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O14595 (CTDS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARP102753EBI-2802973,EBI-608057

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
PRO_0000212574

Regions

Domain97 – 255159FCP1 homology

Sites

Active site10714-aspartylphosphate intermediate By similarity
Active site1091Proton donor By similarity
Metal binding1071Magnesium
Metal binding1091Magnesium; via carbonyl oxygen
Metal binding2181Magnesium
Site1631Transition state stabilizer By similarity
Site2011Transition state stabilizer By similarity

Experimental info

Sequence conflict91Q → H in AAD09331. Ref.3

Secondary structure

....................................... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14595 [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: E4FA4A1657F2B03F

FASTA27130,664
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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 (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. expand/collapse author list , 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.
CCDSCCDS41801.1.
RefSeqNP_005721.3. NM_005730.3.
UniGeneHs.524530.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q5EX-ray2.51A/B/C/D/E/F/G/H87-271[»]
ProteinModelPortalO14595.
SMRO14595. Positions 90-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115412. 3 interactions.
IntActO14595. 5 interactions.
MINTMINT-2735588.
STRING9606.ENSP00000381148.

PTM databases

PhosphoSiteO14595.

Proteomic databases

MaxQBO14595.
PaxDbO14595.
PRIDEO14595.

Protocols and materials databases

DNASU10106.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398073; ENSP00000381148; ENSG00000175215.
GeneID10106.
KEGGhsa:10106.
UCSCuc001sqm.3. human.

Organism-specific databases

CTD10106.
GeneCardsGC12M058213.
HGNCHGNC:17077. CTDSP2.
HPAHPA052607.
MIM608711. gene.
neXtProtNX_O14595.
PharmGKBPA128394568.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5190.
HOGENOMHOG000236379.
HOVERGENHBG053298.
KOK15731.
OMAPRGRSIF.
OrthoDBEOG71P2C3.
PhylomeDBO14595.
TreeFamTF313556.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkO14595.

Gene expression databases

ArrayExpressO14595.
BgeeO14595.
CleanExHS_CTDSP2.
HS_SCP2.
GenevestigatorO14595.

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

ChiTaRSCTDSP2. human.
EvolutionaryTraceO14595.
GeneWikiCTDSP2.
GenomeRNAi10106.
NextBio38225.
PROO14595.
SOURCESearch...

Entry information

Entry nameCTDS2_HUMAN
AccessionPrimary (citable) accession number: O14595
Secondary accession number(s): A8K5H4 expand/collapse secondary AC list , Q53ZR2, Q6NZY3, Q9UEX1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: November 9, 2004
Last modified: July 9, 2014
This is version 116 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM