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O95476

- CNEP1_HUMAN

UniProt

O95476 - CNEP1_HUMAN

Protein

CTD nuclear envelope phosphatase 1

Gene

CTDNEP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (03 Nov 2009)
      Previous versions | rss
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    Functioni

    Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling.2 Publications

    Catalytic activityi

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

    Kineticsi

    1. KM=18 mM for p-nitrophenylphosphate1 Publication

    pH dependencei

    Optimum pH is 5.5.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. nuclear envelope organization Source: UniProtKB
    2. positive regulation of triglyceride biosynthetic process Source: UniProtKB
    3. protein dephosphorylation Source: UniProtKB
    4. protein localization to nucleus Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_200828. Depolymerisation of the Nuclear Lamina.
    SABIO-RKO95476.
    SignaLinkiO95476.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTD nuclear envelope phosphatase 1 (EC:3.1.3.16)
    Alternative name(s):
    Serine/threonine-protein phosphatase dullard
    Gene namesi
    Name:CTDNEP1
    Synonyms:DULLARD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:19085. CTDNEP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. Nem1-Spo7 phosphatase complex Source: UniProtKB
    5. nuclear envelope Source: UniProtKB
    6. nuclear membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671D → N or E: Abolishes phosphatase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134937999.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 244244CTD nuclear envelope phosphatase 1PRO_0000297967Add
    BLAST

    Proteomic databases

    MaxQBiO95476.
    PaxDbiO95476.
    PRIDEiO95476.

    PTM databases

    PhosphoSiteiO95476.

    Expressioni

    Tissue specificityi

    Muscle specific with lower expression in other metabolic tissues.1 Publication

    Gene expression databases

    ArrayExpressiO95476.
    BgeeiO95476.
    CleanExiHS_DULLARD.
    GenevestigatoriO95476.

    Organism-specific databases

    HPAiHPA037439.

    Interactioni

    Subunit structurei

    Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and LPIN2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CNEP1R1Q8N9A84EBI-5323433,EBI-5323455

    Protein-protein interaction databases

    BioGridi116972. 3 interactions.
    IntActiO95476. 2 interactions.
    STRINGi9606.ENSP00000321732.

    Structurei

    3D structure databases

    ProteinModelPortaliO95476.
    SMRiO95476. Positions 57-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 224168FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the dullard family.Curated
    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5190.
    HOGENOMiHOG000236379.
    HOVERGENiHBG098153.
    InParanoidiO95476.
    KOiK17617.
    OMAiLLGIRTF.
    PhylomeDBiO95476.
    TreeFamiTF313962.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR011948. Dullard_phosphatase.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view]
    PfamiPF03031. NIF. 1 hit.
    [Graphical view]
    SMARTiSM00577. CPDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02251. HIF-SF_euk. 1 hit.
    PROSITEiPS50969. FCP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95476-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP    50
    VSRNRLAQVK RKILVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID 100
    KHPVRFFVHK RPHVDFFLEV VSQWYELVVF TASMEIYGSA VADKLDNSRS 150
    ILKRRYYRQH CTLELGSYIK DLSVVHSDLS SIVILDNSPG AYRSHPDNAI 200
    PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ HRLW 244
    Length:244
    Mass (Da):28,377
    Last modified:November 3, 2009 - v2
    Checksum:i062952A90F74575A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121T → A.2 Publications
    Corresponds to variant rs3744399 [ dbSNP | Ensembl ].
    VAR_034699

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011916 mRNA. Translation: CAA09865.1.
    AY364239 mRNA. Translation: AAQ76798.1.
    AC003688 Genomic DNA. No translation available.
    AC120057 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90233.1.
    CH471108 Genomic DNA. Translation: EAW90235.1.
    CH471108 Genomic DNA. Translation: EAW90236.1.
    BC009295 mRNA. Translation: AAH09295.1.
    CCDSiCCDS11093.1.
    RefSeqiNP_001137247.1. NM_001143775.1.
    NP_056158.2. NM_015343.4.
    UniGeneiHs.513913.

    Genome annotation databases

    EnsembliENST00000318988; ENSP00000321732; ENSG00000175826.
    ENST00000573600; ENSP00000461749; ENSG00000175826.
    ENST00000574205; ENSP00000458758; ENSG00000175826.
    ENST00000574322; ENSP00000460683; ENSG00000175826.
    GeneIDi23399.
    KEGGihsa:23399.
    UCSCiuc002gfd.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011916 mRNA. Translation: CAA09865.1 .
    AY364239 mRNA. Translation: AAQ76798.1 .
    AC003688 Genomic DNA. No translation available.
    AC120057 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90233.1 .
    CH471108 Genomic DNA. Translation: EAW90235.1 .
    CH471108 Genomic DNA. Translation: EAW90236.1 .
    BC009295 mRNA. Translation: AAH09295.1 .
    CCDSi CCDS11093.1.
    RefSeqi NP_001137247.1. NM_001143775.1.
    NP_056158.2. NM_015343.4.
    UniGenei Hs.513913.

    3D structure databases

    ProteinModelPortali O95476.
    SMRi O95476. Positions 57-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116972. 3 interactions.
    IntActi O95476. 2 interactions.
    STRINGi 9606.ENSP00000321732.

    PTM databases

    PhosphoSitei O95476.

    Proteomic databases

    MaxQBi O95476.
    PaxDbi O95476.
    PRIDEi O95476.

    Protocols and materials databases

    DNASUi 23399.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318988 ; ENSP00000321732 ; ENSG00000175826 .
    ENST00000573600 ; ENSP00000461749 ; ENSG00000175826 .
    ENST00000574205 ; ENSP00000458758 ; ENSG00000175826 .
    ENST00000574322 ; ENSP00000460683 ; ENSG00000175826 .
    GeneIDi 23399.
    KEGGi hsa:23399.
    UCSCi uc002gfd.2. human.

    Organism-specific databases

    CTDi 23399.
    GeneCardsi GC17M007147.
    HGNCi HGNC:19085. CTDNEP1.
    HPAi HPA037439.
    MIMi 610684. gene.
    neXtProti NX_O95476.
    PharmGKBi PA134937999.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5190.
    HOGENOMi HOG000236379.
    HOVERGENi HBG098153.
    InParanoidi O95476.
    KOi K17617.
    OMAi LLGIRTF.
    PhylomeDBi O95476.
    TreeFami TF313962.

    Enzyme and pathway databases

    Reactomei REACT_200828. Depolymerisation of the Nuclear Lamina.
    SABIO-RK O95476.
    SignaLinki O95476.

    Miscellaneous databases

    ChiTaRSi CTDNEP1. human.
    GenomeRNAii 23399.
    NextBioi 45549.
    PROi O95476.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95476.
    Bgeei O95476.
    CleanExi HS_DULLARD.
    Genevestigatori O95476.

    Family and domain databases

    Gene3Di 3.40.50.1000. 1 hit.
    InterProi IPR011948. Dullard_phosphatase.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view ]
    Pfami PF03031. NIF. 1 hit.
    [Graphical view ]
    SMARTi SM00577. CPDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02251. HIF-SF_euk. 1 hit.
    PROSITEi PS50969. FCP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Keen J., Inglehearn C.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-12.
      Tissue: Brain.
    2. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
      Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
      BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, VARIANT ALA-12.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Muscle.
    6. "Molecular cloning and characterization of dullard: a novel gene required for neural development."
      Satow R., Chan T.C., Asashima M.
      Biochem. Biophys. Res. Commun. 295:85-91(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    7. "A conserved phosphatase cascade that regulates nuclear membrane biogenesis."
      Kim Y., Gentry M.S., Harris T.E., Wiley S.E., Lawrence J.C. Jr., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 104:6596-6601(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-67, SUBCELLULAR LOCATION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is the metazoan SPO7 ortholog and functions in the lipin activation pathway."
      Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R., Graham M., Reue K., Dixon J.E., Goodman J.M.
      J. Biol. Chem. 287:3123-3137(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LPIN1 AND LPIN2 DEPHOSPHORYLATION, INTERACTION WITH CNEP1R1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCNEP1_HUMAN
    AccessioniPrimary (citable) accession number: O95476
    Secondary accession number(s): D3DTN7, Q96GQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 93 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3