MBB1A_RAT
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 03-AUG-2022, entry version 140.
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; O35821; -.
DR PRIDE; O35821; -.
DR GeneID; 60571; -.
DR KEGG; rno:60571; -.
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 OMA; PWVEVMV; -.
DR OrthoDB; 86051at2759; -.
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 tissues.
DR Genevisible; O35821; RN.
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; IDA:RGD.
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 transcription, DNA-templated; 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; PTHR13213; 1.
DR Pfam; PF04931; DNA_pol_phi; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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
