Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01047
Entry Name
UniProt Accession
Theoretical PI
5.71
Molecular Weight
29266.36
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
Protein Synonyms/Alias
3.1.3.16; Golli-interacting protein; GIP; Nuclear LIM interactor-interacting factor 3; NLI-interacting factor 3; Small C-terminal domain phosphatase 1; SCP1; Small CTD phosphatase 1;
Gene Name
Ctdsp1
Gene Synonyms/Alias
Nif3; Nliif;
Created Date
13-DEC-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
44
Canonical
GILHSLFCCVCRDDG
[1]
S-Palmitoylation
45
Canonical
ILHSLFCCVCRDDGE
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Preferentially catalyzes the dephosphorylation of 'Ser- 5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation (By similarity). Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells.
Sequence Annotation
Domain: 86 244 FCP1 homology.
Active site: 96 96 4-aspartylphosphate intermediate.
Active site: 98 98 Proton donor.
Metal binding site: 96 96 Magnesium.
Metal binding site: 98 98 Magnesium; via carbonyl oxygen.
Metal binding site: 207 207 Magnesium.
Functional site: 152 152 Transition state stabilizer.
Functional site: 190 190 Transition state stabilizer.
Modified residue: 1 1 N-acetylmethionine.
Protein Length
261 AA.
Protein Sequence
(Canonical)
MDSSAVITQI SKEEARGPLR GKGDQKSAVS QKPRSRGILH SLFCCVCRDD GEPLPAHSGA  60
PLLVEENGAI PKHTPVQYLL PEAKAQDSDK ICVVIDLDET LVHSSFKPVN NADFIIPVEI  120
DGVVHQVYVL KRPHVDEFLQ RMGELFECVL FTASLAKYAD PVADLLDKWG AFRARLFRES  180
CVFHRGNYVK DLSRLGRDLR RVLILDNSPA SYVFHPDNAV PVASWFDNMS DTELHDLLPF  240
FEQLSRVDDV YSVLRQPRPG S                                            261
FASTA
(Canonical)
>LipidDB-10090-01047|P58466
MDSSAVITQISKEEARGPLRGKGDQKSAVSQKPRSRGILHSLFCCVCRDDGEPLPAHSGA
PLLVEENGAIPKHTPVQYLLPEAKAQDSDKICVVIDLDETLVHSSFKPVNNADFIIPVEI
DGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLAKYADPVADLLDKWGAFRARLFRES
CVFHRGNYVKDLSRLGRDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHDLLPF
FEQLSRVDDVYSVLRQPRPGS
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0008420; F:CTD phosphatase activity; IEA:Ensembl
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI
GO:0050768; P:negative regulation of neurogenesis; IDA:MGI
GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI
GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI
GO:0006470; P:protein dephosphorylation; IEA:Ensembl
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl
Interpro
InterPro; IPR011948; Dullard_phosphatase
InterPro; IPR023214; HAD-like_dom
InterPro; IPR004274; NIF
Pfam
Pfam; PF03031; NIF;
SMART
SMART; SM00577; CPDc;
PROSITE
PROSITE; PS50969; FCP1;
PRINTS