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Protein

RNA polymerase II subunit A C-terminal domain phosphatase

Gene

FCP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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 (RPB1). This promotes the activity of RNA polymerase II.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. protein serine/threonine phosphatase activity Source: SGD

GO - Biological processi

  1. dephosphorylation of RNA polymerase II C-terminal domain Source: SGD
  2. regulation of transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciYEAST:G3O-32948-MONOMER.
ReactomeiREACT_249645. 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
Ordered Locus Names:YMR277W
ORF Names:YM8021.03
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR277w.
SGDiS000004890. FCP1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732RNA polymerase II subunit A C-terminal domain phosphatasePRO_0000212568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei701 – 7011Phosphoserine1 Publication
Modified residuei718 – 7181Phosphoserine1 Publication
Modified residuei720 – 7201Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03254.
PaxDbiQ03254.
PeptideAtlasiQ03254.

Expressioni

Gene expression databases

GenevestigatoriQ03254.

Interactioni

Protein-protein interaction databases

BioGridi35456. 66 interactions.
DIPiDIP-2330N.
IntActiQ03254. 11 interactions.
MINTiMINT-501044.
STRINGi4932.YMR277W.

Structurei

3D structure databases

ProteinModelPortaliQ03254.
SMRiQ03254. Positions 245-327, 526-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 363194FCP1 homologyPROSITE-ProRule annotationAdd
BLAST
Domaini499 – 59395BRCTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5190.
GeneTreeiENSGT00390000015641.
HOGENOMiHOG000197682.
InParanoidiQ03254.
KOiK15732.
OMAiPDKKLFG.
OrthoDBiEOG7TXKSN.

Family and domain databases

Gene3Di3.40.50.1000. 3 hits.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF03031. NIF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03254-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTQIRSPQG LPYPIQIDKL IPSVGSYLHE GDRLLVYKFW YLVERASDTG
60 70 80 90 100
DDDNEHDVSP GGSAGSNGVS PPTKQLRESI EFFESPYEGD LISWNVDVGD
110 120 130 140 150
EVATANQVIC EIKRPCNHDI VYGGLCTQCG KEVSADAFDG VPLDVVGDVD
160 170 180 190 200
LQISETEAIR TGKALKEHLR RDKKLILVVD LDQTIIHCGV DPTIAEWKND
210 220 230 240 250
PNNPNFETLR DVKSFTLDEE LVLPLMYMND DGSMLRPPPV RKCWYYVKVR
260 270 280 290 300
PGLKEFFAKV APLFEMHIYT MATRAYALQI AKIVDPTGEL FGDRILSRDE
310 320 330 340 350
NGSLTTKSLA KLFPTDQSMV VVIDDRGDVW NWCPNLIKVV PYNFFVGVGD
360 370 380 390 400
INSNFLPKQS TGMLQLGRKT RQKSQESQEL LTDIMDNEKK LQEKIDKEVK
410 420 430 440 450
RQEEKLNHQL ATAEEPPANE SKEELTKKLE YSASLEVQQQ NRPLAKLQKH
460 470 480 490 500
LHDQKLLVDD DDELYYLMGT LSNIHKTYYD MLSQQNEPEP NLMEIIPSLK
510 520 530 540 550
QKVFQNCYFV FSGLIPLGTD IQRSDIVIWT STFGATSTPD IDYLTTHLIT
560 570 580 590 600
KNPSTYKARL AKKFNPQIKI VHPDWIFECL VNWKKVDEKP YTLIVDSPIS
610 620 630 640 650
DEELQNFQTQ LQKRQEYLEE TQEQQHMLTS QENLNLFAAG TSWLNNDDDE
660 670 680 690 700
DIPDTASDDD EDDDHDDESD DENNSEGIDR KRSIEDNHDD TSQKKTKAEP
710 720 730
SQDGPVQHKG EGDDNEDSDS QLEEELMDML DD
Length:732
Mass (Da):83,441
Last modified:November 1, 1997 - v1
Checksum:iEACA2A7D33A983C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49704 Genomic DNA. Translation: CAA89775.1.
BK006946 Genomic DNA. Translation: DAA10178.1.
PIRiS54584.
RefSeqiNP_014004.1. NM_001182784.1.

Genome annotation databases

EnsemblFungiiYMR277W; YMR277W; YMR277W.
GeneIDi855320.
KEGGisce:YMR277W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49704 Genomic DNA. Translation: CAA89775.1.
BK006946 Genomic DNA. Translation: DAA10178.1.
PIRiS54584.
RefSeqiNP_014004.1. NM_001182784.1.

3D structure databases

ProteinModelPortaliQ03254.
SMRiQ03254. Positions 245-327, 526-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35456. 66 interactions.
DIPiDIP-2330N.
IntActiQ03254. 11 interactions.
MINTiMINT-501044.
STRINGi4932.YMR277W.

Proteomic databases

MaxQBiQ03254.
PaxDbiQ03254.
PeptideAtlasiQ03254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR277W; YMR277W; YMR277W.
GeneIDi855320.
KEGGisce:YMR277W.

Organism-specific databases

CYGDiYMR277w.
SGDiS000004890. FCP1.

Phylogenomic databases

eggNOGiCOG5190.
GeneTreeiENSGT00390000015641.
HOGENOMiHOG000197682.
InParanoidiQ03254.
KOiK15732.
OMAiPDKKLFG.
OrthoDBiEOG7TXKSN.

Enzyme and pathway databases

BioCyciYEAST:G3O-32948-MONOMER.
ReactomeiREACT_249645. Formation of the Early Elongation Complex.

Miscellaneous databases

NextBioi979023.
PROiQ03254.

Gene expression databases

GenevestigatoriQ03254.

Family and domain databases

Gene3Di3.40.50.1000. 3 hits.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF03031. NIF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR02250. FCP1_euk. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Purification and characterization of an RNA polymerase II phosphatase from yeast."
    Chambers R.S., Kane C.M.
    J. Biol. Chem. 271:24498-24504(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae."
    Kobor M.S., Archambault J., Lester W., Holstege F.C.P., Gileadi O., Jansma D.B., Jennings E.G., Kouyoumdjian F., Davidson A.R., Young R.A., Greenblatt J.
    Mol. Cell 4:55-62(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718 AND SER-720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFCP1_YEAST
AccessioniPrimary (citable) accession number: Q03254
Secondary accession number(s): D6W0A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6550 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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.