Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O15194 (CTDSL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CTD small phosphatase-like protein

Short name=CTDSP-like
EC=3.1.3.16
Alternative name(s):
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3
NIF-like protein
Nuclear LIM interactor-interacting factor 1
Short name=NLI-interacting factor 1
Protein YA22
Short name=hYA22
RBSP3
Small C-terminal domain phosphatase 3
Short name=SCP3
Short name=Small CTD phosphatase 3
Gene names
Name:CTDSPL
Synonyms:C3orf8, NIF1, NIFL, SCP3, YA22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues 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. Ref.5

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per monomer By similarity.

Subunit structure

Monomer. Interacts with REST. Ref.5 Ref.6

Subcellular location

Nucleus By similarity.

Tissue specificity

Expression is restricted to non-neuronal tissues. Ref.5

Sequence similarities

Contains 1 FCP1 homology domain.

Sequence caution

The sequence BAA21667.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15194-1)

Also known as: HYA22B;

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.
Isoform 2 (identifier: O15194-2)

Also known as: HYA22A;

The sequence of this isoform differs from the canonical sequence as follows:
     79-89: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 276276CTD small phosphatase-like protein
PRO_0000212569

Regions

Domain102 – 260159FCP1 homology

Sites

Active site11214-aspartylphosphate intermediate By similarity
Active site1141Proton donor By similarity
Metal binding1121Magnesium By similarity
Metal binding1141Magnesium; via carbonyl oxygen By similarity
Metal binding2231Magnesium By similarity
Site1681Transition state stabilizer By similarity
Site2061Transition state stabilizer By similarity

Natural variations

Alternative sequence79 – 8911Missing in isoform 2.
VSP_011541
Natural variant1211S → P. Ref.3
VAR_019683
Natural variant1271N → S. Ref.3
VAR_019684
Natural variant1321V → G. Ref.3
VAR_019685

Secondary structure

........................................ 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HYA22B) [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 5C7B32A1127B0F59

FASTA27631,129
        10         20         30         40         50         60 
MDGPAIITQV TNPKEDEGRL PGAGEKASQC NVSLKKQRSR SILSSFFCCF RDYNVEAPPP 

        70         80         90        100        110        120 
SSPSVLPPLV EENGGLQKGD QRQVIPIPSP PAKYLLPEVT VLDYGKKCVV IDLDETLVHS 

       130        140        150        160        170        180 
SFKPISNADF IVPVEIDGTI HQVYVLKRPH VDEFLQRMGQ LFECVLFTAS LAKYADPVAD 

       190        200        210        220        230        240 
LLDRWGVFRA RLFRESCVFH RGNYVKDLSR LGRELSKVII VDNSPASYIF HPENAVPVQS 

       250        260        270 
WFDDMTDTEL LDLIPFFEGL SREDDVYSML HRLCNR 

« Hide

Isoform 2 (HYA22A) [UniParc].

Checksum: D19C4461386C1C2F
Show »

FASTA26529,937

References

« Hide 'large scale' references
[1]"Sequence analysis of a 685-kb genomic region on chromosome 3p22-p21.3 that is homozygously deleted in a lung carcinoma cell line."
Ishikawa S., Kai M., Tamari M., Takei Y., Takeuchi K., Bandou H., Yamane Y., Ogawa M., Nakamura Y.
DNA Res. 4:35-43(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal brain, Lung and Pancreas.
[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 2).
[3]"RBSP3 (HYA22) is a tumor suppressor gene implicated in major epithelial malignancies."
Kashuba V.I., Li J., Wang F., Senchenko V.N., Protopopov A., Malyukova A., Kutsenko A.S., Kadyrova E., Zabarovska V.I., Muravenko O.V., Zelenin A.V., Kisselev L.L., Kuzmin I., Minna J.D., Winberg G., Ernberg I., Braga E., Lerman M.I., Klein G., Zabarovsky E.R.
Proc. Natl. Acad. Sci. U.S.A. 101:4906-4911(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-121; SER-127 AND GLY-132.
Tissue: Lung.
[4]"NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Small CTD phosphatases function in silencing neuronal gene expression."
Yeo M., Lee S.-K., Lee B., Ruiz E.C., Pfaff S.L., Gill G.N.
Science 307:596-600(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH REST.
[6]"Structural genomics of protein phosphatases."
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. expand/collapse author list , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.
J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 82-265, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88153 mRNA. Translation: BAA21667.1. Different initiation.
AY279532 mRNA. Translation: AAP34400.1.
AJ575644 mRNA. Translation: CAE11804.1.
AJ575645 mRNA. Translation: CAE11805.1.
AY364238 mRNA. Translation: AAQ76797.1.
PIRJC5707.
RefSeqNP_001008393.1. NM_001008392.1.
NP_005799.2. NM_005808.2.
UniGeneHs.475963.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HHLX-ray2.10A/B/C/D82-265[»]
ProteinModelPortalO15194.
SMRO15194. Positions 82-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115512. 5 interactions.
STRING9606.ENSP00000273179.

PTM databases

PhosphoSiteO15194.

Proteomic databases

PaxDbO15194.
PRIDEO15194.

Protocols and materials databases

DNASU10217.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273179; ENSP00000273179; ENSG00000144677. [O15194-1]
ENST00000443503; ENSP00000398288; ENSG00000144677. [O15194-2]
GeneID10217.
KEGGhsa:10217.
UCSCuc003chg.3. human. [O15194-1]
uc003chh.3. human. [O15194-2]

Organism-specific databases

CTD10217.
GeneCardsGC03P037878.
HGNCHGNC:16890. CTDSPL.
HPAHPA048325.
MIM608592. gene.
neXtProtNX_O15194.
PharmGKBPA128394571.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5190.
HOGENOMHOG000236379.
HOVERGENHBG053298.
InParanoidO15194.
KOK15731.
OrthoDBEOG71P2C3.
PhylomeDBO15194.
TreeFamTF313556.

Gene expression databases

ArrayExpressO15194.
BgeeO15194.
CleanExHS_CTDSPL.
GenevestigatorO15194.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR011948. Dullard_phosphatase.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02251. HIF-SF_euk. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15194.
GeneWikiCTDSPL.
GenomeRNAi10217.
NextBio38686.
PROO15194.
SOURCESearch...

Entry information

Entry nameCTDSL_HUMAN
AccessionPrimary (citable) accession number: O15194
Secondary accession number(s): Q3ZTU0, Q70KI4, Q7Z5Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM