UBIP1_MOUSE
ID UBIP1_MOUSE Reviewed; 540 AA.
AC Q811S7; A4QPG4; Q3UPR3; Q3US11; Q60786; Q8C514;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Upstream-binding protein 1;
DE AltName: Full=Nuclear factor 2d9;
DE Short=NF2d9;
GN Name=Ubp1; Synonyms=Cp2b, Nf2d9;
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] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH CYP2D9.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=7623810; DOI=10.1128/mcb.15.8.4158;
RA Sueyoshi T., Kobayashi R., Nishio K., Aida K., Moore R., Wada T., Handa H.,
RA Negishi M.;
RT "A nuclear factor (NF2d9) that binds to the male-specific P450 (Cyp 2d-9)
RT gene in mouse liver.";
RL Mol. Cell. Biol. 15:4158-4166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH TFCP2 AND PIAS1.
RC STRAIN=DBA/2J; TISSUE=Erythroleukemia;
RX PubMed=15988015; DOI=10.1128/mcb.25.14.6005-6020.2005;
RA Kang H.C., Chae J.H., Lee Y.H., Park M.-A., Shin J.H., Kim S.-H., Ye S.-K.,
RA Cho Y.S., Fiering S., Kim C.G.;
RT "Erythroid cell-specific alpha-globin gene regulation by the CP2
RT transcription factor family.";
RL Mol. Cell. Biol. 25:6005-6020(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 1-241, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 253-540 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head, Oviduct, and Thymus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Functions as a transcriptional activator in a promoter
CC context-dependent manner. Involved in regulation of the alpha-globin
CC gene in erythroid cells. Activation of the alpha-globin promoter in
CC erythroid cells is via synergistic interaction with TFCP2. Functions as
CC a trans-acting factor that regulates the domestic strain CYP2D9 gene
CC through specific association with the regulatory element SDI-A1.
CC Binding to SDI-A1 depends on the type of nucleotide at position 299;
CC binding is abolished by a nucleotide substitution at this position.
CC Modulates the placental expression of CYP11A1 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15988015, ECO:0000269|PubMed:7623810}.
CC -!- SUBUNIT: Interacts with TFCP2 and PIAS1, and is probably part of a
CC complex containing TFCP2, UBP1 and PIAS1. {ECO:0000269|PubMed:15988015,
CC ECO:0000269|PubMed:7623810}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CP2b;
CC IsoId=Q811S7-1; Sequence=Displayed;
CC Name=2; Synonyms=CP2a;
CC IsoId=Q811S7-2; Sequence=VSP_017731;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in erythroid cells.
CC {ECO:0000269|PubMed:15988015, ECO:0000269|PubMed:7623810}.
CC -!- MISCELLANEOUS: Present in both domestic and wild mouse strains.
CC Recognizes the genetic difference at position 299 in the SDI-A1
CC element.
CC -!- SIMILARITY: Belongs to the grh/CP2 family. CP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; U20086; AAC52244.1; -; mRNA.
DR EMBL; AY182062; AAO24130.1; -; mRNA.
DR EMBL; BC139828; AAI39829.1; -; mRNA.
DR EMBL; AK079815; BAC37754.1; -; mRNA.
DR EMBL; AK143282; BAE25332.1; -; mRNA.
DR EMBL; AK140942; BAE24526.1; -; mRNA.
DR CCDS; CCDS40788.1; -. [Q811S7-1]
DR CCDS; CCDS40789.1; -. [Q811S7-2]
DR PIR; I49257; I49257.
DR RefSeq; NP_001076788.1; NM_001083319.1. [Q811S7-1]
DR RefSeq; NP_038727.1; NM_013699.2. [Q811S7-2]
DR RefSeq; XP_006512114.2; XM_006512051.3.
DR RefSeq; XP_006512117.2; XM_006512054.3.
DR AlphaFoldDB; Q811S7; -.
DR SMR; Q811S7; -.
DR BioGRID; 204421; 12.
DR IntAct; Q811S7; 8.
DR MINT; Q811S7; -.
DR STRING; 10090.ENSMUSP00000081946; -.
DR iPTMnet; Q811S7; -.
DR PhosphoSitePlus; Q811S7; -.
DR EPD; Q811S7; -.
DR MaxQB; Q811S7; -.
DR PaxDb; Q811S7; -.
DR PeptideAtlas; Q811S7; -.
DR PRIDE; Q811S7; -.
DR ProteomicsDB; 298406; -. [Q811S7-1]
DR ProteomicsDB; 298407; -. [Q811S7-2]
DR Antibodypedia; 11705; 341 antibodies from 29 providers.
DR DNASU; 22221; -.
DR Ensembl; ENSMUST00000009885; ENSMUSP00000009885; ENSMUSG00000009741. [Q811S7-2]
DR Ensembl; ENSMUST00000084885; ENSMUSP00000081946; ENSMUSG00000009741. [Q811S7-1]
DR Ensembl; ENSMUST00000116492; ENSMUSP00000112192; ENSMUSG00000009741. [Q811S7-2]
DR Ensembl; ENSMUST00000214095; ENSMUSP00000149908; ENSMUSG00000009741. [Q811S7-2]
DR Ensembl; ENSMUST00000216558; ENSMUSP00000150023; ENSMUSG00000009741. [Q811S7-1]
DR GeneID; 22221; -.
DR KEGG; mmu:22221; -.
DR UCSC; uc009rwx.1; mouse. [Q811S7-1]
DR UCSC; uc009rwy.1; mouse. [Q811S7-2]
DR CTD; 7342; -.
DR MGI; MGI:104889; Ubp1.
DR VEuPathDB; HostDB:ENSMUSG00000009741; -.
DR eggNOG; KOG4091; Eukaryota.
DR GeneTree; ENSGT00940000156148; -.
DR HOGENOM; CLU_015127_2_0_1; -.
DR InParanoid; Q811S7; -.
DR OMA; INHVYRQ; -.
DR OrthoDB; 386296at2759; -.
DR PhylomeDB; Q811S7; -.
DR TreeFam; TF314132; -.
DR BioGRID-ORCS; 22221; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Ubp1; mouse.
DR PRO; PR:Q811S7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q811S7; protein.
DR Bgee; ENSMUSG00000009741; Expressed in paneth cell and 263 other tissues.
DR Genevisible; Q811S7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd09588; SAM_LBP1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR007604; CP2.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041418; SAM_3.
DR InterPro; IPR037600; Ubp1_SAM.
DR Pfam; PF04516; CP2; 1.
DR Pfam; PF18016; SAM_3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51968; GRH_CP2_DB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..540
FT /note="Upstream-binding protein 1"
FT /id="PRO_0000229027"
FT DOMAIN 60..296
FT /note="Grh/CP2 DB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT REGION 1..40
FT /note="Transcriptional activation"
FT REGION 235..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..309
FT /note="Erythroid-specific transcriptional activation"
FT REGION 285..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZI7"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 274..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7623810"
FT /id="VSP_017731"
FT CONFLICT 287
FT /note="E -> K (in Ref. 4; BAE24526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 60212 MW; A0D66024E36CCEB9 CRC64;
MAWVLSMDEV IESGLVHDFD SSLSGIGQEL GAGAYSMSDV LALPIFKQED SSLSLEDEAK
HPPFQYVMCA ATSPAVKLHD ETLTYLNQGQ SYEIRMLDNR KMGDMPELSG KLVKSIIRVV
FHDRRLQYTE HQQLEGWKWN RPGDRLLDLD IPMSVGIIDT RTNPSQLNAV EFLWDPAKRT
SAFIQVHCIS TEFTPRKHGG EKGVPFRIQV DTFKQNENGE YTDHLHSASC QIKVFKPKGA
DRKQKNDREK MEKRTAHEKE KYQPSYDTTI LTEMRLEPII EDAVEHEQKK SSKRTLPADY
GDSLAKRGSC SPWPDTPTAY VNNSPSPAPT FTSSQPSTCS VPDSNSSSPN HQGDGAAQAS
GEQIQPSATT QETQQWLLKN RFSSYTRLFS NFSGADLLKL TKEDLVQICG AADGIRLYNS
LKSRSVRPRL TIYVCQEQPS STALQGQPQA AGSGGESGGG TPSVYHAIYL EEMVASEVAR
KLASVFNIPF HQINQVYRQG PTGIHILVSD QMVQNFQDET CFLFSTVKAE NNDGIHIILK
