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Q9Y5B0

- CTDP1_HUMAN

UniProt

Q9Y5B0 - CTDP1_HUMAN

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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

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
Complete GO annotation...

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 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
Complete GO annotation...

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 – 6741Phosphoserine1 Publication
Modified residuei740 – 7401PhosphoserineBy similarity
Modified residuei780 – 7801N6-acetyllysine1 Publication
Modified residuei869 – 8691Phosphoserine2 Publications
Modified residuei872 – 8721Phosphoserine2 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

BgeeiQ9Y5B0.
CleanExiHS_CTDP1.
ExpressionAtlasiQ9Y5B0. baseline and differential.
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. 47 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 – 59813Combined sources
Helixi945 – 95612Combined sources
Turni957 – 9593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015641.
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

        10         20         30         40         50
MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA
60 70 80 90 100
VFEAAASAQS SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ
110 120 130 140 150
VVAPGAVLVR LEGCSHPVVM KGLCAECGQD LTQLQSKNGK QQVPLSTATV
160 170 180 190 200
SMVHSVPELM VSSEQAEQLG REDQQRLHRN RKLVLMVDLD QTLIHTTEQH
210 220 230 240 250
CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY ELHVFTFGSR
260 270 280 290 300
LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI
310 320 330 340 350
IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT
360 370 380 390 400
EVSEPSPPVR DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK
410 420 430 440 450
PDERDIWPPA QAPTSSQELA GAPEPQGSCA QGGRVAPGQR PAQGATGTDL
460 470 480 490 500
DFDLSSDSES SSESEGTKSS SSASDGESEG KRGRQKPKAA PEGAGALAQG
510 520 530 540 550
SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG LCGLGNGCAD
560 570 580 590 600
RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV
610 620 630 640 650
HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP
660 670 680 690 700
IEKTREHYHA TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC
710 720 730 740 750
GHLHVVNPDW LWSCLERWDK VEEQLFPLRD DHTKAQRENS PAAFPDREGV
760 770 780 790 800
PPTALFHPMP VLPKAQPGPE VRIYDSNTGK LIRTGARGPP APSSSLPIRQ
810 820 830 840 850
EPSSFRAVPP PQPQMFGEEL PDAQDGEQPG PSRRKRQPSM SETMPLYTLC
860 870 880 890 900
KEDLESMDKE VDDILGEGSD DSDSEKRRPE EQEEEPQPRK PGTRRERTLG
910 920 930 940 950
APASSERSAA GGRGPRGHKR KLNEEDAASE SSRESSNEDE GSSSEADEMA
960
KALEAELNDL M
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.Curated

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:
EMBLi
GenBanki
DDBJi
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]
ENST00000613122; ENSP00000484525; 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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 47 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 ]
ENST00000613122 ; ENSP00000484525 ; 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.
GeneTreei ENSGT00390000015641.
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

Bgeei Q9Y5B0.
CleanExi HS_CTDP1.
ExpressionAtlasi Q9Y5B0. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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