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O95476

- CNEP1_HUMAN

UniProt

O95476 - CNEP1_HUMAN

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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

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 serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. gamete generation Source: Ensembl
  2. mesoderm development Source: Ensembl
  3. nuclear envelope organization Source: UniProtKB
  4. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  5. positive regulation of triglyceride biosynthetic process Source: UniProtKB
  6. protein dephosphorylation Source: UniProtKB
  7. protein localization to nucleus Source: UniProtKB
Complete GO annotation...

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

Topology

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

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
Complete GO annotation...

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

BgeeiO95476.
CleanExiHS_DULLARD.
ExpressionAtlasiO95476. baseline and differential.
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. 12 interactions.
IntActiO95476. 2 interactions.
STRINGi9606.ENSP00000321732.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00550000075053.
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

        10         20         30         40         50
MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP
60 70 80 90 100
VSRNRLAQVK RKILVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID
110 120 130 140 150
KHPVRFFVHK RPHVDFFLEV VSQWYELVVF TASMEIYGSA VADKLDNSRS
160 170 180 190 200
ILKRRYYRQH CTLELGSYIK DLSVVHSDLS SIVILDNSPG AYRSHPDNAI
210 220 230 240
PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ HRLW
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 12 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.
GeneTreei ENSGT00550000075053.
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

Bgeei O95476.
CleanExi HS_DULLARD.
ExpressionAtlasi O95476. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 94 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