Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O14595

- CTDS2_HUMAN

UniProt

O14595 - CTDS2_HUMAN

Protein

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

Gene

CTDSP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (09 Nov 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 intermediateBy similarity
    Metal bindingi107 – 1071Magnesium1 Publication
    Active sitei109 – 1091Proton donorBy similarity
    Metal bindingi109 – 1091Magnesium; via carbonyl oxygen1 Publication
    Sitei163 – 1631Transition state stabilizerBy similarity
    Sitei201 – 2011Transition state stabilizerBy similarity
    Metal bindingi218 – 2181Magnesium1 Publication

    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

    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

    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 2PRO_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.By similarity2 Publications

    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

    1
    271
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14595.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 255159FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

    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.

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 118 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