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Q9P376

- FCP1_SCHPO

UniProt

Q9P376 - FCP1_SCHPO

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Protein

RNA polymerase II subunit A C-terminal domain phosphatase

Gene

fcp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei170 – 17011 Publication
Active sitei172 – 17211 Publication

GO - Molecular functioni

  1. CTD phosphatase activity Source: PomBase
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein complex assembly Source: PomBase
  2. cellular response to nitrogen starvation Source: PomBase
  3. negative regulation of G0 to G1 transition Source: PomBase
  4. protein dephosphorylation Source: PomBase
  5. regulation of mitotic cytokinesis Source: PomBase
  6. regulation of transcription from RNA polymerase II promoter Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Cobalt, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_215564. RNA Polymerase II Pre-transcription Events.
REACT_230125. RNA Polymerase II Transcription Elongation.
REACT_257250. 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):
CTD phosphatase fcp1
Gene namesi
Name:fcp1
ORF Names:SPAC19B12.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC19B12.05c.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701D → A, N or E: No activity. 1 Publication
Mutagenesisi172 – 1721D → A, N or E: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723RNA polymerase II subunit A C-terminal domain phosphatasePRO_0000212567Add
BLAST

Proteomic databases

MaxQBiQ9P376.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi278698. 14 interactions.
MINTiMINT-1213896.
STRINGi4896.SPAC19B12.05c-1.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi151 – 16212Combined sources
Beta strandi165 – 1695Combined sources
Turni172 – 1743Combined sources
Beta strandi175 – 1795Combined sources
Helixi183 – 1886Combined sources
Turni194 – 1963Combined sources
Helixi197 – 1993Combined sources
Beta strandi203 – 2097Combined sources
Turni210 – 2134Combined sources
Beta strandi214 – 2229Combined sources
Helixi226 – 2349Combined sources
Beta strandi237 – 2426Combined sources
Helixi247 – 25711Combined sources
Beta strandi263 – 2664Combined sources
Turni271 – 2733Combined sources
Helixi282 – 2843Combined sources
Beta strandi293 – 2986Combined sources
Helixi301 – 3033Combined sources
Beta strandi309 – 3113Combined sources
Helixi399 – 4024Combined sources
Helixi403 – 41513Combined sources
Helixi417 – 42711Combined sources
Helixi434 – 4363Combined sources
Helixi445 – 47026Combined sources
Turni471 – 4733Combined sources
Helixi479 – 4879Combined sources
Beta strandi495 – 5028Combined sources
Turni508 – 5103Combined sources
Helixi512 – 5198Combined sources
Beta strandi526 – 5305Combined sources
Beta strandi533 – 5375Combined sources
Helixi543 – 5508Combined sources
Beta strandi551 – 5533Combined sources
Beta strandi556 – 5583Combined sources
Helixi559 – 5679Combined sources
Helixi574 – 5774Combined sources
Beta strandi578 – 5803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EF0X-ray2.10A149-329[»]
A394-580[»]
3EF1X-ray2.15A140-580[»]
ProteinModelPortaliQ9P376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P376.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 341182FCP1 homologyPROSITE-ProRule annotationAdd
BLAST
Domaini486 – 57994BRCTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5190.
HOGENOMiHOG000197682.
InParanoidiQ9P376.
KOiK15732.
OMAiPDKKLFG.
OrthoDBiEOG7TXKSN.
PhylomeDBiQ9P376.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamiPF03031. 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]

Sequencei

Sequence statusi: Complete.

Q9P376-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKRLTPIHL PNSLNYPIEI ASCLVPQGSY VKKGTPLLLY RFFTKVKEDQ
60 70 80 90 100
EDGSEVYVDR EFVEQFECPV EGELVEWAVK KEESIENFSK IVAKLHEPCT
110 120 130 140 150
HEVNYGGLCA ICGKNITSQD YMGYSDMARA NISMTHNTGD LTVSLEEASR
160 170 180 190 200
LESENVKRLR QEKRLSLIVD LDQTIIHATV DPTVGEWMSD PGNVNYDVLR
210 220 230 240 250
DVRSFNLQEG PSGYTSCYYI KFRPGLAQFL QKISELYELH IYTMGTKAYA
260 270 280 290 300
KEVAKIIDPT GKLFQDRVLS RDDSGSLAQK SLRRLFPCDT SMVVVIDDRG
310 320 330 340 350
DVWDWNPNLI KVVPYEFFVG IGDINSNFLA KSTPLPEQEQ LIPLEIPKDE
360 370 380 390 400
PDSVDEINEE NEETPEYDSS NSSYAQDSST IPEKTLLKDT FLQNREALEE
410 420 430 440 450
QNKERVTALE LQKSERPLAK QQNALLEDEG KPTPSHTLLH NRDHELERLE
460 470 480 490 500
KVLKDIHAVY YEEENDISSR SGNHKHANVG LIIPKMKQKV LKGCRLLFSG
510 520 530 540 550
VIPLGVDVLS SDIAKWAMSF GAEVVLDFSV PPTHLIAAKI RTEKVKKAVS
560 570 580 590 600
MGNIKVVKLN WLTESLSQWK RLPESDYLLY PSYDLPDRNL SEHSYSSSSD
610 620 630 640 650
DEQRISELND RELDEIDWQA ADQDVENALK DLSDDNDFDT GSISASQSQP
660 670 680 690 700
EALEVNTPIK RKADLIQPSY NYDGEKRRKE NDNHEGYDLL PNSSTKGEES
710 720
AENENELDDL ADIMEAELSK DTA
Length:723
Mass (Da):81,965
Last modified:October 1, 2000 - v1
Checksum:iA127A06CD2FD3435
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC00553.1.
RefSeqiNP_594768.1. NM_001020195.2.

Genome annotation databases

EnsemblFungiiSPAC19B12.05c.1; SPAC19B12.05c.1:pep; SPAC19B12.05c.
GeneIDi2542225.
KEGGispo:SPAC19B12.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC00553.1 .
RefSeqi NP_594768.1. NM_001020195.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EF0 X-ray 2.10 A 149-329 [» ]
A 394-580 [» ]
3EF1 X-ray 2.15 A 140-580 [» ]
ProteinModelPortali Q9P376.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 278698. 14 interactions.
MINTi MINT-1213896.
STRINGi 4896.SPAC19B12.05c-1.

Proteomic databases

MaxQBi Q9P376.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC19B12.05c.1 ; SPAC19B12.05c.1:pep ; SPAC19B12.05c .
GeneIDi 2542225.
KEGGi spo:SPAC19B12.05c.

Organism-specific databases

PomBasei SPAC19B12.05c.

Phylogenomic databases

eggNOGi COG5190.
HOGENOMi HOG000197682.
InParanoidi Q9P376.
KOi K15732.
OMAi PDKKLFG.
OrthoDBi EOG7TXKSN.
PhylomeDBi Q9P376.

Enzyme and pathway databases

Reactomei REACT_215564. RNA Polymerase II Pre-transcription Events.
REACT_230125. RNA Polymerase II Transcription Elongation.
REACT_257250. Formation of the Early Elongation Complex.

Miscellaneous databases

EvolutionaryTracei Q9P376.
NextBioi 20803293.
PROi Q9P376.

Family and domain databases

Gene3Di 3.40.50.1000. 2 hits.
3.40.50.10190. 1 hit.
InterProi IPR001357. BRCT_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view ]
Pfami 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. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5."
    Hausmann S., Shuman S.
    J. Biol. Chem. 277:21213-21220(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-170 AND ASP-172.

Entry informationi

Entry nameiFCP1_SCHPO
AccessioniPrimary (citable) accession number: Q9P376
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3