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O14595

- CTDS2_HUMAN

UniProt

O14595 - CTDS2_HUMAN

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Protein
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
Gene
CTDSP2, NIF2, OS4, SCP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per monomer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei107 – 10714-aspartylphosphate intermediate By similarity
Metal bindingi107 – 1071Magnesium
Active sitei109 – 1091Proton donor By similarity
Metal bindingi109 – 1091Magnesium; via carbonyl oxygen
Sitei163 – 1631Transition state stabilizer By similarity
Sitei201 – 2011Transition state stabilizer By similarity
Metal bindingi218 – 2181Magnesium

GO - Molecular functioni

  1. CTD phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum unfolded protein response Source: Reactome
  4. protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
SignaLinkiO14595.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CTDSP2
Synonyms:NIF2, OS4, SCP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17077. CTDSP2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394568.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
PRO_0000212574Add
BLAST

Proteomic databases

MaxQBiO14595.
PaxDbiO14595.
PRIDEiO14595.

PTM databases

PhosphoSiteiO14595.

Expressioni

Tissue specificityi

Expression is restricted to non-neuronal tissues. Highest expression in pancreas and lowest in liver.1 Publication

Inductioni

In primary sarcomas.

Gene expression databases

ArrayExpressiO14595.
BgeeiO14595.
CleanExiHS_CTDSP2.
HS_SCP2.
GenevestigatoriO14595.

Organism-specific databases

HPAiHPA052607.

Interactioni

Subunit structurei

Monomer By similarity. Interacts with REST.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP102753EBI-2802973,EBI-608057

Protein-protein interaction databases

BioGridi115412. 3 interactions.
IntActiO14595. 5 interactions.
MINTiMINT-2735588.
STRINGi9606.ENSP00000381148.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni96 – 1005
Beta strandi103 – 1064
Turni110 – 1123
Beta strandi113 – 1186
Beta strandi124 – 1318
Beta strandi134 – 1429
Helixi146 – 15611
Beta strandi157 – 1626
Helixi167 – 17711
Beta strandi183 – 1875
Helixi189 – 1913
Beta strandi192 – 1954
Beta strandi198 – 2003
Helixi203 – 2053
Beta strandi206 – 2083
Helixi210 – 2123
Beta strandi213 – 2186
Helixi220 – 2234
Helixi227 – 2293
Beta strandi230 – 2323
Helixi244 – 25512
Helixi261 – 2688

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q5EX-ray2.51A/B/C/D/E/F/G/H87-271[»]
ProteinModelPortaliO14595.
SMRiO14595. Positions 90-270.

Miscellaneous databases

EvolutionaryTraceiO14595.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 255159FCP1 homology
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5190.
HOGENOMiHOG000236379.
HOVERGENiHBG053298.
KOiK15731.
OMAiPRGRSIF.
OrthoDBiEOG71P2C3.
PhylomeDBiO14595.
TreeFamiTF313556.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR011948. Dullard_phosphatase.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamiPF03031. NIF. 1 hit.
[Graphical view]
SMARTiSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02251. HIF-SF_euk. 1 hit.
PROSITEiPS50969. FCP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14595-1 [UniParc]FASTAAdd to Basket

« Hide

MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRNIFKA LFCCFRAQHV    50
GQSSSSTELA AYKEEANTIA KSDLLQCLQY QFYQIPGTCL LPEVTEEDQG 100
RICVVIDLDE TLVHSSFKPI NNADFIVPIE IEGTTHQVYV LKRPYVDEFL 150
RRMGELFECV LFTASLAKYA DPVTDLLDRC GVFRARLFRE SCVFHQGCYV 200
KDLSRLGRDL RKTLILDNSP ASYIFHPENA VPVQSWFDDM ADTELLNLIP 250
IFEELSGAED VYTSLGQLRA P 271
Length:271
Mass (Da):30,664
Last modified:November 9, 2004 - v2
Checksum:iE4FA4A1657F2B03F
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91Q → H in AAD09331. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41801.1.
RefSeqiNP_005721.3. NM_005730.3.
UniGeneiHs.524530.

Genome annotation databases

EnsembliENST00000398073; ENSP00000381148; ENSG00000175215.
GeneIDi10106.
KEGGihsa:10106.
UCSCiuc001sqm.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS41801.1.
RefSeqi NP_005721.3. NM_005730.3.
UniGenei Hs.524530.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q5E X-ray 2.51 A/B/C/D/E/F/G/H 87-271 [» ]
ProteinModelPortali O14595.
SMRi O14595. Positions 90-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115412. 3 interactions.
IntActi O14595. 5 interactions.
MINTi MINT-2735588.
STRINGi 9606.ENSP00000381148.

PTM databases

PhosphoSitei O14595.

Proteomic databases

MaxQBi O14595.
PaxDbi O14595.
PRIDEi O14595.

Protocols and materials databases

DNASUi 10106.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398073 ; ENSP00000381148 ; ENSG00000175215 .
GeneIDi 10106.
KEGGi hsa:10106.
UCSCi uc001sqm.3. human.

Organism-specific databases

CTDi 10106.
GeneCardsi GC12M058213.
HGNCi HGNC:17077. CTDSP2.
HPAi HPA052607.
MIMi 608711. gene.
neXtProti NX_O14595.
PharmGKBi PA128394568.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5190.
HOGENOMi HOG000236379.
HOVERGENi HBG053298.
KOi K15731.
OMAi PRGRSIF.
OrthoDBi EOG71P2C3.
PhylomeDBi O14595.
TreeFami TF313556.

Enzyme and pathway databases

Reactomei REACT_18273. XBP1(S) activates chaperone genes.
SignaLinki O14595.

Miscellaneous databases

ChiTaRSi CTDSP2. human.
EvolutionaryTracei O14595.
GeneWikii CTDSP2.
GenomeRNAii 10106.
NextBioi 38225.
PROi O14595.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14595.
Bgeei O14595.
CleanExi HS_CTDSP2.
HS_SCP2.
Genevestigatori O14595.

Family and domain databases

Gene3Di 3.40.50.1000. 1 hit.
InterProi IPR011948. Dullard_phosphatase.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view ]
Pfami PF03031. NIF. 1 hit.
[Graphical view ]
SMARTi SM00577. CPDc. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR02251. HIF-SF_euk. 1 hit.
PROSITEi PS50969. FCP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 87-271 IN COMPLEX WITH MAGNESIUM.

Entry informationi

Entry nameiCTDS2_HUMAN
AccessioniPrimary (citable) accession number: O14595
Secondary accession number(s): A8K5H4
, Q53ZR2, Q6NZY3, Q9UEX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: November 9, 2004
Last modified: September 3, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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