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Q7TSG2 (CTDP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II subunit A C-terminal domain phosphatase

EC=3.1.3.16
Alternative name(s):
TFIIF-associating CTD phosphatase
Gene names
Name:Ctdp1
Synonyms:Fcp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length960 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Midbody By similarity. 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.

Post-translational modification

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.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 FCP1 homology domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7TSG2-1)

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.
Isoform 2 (identifier: Q7TSG2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-788: Missing.
     789-796: NHGEPSSF → MSRIILVV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 960960RNA polymerase II subunit A C-terminal domain phosphatase
PRO_0000212565

Regions

Domain178 – 341164FCP1 homology
Domain619 – 718100BRCT
Compositional bias414 – 4174Poly-Ser
Compositional bias568 – 5725Poly-Glu
Compositional bias573 – 5786Poly-Asp

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue6641Phosphoserine By similarity
Modified residue7301Phosphoserine Ref.3
Modified residue7701N6-acetyllysine Ref.4
Modified residue8601Phosphoserine By similarity
Modified residue8631Phosphoserine By similarity

Natural variations

Alternative sequence1 – 788788Missing in isoform 2.
VSP_009866
Alternative sequence789 – 7968NHGEPSSF → MSRIILVV in isoform 2.
VSP_009867

Experimental info

Sequence conflict759 – 7613PEV → GTR in AAH52934. Ref.2
Sequence conflict8971V → I in AAH52934. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7D1EB42C6D15C95C

FASTA960104,554
        10         20         30         40         50         60 
MEAPPAAGVP TECTPAVAGA EVRCPGPTPL RLLEWKVAAG ATVRIGSVLA VCETAASAQP 

        70         80         90        100        110        120 
AGPAPARAAS GGCVRAARTE RRLRSERAGV VRELCAQPGQ VVAPGALLVR LEGCSHPVVM 

       130        140        150        160        170        180 
KGLCAECGQD LTQLQSKNGR QQVPLSTATV SMVHSVPELM VSSEQAEKLG REDQQRLHRN 

       190        200        210        220        230        240 
RKLVLMVDLD QTLIHTTEQH CPQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY 

       250        260        270        280        290        300 
ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 

       310        320        330        340        350        360 
IDDREDVWKF APNLITVKKY VYFPGTGDVN APPAARETQA RRKVNHSSKG GDALEQALSV 

       370        380        390        400        410        420 
RDPEDGRPAP GVEHSNGLGK ASRELNGGEA VPGVFPSKAD EKEAWPLTRA SPASSSSGHE 

       430        440        450        460        470        480 
PTEAPELPVS CEWDGRTTPG VQPTQGDAAT QDLDFDLSSD SESSESSSRS EGQRAPAPQE 

       490        500        510        520        530        540 
RTKAAPEHSG PQDTSGGRAA ASPLGESGPS IHPHDKGSDL DTQEEGERDS LCGLGNGSVD 

       550        560        570        580        590        600 
RKEAETESQN SEQSGVTAGE SLDQSVGEEE EEDTDDDDHL IHLEEILVRV HTDYYTKYDR 

       610        620        630        640        650        660 
YLNKELEEAP DIRKIVPELK SKVLADVAVI FSGLHPTNFP VEKTREHYHA TALGAKVLTQ 

       670        680        690        700        710        720 
LVLSPDAPDR ATHLIAARAG TEKVRQAQEC KHLHVVSPDW LWSCLERWDK VEEQLFPLID 

       730        740        750        760        770        780 
DDTRTHRDNS PAVFPDRHSV LPTALFHPTP IHSKAHPGPE VRIYDSNTGK LIRMGPQGSA 

       790        800        810        820        830        840 
PAPSSAPLNH GEPSSFRAVQ PHQQQMFGEE LPESQDGEQP GPARRKRQPS MSEAMPLYTL 

       850        860        870        880        890        900 
CKEDLESMDK EVDDILGEGS DDSDIEKKKP EDQDNEQERA PKPRKPRAPG IRREQPVGLP 

       910        920        930        940        950        960 
SSGERSTPGM RGPRGHKRKL NEEDAASESS GESSNDDEEG SSSEADEMAA ALEAELNDLM 

« Hide

Isoform 2 [UniParc].

Checksum: E3243D9122FC5811
Show »

FASTA17219,043

References

[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK016213 mRNA. Translation: BAB30150.1.
BC052934 mRNA. Translation: AAH52934.1.
BC053435 mRNA. Translation: AAH53435.1.
CCDSCCDS29368.1. [Q7TSG2-1]
RefSeqNP_080571.2. NM_026295.2. [Q7TSG2-1]
UniGeneMm.312893.

3D structure databases

ProteinModelPortalQ7TSG2.
SMRQ7TSG2. Positions 168-370, 547-718.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ7TSG2.

Proteomic databases

MaxQBQ7TSG2.
PaxDbQ7TSG2.
PRIDEQ7TSG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036229; ENSMUSP00000038938; ENSMUSG00000033323. [Q7TSG2-1]
GeneID67655.
KEGGmmu:67655.
UCSCuc008ftb.1. mouse. [Q7TSG2-1]

Organism-specific databases

CTD9150.
MGIMGI:1926953. Ctdp1.

Phylogenomic databases

eggNOGCOG5190.
GeneTreeENSGT00390000015641.
HOGENOMHOG000112039.
HOVERGENHBG051213.
InParanoidQ7TSG2.
KOK15732.
OMAEAPDIRK.
OrthoDBEOG7WMCJ8.
PhylomeDBQ7TSG2.
TreeFamTF315104.

Gene expression databases

ArrayExpressQ7TSG2.
BgeeQ7TSG2.
GenevestigatorQ7TSG2.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR015388. FCP1_C.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF09309. FCP1_C. 1 hit.
PF03031. NIF. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02250. FCP1_euk. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio325156.
PROQ7TSG2.
SOURCESearch...

Entry information

Entry nameCTDP1_MOUSE
AccessionPrimary (citable) accession number: Q7TSG2
Secondary accession number(s): Q7TSS7, Q9D4S8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot