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Q8WVY7

- UBCP1_HUMAN

UniProt

Q8WVY7 - UBCP1_HUMAN

Protein

Ubiquitin-like domain-containing CTD phosphatase 1

Gene

UBLCP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.1 Publication

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Cofactori

    Magnesium.1 Publication

    pH dependencei

    Optimum pH is 5.0.1 Publication

    GO - Molecular functioni

    1. phosphoprotein phosphatase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like domain-containing CTD phosphatase 1 (EC:3.1.3.16)
    Alternative name(s):
    Nuclear proteasome inhibitor UBLCP1
    Gene namesi
    Name:UBLCP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:28110. UBLCP1.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Colocalizes with nuclear proteasomes.

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441K → A: No binding to proteasome. 1 Publication

    Organism-specific databases

    PharmGKBiPA142670646.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 318317Ubiquitin-like domain-containing CTD phosphatase 1PRO_0000242640Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei117 – 1171N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8WVY7.
    PaxDbiQ8WVY7.
    PeptideAtlasiQ8WVY7.
    PRIDEiQ8WVY7.

    PTM databases

    PhosphoSiteiQ8WVY7.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in placenta, lung, testis and ovary. Up-regulated in tumor tissues.1 Publication

    Gene expression databases

    BgeeiQ8WVY7.
    CleanExiHS_UBLCP1.
    GenevestigatoriQ8WVY7.

    Organism-specific databases

    HPAiHPA039615.

    Interactioni

    Protein-protein interaction databases

    BioGridi126404. 8 interactions.
    IntActiQ8WVY7. 2 interactions.
    MINTiMINT-1445291.
    STRINGi9606.ENSP00000296786.

    Structurei

    Secondary structure

    1
    318
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Beta strandi12 – 165
    Turni21 – 233
    Helixi25 – 3511
    Turni39 – 413
    Beta strandi46 – 494
    Beta strandi57 – 593
    Helixi61 – 644
    Helixi68 – 703
    Beta strandi71 – 766

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KX3NMR-A1-81[»]
    2LGDNMR-A1-81[»]
    2M17NMR-A1-81[»]
    ProteinModelPortaliQ8WVY7.
    SMRiQ8WVY7. Positions 1-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8179Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini133 – 294162FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 294162PhosphataseAdd
    BLAST

    Domaini

    The Ubiquitin-like domain mediates interaction with proteasomes.

    Sequence similaritiesi

    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG310886.
    HOGENOMiHOG000231279.
    HOVERGENiHBG080207.
    InParanoidiQ8WVY7.
    KOiK17618.
    OMAiELNPPRE.
    OrthoDBiEOG74TX01.
    PhylomeDBiQ8WVY7.
    TreeFamiTF323786.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR011943. HAD-SF_hydro_IIID.
    IPR004274. NIF.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF03031. NIF. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00577. CPDc. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02245. HAD_IIID1. 1 hit.
    PROSITEiPS50969. FCP1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8WVY7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALPIIVKWG GQEYSVTTLS EDDTVLDLKQ FLKTLTGVLP ERQKLLGLKV    50
    KGKPAENDVK LGALKLKPNT KIMMMGTREE SLEDVLGPPP DNDDVVNDFD 100
    IEDEVVEVEN REENLLKISR RVKEYKVEIL NPPREGKKLL VLDVDYTLFD 150
    HRSCAETGVE LMRPYLHEFL TSAYEDYDIV IWSATNMKWI EAKMKELGVS 200
    TNANYKITFM LDSAAMITVH TPRRGLIDVK PLGVIWGKFS EFYSKKNTIM 250
    FDDIGRNFLM NPQNGLKIRP FMKAHLNRDK DKELLKLTQY LKEIAKLDDF 300
    LDLNHKYWER YLSKKQGQ 318
    Length:318
    Mass (Da):36,805
    Last modified:October 1, 2002 - v2
    Checksum:i21CB4DB22C3B0E0F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831E → G in BAB71628. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY444562 mRNA. Translation: AAS68538.1.
    AK057996 mRNA. Translation: BAB71628.1.
    CH471062 Genomic DNA. Translation: EAW61577.1.
    CH471062 Genomic DNA. Translation: EAW61578.1.
    BC013425 mRNA. Translation: AAH13425.2.
    CCDSiCCDS4345.1.
    RefSeqiNP_659486.2. NM_145049.3.
    UniGeneiHs.591733.

    Genome annotation databases

    EnsembliENST00000296786; ENSP00000296786; ENSG00000164332.
    GeneIDi134510.
    KEGGihsa:134510.
    UCSCiuc003lxq.2. human.

    Polymorphism databases

    DMDMi74751564.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY444562 mRNA. Translation: AAS68538.1 .
    AK057996 mRNA. Translation: BAB71628.1 .
    CH471062 Genomic DNA. Translation: EAW61577.1 .
    CH471062 Genomic DNA. Translation: EAW61578.1 .
    BC013425 mRNA. Translation: AAH13425.2 .
    CCDSi CCDS4345.1.
    RefSeqi NP_659486.2. NM_145049.3.
    UniGenei Hs.591733.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KX3 NMR - A 1-81 [» ]
    2LGD NMR - A 1-81 [» ]
    2M17 NMR - A 1-81 [» ]
    ProteinModelPortali Q8WVY7.
    SMRi Q8WVY7. Positions 1-311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126404. 8 interactions.
    IntActi Q8WVY7. 2 interactions.
    MINTi MINT-1445291.
    STRINGi 9606.ENSP00000296786.

    PTM databases

    PhosphoSitei Q8WVY7.

    Polymorphism databases

    DMDMi 74751564.

    Proteomic databases

    MaxQBi Q8WVY7.
    PaxDbi Q8WVY7.
    PeptideAtlasi Q8WVY7.
    PRIDEi Q8WVY7.

    Protocols and materials databases

    DNASUi 134510.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296786 ; ENSP00000296786 ; ENSG00000164332 .
    GeneIDi 134510.
    KEGGi hsa:134510.
    UCSCi uc003lxq.2. human.

    Organism-specific databases

    CTDi 134510.
    GeneCardsi GC05P158690.
    HGNCi HGNC:28110. UBLCP1.
    HPAi HPA039615.
    MIMi 609867. gene.
    neXtProti NX_Q8WVY7.
    PharmGKBi PA142670646.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310886.
    HOGENOMi HOG000231279.
    HOVERGENi HBG080207.
    InParanoidi Q8WVY7.
    KOi K17618.
    OMAi ELNPPRE.
    OrthoDBi EOG74TX01.
    PhylomeDBi Q8WVY7.
    TreeFami TF323786.

    Miscellaneous databases

    GenomeRNAii 134510.
    NextBioi 83393.
    PROi Q8WVY7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8WVY7.
    CleanExi HS_UBLCP1.
    Genevestigatori Q8WVY7.

    Family and domain databases

    Gene3Di 3.40.50.1000. 1 hit.
    InterProi IPR023214. HAD-like_dom.
    IPR011943. HAD-SF_hydro_IIID.
    IPR004274. NIF.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF03031. NIF. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00577. CPDc. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02245. HAD_IIID1. 1 hit.
    PROSITEi PS50969. FCP1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase."
      Zheng H., Ji C., Gu S., Shi B., Wang J., Xie Y., Mao Y.
      Biochem. Biophys. Res. Commun. 331:1401-1407(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PRELIMINARY FUNCTION.
      Tissue: Fetal brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Gastric mucosa.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity."
      Guo X., Engel J.L., Xiao J., Tagliabracci V.S., Wang X., Huang L., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:18649-18654(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ABSENCE OF INFLUENCE ON POLR2A CTD PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-44.
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBCP1_HUMAN
    AccessioniPrimary (citable) accession number: Q8WVY7
    Secondary accession number(s): D3DQJ7, Q96DK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3