CTDP1_MOUSE
ID CTDP1_MOUSE Reviewed; 960 AA.
AC Q7TSG2; Q7TSS7; Q9D4S8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase;
DE EC=3.1.3.16;
DE AltName: Full=TFIIF-associating CTD phosphatase;
GN Name=Ctdp1; Synonyms=Fcp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-830; SER-860 AND
RP SER-863, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-770, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the
CC heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC polymerase II subunit. This promotes the activity of RNA polymerase II.
CC Plays a role in the exit from mitosis by dephosphorylating crucial
CC mitotic substrates (USP44, CDC20 and WEE1) that are required for M-
CC phase-promoting factor (MPF)/CDK1 inactivation (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Homodimer. Interacts with GTF2F1 (By similarity). Interacts
CC with WDR77, SNRPB and SNRNP70 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000250}. Midbody {ECO:0000250}. Note=Found at centrosomes in
CC prometaphase, at spindle and spindle poles in metaphase and at spindle
CC midzone and midbody in anaphase and telophase-G1 respectively.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TSG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSG2-2; Sequence=VSP_009866, VSP_009867;
CC -!- PTM: Phosphorylated. In the presence of TFIIF, the phosphorylated form
CC has an increased CTD phosphatase activity. The phosphorylation is
CC required for the physical interaction with GTF2F1 (By similarity).
CC {ECO:0000250}.
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DR EMBL; AK016213; BAB30150.1; -; mRNA.
DR EMBL; BC052934; AAH52934.1; -; mRNA.
DR EMBL; BC053435; AAH53435.1; -; mRNA.
DR CCDS; CCDS29368.1; -. [Q7TSG2-1]
DR RefSeq; NP_080571.2; NM_026295.2. [Q7TSG2-1]
DR AlphaFoldDB; Q7TSG2; -.
DR SMR; Q7TSG2; -.
DR BioGRID; 212340; 6.
DR STRING; 10090.ENSMUSP00000038938; -.
DR iPTMnet; Q7TSG2; -.
DR PhosphoSitePlus; Q7TSG2; -.
DR EPD; Q7TSG2; -.
DR jPOST; Q7TSG2; -.
DR MaxQB; Q7TSG2; -.
DR PaxDb; Q7TSG2; -.
DR PRIDE; Q7TSG2; -.
DR ProteomicsDB; 285214; -. [Q7TSG2-1]
DR ProteomicsDB; 285215; -. [Q7TSG2-2]
DR Antibodypedia; 23481; 145 antibodies from 23 providers.
DR DNASU; 67655; -.
DR Ensembl; ENSMUST00000036229; ENSMUSP00000038938; ENSMUSG00000033323. [Q7TSG2-1]
DR GeneID; 67655; -.
DR KEGG; mmu:67655; -.
DR UCSC; uc008ftb.1; mouse. [Q7TSG2-1]
DR CTD; 9150; -.
DR MGI; MGI:1926953; Ctdp1.
DR VEuPathDB; HostDB:ENSMUSG00000033323; -.
DR eggNOG; KOG0323; Eukaryota.
DR GeneTree; ENSGT00390000015641; -.
DR HOGENOM; CLU_007683_1_2_1; -.
DR InParanoid; Q7TSG2; -.
DR OMA; FARYETY; -.
DR OrthoDB; 683531at2759; -.
DR PhylomeDB; Q7TSG2; -.
DR TreeFam; TF315104; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 67655; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Ctdp1; mouse.
DR PRO; PR:Q7TSG2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSG2; protein.
DR Bgee; ENSMUSG00000033323; Expressed in cleaving embryo and 244 other tissues.
DR ExpressionAtlas; Q7TSG2; baseline and differential.
DR Genevisible; Q7TSG2; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISO:MGI.
DR GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR GO; GO:0001096; F:TFIIF-class transcription factor complex binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR015388; FCP1_C.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23081; PTHR23081; 1.
DR Pfam; PF09309; FCP1_C; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02250; FCP1_euk; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Hydrolase; Mitosis; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..960
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase"
FT /id="PRO_0000212565"
FT DOMAIN 178..341
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT DOMAIN 619..718
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 331..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B0"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5B0"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 770
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..788
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009866"
FT VAR_SEQ 789..796
FT /note="NHGEPSSF -> MSRIILVV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009867"
FT CONFLICT 759..761
FT /note="PEV -> GTR (in Ref. 2; AAH52934)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="V -> I (in Ref. 2; AAH52934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 960 AA; 104554 MW; 7D1EB42C6D15C95C CRC64;
MEAPPAAGVP TECTPAVAGA EVRCPGPTPL RLLEWKVAAG ATVRIGSVLA VCETAASAQP
AGPAPARAAS GGCVRAARTE RRLRSERAGV VRELCAQPGQ VVAPGALLVR LEGCSHPVVM
KGLCAECGQD LTQLQSKNGR QQVPLSTATV SMVHSVPELM VSSEQAEKLG REDQQRLHRN
RKLVLMVDLD QTLIHTTEQH CPQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY
ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI
IDDREDVWKF APNLITVKKY VYFPGTGDVN APPAARETQA RRKVNHSSKG GDALEQALSV
RDPEDGRPAP GVEHSNGLGK ASRELNGGEA VPGVFPSKAD EKEAWPLTRA SPASSSSGHE
PTEAPELPVS CEWDGRTTPG VQPTQGDAAT QDLDFDLSSD SESSESSSRS EGQRAPAPQE
RTKAAPEHSG PQDTSGGRAA ASPLGESGPS IHPHDKGSDL DTQEEGERDS LCGLGNGSVD
RKEAETESQN SEQSGVTAGE SLDQSVGEEE EEDTDDDDHL IHLEEILVRV HTDYYTKYDR
YLNKELEEAP DIRKIVPELK SKVLADVAVI FSGLHPTNFP VEKTREHYHA TALGAKVLTQ
LVLSPDAPDR ATHLIAARAG TEKVRQAQEC KHLHVVSPDW LWSCLERWDK VEEQLFPLID
DDTRTHRDNS PAVFPDRHSV LPTALFHPTP IHSKAHPGPE VRIYDSNTGK LIRMGPQGSA
PAPSSAPLNH GEPSSFRAVQ PHQQQMFGEE LPESQDGEQP GPARRKRQPS MSEAMPLYTL
CKEDLESMDK EVDDILGEGS DDSDIEKKKP EDQDNEQERA PKPRKPRAPG IRREQPVGLP
SSGERSTPGM RGPRGHKRKL NEEDAASESS GESSNDDEEG SSSEADEMAA ALEAELNDLM
