| Tag |
Content |
LipidDB ID |
LipidDB-9606-01062 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
5.62 |
Molecular Weight |
29203.26 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 |
Protein Synonyms/Alias |
3.1.3.16; Nuclear LIM interactor-interacting factor 3; NLI-IF; NLI-interacting factor 3; Small C-terminal domain phosphatase 1; SCP1; Small CTD phosphatase 1; |
Gene Name |
CTDSP1 |
Gene Synonyms/Alias |
NIF3; NLIIF; SCP1; |
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 |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
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. 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 GKGDQKSAAS QKPRSRGILH SLFCCVCRDD GEALPAHSGA 60
PLLVEENGAI PKQTPVQYLL 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-9606-01062|Q9GZU7
MDSSAVITQISKEEARGPLRGKGDQKSAASQKPRSRGILHSLFCCVCRDDGEALPAHSGA
PLLVEENGAIPKQTPVQYLLPEAKAQDSDKICVVIDLDETLVHSSFKPVNNADFIIPVEI
DGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLAKYADPVADLLDKWGAFRARLFRES
CVFHRGNYVKDLSRLGRDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHDLLPF
FEQLSRVDDVYSVLRQPRPGS
|
Gene Ontology |
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB GO:0005634; C:nucleus; IDA:UniProtKB GO:0008420; F:CTD phosphatase activity; IDA:UniProtKB GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl GO:0006470; P:protein dephosphorylation; IDA:UniProtKB GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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