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O95476 (CNEP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CTD nuclear envelope phosphatase 1

EC=3.1.3.16
Alternative name(s):
Serine/threonine-protein phosphatase dullard
Gene names
Name:CTDNEP1
Synonyms:DULLARD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.9

Catalytic activity

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

Subunit structure

Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and LPIN2. Ref.9

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein Ref.2 Ref.7 Ref.9.

Tissue specificity

Muscle specific with lower expression in other metabolic tissues. Ref.9

Sequence similarities

Belongs to the dullard family.

Contains 1 FCP1 homology domain.

Biophysicochemical properties

Kinetic parameters:

KM=18 mM for p-nitrophenylphosphate Ref.7

pH dependence:

Optimum pH is 5.5.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CNEP1R1Q8N9A84EBI-5323433,EBI-5323455

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244CTD nuclear envelope phosphatase 1
PRO_0000297967

Regions

Transmembrane7 – 2923Helical; Potential
Domain57 – 224168FCP1 homology

Natural variations

Natural variant121T → A. Ref.1 Ref.2
Corresponds to variant rs3744399 [ dbSNP | Ensembl ].
VAR_034699

Experimental info

Mutagenesis671D → N or E: Abolishes phosphatase activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
O95476 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: 062952A90F74575A

FASTA24428,377
        10         20         30         40         50         60 
MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP VSRNRLAQVK 

        70         80         90        100        110        120 
RKILVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV 

       130        140        150        160        170        180 
VSQWYELVVF TASMEIYGSA VADKLDNSRS ILKRRYYRQH CTLELGSYIK DLSVVHSDLS 

       190        200        210        220        230        240 
SIVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ 


HRLW 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11093.1.
RefSeqNP_001137247.1. NM_001143775.1.
NP_056158.2. NM_015343.4.
UniGeneHs.513913.

3D structure databases

ProteinModelPortalO95476.
SMRO95476. Positions 57-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116972. 3 interactions.
IntActO95476. 2 interactions.
STRING9606.ENSP00000321732.

PTM databases

PhosphoSiteO95476.

Proteomic databases

MaxQBO95476.
PaxDbO95476.
PRIDEO95476.

Protocols and materials databases

DNASU23399.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318988; ENSP00000321732; ENSG00000175826.
ENST00000573600; ENSP00000461749; ENSG00000175826.
ENST00000574205; ENSP00000458758; ENSG00000175826.
ENST00000574322; ENSP00000460683; ENSG00000175826.
GeneID23399.
KEGGhsa:23399.
UCSCuc002gfd.2. human.

Organism-specific databases

CTD23399.
GeneCardsGC17M007147.
HGNCHGNC:19085. CTDNEP1.
HPAHPA037439.
MIM610684. gene.
neXtProtNX_O95476.
PharmGKBPA134937999.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5190.
HOGENOMHOG000236379.
HOVERGENHBG098153.
InParanoidO95476.
KOK17617.
OMALLGIRTF.
PhylomeDBO95476.
TreeFamTF313962.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SABIO-RKO95476.
SignaLinkO95476.

Gene expression databases

ArrayExpressO95476.
BgeeO95476.
CleanExHS_DULLARD.
GenevestigatorO95476.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR011948. Dullard_phosphatase.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02251. HIF-SF_euk. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTDNEP1. human.
GenomeRNAi23399.
NextBio45549.
PROO95476.
SOURCESearch...

Entry information

Entry nameCNEP1_HUMAN
AccessionPrimary (citable) accession number: O95476
Secondary accession number(s): D3DTN7, Q96GQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: November 3, 2009
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM