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Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2 (EC 3.1.3.16) (Nuclear LIM interactor-interacting factor 2) (NLI-interacting factor 2) (Protein OS-4) (Small C-terminal domain phosphatase 2) (Small CTD phosphatase 2) (SCP2)

 CTDS2_HUMAN             Reviewed;         271 AA.
O14595; A8K5H4; Q53ZR2; Q6NZY3; Q9UEX1;
13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
09-NOV-2004, sequence version 2.
05-DEC-2018, entry version 154.
RecName: Full=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2;
EC=3.1.3.16;
AltName: Full=Nuclear LIM interactor-interacting factor 2;
Short=NLI-interacting factor 2;
AltName: Full=Protein OS-4;
AltName: Full=Small C-terminal domain phosphatase 2;
AltName: Full=Small CTD phosphatase 2;
Short=SCP2;
Name=CTDSP2; Synonyms=NIF2, OS4, SCP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9315096; DOI=10.1038/sj.onc.1201294;
Su Y.A., Lee M.M., Hutter C.M., Meltzer P.S.;
"Characterization of a highly conserved gene (OS4) amplified with CDK4
in human sarcomas.";
Oncogene 15:1289-1294(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=12721286; DOI=10.1074/jbc.M301791200;
Yeo M., Lin P.S., Dahmus M.E., Gill G.N.;
"A novel RNA polymerase II C-terminal domain phosphatase that
preferentially dephosphorylates serine 5.";
J. Biol. Chem. 278:26078-26085(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal pancreas;
Morikane K., Hollingsworth M.A.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukocyte;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH REST.
PubMed=15681389; DOI=10.1126/science.1100801;
Yeo M., Lee S.-K., Lee B., Ruiz E.C., Pfaff S.L., Gill G.N.;
"Small CTD phosphatases function in silencing neuronal gene
expression.";
Science 307:596-600(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 87-271 IN COMPLEX WITH
MAGNESIUM.
PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
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.;
"Structural genomics of protein phosphatases.";
J. Struct. Funct. Genomics 8:121-140(2007).
-!- 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.
{ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:15681389}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
EC=3.1.3.16;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per monomer.;
-!- SUBUNIT: Monomer (By similarity). Interacts with REST.
{ECO:0000250, ECO:0000269|PubMed:15681389,
ECO:0000269|PubMed:18058037}.
-!- INTERACTION:
P10275:AR; NbExp=3; IntAct=EBI-2802973, EBI-608057;
Q99618:CDCA3; NbExp=7; IntAct=EBI-2802973, EBI-739534;
Q15797:SMAD1; NbExp=2; IntAct=EBI-2802973, EBI-1567153;
P14079:tax (xeno); NbExp=3; IntAct=EBI-2802973, EBI-9675698;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expression is restricted to non-neuronal
tissues. Highest expression in pancreas and lowest in liver.
{ECO:0000269|PubMed:15681389}.
-!- INDUCTION: In primary sarcomas.
-!- SEQUENCE CAUTION:
Sequence=AAB71816.1; Type=Frameshift; Positions=267; Evidence={ECO:0000305};
Sequence=AAP34399.1; Type=Frameshift; Positions=267; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF000152; AAB71816.1; ALT_FRAME; mRNA.
EMBL; AY279531; AAP34399.1; ALT_FRAME; mRNA.
EMBL; AF022231; AAD09331.1; -; mRNA.
EMBL; AK291289; BAF83978.1; -; mRNA.
EMBL; CH471054; EAW97083.1; -; Genomic_DNA.
EMBL; BC065920; AAH65920.1; -; mRNA.
CCDS; CCDS41801.1; -.
RefSeq; NP_005721.3; NM_005730.3.
UniGene; Hs.524530; -.
PDB; 2Q5E; X-ray; 2.51 A; A/B/C/D/E/F/G/H=87-271.
PDBsum; 2Q5E; -.
ProteinModelPortal; O14595; -.
SMR; O14595; -.
BioGrid; 115412; 39.
DIP; DIP-61245N; -.
IntAct; O14595; 11.
MINT; O14595; -.
STRING; 9606.ENSP00000381148; -.
DEPOD; O14595; -.
iPTMnet; O14595; -.
PhosphoSitePlus; O14595; -.
SwissPalm; O14595; -.
BioMuta; CTDSP2; -.
MaxQB; O14595; -.
PaxDb; O14595; -.
PeptideAtlas; O14595; -.
PRIDE; O14595; -.
ProteomicsDB; 48104; -.
DNASU; 10106; -.
Ensembl; ENST00000398073; ENSP00000381148; ENSG00000175215.
GeneID; 10106; -.
KEGG; hsa:10106; -.
UCSC; uc001sqm.4; human.
CTD; 10106; -.
DisGeNET; 10106; -.
EuPathDB; HostDB:ENSG00000175215.9; -.
GeneCards; CTDSP2; -.
HGNC; HGNC:17077; CTDSP2.
HPA; HPA052607; -.
MIM; 608711; gene.
neXtProt; NX_O14595; -.
OpenTargets; ENSG00000175215; -.
PharmGKB; PA128394568; -.
eggNOG; KOG1605; Eukaryota.
eggNOG; COG5190; LUCA.
GeneTree; ENSGT00390000017194; -.
HOGENOM; HOG000236379; -.
HOVERGEN; HBG053298; -.
InParanoid; O14595; -.
KO; K15731; -.
OMA; ANTIAKX; -.
PhylomeDB; O14595; -.
TreeFam; TF313556; -.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
SignaLink; O14595; -.
SIGNOR; O14595; -.
ChiTaRS; CTDSP2; human.
EvolutionaryTrace; O14595; -.
GeneWiki; CTDSP2; -.
GenomeRNAi; 10106; -.
PRO; PR:O14595; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000175215; Expressed in 242 organ(s), highest expression level in urinary bladder.
CleanEx; HS_CTDSP2; -.
CleanEx; HS_SCP2; -.
ExpressionAtlas; O14595; baseline and differential.
Genevisible; O14595; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:UniProtKB.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR011948; Dullard_phosphatase.
InterPro; IPR004274; FCP1_dom.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
Pfam; PF03031; NIF; 1.
SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase_; 1.
SMART; SM00577; CPDc; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
PROSITE; PS50969; FCP1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Metal-binding; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome.
CHAIN 1 271 Carboxy-terminal domain RNA polymerase II
polypeptide A small phosphatase 2.
/FTId=PRO_0000212574.
DOMAIN 97 255 FCP1 homology. {ECO:0000255|PROSITE-
ProRule:PRU00336}.
ACT_SITE 107 107 4-aspartylphosphate intermediate.
{ECO:0000250}.
ACT_SITE 109 109 Proton donor. {ECO:0000250}.
METAL 107 107 Magnesium. {ECO:0000269|PubMed:18058037}.
METAL 109 109 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:18058037}.
METAL 218 218 Magnesium. {ECO:0000269|PubMed:18058037}.
SITE 163 163 Transition state stabilizer.
{ECO:0000250}.
SITE 201 201 Transition state stabilizer.
{ECO:0000250}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CONFLICT 9 9 Q -> H (in Ref. 3; AAD09331).
{ECO:0000305}.
TURN 96 100 {ECO:0000244|PDB:2Q5E}.
STRAND 103 106 {ECO:0000244|PDB:2Q5E}.
TURN 110 112 {ECO:0000244|PDB:2Q5E}.
STRAND 113 118 {ECO:0000244|PDB:2Q5E}.
STRAND 124 131 {ECO:0000244|PDB:2Q5E}.
STRAND 134 142 {ECO:0000244|PDB:2Q5E}.
HELIX 146 156 {ECO:0000244|PDB:2Q5E}.
STRAND 157 162 {ECO:0000244|PDB:2Q5E}.
HELIX 167 177 {ECO:0000244|PDB:2Q5E}.
STRAND 183 187 {ECO:0000244|PDB:2Q5E}.
HELIX 189 191 {ECO:0000244|PDB:2Q5E}.
STRAND 192 195 {ECO:0000244|PDB:2Q5E}.
STRAND 198 200 {ECO:0000244|PDB:2Q5E}.
HELIX 203 205 {ECO:0000244|PDB:2Q5E}.
STRAND 206 208 {ECO:0000244|PDB:2Q5E}.
HELIX 210 212 {ECO:0000244|PDB:2Q5E}.
STRAND 213 218 {ECO:0000244|PDB:2Q5E}.
HELIX 220 223 {ECO:0000244|PDB:2Q5E}.
HELIX 227 229 {ECO:0000244|PDB:2Q5E}.
STRAND 230 232 {ECO:0000244|PDB:2Q5E}.
HELIX 244 255 {ECO:0000244|PDB:2Q5E}.
HELIX 261 268 {ECO:0000244|PDB:2Q5E}.
SEQUENCE 271 AA; 30664 MW; E4FA4A1657F2B03F CRC64;
MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRNIFKA LFCCFRAQHV GQSSSSTELA
AYKEEANTIA KSDLLQCLQY QFYQIPGTCL LPEVTEEDQG RICVVIDLDE TLVHSSFKPI
NNADFIVPIE IEGTTHQVYV LKRPYVDEFL RRMGELFECV LFTASLAKYA DPVTDLLDRC
GVFRARLFRE SCVFHQGCYV KDLSRLGRDL RKTLILDNSP ASYIFHPENA VPVQSWFDDM
ADTELLNLIP IFEELSGAED VYTSLGQLRA P


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