O14595 (CTDS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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):
Nuclear LIM interactor-interacting factor 2
Short name=NLI-interacting factor 2
Protein OS-4
Small C-terminal domain phosphatase 2
Small CTD phosphatase 2
Short name=SCP2

Gene names

Name:	CTDSP2
Synonyms:	NIF2, OS4, SCP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. May contribute to the development of sarcomas. Ref.2 Ref.7
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 magnesium ion per monomer.
Subunit structure	Monomer By similarity. Interacts with REST. Ref.7
Subcellular location	Nucleus By similarity.
Tissue specificity	Expression is restricted to non-neuronal tissues. Highest expression in pancreas and lowest in liver. Ref.7
Induction	In primary sarcomas.
Sequence similarities	Contains 1 FCP1 homology domain.
Sequence caution	The sequence AAB71816.1 differs from that shown. Reason: Frameshift at position 267. The sequence AAP34399.1 differs from that shown. Reason: Frameshift at position 267.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome protein dephosphorylation Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	CTD phosphatase activity Inferred from direct assay Ref.2. Source: UniProtKB metal ion binding 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 – 271

271

Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2

PRO_0000212574

Regions

Domain

97 – 255

159

FCP1 homology

Sites

Active site

107

1

4-aspartylphosphate intermediate By similarity

Active site

109

1

Proton donor By similarity

Metal binding

107

1

Magnesium

Metal binding

109

1

Magnesium; via carbonyl oxygen

Metal binding

218

1

Magnesium

Site

163

1

Transition state stabilizer By similarity

Site

201

1

Transition state stabilizer By similarity

Experimental info

Sequence conflict

9

1

Q → H in AAD09331. Ref.3

Secondary structure

1

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271

Helix Strand Turn

Details...

Turn

96 – 100

5

Beta strand

103 – 106

4

Turn

110 – 112

3

Beta strand

113 – 118

6

Beta strand

124 – 131

8

Beta strand

134 – 142

9

Helix

146 – 156

11

Beta strand

157 – 162

6

Helix

167 – 177

11

Beta strand

183 – 187

5

Helix

189 – 191

3

Beta strand

192 – 195

4

Beta strand

198 – 200

3

Helix

203 – 205

3

Beta strand

206 – 208

3

Helix

210 – 212

3

Beta strand

213 – 218

6

Helix

220 – 223

4

Helix

227 – 229

3

Beta strand

230 – 232

3

Helix

244 – 255

12

Helix

261 – 268

8

Sequences

	Sequence		Length	Mass (Da)
	O14595 [UniParc]. Last modified November 9, 2004. Version 2. Checksum: E4FA4A1657F2B03F	FASTA	271	30,664
	10 20 30 40 50 60 MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRNIFKA LFCCFRAQHV GQSSSSTELA 70 80 90 100 110 120 AYKEEANTIA KSDLLQCLQY QFYQIPGTCL LPEVTEEDQG RICVVIDLDE TLVHSSFKPI 130 140 150 160 170 180 NNADFIVPIE IEGTTHQVYV LKRPYVDEFL RRMGELFECV LFTASLAKYA DPVTDLLDRC 190 200 210 220 230 240 GVFRARLFRE SCVFHQGCYV KDLSRLGRDL RKTLILDNSP ASYIFHPENA VPVQSWFDDM 250 260 270 ADTELLNLIP IFEELSGAED VYTSLGQLRA P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a highly conserved gene (OS4) amplified with CDK4 in human sarcomas." Su Y.A., Lee M.M., Hutter C.M., Meltzer P.S. Oncogene 15:1289-1294(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5." Yeo M., Lin P.S., Dahmus M.E., Gill G.N. J. Biol. Chem. 278:26078-26085(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[3]	Morikane K., Hollingsworth M.A. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal pancreas.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Leukocyte.
[7]	"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: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH REST.
[8]	"Structural genomics of protein phosphatases." Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K. J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 87-271 IN COMPLEX WITH MAGNESIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF000152 mRNA. Translation: AAB71816.1. Frameshift.
AY279531 mRNA. Translation: AAP34399.1. Frameshift.
AF022231 mRNA. Translation: AAD09331.1.
AK291289 mRNA. Translation: BAF83978.1.
CH471054 Genomic DNA. Translation: EAW97083.1.
BC065920 mRNA. Translation: AAH65920.1.

IPI

IPI00873134.

RefSeq

NP_005721.3. NM_005730.3.

UniGene

Hs.524530.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Q5E	X-ray	2.51	A/B/C/D/E/F/G/H	87-271	[»]

ProteinModelPortal

O14595.

ModBase

Search...

Protein-protein interaction databases

IntAct

O14595. 4 interactions.

MINT

MINT-2735588.

STRING

9606.ENSP00000381148.

PTM databases

PhosphoSite

O14595.

Proteomic databases

PaxDb

O14595.

PRIDE

O14595.

Protocols and materials databases

DNASU

10106.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398073; ENSP00000381148; ENSG00000175215.

GeneID

10106.

KEGG

hsa:10106.

UCSC

uc001sqm.3. human.

Organism-specific databases

CTD

10106.

GeneCards

GC12M058213.

HGNC

HGNC:17077. CTDSP2.

HPA

HPA052607.

MIM

608711. gene.

neXtProt

NX_O14595.

PharmGKB

PA128394568.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5190.

HOGENOM

HOG000236379.

HOVERGEN

HBG053298.

KO

K15731.

OMA

VGQSSSC.

OrthoDB

EOG4MSCZS.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.
ar_pathway. Coregulation of Androgen receptor activity.
smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.

Reactome

REACT_116125. Disease.

SignaLink

O14595.

Gene expression databases

ArrayExpress

O14595.

Bgee

O14595.

CleanEx

HS_CTDSP2.
HS_SCP2.

Genevestigator

O14595.

GermOnline

ENSG00000175215. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 1 hit.

InterPro

IPR011948. Dullard_phosphatase.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]

Pfam

PF03031. NIF. 1 hit.
[Graphical view]

SMART

SM00577. CPDc. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR02251. HIF-SF_euk. 1 hit.

PROSITE

PS50969. FCP1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CTDSP2. human.

EvolutionaryTrace

O14595.

GenomeRNAi

10106.

NextBio

38225.

SOURCE

Search...

Entry information

Entry name

CTDS2_HUMAN

Accession

Primary (citable) accession number: O14595
Secondary accession number(s): A8K5H4 , Q53ZR2, Q6NZY3, Q9UEX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	November 9, 2004
Last modified:	May 29, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.