Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q3TP92

- CNEP1_MOUSE

UniProt

Q3TP92 - CNEP1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

CTD nuclear envelope phosphatase 1

Gene

Ctdnep1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. gamete generation Source: MGI
  2. mesoderm development Source: MGI
  3. nuclear envelope organization Source: UniProtKB
  4. positive regulation of canonical Wnt signaling pathway Source: MGI
  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_208718. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1914431. 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
  7. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244CTD nuclear envelope phosphatase 1PRO_0000297968Add
BLAST

Proteomic databases

MaxQBiQ3TP92.
PaxDbiQ3TP92.
PRIDEiQ3TP92.

PTM databases

PhosphoSiteiQ3TP92.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ3TP92.
CleanExiMM_DULLARD.
ExpressionAtlasiQ3TP92. baseline and differential.
GenevestigatoriQ3TP92.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ3TP92.
SMRiQ3TP92. 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.
HOVERGENiHBG098153.
InParanoidiQ3TP92.
KOiK17617.
OMAiLLGIRTF.
OrthoDBiEOG7MKW6W.
PhylomeDBiQ3TP92.
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.

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131A → S in BAE37845. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK164602 mRNA. Translation: BAE37845.1.
AL596185 Genomic DNA. Translation: CAI35161.1.
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK164602 mRNA. Translation: BAE37845.1 .
AL596185 Genomic DNA. Translation: CAI35161.1 .
BC018265 mRNA. Translation: AAH18265.1 .
CCDSi CCDS24927.1.
RefSeqi NP_080293.1. NM_026017.2.
UniGenei Mm.41678.

3D structure databases

ProteinModelPortali Q3TP92.
SMRi Q3TP92. Positions 57-234.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q3TP92.

Proteomic databases

MaxQBi Q3TP92.
PaxDbi Q3TP92.
PRIDEi Q3TP92.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000108593 ; ENSMUSP00000104234 ; ENSMUSG00000018559 .
GeneIDi 67181.
KEGGi mmu:67181.
UCSCi uc007jtf.1. mouse.

Organism-specific databases

CTDi 23399.
MGIi MGI:1914431. Ctdnep1.

Phylogenomic databases

eggNOGi COG5190.
GeneTreei ENSGT00550000075053.
HOVERGENi HBG098153.
InParanoidi Q3TP92.
KOi K17617.
OMAi LLGIRTF.
OrthoDBi EOG7MKW6W.
PhylomeDBi Q3TP92.
TreeFami TF313962.

Enzyme and pathway databases

Reactomei REACT_208718. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

NextBioi 323816.
PROi Q3TP92.
SOURCEi Search...

Gene expression databases

Bgeei Q3TP92.
CleanExi MM_DULLARD.
ExpressionAtlasi Q3TP92. baseline and differential.
Genevestigatori Q3TP92.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "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.
  5. "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: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCNEP1_MOUSE
AccessioniPrimary (citable) accession number: Q3TP92
Secondary accession number(s): Q5NCW4, Q8VEL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: October 29, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3