ID UBCP1_BOVIN Reviewed; 318 AA. AC Q2KJD7; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Ubiquitin-like domain-containing CTD phosphatase 1; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8WVY7}; DE AltName: Full=Nuclear proteasome inhibitor UBLCP1; GN Name=UBLCP1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby decreasing CC their proteolytic activity. Recruited to the 19S regulatory particle of CC the 26S proteasome through its interaction with 19S component CC PSMD2/RPN1. Once recruited, dephosphorylates 19S component PSMC2/RPT1 CC which impairs PSMC2 ATPase activity and disrupts 26S proteasome CC assembly. Has also been reported to stimulate the proteolytic activity CC of the 26S proteasome. {ECO:0000250|UniProtKB:Q8WVY7}. 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 Evidence={ECO:0000250|UniProtKB:Q8WVY7}; 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 Evidence={ECO:0000250|UniProtKB:Q8WVY7}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q8WVY7}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WVY7}. CC Note=Colocalizes with nuclear proteasomes. CC {ECO:0000250|UniProtKB:Q8WVY7}. CC -!- DOMAIN: The Ubiquitin-like domain mediates interaction with CC proteasomes. {ECO:0000250|UniProtKB:Q8WVY7}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC105394; AAI05395.1; -; mRNA. DR RefSeq; NP_001039459.1; NM_001045994.1. DR RefSeq; XP_010805865.1; XM_010807563.2. DR AlphaFoldDB; Q2KJD7; -. DR BMRB; Q2KJD7; -. DR SMR; Q2KJD7; -. DR STRING; 9913.ENSBTAP00000011999; -. DR PaxDb; 9913-ENSBTAP00000011999; -. DR Ensembl; ENSBTAT00000011999.4; ENSBTAP00000011999.3; ENSBTAG00000009103.4. DR GeneID; 508163; -. DR KEGG; bta:508163; -. DR CTD; 134510; -. DR VEuPathDB; HostDB:ENSBTAG00000009103; -. DR VGNC; VGNC:36609; UBLCP1. DR eggNOG; KOG1605; Eukaryota. DR eggNOG; KOG1872; Eukaryota. DR GeneTree; ENSGT00390000010107; -. DR HOGENOM; CLU_046931_1_0_1; -. DR InParanoid; Q2KJD7; -. DR OMA; DSNAMIS; -. DR OrthoDB; 49886at2759; -. DR TreeFam; TF323786; -. DR Proteomes; UP000009136; Chromosome 7. DR Bgee; ENSBTAG00000009103; Expressed in oocyte and 107 other cell types or tissues. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:1904855; F:proteasome regulatory particle binding; IEA:Ensembl. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0090364; P:regulation of proteasome assembly; IEA:Ensembl. DR CDD; cd01813; Ubl_UBLCP1; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR02245; HAD_IIID1; 1. DR PANTHER; PTHR48405; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1. DR PANTHER; PTHR48405:SF1; UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; 1. DR Pfam; PF03031; NIF; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00577; CPDc; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50969; FCP1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 2: Evidence at transcript level; KW Acetylation; Hydrolase; Magnesium; Metal-binding; 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_0000242639" 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 BINDING 143 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9XZ16" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9XZ16" FT BINDING 253 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9XZ16" 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" SQ SEQUENCE 318 AA; 36805 MW; 21CB4DB22C3B0E0F CRC64; MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV KGKPAENDVK LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVVNDFD IEDEVVEVEN REENLLKISR RVKEYKVEIL NPPREGKKLL VLDVDYTLFD HRSCAETGVE LMRPYLHEFL TSAYEDYDIV IWSATNMKWI EAKMKELGVS TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS EFYSKKNTIM FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLTQY LKEIAKLDDF LDLNHKYWER YLSKKQGQ //