2 (By similarity). Preferentially binds to dimethylated histone H3
CC       'Lys-9' (H3K9me2) on the PER2 promoter (By similarity). Has a role in
CC       rRNA biogenesis together with PWP1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q7TPV4, ECO:0000250|UniProtKB:Q9BQG0}.
CC   -!- SUBUNIT: Binds to and represses JUN and MYB via the leucine zipper
CC       regions present in these proteins. Also binds to and represses
CC       PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated
CC       by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to
CC       KPNA2. Component of the B-WICH complex, at least composed of
CC       SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21.
CC       Interacts with CLOCK and CRY1. {ECO:0000250|UniProtKB:Q7TPV4,
CC       ECO:0000250|UniProtKB:Q9BQG0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TPV4}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:Q7TPV4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q7TPV4}. Note=Predominantly nucleolar. Also
CC       shuttles between the nucleus and cytoplasm. Nuclear import may be
CC       mediated by KPNA2, while export appears to depend partially on
CC       XPO1/CRM1. {ECO:0000250|UniProtKB:Q7TPV4}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q7TPV4}.
CC   -!- SIMILARITY: Belongs to the MYBBP1A family. {ECO:0000305}.
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DR   EMBL; AABR03073819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U83590; AAB62878.1; -; mRNA.
DR   PIR; T32731; T32731.
DR   RefSeq; NP_113856.1; NM_031668.1.
DR   RefSeq; XP_006246864.1; XM_006246802.2.
DR   AlphaFoldDB; O35821; -.
DR   IntAct; O35821; 6.
DR   STRING; 10116.ENSRNOP00000021134; -.
DR   iPTMnet; O35821; -.
DR   PhosphoSitePlus; O35821; -.
DR   jPOST; O35821; -.
DR   PaxDb; 10116-ENSRNOP00000021134; -.
DR   GeneID; 60571; -.
DR   KEGG; rno:60571; -.
DR   AGR; RGD:62062; -.
DR   CTD; 10514; -.
DR   RGD; 62062; Mybbp1a.
DR   VEuPathDB; HostDB:ENSRNOG00000015236; -.
DR   eggNOG; KOG1926; Eukaryota.
DR   HOGENOM; CLU_005997_1_0_1; -.
DR   InParanoid; O35821; -.
DR   OrthoDB; 2911826at2759; -.
DR   PhylomeDB; O35821; -.
DR   TreeFam; TF317401; -.
DR   Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR   PRO; PR:O35821; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000015236; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR   GO; GO:0110016; C:B-WICH complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:2000210; P:positive regulation of anoikis; ISO:RGD.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:RGD.
DR   GO; GO:1903450; P:regulation of G1 to G0 transition; ISO:RGD.
DR   GO; GO:0022904; P:respiratory electron transport chain; ISO:RGD.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR007015; DNA_pol_V/MYBBP1A.
DR   PANTHER; PTHR13213:SF2; MYB-BINDING PROTEIN 1A; 1.
DR   PANTHER; PTHR13213; MYB-BINDING PROTEIN 1A FAMILY MEMBER; 1.
DR   Pfam; PF04931; DNA_pol_phi; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; O35821; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Biological rhythms; Citrullination; Cytoplasm;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Ribosome biogenesis; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   CHAIN           2..1344
FT                   /note="Myb-binding protein 1A"
FT                   /id="PRO_0000096257"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..580
FT                   /note="Interaction with MYB"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   REGION          696..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1344
FT                   /note="Required for nuclear and nucleolar localization"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   MOTIF           238..256
FT                   /note="Nuclear export signal 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   MOTIF           261..279
FT                   /note="Nuclear export signal 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   COMPBIAS        706..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..747
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1287..1307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         156
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1193
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1253
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1258
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   MOD_RES         1280
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   MOD_RES         1283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1322
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT   MOD_RES         1323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   CROSSLNK        1151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   CONFLICT        137
FT                   /note="G -> A (in Ref. 2; AAB62878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        433
FT                   /note="V -> D (in Ref. 2; AAB62878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        905
FT                   /note="L -> F (in Ref. 2; AAB62878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1204
FT                   /note="A -> R (in Ref. 2; AAB62878)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1344 AA;  152286 MW;  A5721894AD80BDF0 CRC64;
     MAEMKSPTKA EPASPAEAPQ GDRRSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR
     TRPSDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIQLCDIL GQIQEKYNLQ
     AMNKAMMRPT LFANLFGVLA LFQSGRLVKD KEALMKCVRL LKILSHHYNH LQGQPVKALV
     DILSEVPESM FQEILPKVLK GDMKVILSSP KYLELFLLAR QRVPAELESL VGSVDLFSED
     NIPSLVNILK VAANSVKKEQ KLPDVALNLL RLALQENKFE RFWKEVLEEG LLKKPSYTSS
     YMCFRLLGAS LPLLSDEQLQ LVMRGDLIRH FGEHMVVSKS QNPLRFIPEI SAYVGTFLEG
     CQDDPKRQFT VMVAFTAITN QGLPVMPTFW RVTRFLNTEA LQNYVTWLRD MFLQPDLDSL
     VDFSTANQKR VQVASLNVPE RTVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH
     AFFKTKKATP QIPETKQHFS FPLEDGNRGV IVSAFFSLLQ TLSVKFRQTP DLAENGKPWT
     YRLVQLADML LKHNRNVANV TPLTAQQRQA WDQMMSTLKE LEAQSSETRA IAFQHLLLLV
     GLHLFKSPAE SCDVLGDIQT CIKKSMEQNL RRSRSRAKAS QEPVWVEVMV EILLSLLAQP
     SNLMRQVVRS VFGHVCSHLT PRGLQLILAV LNPETNEDEE DNVVVTDTDE KQLKHGEDAD
     SDSEDSKNSE SDVDSEDGEE SEEEDRDKDV DPGFRQQLME VLQAGNALGG EEEEEEELGD
     EAMMALDQNL ASLFAEQKMR IQARHEEKNK LQKEKQLRRD FQIRALDLIE VLVTKQPEHP
     LILELLEPLL NIIQRSMRSR GSTKQEQDLL HKTARIFMHH LCRARHYCHE VEPGAEALHA
     QVERLVQQAG NQADASVALY YFNASLYLLR VLKGNTTKRY QDGQKLEGAD IKSEPKDSEV
     QTTSCLDLDF VTRVYSASLE SLLTKRNSPL TIPMFLDLFS RYPVICKNLL PIVVQHVAGS
     SRPRHQAQAC LLLQKALSAR ELRVCFEDPE WEQLISQVLG KTTQTLQTLG EAQSKGEHQR
     ELSILELLNT VFRIVNHEKL SVDLTAFLGM LQGKQQKLQQ NLQQGNHSSG SSRLYDLYWQ
     AMNLLGVQRP KSEKKNVKDI PSDSQSPIST KRKKKGFLPE TKKRKKLKSE GTTSEKKAAS
     QQDAVTEGAM PAATGKDQPP STGKKRRKRV KANTPSQVNG VTVAKSPAPN NPTLSPSTPP
     AKTPKVQKKK EKLSQVNGST PVSPVEPESK KHQKALSTKE VKRRSSQSAL PKKRARLSLV
     SRSPSLLQSG IRKRRVARRR VQTP
//