UBCP1_MOUSE
ID UBCP1_MOUSE Reviewed; 318 AA.
AC Q8BGR9; A2ACX3; Q52L62; Q5XJH1; Q6PH96; Q99LT3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ubiquitin-like domain-containing CTD phosphatase 1;
DE EC=3.1.3.16;
DE AltName: Full=Nuclear proteasome inhibitor UBLCP1;
GN Name=Ublcp1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and 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 [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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II, FVB/N, and ICR;
RC TISSUE=Brain, Liver, Mammary tumor, and Trophoblast stem cell;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, 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).
RN [5]
RP STRUCTURE BY NMR OF 3-79.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ubiquitin-like domain from mouse hypothetical
RT 8430435i17RIK protein.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing
CC their proteolytic activity. The dephosphorylation may prevent assembly
CC of the core and regulatory particles (CP and RP) into mature 26S
CC proteasome (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC nuclear proteasomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGR9-2; Sequence=VSP_019458;
CC -!- DOMAIN: The Ubiquitin-like domain mediates interaction with
CC proteasomes. {ECO:0000250}.
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DR EMBL; AK043952; BAC31711.1; -; mRNA.
DR EMBL; AK050031; BAC34039.1; -; mRNA.
DR EMBL; AK147744; BAE28110.1; -; mRNA.
DR EMBL; AL669944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002236; AAH02236.1; -; mRNA.
DR EMBL; BC056652; AAH56652.1; -; mRNA.
DR EMBL; BC083331; AAH83331.1; -; mRNA.
DR EMBL; BC085111; AAH85111.1; -; mRNA.
DR EMBL; BC106093; AAI06094.1; -; mRNA.
DR CCDS; CCDS24564.1; -. [Q8BGR9-1]
DR RefSeq; NP_077795.2; NM_024475.5. [Q8BGR9-1]
DR RefSeq; XP_006534585.1; XM_006534522.3. [Q8BGR9-1]
DR PDB; 1V5T; NMR; -; A=3-79.
DR PDBsum; 1V5T; -.
DR AlphaFoldDB; Q8BGR9; -.
DR BMRB; Q8BGR9; -.
DR SMR; Q8BGR9; -.
DR BioGRID; 219765; 17.
DR STRING; 10090.ENSMUSP00000099859; -.
DR iPTMnet; Q8BGR9; -.
DR PhosphoSitePlus; Q8BGR9; -.
DR EPD; Q8BGR9; -.
DR MaxQB; Q8BGR9; -.
DR PaxDb; Q8BGR9; -.
DR PeptideAtlas; Q8BGR9; -.
DR PRIDE; Q8BGR9; -.
DR ProteomicsDB; 297784; -. [Q8BGR9-1]
DR ProteomicsDB; 297785; -. [Q8BGR9-2]
DR Antibodypedia; 28498; 189 antibodies from 24 providers.
DR DNASU; 79560; -.
DR Ensembl; ENSMUST00000102795; ENSMUSP00000099859; ENSMUSG00000041231. [Q8BGR9-1]
DR GeneID; 79560; -.
DR KEGG; mmu:79560; -.
DR UCSC; uc007ind.1; mouse. [Q8BGR9-2]
DR UCSC; uc007ing.2; mouse. [Q8BGR9-1]
DR CTD; 134510; -.
DR MGI; MGI:1933105; Ublcp1.
DR VEuPathDB; HostDB:ENSMUSG00000041231; -.
DR eggNOG; KOG1605; Eukaryota.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000010107; -.
DR HOGENOM; CLU_046931_1_0_1; -.
DR InParanoid; Q8BGR9; -.
DR OMA; DSNAMIS; -.
DR OrthoDB; 1376145at2759; -.
DR PhylomeDB; Q8BGR9; -.
DR TreeFam; TF323786; -.
DR BioGRID-ORCS; 79560; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ublcp1; mouse.
DR EvolutionaryTrace; Q8BGR9; -.
DR PRO; PR:Q8BGR9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BGR9; protein.
DR Bgee; ENSMUSG00000041231; Expressed in undifferentiated genital tubercle and 59 other tissues.
DR Genevisible; Q8BGR9; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR011943; HAD-SF_hydro_IIID.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02245; HAD_IIID1; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WVY7"
FT CHAIN 2..318
FT /note="Ubiquitin-like domain-containing CTD phosphatase 1"
FT /id="PRO_0000242641"
FT DOMAIN 3..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 133..294
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 133..294
FT /note="Phosphatase"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVY7"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVY7"
FT VAR_SEQ 1..215
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019458"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1V5T"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1V5T"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1V5T"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:1V5T"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1V5T"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1V5T"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1V5T"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1V5T"
SQ SEQUENCE 318 AA; 36837 MW; 77949D660DC7E3A4 CRC64;
MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV KGKPAENDVK
LGALKLKPNT KIMMMGTREE SLEDVLCPPP DNDDVINDFD IEDEVVEVEN REENLLKVSR
RVKEYKVEVL NPPREGKKLL VLDVDYTLFD HRSCAETGVE LMRPYLHEFL TSAYEDYDIV
IWSATNMKWI EAKMKELGVS TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS
EFYSKKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELVKLTQY LKEIAKLDDF
LELNHKYWER YLSKKQGQ
