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Q9Y5B0 (CTDP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II subunit A C-terminal domain phosphatase

EC=3.1.3.16
Alternative name(s):
TFIIF-associating CTD phosphatase
Gene names
Name:CTDP1
Synonyms:FCP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length961 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation. Ref.14

Catalytic activity

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

Subunit structure

Homodimer. Interacts with GTF2F1. Interacts with WDR77, SNRPB and SNRNP70. Ref.5 Ref.6

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Midbody. Note: Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in anaphase and telophase-G1 respectively. Ref.14

Tissue specificity

Ubiquitously expressed. Ref.5

Post-translational modification

Phosphorylated. In the presence of TFIIF, the phosphorylated form has an increased CTD phosphatase activity. The phosphorylation is required for the physical interaction with GTF2F1. Ref.7

Involvement in disease

Congenital cataracts, facial dysmorphism, and neuropathy (CCFDN) [MIM:604168]: An autosomal recessive developmental disorder characterized by a complex clinical phenotype with seemingly unrelated features involving multiple organs and systems. Developmental abnormalities include congenital cataracts and microcorneae, hypomyelination of the peripheral nervous system, impaired physical growth, delayed early motor and intellectual development, facial dysmorphism and hypogonadism. Central nervous system involvement, with cerebral and spinal cord atrophy, may be the result of disrupted development with superimposed degenerative changes. Affected individuals are prone to severe rhabdomyolysis after viral infections and to serious complications related to general anesthesia (such as pulmonary edema and epileptic seizures).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Sequence similarities

Contains 1 BRCT domain.

Contains 1 FCP1 homology domain.

Sequence caution

The sequence AAC64549.1 differs from that shown. Reason: Cloning artifact.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCataract
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processexit from mitosis

Inferred from mutant phenotype Ref.14. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

protein dephosphorylation

Inferred from direct assay Ref.14. Source: UniProtKB

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

centrosome

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.14. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spindle

Inferred from direct assay Ref.14. Source: UniProtKB

spindle midzone

Inferred from direct assay Ref.14. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionCTD phosphatase activity

Inferred from direct assay PubMed 12721286. Source: UniProtKB

DNA-directed RNA polymerase activity

Traceable author statement Ref.5. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5B0-1)

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 4 (identifier: Q9Y5B0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     807-961: AVPPPQPQMF...ALEAELNDLM → WTTSLEKAAT...AGGPEATRGS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 961961RNA polymerase II subunit A C-terminal domain phosphatase
PRO_0000212564

Regions

Domain178 – 344167FCP1 homology
Domain629 – 728100BRCT
Compositional bias455 – 47824Ser-rich
Compositional bias577 – 5826Poly-Glu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue6741Phosphoserine Ref.11
Modified residue7401Phosphoserine By similarity
Modified residue7801N6-acetyllysine Ref.10
Modified residue8691Phosphoserine Ref.8 Ref.11
Modified residue8721Phosphoserine Ref.11 Ref.13

Natural variations

Alternative sequence807 – 961155AVPPP…LNDLM → WTTSLEKAATTATARRGGLR SRRRSPSPGSQGPAGSGRSG HLRPARGARQGAGGPEATRG S in isoform 4.
VSP_009865
Natural variant2821S → F.
Corresponds to variant rs4799078 [ dbSNP | Ensembl ].
VAR_060440
Natural variant3401T → M.
Corresponds to variant rs2279103 [ dbSNP | Ensembl ].
VAR_018264
Natural variant5191P → H.
Corresponds to variant rs557503 [ dbSNP | Ensembl ].
VAR_060441
Natural variant7551L → S.
Corresponds to variant rs34967023 [ dbSNP | Ensembl ].
VAR_032763

Experimental info

Sequence conflict611S → A in AAD42088. Ref.1
Sequence conflict611S → A in AAH63447. Ref.4
Sequence conflict1571P → A in AAC64549. Ref.5
Sequence conflict2811F → I in AAH52576. Ref.4
Sequence conflict3051E → K in AAD42088. Ref.1
Sequence conflict3901A → P in AAC64549. Ref.5
Sequence conflict4781S → T in AAC64549. Ref.5
Sequence conflict486 – 4872KP → NA in AAC64549. Ref.5
Sequence conflict504 – 5052EP → DA in AAC64549. Ref.5
Sequence conflict5131L → V in AAC64549. Ref.5
Sequence conflict656 – 6572EH → DD in AAC64549. Ref.5
Sequence conflict896 – 9005ERTLG → GADAR in AAD42088. Ref.1

Secondary structure

...... 961
Helix Strand Turn

Details...

Sequences

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

Last modified April 5, 2011. Version 3.
Checksum: 62B88FFD9CE4B157

FASTA961104,399
        10         20         30         40         50         60 
MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA VFEAAASAQS 

        70         80         90        100        110        120 
SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ VVAPGAVLVR LEGCSHPVVM 

       130        140        150        160        170        180 
KGLCAECGQD LTQLQSKNGK QQVPLSTATV SMVHSVPELM VSSEQAEQLG REDQQRLHRN 

       190        200        210        220        230        240 
RKLVLMVDLD QTLIHTTEQH CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY 

       250        260        270        280        290        300 
ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI 

       310        320        330        340        350        360 
IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT EVSEPSPPVR 

       370        380        390        400        410        420 
DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK PDERDIWPPA QAPTSSQELA 

       430        440        450        460        470        480 
GAPEPQGSCA QGGRVAPGQR PAQGATGTDL DFDLSSDSES SSESEGTKSS SSASDGESEG 

       490        500        510        520        530        540 
KRGRQKPKAA PEGAGALAQG SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG 

       550        560        570        580        590        600 
LCGLGNGCAD RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV 

       610        620        630        640        650        660 
HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP IEKTREHYHA 

       670        680        690        700        710        720 
TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC GHLHVVNPDW LWSCLERWDK 

       730        740        750        760        770        780 
VEEQLFPLRD DHTKAQRENS PAAFPDREGV PPTALFHPMP VLPKAQPGPE VRIYDSNTGK 

       790        800        810        820        830        840 
LIRTGARGPP APSSSLPIRQ EPSSFRAVPP PQPQMFGEEL PDAQDGEQPG PSRRKRQPSM 

       850        860        870        880        890        900 
SETMPLYTLC KEDLESMDKE VDDILGEGSD DSDSEKRRPE EQEEEPQPRK PGTRRERTLG 

       910        920        930        940        950        960 
APASSERSAA GGRGPRGHKR KLNEEDAASE SSRESSNEDE GSSSEADEMA KALEAELNDL 


M 

« Hide

Isoform 4 [UniParc].

Checksum: 8B4B87B24644BA6E
Show »

FASTA86793,485

References

« Hide 'large scale' references
[1]"A protein phosphatase functions to recycle RNA polymerase II."
Cho H., Kim T.-K., Mancebo H., Lane W.S., Flores O., Reinberg D.
Genes Dev. 13:1540-1552(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix carcinoma.
[2]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-961 (ISOFORM 1).
Tissue: Colon, Lymph and Ovary.
[5]"FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO."
Archambault J., Pan G., Dahmus G.K., Cartier M., Marshall N., Zhang S., Dahmus M.E., Greenblatt J.
J. Biol. Chem. 273:27593-27601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-961 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 106-961 (ISOFORM 4), TISSUE SPECIFICITY, INTERACTION WITH GTF2F1.
Tissue: Placenta.
[6]"The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP."
Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L., Majello B.
Nucleic Acids Res. 31:999-1005(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WDR77; SNRPB AND SNRNP70.
[7]"The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation."
Friedl E.M., Lane W.S., Erdjument-Bromage H., Tempst P., Reinberg D.
Proc. Natl. Acad. Sci. U.S.A. 100:2328-2333(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-869 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
Visconti R., Palazzo L., Della Monica R., Grieco D.
Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF."
Kamada K., Roeder R.G., Burley S.K.
Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 944-961 IN COMPLEX WITH GTF2F1.
[17]"Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome."
Varon R., Gooding R., Steglich C., Marns L., Tang H., Angelicheva D., Yong K.K., Ambrugger P., Reinhold A., Morar B., Baas F., Kwa M., Tournev I., Guerguelcheva V., Kremensky I., Lochmueller H., Muellner-Eidenboeck A., Merlini L. expand/collapse author list , Neumann L., Buerger J., Walter M., Swoboda K., Thomas P.K., von Moers A., Risch N., Kalaydjieva L.
Nat. Genet. 35:185-189(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CCFDN.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF154115 mRNA. Translation: AAD42088.1.
AC021594 Genomic DNA. No translation available.
AC068473 Genomic DNA. No translation available.
CH471117 Genomic DNA. Translation: EAW66631.1.
BC015010 mRNA. Translation: AAH15010.1.
BC052576 mRNA. Translation: AAH52576.1.
BC063447 mRNA. Translation: AAH63447.1.
AF081287 mRNA. Translation: AAC64549.1. Sequence problems.
RefSeqNP_001189433.1. NM_001202504.1.
NP_004706.3. NM_004715.4.
NP_430255.2. NM_048368.3.
UniGeneHs.465490.
Hs.734021.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2XX-ray2.00B944-961[»]
1ONVNMR-B879-961[»]
2K7LNMR-B582-600[»]
DisProtDP00177.
ProteinModelPortalQ9Y5B0.
SMRQ9Y5B0. Positions 26-111, 168-728.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114597. 45 interactions.
DIPDIP-41788N.
IntActQ9Y5B0. 2 interactions.
MINTMINT-275991.
STRING9606.ENSP00000299543.

PTM databases

PhosphoSiteQ9Y5B0.

Polymorphism databases

DMDM327478586.

Proteomic databases

PaxDbQ9Y5B0.
PRIDEQ9Y5B0.

Protocols and materials databases

DNASU9150.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000075430; ENSP00000075430; ENSG00000060069. [Q9Y5B0-4]
ENST00000299543; ENSP00000299543; ENSG00000060069. [Q9Y5B0-1]
GeneID9150.
KEGGhsa:9150.
UCSCuc002lnh.2. human. [Q9Y5B0-1]
uc002lni.2. human. [Q9Y5B0-4]

Organism-specific databases

CTD9150.
GeneCardsGC18P077494.
HGNCHGNC:2498. CTDP1.
HPACAB032641.
HPA040394.
HPA044201.
MIM604168. phenotype.
604927. gene.
neXtProtNX_Q9Y5B0.
Orphanet48431. Congenital cataracts - facial dysmorphism - neuropathy.
PharmGKBPA27001.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5190.
HOGENOMHOG000112039.
HOVERGENHBG051213.
InParanoidQ9Y5B0.
KOK15732.
OMAEAPDIRK.
OrthoDBEOG7WMCJ8.
PhylomeDBQ9Y5B0.
TreeFamTF315104.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9Y5B0.
BgeeQ9Y5B0.
CleanExHS_CTDP1.
GenevestigatorQ9Y5B0.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR015388. FCP1_C.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF09309. FCP1_C. 1 hit.
PF03031. NIF. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02250. FCP1_euk. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTDP1. human.
EvolutionaryTraceQ9Y5B0.
GeneWikiCTDP1.
GenomeRNAi9150.
NextBio34327.
PROQ9Y5B0.
SOURCESearch...

Entry information

Entry nameCTDP1_HUMAN
AccessionPrimary (citable) accession number: Q9Y5B0
Secondary accession number(s): A8MY97 expand/collapse secondary AC list , Q7Z644, Q96BZ1, Q9Y6F5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 133 of the entry and version 3 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 18

Human chromosome 18: entries, gene names and cross-references to MIM