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Protein

RNA polymerase II subunit A C-terminal domain phosphatase

Gene

Ctdp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. CTD phosphatase activity Source: MGI

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. exit from mitosis Source: UniProtKB
  3. protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_308057. Formation of the Early Elongation Complex.
REACT_315215. RNA Polymerase II Transcription Elongation.
REACT_326102. Formation of RNA Pol II 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1926953. Ctdp1.

Subcellular locationi

  1. Nucleus By similarity
  2. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  3. Cytoplasmcytoskeletonspindle By similarity
  4. Cytoplasmcytoskeletonspindle pole By similarity
  5. Midbody By similarity

  6. 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.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. midbody Source: UniProtKB
  5. nucleoplasm Source: MGI
  6. spindle Source: UniProtKB
  7. spindle midzone Source: UniProtKB
  8. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 960960RNA polymerase II subunit A C-terminal domain phosphatasePRO_0000212565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei664 – 6641PhosphoserineBy similarity
Modified residuei730 – 7301Phosphoserine1 Publication
Modified residuei770 – 7701N6-acetyllysine1 Publication
Modified residuei860 – 8601PhosphoserineBy similarity
Modified residuei863 – 8631PhosphoserineBy similarity

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7TSG2.
PaxDbiQ7TSG2.
PRIDEiQ7TSG2.

PTM databases

PhosphoSiteiQ7TSG2.

Expressioni

Gene expression databases

BgeeiQ7TSG2.
ExpressionAtlasiQ7TSG2. baseline and differential.
GenevestigatoriQ7TSG2.

Interactioni

Subunit structurei

Homodimer. Interacts with GTF2F1 (By similarity). Interacts with WDR77, SNRPB and SNRNP70 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ7TSG2.
SMRiQ7TSG2. Positions 1-113, 168-720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 341164FCP1 homologyPROSITE-ProRule annotationAdd
BLAST
Domaini619 – 718100BRCTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi414 – 4174Poly-Ser
Compositional biasi568 – 5725Poly-Glu
Compositional biasi573 – 5786Poly-Asp

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5190.
GeneTreeiENSGT00390000015641.
HOGENOMiHOG000112039.
HOVERGENiHBG051213.
InParanoidiQ7TSG2.
KOiK15732.
OMAiEAPDIRK.
OrthoDBiEOG7WMCJ8.
PhylomeDBiQ7TSG2.
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.
IPR011053. Single_hybrid_motif.
[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]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF52113. 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. AlignAdd to basket

Isoform 1 (identifier: Q7TSG2-1) [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
MEAPPAAGVP TECTPAVAGA EVRCPGPTPL RLLEWKVAAG ATVRIGSVLA
60 70 80 90 100
VCETAASAQP AGPAPARAAS GGCVRAARTE RRLRSERAGV VRELCAQPGQ
110 120 130 140 150
VVAPGALLVR LEGCSHPVVM KGLCAECGQD LTQLQSKNGR QQVPLSTATV
160 170 180 190 200
SMVHSVPELM VSSEQAEKLG REDQQRLHRN RKLVLMVDLD QTLIHTTEQH
210 220 230 240 250
CPQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY ELHVFTFGSR
260 270 280 290 300
LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI
310 320 330 340 350
IDDREDVWKF APNLITVKKY VYFPGTGDVN APPAARETQA RRKVNHSSKG
360 370 380 390 400
GDALEQALSV RDPEDGRPAP GVEHSNGLGK ASRELNGGEA VPGVFPSKAD
410 420 430 440 450
EKEAWPLTRA SPASSSSGHE PTEAPELPVS CEWDGRTTPG VQPTQGDAAT
460 470 480 490 500
QDLDFDLSSD SESSESSSRS EGQRAPAPQE RTKAAPEHSG PQDTSGGRAA
510 520 530 540 550
ASPLGESGPS IHPHDKGSDL DTQEEGERDS LCGLGNGSVD RKEAETESQN
560 570 580 590 600
SEQSGVTAGE SLDQSVGEEE EEDTDDDDHL IHLEEILVRV HTDYYTKYDR
610 620 630 640 650
YLNKELEEAP DIRKIVPELK SKVLADVAVI FSGLHPTNFP VEKTREHYHA
660 670 680 690 700
TALGAKVLTQ LVLSPDAPDR ATHLIAARAG TEKVRQAQEC KHLHVVSPDW
710 720 730 740 750
LWSCLERWDK VEEQLFPLID DDTRTHRDNS PAVFPDRHSV LPTALFHPTP
760 770 780 790 800
IHSKAHPGPE VRIYDSNTGK LIRMGPQGSA PAPSSAPLNH GEPSSFRAVQ
810 820 830 840 850
PHQQQMFGEE LPESQDGEQP GPARRKRQPS MSEAMPLYTL CKEDLESMDK
860 870 880 890 900
EVDDILGEGS DDSDIEKKKP EDQDNEQERA PKPRKPRAPG IRREQPVGLP
910 920 930 940 950
SSGERSTPGM RGPRGHKRKL NEEDAASESS GESSNDDEEG SSSEADEMAA
960
ALEAELNDLM
Length:960
Mass (Da):104,554
Last modified:October 1, 2003 - v1
Checksum:i7D1EB42C6D15C95C
GO
Isoform 2 (identifier: Q7TSG2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-788: Missing.
     789-796: NHGEPSSF → MSRIILVV

Note: No experimental confirmation available.

Show »
Length:172
Mass (Da):19,043
Checksum:iE3243D9122FC5811
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti759 – 7613PEV → GTR in AAH52934 (PubMed:15489334).Curated
Sequence conflicti897 – 8971V → I in AAH52934 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 788788Missing in isoform 2. 1 PublicationVSP_009866Add
BLAST
Alternative sequencei789 – 7968NHGEPSSF → MSRIILVV in isoform 2. 1 PublicationVSP_009867

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016213 mRNA. Translation: BAB30150.1.
BC052934 mRNA. Translation: AAH52934.1.
BC053435 mRNA. Translation: AAH53435.1.
CCDSiCCDS29368.1. [Q7TSG2-1]
RefSeqiNP_080571.2. NM_026295.2. [Q7TSG2-1]
UniGeneiMm.312893.

Genome annotation databases

EnsembliENSMUST00000036229; ENSMUSP00000038938; ENSMUSG00000033323. [Q7TSG2-1]
GeneIDi67655.
KEGGimmu:67655.
UCSCiuc008ftb.1. mouse. [Q7TSG2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016213 mRNA. Translation: BAB30150.1.
BC052934 mRNA. Translation: AAH52934.1.
BC053435 mRNA. Translation: AAH53435.1.
CCDSiCCDS29368.1. [Q7TSG2-1]
RefSeqiNP_080571.2. NM_026295.2. [Q7TSG2-1]
UniGeneiMm.312893.

3D structure databases

ProteinModelPortaliQ7TSG2.
SMRiQ7TSG2. Positions 1-113, 168-720.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ7TSG2.

Proteomic databases

MaxQBiQ7TSG2.
PaxDbiQ7TSG2.
PRIDEiQ7TSG2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036229; ENSMUSP00000038938; ENSMUSG00000033323. [Q7TSG2-1]
GeneIDi67655.
KEGGimmu:67655.
UCSCiuc008ftb.1. mouse. [Q7TSG2-1]

Organism-specific databases

CTDi9150.
MGIiMGI:1926953. Ctdp1.

Phylogenomic databases

eggNOGiCOG5190.
GeneTreeiENSGT00390000015641.
HOGENOMiHOG000112039.
HOVERGENiHBG051213.
InParanoidiQ7TSG2.
KOiK15732.
OMAiEAPDIRK.
OrthoDBiEOG7WMCJ8.
PhylomeDBiQ7TSG2.
TreeFamiTF315104.

Enzyme and pathway databases

ReactomeiREACT_282911. RNA Polymerase II Pre-transcription Events.
REACT_308057. Formation of the Early Elongation Complex.
REACT_315215. RNA Polymerase II Transcription Elongation.
REACT_326102. Formation of RNA Pol II elongation complex.

Miscellaneous databases

NextBioi325156.
PROiQ7TSG2.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TSG2.
ExpressionAtlasiQ7TSG2. baseline and differential.
GenevestigatoriQ7TSG2.

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.
IPR011053. Single_hybrid_motif.
[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]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "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 1).
    Tissue: Embryo and Lung.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-770, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCTDP1_MOUSE
AccessioniPrimary (citable) accession number: Q7TSG2
Secondary accession number(s): Q7TSS7, Q9D4S8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: April 1, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.