CTDSP1

Functionⁱ

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.2 Publications

Catalytic activityⁱ

H₂O
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See the description of this molecule in ChEBI.
+
O-phospho-L-seryl-[protein]
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=
L-seryl-[protein]
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+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5."
  Yeo M., Lin P.S., Dahmus M.E., Gill G.N.
  J. Biol. Chem. 278:26078-26085(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 50-260 (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-96 AND ASP-98.
- Ref.9
  "Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1."
  Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., Dixon J.E., Noel J.P.
  Mol. Cell 24:759-770(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-256 OF MUTANT ASN-96 IN COMPLEX WITH SUBSTRATE PEPTIDES AND MAGNESIUM, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVE SITE.
EC:
3.1.3.16
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5."
  Yeo M., Lin P.S., Dahmus M.E., Gill G.N.
  J. Biol. Chem. 278:26078-26085(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 50-260 (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-96 AND ASP-98.
- Ref.9
  "Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1."
  Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., Dixon J.E., Noel J.P.
  Mol. Cell 24:759-770(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-256 OF MUTANT ASN-96 IN COMPLEX WITH SUBSTRATE PEPTIDES AND MAGNESIUM, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVE SITE.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
+
O-phospho-L-seryl-[protein]
O-phospho-L-serine residue
zoom
=
L-seryl-[protein]
L-serine residue
zoom
+
phosphate
zoom
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-threonyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-threonyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5."
  Yeo M., Lin P.S., Dahmus M.E., Gill G.N.
  J. Biol. Chem. 278:26078-26085(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 50-260 (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-96 AND ASP-98.
- Ref.9
  "Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1."
  Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., Dixon J.E., Noel J.P.
  Mol. Cell 24:759-770(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-256 OF MUTANT ASN-96 IN COMPLEX WITH SUBSTRATE PEPTIDES AND MAGNESIUM, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVE SITE.
EC:
3.1.3.16
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5."
  Yeo M., Lin P.S., Dahmus M.E., Gill G.N.
  J. Biol. Chem. 278:26078-26085(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 50-260 (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-96 AND ASP-98.
- Ref.9
  "Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1."
  Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., Dixon J.E., Noel J.P.
  Mol. Cell 24:759-770(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-256 OF MUTANT ASN-96 IN COMPLEX WITH SUBSTRATE PEPTIDES AND MAGNESIUM, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVE SITE.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
+
O-phospho-L-threonyl-[protein]
O-phospho-L-threonine residue
zoom
=
L-threonyl-[protein]
L-threonine residue
zoom
+
phosphate
zoom

Cofactorⁱ

Mg²⁺1 PublicationNote: Binds 1 Mg²⁺ ion per monomer.2 Publications

Activity regulationⁱ

Stimulated by GTF2F1. Inhibited by beryllofluoride anions.1 Publication

pH dependenceⁱ

Optimum pH is 5.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	96	4-aspartylphosphate intermediate2 Publications	1
Metal bindingⁱ	96	Magnesium1 Publication	1
Active siteⁱ	98	Proton donor1 Publication	1
Metal bindingⁱ	98	Magnesium; via carbonyl oxygen1 Publication	1
Siteⁱ	152	Transition state stabilizer1 Publication	1
Siteⁱ	190	Transition state stabilizer1 Publication	1
Metal bindingⁱ	207	Magnesium1 Publication	1

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protein phosphatase
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

SignaLinkⁱ	Q9GZU7
SIGNORⁱ	Q9GZU7

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 (EC:3.1.3.162 Publications) Alternative name(s): Nuclear LIM interactor-interacting factor 3 Short name: NLI-IF Short name: NLI-interacting factor 3 Small C-terminal domain phosphatase 1 Short name: SCP1 Short name: Small CTD phosphatase 1
Gene namesⁱ	Name:CTDSP1 Synonyms:NIF3, NLIIF, SCP1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:21614 CTDSP1
MIMⁱ	605323 gene
neXtProtⁱ	NX_Q9GZU7

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	96	D → E: No effect. Completely abolishes phosphatase activity; when associated with N-98. 1 Publication		1
Mutagenesisⁱ	98	D → N: Completely abolishes phosphatase activity; when associated with E-96. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	58190
Open Targets More...OpenTargetsⁱ	ENSG00000144579
PharmGKBⁱ	PA134938848

Chemistry databases

ChEMBLⁱ	CHEMBL1795098
Drug and drug target database More...DrugBankⁱ	DB04156 Aspartate Beryllium Trifluoride DB04272 Citric Acid

Polymorphism and mutation databases

BioMutaⁱ	CTDSP1
DMDMⁱ	17865510

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000212572	1 – 261	Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1Add BLAST		261

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources		1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q9GZU7
jPOSTⁱ	Q9GZU7
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9GZU7
PaxDbⁱ	Q9GZU7
PeptideAtlas More...PeptideAtlasⁱ	Q9GZU7
PRIDEⁱ	Q9GZU7
ProteomicsDBⁱ	80150 80151 [Q9GZU7-2]

PTM databases

DEPODⁱ	Q9GZU7
iPTMnetⁱ	Q9GZU7
PhosphoSitePlusⁱ	Q9GZU7
SwissPalmⁱ	Q9GZU7

Expressionⁱ

Tissue specificityⁱ

Expression is restricted to non-neuronal tissues. Highest expression in skeletal muscle, spleen, lung and placenta.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000144579 Expressed in 212 organ(s), highest expression level in blood
ExpressionAtlasⁱ	Q9GZU7 baseline and differential
Genevisibleⁱ	Q9GZU7 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA062654

HPAⁱ

HPA062654

Interactionⁱ

Subunit structureⁱ

Monomer (By similarity). Interacts with GTF2F1. Interacts with REST.By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
CDCA3	Q99618	6	EBI-751587,EBI-739534
Ctdsp1	P58466	2	EBI-751587,EBI-7091612	From Mus musculus.
MBP	P02686	3	EBI-751587,EBI-947410
SMAD1	Q15797	2	EBI-751587,EBI-1567153

Protein-protein interaction databases

BioGridⁱ	121804, 24 interactors
Database of interacting proteins More...DIPⁱ	DIP-61246N
IntActⁱ	Q9GZU7, 28 interactors
Molecular INTeraction database More...MINTⁱ	Q9GZU7
STRINGⁱ	9606.ENSP00000273062

Chemistry databases

BindingDBⁱ

Q9GZU7

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	85 – 87	Combined sources	3
Beta strandⁱ	92 – 95	Combined sources	4
Turnⁱ	99 – 101	Combined sources	3
Beta strandⁱ	102 – 107	Combined sources	6
Beta strandⁱ	113 – 120	Combined sources	8
Beta strandⁱ	123 – 131	Combined sources	9
Helixⁱ	135 – 145	Combined sources	11
Beta strandⁱ	146 – 151	Combined sources	6
Helixⁱ	156 – 166	Combined sources	11
Beta strandⁱ	172 – 176	Combined sources	5
Helixⁱ	178 – 180	Combined sources	3
Beta strandⁱ	181 – 184	Combined sources	4
Beta strandⁱ	187 – 189	Combined sources	3
Helixⁱ	192 – 194	Combined sources	3
Beta strandⁱ	195 – 197	Combined sources	3
Helixⁱ	199 – 201	Combined sources	3
Beta strandⁱ	202 – 205	Combined sources	4
Helixⁱ	209 – 212	Combined sources	4
Helixⁱ	216 – 218	Combined sources	3
Beta strandⁱ	219 – 221	Combined sources	3
Helixⁱ	233 – 244	Combined sources	12
Helixⁱ	251 – 254	Combined sources	4

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1T9Z	X-ray	2.30	A	77-261	[»]
	1TA0	X-ray	2.10	A	77-261	[»]
	2GHQ	X-ray	2.05	A/B	77-256	[»]
	2GHT	X-ray	1.80	A/B	77-256	[»]
	3L0B	X-ray	2.35	A/B	77-256	[»]
	3L0C	X-ray	2.45	A/B	77-256	[»]
	3L0Y	X-ray	2.30	A/B	77-256	[»]
	3PGL	X-ray	2.35	A/B	77-256	[»]
	4YGY	X-ray	2.36	A/B	77-261	[»]
	4YH1	X-ray	2.20	A/B	77-255	[»]
	6DU3	X-ray	2.58	A/B	77-256	[»]
SMRⁱ	Q9GZU7
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9GZU7

EvolutionaryTraceⁱ

Q9GZU7

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	86 – 244	FCP1 homologyPROSITE-ProRule annotationAdd BLAST		159

Phylogenomic databases

eggNOGⁱ	KOG1605 Eukaryota COG5190 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00950000182674
HOGENOMⁱ	HOG000236379
InParanoidⁱ	Q9GZU7
KEGG Orthology (KO) More...KOⁱ	K15731
Database of Orthologous Groups More...OrthoDBⁱ	1176152at2759
PhylomeDBⁱ	Q9GZU7
TreeFamⁱ	TF313556

Family and domain databases

Gene3Dⁱ	3.40.50.1000, 1 hit
InterProⁱ	View protein in InterPro IPR011948 Dullard_phosphatase IPR004274 FCP1_dom IPR036412 HAD-like_sf IPR023214 HAD_sf IPR040078 RNA_Pol_CTD_Phosphatase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03031 NIF, 1 hit
SFLDⁱ	SFLDG01124 C0.1:_RNA_Pol_CTD_Phosphatase_, 1 hit
SMARTⁱ	View protein in SMART SM00577 CPDc, 1 hit
SUPFAMⁱ	SSF56784 SSF56784, 1 hit
TIGRFAMsⁱ	TIGR02251 HIF-SF_euk, 1 hit
PROSITEⁱ	View protein in PROSITE PS50969 FCP1, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9GZU7-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDSSAVITQI SKEEARGPLR GKGDQKSAAS QKPRSRGILH SLFCCVCRDD 
        60         70         80         90        100
GEALPAHSGA PLLVEENGAI PKQTPVQYLL PEAKAQDSDK ICVVIDLDET 
       110        120        130        140        150
LVHSSFKPVN NADFIIPVEI DGVVHQVYVL KRPHVDEFLQ RMGELFECVL 
       160        170        180        190        200
FTASLAKYAD PVADLLDKWG AFRARLFRES CVFHRGNYVK DLSRLGRDLR 
       210        220        230        240        250
RVLILDNSPA SYVFHPDNAV PVASWFDNMS DTELHDLLPF FEQLSRVDDV 
       260 
YSVLRQPRPG S

Length:261

Mass (Da):29,203

Last modified:March 1, 2001 - v1

Checksum:ⁱ75A430BCA2748FEA

GO

Isoform 2 (identifier: Q9GZU7-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
73-73: Missing.

« Hide

        10         20         30         40         50
MDSSAVITQI SKEEARGPLR GKGDQKSAAS QKPRSRGILH SLFCCVCRDD 
        60         70         80         90        100
GEALPAHSGA PLLVEENGAI PKTPVQYLLP EAKAQDSDKI CVVIDLDETL 
       110        120        130        140        150
VHSSFKPVNN ADFIIPVEID GVVHQVYVLK RPHVDEFLQR MGELFECVLF 
       160        170        180        190        200
TASLAKYADP VADLLDKWGA FRARLFRESC VFHRGNYVKD LSRLGRDLRR 
       210        220        230        240        250
VLILDNSPAS YVFHPDNAVP VASWFDNMSD TELHDLLPFF EQLSRVDDVY 
       260
SVLRQPRPGS

Show »

Length:260

Mass (Da):29,075

Checksum:ⁱ30B0CCD745F26DBB

GO

Isoform 3 (identifier: Q9GZU7-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-22: MDSSAVITQISKEEARGPLRGK → MVAAPWATQEQEEGRGIQPGDR
73-73: Missing.

« Hide

        10         20         30         40         50
MVAAPWATQE QEEGRGIQPG DRGDQKSAAS QKPRSRGILH SLFCCVCRDD 
        60         70         80         90        100
GEALPAHSGA PLLVEENGAI PKTPVQYLLP EAKAQDSDKI CVVIDLDETL 
       110        120        130        140        150
VHSSFKPVNN ADFIIPVEID GVVHQVYVLK RPHVDEFLQR MGELFECVLF 
       160        170        180        190        200
TASLAKYADP VADLLDKWGA FRARLFRESC VFHRGNYVKD LSRLGRDLRR 
       210        220        230        240        250
VLILDNSPAS YVFHPDNAVP VASWFDNMSD TELHDLLPFF EQLSRVDDVY 
       260
SVLRQPRPGS

Note: No experimental confirmation available.

Show »

Length:260

Mass (Da):29,128

Checksum:ⁱD7741284DEE4D3B5

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H7C1Z7	H7C1Z7_HUMAN	Carboxy-terminal domain RNA polymer... Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1	CTDSP1	262	Annotation score:
H7C270	H7C270_HUMAN	Carboxy-terminal domain RNA polymer... Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1	CTDSP1	254	Annotation score:
H7C3E0	H7C3E0_HUMAN	Carboxy-terminal domain RNA polymer... Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1	CTDSP1	195	Annotation score:

Sequence cautionⁱ

The sequence AAP34398 differs from that shown. Reason: Frameshift at position 72.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	180	S → F in BX446444 (Ref. 3) Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_049054	56	A → T. Corresponds to variant dbSNP:rs2227249Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_045865	1 – 22	MDSSA…PLRGK → MVAAPWATQEQEEGRGIQPG DR in isoform 3. 1 PublicationAdd BLAST		22
Alternative sequenceⁱVSP_045866	73	Missing in isoform 2 and isoform 3. 2 Publications		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF229163 Genomic DNA Translation: AAG15404.1 AF229162 mRNA Translation: AAG15402.1 AY279529 mRNA Translation: AAP34397.1 AY279530 mRNA Translation: AAP34398.1 Frameshift. BX446444 mRNA No translation available. AC021016 Genomic DNA No translation available. BC012977 mRNA Translation: AAH12977.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2416.1 [Q9GZU7-1] CCDS56166.1 [Q9GZU7-3]
NCBI Reference Sequences More...RefSeqⁱ	NP_001193807.1, NM_001206878.1 [Q9GZU7-3] NP_067021.1, NM_021198.2 [Q9GZU7-1] NP_872580.1, NM_182642.2 [Q9GZU7-2]

Genome annotation databases

Ensemblⁱ	ENST00000273062; ENSP00000273062; ENSG00000144579 [Q9GZU7-1] ENST00000443891; ENSP00000392248; ENSG00000144579 [Q9GZU7-3]
GeneIDⁱ	58190
KEGGⁱ	hsa:58190
UCSC genome browser More...UCSCⁱ	uc002vhy.3 human [Q9GZU7-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9GZU7	CTD (Carboxy-terminal domain, RNA polymerase II, polypeptide A) small phosphatase 1, isoform CRA_a		HUMAN		261	UniRef100_Q9GZU7
CTD small phosphatase 1		PANTR		261
Uncharacterized protein		CERAT		261
Uncharacterized protein		PAPAN		261
Uncharacterized protein		PANPA		261
+1
Q9GZU7-2	CTD (Carboxy-terminal domain, RNA polymerase II, polypeptide A) small phosphatase 1		PANTR		260	UniRef100_K7DJK8
Uncharacterized protein		CHLSB		260
Q9GZU7-3	CTD small phosphatase 1		PANTR		260	UniRef100_A0A2I3TEG6
Uncharacterized protein		PANPA		260
CTD small phosphatase 1		GORGO		260

Protein	Similar proteins		Species	Score	Length	Source
Q9GZU7	CTD (Carboxy-terminal domain, RNA polymerase II, polypeptide A) small phosphatase 1, isoform CRA_a		HUMAN		261	UniRef90_Q9GZU7
CTD small phosphatase 1		PANTR		261
Uncharacterized protein		CERAT		261
Uncharacterized protein		PAPAN		261
Uncharacterized protein		PANPA		261
+150

Protein	Similar proteins		Species	Score	Length	Source
Q9GZU7	CTD (Carboxy-terminal domain, RNA polymerase II, polypeptide A) small phosphatase 1, isoform CRA_a		HUMAN		261	UniRef50_Q9GZU7
CTD small phosphatase 1		PANTR		261
Uncharacterized protein		CERAT		261
Uncharacterized protein		PAPAN		261
Uncharacterized protein		PANPA		261
+735

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF229163 Genomic DNA Translation: AAG15404.1 AF229162 mRNA Translation: AAG15402.1 AY279529 mRNA Translation: AAP34397.1 AY279530 mRNA Translation: AAP34398.1 Frameshift. BX446444 mRNA No translation available. AC021016 Genomic DNA No translation available. BC012977 mRNA Translation: AAH12977.1
CCDSⁱ	CCDS2416.1 [Q9GZU7-1] CCDS56166.1 [Q9GZU7-3]
RefSeqⁱ	NP_001193807.1, NM_001206878.1 [Q9GZU7-3] NP_067021.1, NM_021198.2 [Q9GZU7-1] NP_872580.1, NM_182642.2 [Q9GZU7-2]

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1T9Z	X-ray	2.30	A	77-261	[»]
	1TA0	X-ray	2.10	A	77-261	[»]
	2GHQ	X-ray	2.05	A/B	77-256	[»]
	2GHT	X-ray	1.80	A/B	77-256	[»]
	3L0B	X-ray	2.35	A/B	77-256	[»]
	3L0C	X-ray	2.45	A/B	77-256	[»]
	3L0Y	X-ray	2.30	A/B	77-256	[»]
	3PGL	X-ray	2.35	A/B	77-256	[»]
	4YGY	X-ray	2.36	A/B	77-261	[»]
	4YH1	X-ray	2.20	A/B	77-255	[»]
	6DU3	X-ray	2.58	A/B	77-256	[»]
SMRⁱ	Q9GZU7
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	121804, 24 interactors
DIPⁱ	DIP-61246N
IntActⁱ	Q9GZU7, 28 interactors
MINTⁱ	Q9GZU7
STRINGⁱ	9606.ENSP00000273062

Chemistry databases

BindingDBⁱ	Q9GZU7
ChEMBLⁱ	CHEMBL1795098
DrugBankⁱ	DB04156 Aspartate Beryllium Trifluoride DB04272 Citric Acid

PTM databases

DEPODⁱ	Q9GZU7
iPTMnetⁱ	Q9GZU7
PhosphoSitePlusⁱ	Q9GZU7
SwissPalmⁱ	Q9GZU7

Polymorphism and mutation databases

BioMutaⁱ	CTDSP1
DMDMⁱ	17865510

Proteomic databases

EPDⁱ	Q9GZU7
jPOSTⁱ	Q9GZU7
MaxQBⁱ	Q9GZU7
PaxDbⁱ	Q9GZU7
PeptideAtlasⁱ	Q9GZU7
PRIDEⁱ	Q9GZU7
ProteomicsDBⁱ	80150 80151 [Q9GZU7-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	58190
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000273062; ENSP00000273062; ENSG00000144579 [Q9GZU7-1] ENST00000443891; ENSP00000392248; ENSG00000144579 [Q9GZU7-3]
GeneIDⁱ	58190
KEGGⁱ	hsa:58190
UCSCⁱ	uc002vhy.3 human [Q9GZU7-1]

Organism-specific databases

CTDⁱ	58190
DisGeNETⁱ	58190
GeneCardsⁱ	CTDSP1
HGNCⁱ	HGNC:21614 CTDSP1
HPAⁱ	HPA062654
MIMⁱ	605323 gene
neXtProtⁱ	NX_Q9GZU7
OpenTargetsⁱ	ENSG00000144579
PharmGKBⁱ	PA134938848
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1605 Eukaryota COG5190 LUCA
GeneTreeⁱ	ENSGT00950000182674
HOGENOMⁱ	HOG000236379
InParanoidⁱ	Q9GZU7
KOⁱ	K15731
OrthoDBⁱ	1176152at2759
PhylomeDBⁱ	Q9GZU7
TreeFamⁱ	TF313556

Enzyme and pathway databases

SignaLinkⁱ	Q9GZU7
SIGNORⁱ	Q9GZU7

Miscellaneous databases

ChiTaRSⁱ	CTDSP1 human
EvolutionaryTraceⁱ	Q9GZU7
GeneWikiⁱ	CTDSP1
GenomeRNAiⁱ	58190
Protein Ontology More...PROⁱ	PR:Q9GZU7
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000144579 Expressed in 212 organ(s), highest expression level in blood
ExpressionAtlasⁱ	Q9GZU7 baseline and differential
Genevisibleⁱ	Q9GZU7 HS

Family and domain databases

Gene3Dⁱ	3.40.50.1000, 1 hit
InterProⁱ	View protein in InterPro IPR011948 Dullard_phosphatase IPR004274 FCP1_dom IPR036412 HAD-like_sf IPR023214 HAD_sf IPR040078 RNA_Pol_CTD_Phosphatase
Pfamⁱ	View protein in Pfam PF03031 NIF, 1 hit
SFLDⁱ	SFLDG01124 C0.1:_RNA_Pol_CTD_Phosphatase_, 1 hit
SMARTⁱ	View protein in SMART SM00577 CPDc, 1 hit
SUPFAMⁱ	SSF56784 SSF56784, 1 hit
TIGRFAMsⁱ	TIGR02251 HIF-SF_euk, 1 hit
PROSITEⁱ	View protein in PROSITE PS50969 FCP1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CTDS1_HUMAN
Accessionⁱ	Q9GZU7Primary (citable) accession number: Q9GZU7 Secondary accession number(s): C9IYG0, Q7Z5Q3, Q7Z5Q4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
	Last sequence update:	March 1, 2001
	Last modified:	May 8, 2019
	This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - Q9GZU7 (CTDS1_HUMAN)

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Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

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GO - Biological processi

Enzyme and pathway databases

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<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Nucleus

Keywords - Cellular componenti

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Organism-specific databases

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<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ