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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, SPAC19B12.05c
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

Magnesium or manganese or cobalt.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
  3. protein binding Source: PomBase

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 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.

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 Inferred

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 – 16212
Beta strandi165 – 1695
Turni172 – 1743
Beta strandi175 – 1795
Helixi183 – 1886
Turni194 – 1963
Helixi197 – 1993
Beta strandi203 – 2097
Turni210 – 2134
Beta strandi214 – 2229
Helixi226 – 2349
Beta strandi237 – 2426
Helixi247 – 25711
Beta strandi263 – 2664
Turni271 – 2733
Helixi282 – 2843
Beta strandi293 – 2986
Helixi301 – 3033
Beta strandi309 – 3113
Helixi399 – 4024
Helixi403 – 41513
Helixi417 – 42711
Helixi434 – 4363
Helixi445 – 47026
Turni471 – 4733
Helixi479 – 4879
Beta strandi495 – 5028
Turni508 – 5103
Helixi512 – 5198
Beta strandi526 – 5305
Beta strandi533 – 5375
Helixi543 – 5508
Beta strandi551 – 5533
Beta strandi556 – 5583
Helixi559 – 5679
Helixi574 – 5774
Beta strandi578 – 5803

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EF0X-ray2.10A149-329[»]
A394-580[»]
3EF1X-ray2.15A140-580[»]
ProteinModelPortaliQ9P376.

Miscellaneous databases

EvolutionaryTraceiQ9P376.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 341182FCP1 homologyAdd
BLAST
Domaini486 – 57994BRCTAdd
BLAST

Sequence similaritiesi

Contains 1 BRCT domain.

Phylogenomic databases

eggNOGiCOG5190.
HOGENOMiHOG000197682.
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

MSKRLTPIHL PNSLNYPIEI ASCLVPQGSY VKKGTPLLLY RFFTKVKEDQ    50
EDGSEVYVDR EFVEQFECPV EGELVEWAVK KEESIENFSK IVAKLHEPCT 100
HEVNYGGLCA ICGKNITSQD YMGYSDMARA NISMTHNTGD LTVSLEEASR 150
LESENVKRLR QEKRLSLIVD LDQTIIHATV DPTVGEWMSD PGNVNYDVLR 200
DVRSFNLQEG PSGYTSCYYI KFRPGLAQFL QKISELYELH IYTMGTKAYA 250
KEVAKIIDPT GKLFQDRVLS RDDSGSLAQK SLRRLFPCDT SMVVVIDDRG 300
DVWDWNPNLI KVVPYEFFVG IGDINSNFLA KSTPLPEQEQ LIPLEIPKDE 350
PDSVDEINEE NEETPEYDSS NSSYAQDSST IPEKTLLKDT FLQNREALEE 400
QNKERVTALE LQKSERPLAK QQNALLEDEG KPTPSHTLLH NRDHELERLE 450
KVLKDIHAVY YEEENDISSR SGNHKHANVG LIIPKMKQKV LKGCRLLFSG 500
VIPLGVDVLS SDIAKWAMSF GAEVVLDFSV PPTHLIAAKI RTEKVKKAVS 550
MGNIKVVKLN WLTESLSQWK RLPESDYLLY PSYDLPDRNL SEHSYSSSSD 600
DEQRISELND RELDEIDWQA ADQDVENALK DLSDDNDFDT GSISASQSQP 650
EALEVNTPIK RKADLIQPSY NYDGEKRRKE NDNHEGYDLL PNSSTKGEES 700
AENENELDDL ADIMEAELSK DTA 723
Length:723
Mass (Da):81,965
Last modified:October 1, 2000 - v1
Checksum:iA127A06CD2FD3435
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAC00553.1 .
RefSeqi NP_594768.1. NM_001020195.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
KOi K15732.
OMAi PDKKLFG.
OrthoDBi EOG7TXKSN.
PhylomeDBi Q9P376.

Enzyme and pathway databases

Reactomei REACT_215564. RNA Polymerase II Pre-transcription Events.

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: September 3, 2014
This is version 93 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

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