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Q8BX07 (CTDS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
EC=3.1.3.16
Alternative name(s):
Small C-terminal domain phosphatase 2
Small CTD phosphatase 2
Short name=SCP2
Gene names
Name:Ctdsp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells By similarity.

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 magnesium ion per monomer By similarity.

Subunit structure

Monomer By similarity. Interacts with REST By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expression is restricted to non-neuronal tissues. Ref.3

Sequence similarities

Contains 1 FCP1 homology domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein dephosphorylation

Inferred from electronic annotation. Source: Compara

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionCTD phosphatase activity

Inferred from electronic annotation. Source: Compara

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
PRO_0000212575

Regions

Domain96 – 254159FCP1 homology

Sites

Active site10614-aspartylphosphate intermediate By similarity
Active site1081Proton donor By similarity
Metal binding1061Magnesium By similarity
Metal binding1081Magnesium; via carbonyl oxygen By similarity
Metal binding2171Magnesium By similarity
Site1621Transition state stabilizer By similarity
Site2001Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BX07 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0098B97E0AEC1B1D

FASTA27030,546
        10         20         30         40         50         60 
MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRSIFKA LLCCFHTQHV VQSSSSTELT 

        70         80         90        100        110        120 
HKEEANTIAK SDLLQCLQYQ FYQIPGTCLL PEVTEQDQGR ICVVIDLDET LVHSSFKPIN 

       130        140        150        160        170        180 
NADFIVPVEI EGTTHQVYVL KRPYVDEFLR RMGELFECVL FTASLAKYAD PVTDLLDRCG 

       190        200        210        220        230        240 
VFRARLFREA CVFHQGCYVK DLSRLGRDLR KTVILDNSPA SYIFHPENAV PVQSWFDDMA 

       250        260        270 
DTELLNLIPV FEELSGTDDV YTSLGQLRAP

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
[2]"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: C57BL/6.
Tissue: Brain.
[3]"Small CTD phosphatases function in silencing neuronal gene expression."
Yeo M., Lee S.-K., Lee B., Ruiz E.C., Pfaff S.L., Gill G.N.
Science 307:596-600(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK049271 mRNA. Translation: BAC33649.1.
BC085142 mRNA. Translation: AAH85142.1.
IPIIPI00226378.
RefSeqNP_001106941.1. NM_001113470.1.
NP_666124.1. NM_146012.2.
UniGeneMm.29490.

3D structure databases

ProteinModelPortalQ8BX07.
SMRQ8BX07. Positions 89-269.
ModBaseSearch...

PTM databases

PhosphoSiteQ8BX07.

Proteomic databases

PRIDEQ8BX07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000105256; ENSMUSP00000100891; ENSMUSG00000078429.
GeneID52468.
KEGGmmu:52468.
UCSCuc007hhj.2. mouse.

Organism-specific databases

CTD10106.
MGIMGI:1098748. Ctdsp2.

Phylogenomic databases

eggNOGCOG5190.
GeneTreeENSGT00390000017194.
HOVERGENHBG053298.
KOK15731.
OMAVGQSSSC.

Gene expression databases

ArrayExpressQ8BX07.
BgeeQ8BX07.
GenevestigatorQ8BX07.

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. HAD-like_dom. 1 hit.
TIGRFAMsTIGR02251. HIF-SF_euk. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio309001.
SOURCESearch...

Entry information

Entry nameCTDS2_MOUSE
AccessionPrimary (citable) accession number: Q8BX07
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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