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Protein

CTD nuclear envelope phosphatase 1

Gene

Ctdnep1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 different 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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiR-MMU-4419969 Depolymerisation of the Nuclear Lamina

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1914431 Ctdnep1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei7 – 29HelicalSequence analysisAdd BLAST23

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002979681 – 244CTD nuclear envelope phosphatase 1Add BLAST244

Proteomic databases

EPDiQ3TP92
MaxQBiQ3TP92
PaxDbiQ3TP92
PeptideAtlasiQ3TP92
PRIDEiQ3TP92

PTM databases

iPTMnetiQ3TP92
PhosphoSitePlusiQ3TP92

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000018559 Expressed in 273 organ(s), highest expression level in skeletal muscle tissue
CleanExiMM_DULLARD
ExpressionAtlasiQ3TP92 baseline and differential
GenevisibleiQ3TP92 MM

Interactioni

Subunit structurei

Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and LPIN2.By similarity

Protein-protein interaction databases

BioGridi211999, 1 interactor
STRINGi10090.ENSMUSP00000104234

Structurei

3D structure databases

ProteinModelPortaliQ3TP92
SMRiQ3TP92
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 224FCP1 homologyPROSITE-ProRule annotationAdd BLAST168

Sequence similaritiesi

Belongs to the dullard family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1605 Eukaryota
COG5190 LUCA
GeneTreeiENSGT00390000017194
HOVERGENiHBG098153
InParanoidiQ3TP92
KOiK17617
OMAiSRIWGFI
OrthoDBiEOG091G0GIO
PhylomeDBiQ3TP92
TreeFamiTF313962

Family and domain databases

Gene3Di3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR011948 Dullard_phosphatase
IPR004274 FCP1_dom
IPR036412 HAD-like_sf
IPR023214 HAD_sf
PfamiView protein in Pfam
PF03031 NIF, 1 hit
SMARTiView protein in SMART
SM00577 CPDc, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR02251 HIF-SF_euk, 1 hit
PROSITEiView protein in PROSITE
PS50969 FCP1, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q3TP92-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP
60 70 80 90 100
LSRNRLAQVK 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):28,391
Last modified:August 21, 2007 - v2
Checksum:i1AD25540018F50BA
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QPC9J3QPC9_MOUSE
CTD nuclear envelope phosphatase 1
Ctdnep1
89Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti213A → S in BAE37845 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK164602 mRNA Translation: BAE37845.1
AL596185 Genomic DNA No translation available.
BC018265 mRNA Translation: AAH18265.1
CCDSiCCDS24927.1
RefSeqiNP_080293.1, NM_026017.2
UniGeneiMm.41678

Genome annotation databases

EnsembliENSMUST00000108593; ENSMUSP00000104234; ENSMUSG00000018559
GeneIDi67181
KEGGimmu:67181
UCSCiuc007jtf.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK164602 mRNA Translation: BAE37845.1
AL596185 Genomic DNA No translation available.
BC018265 mRNA Translation: AAH18265.1
CCDSiCCDS24927.1
RefSeqiNP_080293.1, NM_026017.2
UniGeneiMm.41678

3D structure databases

ProteinModelPortaliQ3TP92
SMRiQ3TP92
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211999, 1 interactor
STRINGi10090.ENSMUSP00000104234

PTM databases

iPTMnetiQ3TP92
PhosphoSitePlusiQ3TP92

Proteomic databases

EPDiQ3TP92
MaxQBiQ3TP92
PaxDbiQ3TP92
PeptideAtlasiQ3TP92
PRIDEiQ3TP92

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108593; ENSMUSP00000104234; ENSMUSG00000018559
GeneIDi67181
KEGGimmu:67181
UCSCiuc007jtf.1 mouse

Organism-specific databases

CTDi23399
MGIiMGI:1914431 Ctdnep1

Phylogenomic databases

eggNOGiKOG1605 Eukaryota
COG5190 LUCA
GeneTreeiENSGT00390000017194
HOVERGENiHBG098153
InParanoidiQ3TP92
KOiK17617
OMAiSRIWGFI
OrthoDBiEOG091G0GIO
PhylomeDBiQ3TP92
TreeFamiTF313962

Enzyme and pathway databases

ReactomeiR-MMU-4419969 Depolymerisation of the Nuclear Lamina

Miscellaneous databases

PROiPR:Q3TP92
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018559 Expressed in 273 organ(s), highest expression level in skeletal muscle tissue
CleanExiMM_DULLARD
ExpressionAtlasiQ3TP92 baseline and differential
GenevisibleiQ3TP92 MM

Family and domain databases

Gene3Di3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR011948 Dullard_phosphatase
IPR004274 FCP1_dom
IPR036412 HAD-like_sf
IPR023214 HAD_sf
PfamiView protein in Pfam
PF03031 NIF, 1 hit
SMARTiView protein in SMART
SM00577 CPDc, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR02251 HIF-SF_euk, 1 hit
PROSITEiView protein in PROSITE
PS50969 FCP1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCNEP1_MOUSE
AccessioniPrimary (citable) accession number: Q3TP92
Secondary accession number(s): Q5NCW4, Q8VEL4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: September 12, 2018
This is version 98 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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