UBCP1_HUMAN
ID UBCP1_HUMAN Reviewed; 318 AA.
AC Q8WVY7; D3DQJ7; Q96DK5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PRELIMINARY FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=15883030; DOI=10.1016/j.bbrc.2005.04.065;
RA Zheng H., Ji C., Gu S., Shi B., Wang J., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel RNA polymerase II C-terminal
RT domain phosphatase.";
RL Biochem. Biophys. Res. Commun. 331:1401-1407(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, ABSENCE OF INFLUENCE ON POLR2A CTD PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-44.
RX PubMed=21949367; DOI=10.1073/pnas.1113170108;
RA Guo X., Engel J.L., Xiao J., Tagliabracci V.S., Wang X., Huang L.,
RA Dixon J.E.;
RT "UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18649-18654(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. {ECO:0000269|PubMed:21949367}.
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:0000269|PubMed:15883030};
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:0000269|PubMed:15883030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15883030};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:15883030};
CC -!- INTERACTION:
CC Q8WVY7; Q13200: PSMD2; NbExp=13; IntAct=EBI-750011, EBI-357648;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15883030,
CC ECO:0000269|PubMed:21949367}. Note=Colocalizes with nuclear
CC proteasomes.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in placenta,
CC lung, testis and ovary. Up-regulated in tumor tissues.
CC {ECO:0000269|PubMed:15883030}.
CC -!- DOMAIN: The Ubiquitin-like domain mediates interaction with
CC proteasomes.
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DR EMBL; AY444562; AAS68538.1; -; mRNA.
DR EMBL; AK057996; BAB71628.1; -; mRNA.
DR EMBL; CH471062; EAW61577.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61578.1; -; Genomic_DNA.
DR EMBL; BC013425; AAH13425.2; -; mRNA.
DR CCDS; CCDS4345.1; -.
DR RefSeq; NP_659486.2; NM_145049.4.
DR PDB; 2KX3; NMR; -; A=1-81.
DR PDB; 2LGD; NMR; -; A=1-81.
DR PDB; 2M17; NMR; -; A=1-81.
DR PDBsum; 2KX3; -.
DR PDBsum; 2LGD; -.
DR PDBsum; 2M17; -.
DR AlphaFoldDB; Q8WVY7; -.
DR BMRB; Q8WVY7; -.
DR SMR; Q8WVY7; -.
DR BioGRID; 126404; 87.
DR IntAct; Q8WVY7; 28.
DR MINT; Q8WVY7; -.
DR STRING; 9606.ENSP00000296786; -.
DR BindingDB; Q8WVY7; -.
DR ChEMBL; CHEMBL3317333; -.
DR DEPOD; UBLCP1; -.
DR GlyGen; Q8WVY7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WVY7; -.
DR PhosphoSitePlus; Q8WVY7; -.
DR BioMuta; UBLCP1; -.
DR DMDM; 74751564; -.
DR EPD; Q8WVY7; -.
DR jPOST; Q8WVY7; -.
DR MassIVE; Q8WVY7; -.
DR MaxQB; Q8WVY7; -.
DR PaxDb; Q8WVY7; -.
DR PeptideAtlas; Q8WVY7; -.
DR PRIDE; Q8WVY7; -.
DR ProteomicsDB; 74835; -.
DR Antibodypedia; 28498; 189 antibodies from 24 providers.
DR DNASU; 134510; -.
DR Ensembl; ENST00000296786.8; ENSP00000296786.6; ENSG00000164332.8.
DR GeneID; 134510; -.
DR KEGG; hsa:134510; -.
DR MANE-Select; ENST00000296786.8; ENSP00000296786.6; NM_145049.5; NP_659486.2.
DR UCSC; uc003lxq.2; human.
DR CTD; 134510; -.
DR DisGeNET; 134510; -.
DR GeneCards; UBLCP1; -.
DR HGNC; HGNC:28110; UBLCP1.
DR HPA; ENSG00000164332; Low tissue specificity.
DR MIM; 609867; gene.
DR neXtProt; NX_Q8WVY7; -.
DR OpenTargets; ENSG00000164332; -.
DR PharmGKB; PA142670646; -.
DR VEuPathDB; HostDB:ENSG00000164332; -.
DR eggNOG; KOG1605; Eukaryota.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000010107; -.
DR HOGENOM; CLU_046931_1_0_1; -.
DR InParanoid; Q8WVY7; -.
DR OMA; DSNAMIS; -.
DR OrthoDB; 1376145at2759; -.
DR PhylomeDB; Q8WVY7; -.
DR TreeFam; TF323786; -.
DR PathwayCommons; Q8WVY7; -.
DR SignaLink; Q8WVY7; -.
DR BioGRID-ORCS; 134510; 14 hits in 1049 CRISPR screens.
DR ChiTaRS; UBLCP1; human.
DR GenomeRNAi; 134510; -.
DR Pharos; Q8WVY7; Tchem.
DR PRO; PR:Q8WVY7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WVY7; protein.
DR Bgee; ENSG00000164332; Expressed in oocyte and 187 other tissues.
DR Genevisible; Q8WVY7; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
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; Hydrolase; Nucleus; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..318
FT /note="Ubiquitin-like domain-containing CTD phosphatase 1"
FT /id="PRO_0000242640"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 44
FT /note="K->A: No binding to proteasome."
FT /evidence="ECO:0000269|PubMed:21949367"
FT CONFLICT 83
FT /note="E -> G (in Ref. 2; BAB71628)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2KX3"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2KX3"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2LGD"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:2KX3"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2KX3"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2KX3"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2M17"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2KX3"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2KX3"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2M17"
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
