Reviewed, UniProtKB/Swiss-Prot Q8BX07 (CTDS2_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 270	270	Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2		PRO_0000212575
Regions
	Domain	96 – 254	159	FCP1 homology
Sites
	Active site	106	1	4-aspartylphosphate intermediate By similarity
	Active site	108	1	Proton donor By similarity
	Metal binding	106	1	Magnesium By similarity
	Metal binding	108	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	217	1	Magnesium By similarity
	Site	162	1	Transition state stabilizer By similarity
	Site	200	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BX07-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 0098B97E0AEC1B1D	FASTA	270	30,546
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [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: 15681389] [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.
IPI	IPI00226378.
RefSeq	NP_001106941.1. NP_666124.1.
UniGene	Mm.29490
3D structure databases
SMR	Q8BX07. Positions 89-269.
ModBase	Search...
Proteomic databases
PRIDE	Q8BX07.
Genome annotation databases
GeneID	52468.
KEGG	mmu:52468.
UCSC	uc007hhj.1. mouse.
Organism-specific databases
CTD	52468.
MGI	MGI:1098748. Ctdsp2.
Phylogenomic databases
HOVERGEN	Q8BX07.
Enzyme and pathway databases
BRENDA	3.1.3.16. 244.
Gene expression databases
Genevestigator	Q8BX07.
Family and domain databases
InterPro	IPR011948. Dullard. IPR004274. NIF. [Graphical view]
Pfam	PF03031. NIF. 1 hit. [Graphical view]
SMART	SM00577. CPDc. 1 hit. [Graphical view]
TIGRFAMs	TIGR02251. HIF-SF_euk. 1 hit.
PROSITE	PS50969. FCP1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	309001.
SOURCE	Search...

Entry information

Entry name

CTDS2_MOUSE

Accession

Primary (citable) accession number: Q8BX07

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)