Full text data of UBLCP1
UBLCP1
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-like domain-containing CTD phosphatase 1; 3.1.3.16 (Nuclear proteasome inhibitor UBLCP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-like domain-containing CTD phosphatase 1; 3.1.3.16 (Nuclear proteasome inhibitor UBLCP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8WVY7
ID UBCP1_HUMAN Reviewed; 318 AA.
AC Q8WVY7; D3DQJ7; Q96DK5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2002, sequence version 2.
DT 22-JAN-2014, entry version 97.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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,
RP SUBCELLULAR 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
RT proteasome activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18649-18654(2011).
CC -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby
CC decreasing their proteolytic activity. The dephosphorylation may
CC prevent assembly of the core and regulatory particles (CP and RP)
CC into mature 26S proteasome.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with nuclear
CC proteasomes.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC placenta, lung, testis and ovary. Up-regulated in tumor tissues.
CC -!- DOMAIN: The Ubiquitin-like domain mediates interaction with
CC proteasomes.
CC -!- SIMILARITY: Contains 1 FCP1 homology domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_659486.2; NM_145049.3.
DR UniGene; Hs.591733; -.
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 ProteinModelPortal; Q8WVY7; -.
DR SMR; Q8WVY7; 1-311.
DR IntAct; Q8WVY7; 2.
DR MINT; MINT-1445291; -.
DR STRING; 9606.ENSP00000296786; -.
DR PhosphoSite; Q8WVY7; -.
DR DMDM; 74751564; -.
DR PaxDb; Q8WVY7; -.
DR PeptideAtlas; Q8WVY7; -.
DR PRIDE; Q8WVY7; -.
DR DNASU; 134510; -.
DR Ensembl; ENST00000296786; ENSP00000296786; ENSG00000164332.
DR GeneID; 134510; -.
DR KEGG; hsa:134510; -.
DR UCSC; uc003lxq.2; human.
DR CTD; 134510; -.
DR GeneCards; GC05P158690; -.
DR HGNC; HGNC:28110; UBLCP1.
DR HPA; HPA039615; -.
DR MIM; 609867; gene.
DR neXtProt; NX_Q8WVY7; -.
DR PharmGKB; PA142670646; -.
DR eggNOG; NOG310886; -.
DR HOGENOM; HOG000231279; -.
DR HOVERGEN; HBG080207; -.
DR InParanoid; Q8WVY7; -.
DR KO; K17618; -.
DR OMA; ELNPPRE; -.
DR OrthoDB; EOG74TX01; -.
DR PhylomeDB; Q8WVY7; -.
DR GenomeRNAi; 134510; -.
DR NextBio; 83393; -.
DR PRO; PR:Q8WVY7; -.
DR Bgee; Q8WVY7; -.
DR CleanEx; HS_UBLCP1; -.
DR Genevestigator; Q8WVY7; -.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR011943; HAD-SF_hydro_IIID.
DR InterPro; IPR004274; NIF.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02245; HAD_IIID1; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 318 Ubiquitin-like domain-containing CTD
FT phosphatase 1.
FT /FTId=PRO_0000242640.
FT DOMAIN 3 81 Ubiquitin-like.
FT DOMAIN 133 294 FCP1 homology.
FT REGION 133 294 Phosphatase.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 117 117 N6-acetyllysine.
FT MUTAGEN 44 44 K->A: No binding to proteasome.
FT CONFLICT 83 83 E -> G (in Ref. 2; BAB71628).
FT STRAND 5 9
FT STRAND 12 16
FT TURN 21 23
FT HELIX 25 35
FT TURN 39 41
FT STRAND 46 49
FT STRAND 57 59
FT HELIX 61 64
FT HELIX 68 70
FT STRAND 71 76
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
//
ID UBCP1_HUMAN Reviewed; 318 AA.
AC Q8WVY7; D3DQJ7; Q96DK5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2002, sequence version 2.
DT 22-JAN-2014, entry version 97.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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,
RP SUBCELLULAR 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
RT proteasome activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18649-18654(2011).
CC -!- FUNCTION: Dephosphorylates 26S nuclear proteasomes, thereby
CC decreasing their proteolytic activity. The dephosphorylation may
CC prevent assembly of the core and regulatory particles (CP and RP)
CC into mature 26S proteasome.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with nuclear
CC proteasomes.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC placenta, lung, testis and ovary. Up-regulated in tumor tissues.
CC -!- DOMAIN: The Ubiquitin-like domain mediates interaction with
CC proteasomes.
CC -!- SIMILARITY: Contains 1 FCP1 homology domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_659486.2; NM_145049.3.
DR UniGene; Hs.591733; -.
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 ProteinModelPortal; Q8WVY7; -.
DR SMR; Q8WVY7; 1-311.
DR IntAct; Q8WVY7; 2.
DR MINT; MINT-1445291; -.
DR STRING; 9606.ENSP00000296786; -.
DR PhosphoSite; Q8WVY7; -.
DR DMDM; 74751564; -.
DR PaxDb; Q8WVY7; -.
DR PeptideAtlas; Q8WVY7; -.
DR PRIDE; Q8WVY7; -.
DR DNASU; 134510; -.
DR Ensembl; ENST00000296786; ENSP00000296786; ENSG00000164332.
DR GeneID; 134510; -.
DR KEGG; hsa:134510; -.
DR UCSC; uc003lxq.2; human.
DR CTD; 134510; -.
DR GeneCards; GC05P158690; -.
DR HGNC; HGNC:28110; UBLCP1.
DR HPA; HPA039615; -.
DR MIM; 609867; gene.
DR neXtProt; NX_Q8WVY7; -.
DR PharmGKB; PA142670646; -.
DR eggNOG; NOG310886; -.
DR HOGENOM; HOG000231279; -.
DR HOVERGEN; HBG080207; -.
DR InParanoid; Q8WVY7; -.
DR KO; K17618; -.
DR OMA; ELNPPRE; -.
DR OrthoDB; EOG74TX01; -.
DR PhylomeDB; Q8WVY7; -.
DR GenomeRNAi; 134510; -.
DR NextBio; 83393; -.
DR PRO; PR:Q8WVY7; -.
DR Bgee; Q8WVY7; -.
DR CleanEx; HS_UBLCP1; -.
DR Genevestigator; Q8WVY7; -.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR011943; HAD-SF_hydro_IIID.
DR InterPro; IPR004274; NIF.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02245; HAD_IIID1; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 318 Ubiquitin-like domain-containing CTD
FT phosphatase 1.
FT /FTId=PRO_0000242640.
FT DOMAIN 3 81 Ubiquitin-like.
FT DOMAIN 133 294 FCP1 homology.
FT REGION 133 294 Phosphatase.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 117 117 N6-acetyllysine.
FT MUTAGEN 44 44 K->A: No binding to proteasome.
FT CONFLICT 83 83 E -> G (in Ref. 2; BAB71628).
FT STRAND 5 9
FT STRAND 12 16
FT TURN 21 23
FT HELIX 25 35
FT TURN 39 41
FT STRAND 46 49
FT STRAND 57 59
FT HELIX 61 64
FT HELIX 68 70
FT STRAND 71 76
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
//
MIM
609867
*RECORD*
*FIELD* NO
609867
*FIELD* TI
*609867 UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; UBLCP1
*FIELD* TX
CLONING
read more
During large-scale cDNA sequencing, Zheng et al. (2005) cloned a novel
phosphatase, which they named ubiquitin-like domain-containing CTD
phosphatase-1 (UBLCP1), from a human fetal brain cDNA library. UBLCP1
encodes a 318-amino acid protein with a predicted molecular mass of 36.8
kD. It has a CTD phosphatase catalytic domain containing several
residues essential for catalytic activity that are conserved with those
in the CTD phosphatases CTDSP1 (605323) and CTDP1 (604927). UBLCP1 also
contains an N-terminal ubiquitin-like domain that harbors a
proteasome-interacting motif. RT-PCR detected relatively high expression
of UBLCP1 in placenta, lung, testis, and ovary, with weaker expression
in heart, liver, kidney, spleen, thymus, colon, and peripheral blood
leukocytes. UBLCP1 expression was particularly high in breast, lung,
colon, prostate, ovarian, and pancreas tumor tissues. Immunofluorescence
analysis localized UBLCP1 to the nucleus.
GENE FUNCTION
Using in vitro phosphatase assays, Zheng et al. (2005) demonstrated that
UBLCP1 shows magnesium-dependent phosphatase activity towards the
substrate p-nitrophenyl phosphate that is optimal at pH 5. In vitro
assays also showed that UBLCP1 dephosphorylates the C-terminal domain of
RNA polymerase II (180660), with highest activity at serine-5.
GENE STRUCTURE
Zheng et al. (2005) determined that the UBLCP1 gene contains 11 exons
spanning over 22.7 kb.
MAPPING
By sequence analysis, Zheng et al. (2005) mapped the UBLCP1 gene to
chromosome 5q33.3.
*FIELD* RF
1. Zheng, H.; Ji, C.; Gu, S.; Shi, B.; Wang, J.; Xie, Y.; Mao, Y.
: Cloning and characterization of a novel RNA polymerase II C-terminal
domain phosphatase. Biochem. Biophys. Res. Commun. 331: 1401-1407,
2005.
*FIELD* CD
Laura L. Baxter: 1/31/2006
*FIELD* ED
carol: 12/26/2007
carol: 1/31/2006
*RECORD*
*FIELD* NO
609867
*FIELD* TI
*609867 UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1; UBLCP1
*FIELD* TX
CLONING
read more
During large-scale cDNA sequencing, Zheng et al. (2005) cloned a novel
phosphatase, which they named ubiquitin-like domain-containing CTD
phosphatase-1 (UBLCP1), from a human fetal brain cDNA library. UBLCP1
encodes a 318-amino acid protein with a predicted molecular mass of 36.8
kD. It has a CTD phosphatase catalytic domain containing several
residues essential for catalytic activity that are conserved with those
in the CTD phosphatases CTDSP1 (605323) and CTDP1 (604927). UBLCP1 also
contains an N-terminal ubiquitin-like domain that harbors a
proteasome-interacting motif. RT-PCR detected relatively high expression
of UBLCP1 in placenta, lung, testis, and ovary, with weaker expression
in heart, liver, kidney, spleen, thymus, colon, and peripheral blood
leukocytes. UBLCP1 expression was particularly high in breast, lung,
colon, prostate, ovarian, and pancreas tumor tissues. Immunofluorescence
analysis localized UBLCP1 to the nucleus.
GENE FUNCTION
Using in vitro phosphatase assays, Zheng et al. (2005) demonstrated that
UBLCP1 shows magnesium-dependent phosphatase activity towards the
substrate p-nitrophenyl phosphate that is optimal at pH 5. In vitro
assays also showed that UBLCP1 dephosphorylates the C-terminal domain of
RNA polymerase II (180660), with highest activity at serine-5.
GENE STRUCTURE
Zheng et al. (2005) determined that the UBLCP1 gene contains 11 exons
spanning over 22.7 kb.
MAPPING
By sequence analysis, Zheng et al. (2005) mapped the UBLCP1 gene to
chromosome 5q33.3.
*FIELD* RF
1. Zheng, H.; Ji, C.; Gu, S.; Shi, B.; Wang, J.; Xie, Y.; Mao, Y.
: Cloning and characterization of a novel RNA polymerase II C-terminal
domain phosphatase. Biochem. Biophys. Res. Commun. 331: 1401-1407,
2005.
*FIELD* CD
Laura L. Baxter: 1/31/2006
*FIELD* ED
carol: 12/26/2007
carol: 1/31/2006