CTDP1 | ENSG00000060069 | NCBI 9150

Details for: CTDP1

Gene ID: 9150

Symbol: CTDP1

Ensembl ID: ENSG00000060069

Description: CTD phosphatase subunit 1

Associated with

Abortive elongation of hiv-1 transcript in the absence of tat
(R-HSA-167242)
Disease
(R-HSA-1643685)
Formation of hiv-1 elongation complex containing hiv-1 tat
(R-HSA-167200)
Formation of hiv elongation complex in the absence of hiv tat
(R-HSA-167152)
Formation of rna pol ii elongation complex
(R-HSA-112382)
Formation of the early elongation complex
(R-HSA-113418)
Formation of the hiv-1 early elongation complex
(R-HSA-167158)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hiv elongation arrest and recovery
(R-HSA-167287)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Hiv transcription elongation
(R-HSA-167169)
Infectious disease
(R-HSA-5663205)
Late phase of hiv life cycle
(R-HSA-162599)
Pausing and recovery of hiv elongation
(R-HSA-167290)
Pausing and recovery of tat-mediated hiv elongation
(R-HSA-167238)
Rna polymerase ii pre-transcription events
(R-HSA-674695)
Rna polymerase ii transcription
(R-HSA-73857)
Rna polymerase ii transcription elongation
(R-HSA-75955)
Tat-mediated elongation of the hiv-1 transcript
(R-HSA-167246)
Tat-mediated hiv elongation arrest and recovery
(R-HSA-167243)
Tp53 regulates transcription of dna repair genes
(R-HSA-6796648)
Transcriptional regulation by tp53
(R-HSA-3700989)
Transcription of the hiv genome
(R-HSA-167172)
Viral infection pathways
(R-HSA-9824446)
Cell division
(GO:0051301)
Centrosome
(GO:0005813)
Cytoplasm
(GO:0005737)
Exit from mitosis
(GO:0010458)
Intracellular membrane-bounded organelle
(GO:0043231)
Midbody
(GO:0030496)
Myosin phosphatase activity
(GO:0017018)
Negative regulation of cell growth involved in cardiac muscle cell development
(GO:0061052)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Phosphoprotein phosphatase activity
(GO:0004721)
Positive regulation by host of viral transcription
(GO:0043923)
Protein-containing complex
(GO:0032991)
Protein binding
(GO:0005515)
Protein dephosphorylation
(GO:0006470)
Regulation of transcription by rna polymerase ii
(GO:0006357)
Rna polymerase ii ctd heptapeptide repeat phosphatase activity
(GO:0008420)
Spindle
(GO:0005819)
Spindle midzone
(GO:0051233)
Spindle pole
(GO:0000922)
Tat protein binding
(GO:0030957)
Tfiif-class transcription factor complex binding
(GO:0001096)
Transcription elongation by rna polymerase ii
(GO:0006368)

Other Information

Proteins

RNA polymerase II subunit A C-terminal domain phosphatase

Genular Protein ID: 585086987

Symbol: CTDP1_HUMAN

Name: RNA polymerase II subunit A C-terminal domain phosphatase

UniProtKB Accession Codes:

Q9Y5B0 A8MY97 Q7Z644 Q96BZ1 Q9Y6F5

Database IDs:

Citations:

PubMed ID: 10385623

Title: A protein phosphatase functions to recycle RNA polymerase II.

PubMed ID: 10385623

DOI: 10.1101/gad.13.12.1540

PubMed ID: 16177791

Title: DNA sequence and analysis of human chromosome 18.

PubMed ID: 16177791

DOI: 10.1038/nature03983

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9765293

Title: FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO.

PubMed ID: 9765293

DOI: 10.1074/jbc.273.42.27593

PubMed ID: 12560496

Title: The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP.

PubMed ID: 12560496

DOI: 10.1093/nar/gkg197

PubMed ID: 12591939

Title: The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation.

PubMed ID: 12591939

DOI: 10.1073/pnas.2628049100

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22692537

Title: Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit.

PubMed ID: 22692537

DOI: 10.1038/ncomms1886

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 12591941

Title: Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.

PubMed ID: 12591941

DOI: 10.1073/pnas.262798199

PubMed ID: 14517542

Title: Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome.

PubMed ID: 14517542

DOI: 10.1038/ng1243

Sequence Information:

Length: 961
Mass: 104399
Checksum: 62B88FFD9CE4B157
Sequence:

MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA VFEAAASAQS 
SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ VVAPGAVLVR LEGCSHPVVM 
KGLCAECGQD LTQLQSKNGK QQVPLSTATV SMVHSVPELM VSSEQAEQLG REDQQRLHRN 
RKLVLMVDLD QTLIHTTEQH CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY 
ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 
IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT EVSEPSPPVR 
DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK PDERDIWPPA QAPTSSQELA 
GAPEPQGSCA QGGRVAPGQR PAQGATGTDL DFDLSSDSES SSESEGTKSS SSASDGESEG 
KRGRQKPKAA PEGAGALAQG SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG 
LCGLGNGCAD RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV 
HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP IEKTREHYHA 
TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC GHLHVVNPDW LWSCLERWDK 
VEEQLFPLRD DHTKAQRENS PAAFPDREGV PPTALFHPMP VLPKAQPGPE VRIYDSNTGK 
LIRTGARGPP APSSSLPIRQ EPSSFRAVPP PQPQMFGEEL PDAQDGEQPG PSRRKRQPSM 
SETMPLYTLC KEDLESMDKE VDDILGEGSD DSDSEKRRPE EQEEEPQPRK PGTRRERTLG 
APASSERSAA GGRGPRGHKR KLNEEDAASE SSRESSNEDE GSSSEADEMA KALEAELNDL 
M

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: CTDP1

Associated with

Other Information

A protein phosphatase functions to recycle RNA polymerase II. PubMed ID: 10385623

DNA sequence and analysis of human chromosome 18. PubMed ID: 16177791

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO. PubMed ID: 9765293

The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP. PubMed ID: 12560496

The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation. PubMed ID: 12591939

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit. PubMed ID: 22692537

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF. PubMed ID: 12591941

Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome. PubMed ID: 14517542