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)

Q9Y5B0

- CTDP1_HUMAN

UniProt

Q9Y5B0 - CTDP1_HUMAN

Protein

RNA polymerase II subunit A C-terminal domain phosphatase

Gene

CTDP1

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 138 (01 Oct 2014)
      Sequence version 3 (05 Apr 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. CTD phosphatase activity Source: UniProtKB
    2. DNA-directed RNA polymerase activity Source: ProtInc

    GO - Biological processi

    1. exit from mitosis Source: UniProtKB
    2. gene expression Source: Reactome
    3. positive regulation of viral transcription Source: Reactome
    4. protein dephosphorylation Source: UniProtKB
    5. transcription elongation from RNA polymerase II promoter Source: Reactome
    6. transcription from RNA polymerase II promoter Source: Reactome
    7. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_846. Formation of the Early Elongation Complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II subunit A C-terminal domain phosphatase (EC:3.1.3.16)
    Alternative name(s):
    TFIIF-associating CTD phosphatase
    Gene namesi
    Name:CTDP1
    Synonyms:FCP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:2498. CTDP1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication. Midbody 1 Publication
    Note: Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in anaphase and telophase-G1 respectively.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: UniProtKB-KW
    4. midbody Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA
    7. spindle Source: UniProtKB
    8. spindle midzone Source: UniProtKB
    9. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Congenital cataracts, facial dysmorphism, and neuropathy (CCFDN) [MIM:604168]: An autosomal recessive developmental disorder characterized by a complex clinical phenotype with seemingly unrelated features involving multiple organs and systems. Developmental abnormalities include congenital cataracts and microcorneae, hypomyelination of the peripheral nervous system, impaired physical growth, delayed early motor and intellectual development, facial dysmorphism and hypogonadism. Central nervous system involvement, with cerebral and spinal cord atrophy, may be the result of disrupted development with superimposed degenerative changes. Affected individuals are prone to severe rhabdomyolysis after viral infections and to serious complications related to general anesthesia (such as pulmonary edema and epileptic seizures).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Cataract

    Organism-specific databases

    MIMi604168. phenotype.
    Orphaneti48431. Congenital cataracts - facial dysmorphism - neuropathy.
    PharmGKBiPA27001.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 961961RNA polymerase II subunit A C-terminal domain phosphatasePRO_0000212564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei674 – 6741Phosphoserine2 Publications
    Modified residuei740 – 7401PhosphoserineBy similarity
    Modified residuei780 – 7801N6-acetyllysine1 Publication
    Modified residuei869 – 8691Phosphoserine3 Publications
    Modified residuei872 – 8721Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated. In the presence of TFIIF, the phosphorylated form has an increased CTD phosphatase activity. The phosphorylation is required for the physical interaction with GTF2F1.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y5B0.
    PaxDbiQ9Y5B0.
    PRIDEiQ9Y5B0.

    PTM databases

    PhosphoSiteiQ9Y5B0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y5B0.
    BgeeiQ9Y5B0.
    CleanExiHS_CTDP1.
    GenevestigatoriQ9Y5B0.

    Organism-specific databases

    HPAiCAB032641.
    HPA040394.
    HPA044201.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with GTF2F1. Interacts with WDR77, SNRPB and SNRNP70.3 Publications

    Protein-protein interaction databases

    BioGridi114597. 45 interactions.
    DIPiDIP-41788N.
    IntActiQ9Y5B0. 2 interactions.
    MINTiMINT-275991.
    STRINGi9606.ENSP00000299543.

    Structurei

    Secondary structure

    1
    961
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi586 – 59813
    Helixi945 – 95612
    Turni957 – 9593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J2XX-ray2.00B944-961[»]
    1ONVNMR-B879-961[»]
    2K7LNMR-B582-600[»]
    DisProtiDP00177.
    ProteinModelPortaliQ9Y5B0.
    SMRiQ9Y5B0. Positions 168-344, 585-728.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5B0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 344167FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini629 – 728100BRCTPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi455 – 47824Ser-richAdd
    BLAST
    Compositional biasi577 – 5826Poly-Glu

    Sequence similaritiesi

    Contains 1 BRCT domain.PROSITE-ProRule annotation
    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5190.
    HOGENOMiHOG000112039.
    HOVERGENiHBG051213.
    InParanoidiQ9Y5B0.
    KOiK15732.
    OMAiEAPDIRK.
    OrthoDBiEOG7WMCJ8.
    PhylomeDBiQ9Y5B0.
    TreeFamiTF315104.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR015388. FCP1_C.
    IPR011947. FCP1_euk.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view]
    PfamiPF09309. FCP1_C. 1 hit.
    PF03031. NIF. 1 hit.
    PF12738. PTCB-BRCT. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    SM00577. CPDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS50969. FCP1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y5B0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA    50
    VFEAAASAQS SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ 100
    VVAPGAVLVR LEGCSHPVVM KGLCAECGQD LTQLQSKNGK QQVPLSTATV 150
    SMVHSVPELM VSSEQAEQLG REDQQRLHRN RKLVLMVDLD QTLIHTTEQH 200
    CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY ELHVFTFGSR 250
    LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 300
    IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT 350
    EVSEPSPPVR DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK 400
    PDERDIWPPA QAPTSSQELA GAPEPQGSCA QGGRVAPGQR PAQGATGTDL 450
    DFDLSSDSES SSESEGTKSS SSASDGESEG KRGRQKPKAA PEGAGALAQG 500
    SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG LCGLGNGCAD 550
    RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV 600
    HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP 650
    IEKTREHYHA TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC 700
    GHLHVVNPDW LWSCLERWDK VEEQLFPLRD DHTKAQRENS PAAFPDREGV 750
    PPTALFHPMP VLPKAQPGPE VRIYDSNTGK LIRTGARGPP APSSSLPIRQ 800
    EPSSFRAVPP PQPQMFGEEL PDAQDGEQPG PSRRKRQPSM SETMPLYTLC 850
    KEDLESMDKE VDDILGEGSD DSDSEKRRPE EQEEEPQPRK PGTRRERTLG 900
    APASSERSAA GGRGPRGHKR KLNEEDAASE SSRESSNEDE GSSSEADEMA 950
    KALEAELNDL M 961
    Length:961
    Mass (Da):104,399
    Last modified:April 5, 2011 - v3
    Checksum:i62B88FFD9CE4B157
    GO
    Isoform 4 (identifier: Q9Y5B0-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         807-961: AVPPPQPQMF...ALEAELNDLM → WTTSLEKAAT...AGGPEATRGS

    Show »
    Length:867
    Mass (Da):93,485
    Checksum:i8B4B87B24644BA6E
    GO

    Sequence cautioni

    The sequence AAC64549.1 differs from that shown. Reason: Cloning artifact.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611S → A in AAD42088. (PubMed:10385623)Curated
    Sequence conflicti61 – 611S → A in AAH63447. (PubMed:15489334)Curated
    Sequence conflicti157 – 1571P → A in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti281 – 2811F → I in AAH52576. (PubMed:15489334)Curated
    Sequence conflicti305 – 3051E → K in AAD42088. (PubMed:10385623)Curated
    Sequence conflicti390 – 3901A → P in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti478 – 4781S → T in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti486 – 4872KP → NA in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti504 – 5052EP → DA in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti513 – 5131L → V in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti656 – 6572EH → DD in AAC64549. (PubMed:9765293)Curated
    Sequence conflicti896 – 9005ERTLG → GADAR in AAD42088. (PubMed:10385623)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti282 – 2821S → F.
    Corresponds to variant rs4799078 [ dbSNP | Ensembl ].
    VAR_060440
    Natural varianti340 – 3401T → M.
    Corresponds to variant rs2279103 [ dbSNP | Ensembl ].
    VAR_018264
    Natural varianti519 – 5191P → H.
    Corresponds to variant rs557503 [ dbSNP | Ensembl ].
    VAR_060441
    Natural varianti755 – 7551L → S.
    Corresponds to variant rs34967023 [ dbSNP | Ensembl ].
    VAR_032763

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei807 – 961155AVPPP…LNDLM → WTTSLEKAATTATARRGGLR SRRRSPSPGSQGPAGSGRSG HLRPARGARQGAGGPEATRG S in isoform 4. 2 PublicationsVSP_009865Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154115 mRNA. Translation: AAD42088.1.
    AC021594 Genomic DNA. No translation available.
    AC068473 Genomic DNA. No translation available.
    CH471117 Genomic DNA. Translation: EAW66631.1.
    BC015010 mRNA. Translation: AAH15010.1.
    BC052576 mRNA. Translation: AAH52576.1.
    BC063447 mRNA. Translation: AAH63447.1.
    AF081287 mRNA. Translation: AAC64549.1. Sequence problems.
    CCDSiCCDS12017.1. [Q9Y5B0-1]
    CCDS12018.1. [Q9Y5B0-4]
    RefSeqiNP_001189433.1. NM_001202504.1.
    NP_004706.3. NM_004715.4. [Q9Y5B0-1]
    NP_430255.2. NM_048368.3. [Q9Y5B0-4]
    UniGeneiHs.465490.
    Hs.734021.

    Genome annotation databases

    EnsembliENST00000075430; ENSP00000075430; ENSG00000060069. [Q9Y5B0-4]
    ENST00000299543; ENSP00000299543; ENSG00000060069. [Q9Y5B0-1]
    GeneIDi9150.
    KEGGihsa:9150.
    UCSCiuc002lnh.2. human. [Q9Y5B0-1]
    uc002lni.2. human. [Q9Y5B0-4]

    Polymorphism databases

    DMDMi327478586.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154115 mRNA. Translation: AAD42088.1 .
    AC021594 Genomic DNA. No translation available.
    AC068473 Genomic DNA. No translation available.
    CH471117 Genomic DNA. Translation: EAW66631.1 .
    BC015010 mRNA. Translation: AAH15010.1 .
    BC052576 mRNA. Translation: AAH52576.1 .
    BC063447 mRNA. Translation: AAH63447.1 .
    AF081287 mRNA. Translation: AAC64549.1 . Sequence problems.
    CCDSi CCDS12017.1. [Q9Y5B0-1 ]
    CCDS12018.1. [Q9Y5B0-4 ]
    RefSeqi NP_001189433.1. NM_001202504.1.
    NP_004706.3. NM_004715.4. [Q9Y5B0-1 ]
    NP_430255.2. NM_048368.3. [Q9Y5B0-4 ]
    UniGenei Hs.465490.
    Hs.734021.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J2X X-ray 2.00 B 944-961 [» ]
    1ONV NMR - B 879-961 [» ]
    2K7L NMR - B 582-600 [» ]
    DisProti DP00177.
    ProteinModelPortali Q9Y5B0.
    SMRi Q9Y5B0. Positions 168-344, 585-728.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114597. 45 interactions.
    DIPi DIP-41788N.
    IntActi Q9Y5B0. 2 interactions.
    MINTi MINT-275991.
    STRINGi 9606.ENSP00000299543.

    PTM databases

    PhosphoSitei Q9Y5B0.

    Polymorphism databases

    DMDMi 327478586.

    Proteomic databases

    MaxQBi Q9Y5B0.
    PaxDbi Q9Y5B0.
    PRIDEi Q9Y5B0.

    Protocols and materials databases

    DNASUi 9150.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000075430 ; ENSP00000075430 ; ENSG00000060069 . [Q9Y5B0-4 ]
    ENST00000299543 ; ENSP00000299543 ; ENSG00000060069 . [Q9Y5B0-1 ]
    GeneIDi 9150.
    KEGGi hsa:9150.
    UCSCi uc002lnh.2. human. [Q9Y5B0-1 ]
    uc002lni.2. human. [Q9Y5B0-4 ]

    Organism-specific databases

    CTDi 9150.
    GeneCardsi GC18P077494.
    GeneReviewsi CTDP1.
    HGNCi HGNC:2498. CTDP1.
    HPAi CAB032641.
    HPA040394.
    HPA044201.
    MIMi 604168. phenotype.
    604927. gene.
    neXtProti NX_Q9Y5B0.
    Orphaneti 48431. Congenital cataracts - facial dysmorphism - neuropathy.
    PharmGKBi PA27001.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5190.
    HOGENOMi HOG000112039.
    HOVERGENi HBG051213.
    InParanoidi Q9Y5B0.
    KOi K15732.
    OMAi EAPDIRK.
    OrthoDBi EOG7WMCJ8.
    PhylomeDBi Q9Y5B0.
    TreeFami TF315104.

    Enzyme and pathway databases

    Reactomei REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_846. Formation of the Early Elongation Complex.

    Miscellaneous databases

    ChiTaRSi CTDP1. human.
    EvolutionaryTracei Q9Y5B0.
    GeneWikii CTDP1.
    GenomeRNAii 9150.
    NextBioi 34327.
    PROi Q9Y5B0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5B0.
    Bgeei Q9Y5B0.
    CleanExi HS_CTDP1.
    Genevestigatori Q9Y5B0.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR015388. FCP1_C.
    IPR011947. FCP1_euk.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view ]
    Pfami PF09309. FCP1_C. 1 hit.
    PF03031. NIF. 1 hit.
    PF12738. PTCB-BRCT. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    SM00577. CPDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02250. FCP1_euk. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS50969. FCP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A protein phosphatase functions to recycle RNA polymerase II."
      Cho H., Kim T.-K., Mancebo H., Lane W.S., Flores O., Reinberg D.
      Genes Dev. 13:1540-1552(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cervix carcinoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-961 (ISOFORM 1).
      Tissue: Colon, Lymph and Ovary.
    5. "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO."
      Archambault J., Pan G., Dahmus G.K., Cartier M., Marshall N., Zhang S., Dahmus M.E., Greenblatt J.
      J. Biol. Chem. 273:27593-27601(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-961 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 106-961 (ISOFORM 4), TISSUE SPECIFICITY, INTERACTION WITH GTF2F1.
      Tissue: Placenta.
    6. "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP."
      Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L., Majello B.
      Nucleic Acids Res. 31:999-1005(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WDR77; SNRPB AND SNRNP70.
    7. "The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation."
      Friedl E.M., Lane W.S., Erdjument-Bromage H., Tempst P., Reinberg D.
      Proc. Natl. Acad. Sci. U.S.A. 100:2328-2333(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-869 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
      Visconti R., Palazzo L., Della Monica R., Grieco D.
      Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF."
      Kamada K., Roeder R.G., Burley S.K.
      Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 944-961 IN COMPLEX WITH GTF2F1.
    17. Cited for: INVOLVEMENT IN CCFDN.

    Entry informationi

    Entry nameiCTDP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5B0
    Secondary accession number(s): A8MY97
    , Q7Z644, Q96BZ1, Q9Y6F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 5, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 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 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3