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Q9UNH5 (CC14A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Dual specificity protein phosphatase CDC14A

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
CDC14 cell division cycle 14 homolog A
Gene names
Name:CDC14A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. Ref.1 Ref.10 Ref.11

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Interacts with KIF20A, which is required to localize CDC14 to the midzone of the mitotic spindle. Ref.12

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Note: Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the midzone of the mitotic spindle. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12

Domain

Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.

Sequence caution

The sequence AAB88277.1 differs from that shown. Reason: Frameshift at position 6.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UNH5-1)

Also known as: CDC14A1;

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: Q9UNH5-2)

Also known as: CDC14A2;

The sequence of this isoform differs from the canonical sequence as follows:
     586-594: SLQSEYVHY → VSAQTPPPGPQNPECNFCALPSQPRLPPKKFNSAKEAF
Isoform 3 (identifier: Q9UNH5-3)

Also known as: CDC14A3;

The sequence of this isoform differs from the canonical sequence as follows:
     380-383: DNLE → VSFP
     384-594: Missing.
Isoform 4 (identifier: Q9UNH5-4)

Also known as: CDC14A4;

The sequence of this isoform differs from the canonical sequence as follows:
     174-191: RVENGDFNWIVPGKFLAF → VILFTPLKPTFLISKSIM
     192-594: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9UNH5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     586-594: SLQSEYVHY → CSCLLLVFRKPFLGSPLLSLPISHL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Dual specificity protein phosphatase CDC14A
PRO_0000094876

Regions

Region7 – 162156A
Region163 – 17614Linker
Region177 – 343167B

Sites

Active site2781Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence174 – 19118RVENG…KFLAF → VILFTPLKPTFLISKSIM in isoform 4.
VSP_012322
Alternative sequence192 – 594403Missing in isoform 4.
VSP_012323
Alternative sequence380 – 3834DNLE → VSFP in isoform 3.
VSP_012035
Alternative sequence384 – 594211Missing in isoform 3.
VSP_012036
Alternative sequence586 – 5949SLQSEYVHY → VSAQTPPPGPQNPECNFCAL PSQPRLPPKKFNSAKEAF in isoform 2.
VSP_012037
Alternative sequence586 – 5949SLQSEYVHY → CSCLLLVFRKPFLGSPLLSL PISHL in isoform 5.
VSP_047597
Natural variant3451R → Q. Ref.5
Corresponds to variant rs28364897 [ dbSNP | Ensembl ].
VAR_019957
Natural variant4931D → Y in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035655
Natural variant5891S → F. Ref.5
Corresponds to variant rs28364923 [ dbSNP | Ensembl ].
VAR_019958

Experimental info

Mutagenesis2511D → A: Loss of phosphatase activity. Ref.10
Mutagenesis2781C → S: Loss of phosphatase activity. Ref.9 Ref.10
Mutagenesis2841R → A: Loss of phosphatase activity. Ref.10
Mutagenesis3621M → A: Inappropriate nucleolar localization; when associated with A-364. Ref.11
Mutagenesis3641I → A: Inappropriate nucleolar localization; when associated with A-362. Ref.11
Sequence conflict1641F → I in AAB88277. Ref.1
Sequence conflict1821W → C in AAB88277. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CDC14A1) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D5552E2BAEEA84DF

FASTA59466,574
        10         20         30         40         50         60 
MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV 

        70         80         90        100        110        120 
YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS 

       130        140        150        160        170        180 
GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF 

       190        200        210        220        230        240 
NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA 

       250        260        270        280        290        300 
GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT 

       310        320        330        340        350        360 
HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD 

       370        380        390        400        410        420 
DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD 

       430        440        450        460        470        480 
TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR 

       490        500        510        520        530        540 
LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS 

       550        560        570        580        590 
NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY 

« Hide

Isoform 2 (CDC14A2) [UniParc].

Checksum: CAB2041A59DB3350
Show »

FASTA62369,543
Isoform 3 (CDC14A3) [UniParc].

Checksum: 28295D04793D00B7
Show »

FASTA38343,908
Isoform 4 (CDC14A4) [UniParc].

Checksum: 14E97BCF291E4D81
Show »

FASTA19122,175
Isoform 5 [UniParc].

Checksum: CA0AC7B44CAE4947
Show »

FASTA61068,203

References

« Hide 'large scale' references
[1]"A family of putative tumor suppressors is structurally and functionally conserved in humans and yeast."
Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E.
J. Biol. Chem. 272:29403-29406(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
[2]"Genomic structure, chromosomal location, and mutation analysis of the human CDC14A gene."
Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K., Carillo A., Emerson M., Heichman K., Gupte J., Tavtigian S.V., Teng D.H.-F.
Genomics 59:248-251(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Hao L., Baskerville C., Charbonneau H.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Placenta.
[4]"Human CDC14A splice variant."
Belyaev A.S., Kolokithas A., Monell C.R.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[5]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-345 AND PHE-589.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 3 AND 4).
Tissue: Brain.
[9]"Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a."
Bembenek J., Yu H.
J. Biol. Chem. 276:48237-48242(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-278.
[10]"Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase."
Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K.
Mol. Biol. Cell 13:2289-2300(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-251; CYS-278 AND ARG-284.
[11]"Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation."
Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J.
Nat. Cell Biol. 4:317-322(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-362 AND ILE-364.
[12]"Relocation of Aurora B from centromeres to the central spindle at the metaphase to anaphase transition requires MKlp2."
Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A.
J. Cell Biol. 166:167-172(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF20A, SUBCELLULAR LOCATION.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-493.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF000367 mRNA. Translation: AAB88277.1. Frameshift.
AF122013 mRNA. Translation: AAD49217.1.
AF064102 mRNA. Translation: AAC16659.1.
AF064103 mRNA. Translation: AAC16660.1.
DQ530256 mRNA. Translation: ABF74568.1.
AY623111 Genomic DNA. Translation: AAT38107.1.
AL589990, AC104457 Genomic DNA. Translation: CAH70068.1.
AL589990, AC104457 Genomic DNA. Translation: CAH70069.1.
AL589990, AC104457 Genomic DNA. Translation: CAH70070.1.
CH471097 Genomic DNA. Translation: EAW72956.1.
CH471097 Genomic DNA. Translation: EAW72958.1.
CH471097 Genomic DNA. Translation: EAW72959.1.
BC038979 mRNA. Translation: AAH38979.1.
BC093916 mRNA. Translation: AAH93916.1.
BC093918 mRNA. Translation: AAH93918.1.
CCDSCCDS769.1. [Q9UNH5-1]
CCDS770.1. [Q9UNH5-2]
CCDS771.1. [Q9UNH5-3]
RefSeqNP_003663.2. NM_003672.3. [Q9UNH5-1]
NP_201569.1. NM_033312.2. [Q9UNH5-2]
NP_201570.1. NM_033313.2. [Q9UNH5-3]
UniGeneHs.127411.

3D structure databases

ProteinModelPortalQ9UNH5.
SMRQ9UNH5. Positions 15-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114126. 10 interactions.
IntActQ9UNH5. 1 interaction.
MINTMINT-8330048.
STRING9606.ENSP00000354916.

Chemistry

BindingDBQ9UNH5.
ChEMBLCHEMBL1772926.

PTM databases

PhosphoSiteQ9UNH5.

Polymorphism databases

DMDM55976620.

Proteomic databases

PaxDbQ9UNH5.
PRIDEQ9UNH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336454; ENSP00000336739; ENSG00000079335. [Q9UNH5-1]
ENST00000361544; ENSP00000354916; ENSG00000079335. [Q9UNH5-2]
ENST00000370124; ENSP00000359142; ENSG00000079335. [Q9UNH5-3]
ENST00000370125; ENSP00000359143; ENSG00000079335. [Q9UNH5-4]
ENST00000544534; ENSP00000442543; ENSG00000079335. [Q9UNH5-5]
GeneID8556.
KEGGhsa:8556.
UCSCuc001dte.4. human. [Q9UNH5-3]
uc001dtf.2. human. [Q9UNH5-2]
uc001dtg.4. human. [Q9UNH5-1]
uc009wec.1. human. [Q9UNH5-4]

Organism-specific databases

CTD8556.
GeneCardsGC01P100817.
HGNCHGNC:1718. CDC14A.
HPAHPA023783.
MIM603504. gene.
neXtProtNX_Q9UNH5.
PharmGKBPA26254.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOVERGENHBG050818.
KOK06639.
OMANNQYSRS.
OrthoDBEOG776SPM.
PhylomeDBQ9UNH5.
TreeFamTF101053.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ9UNH5.
BgeeQ9UNH5.
CleanExHS_CDC14A.
GenevestigatorQ9UNH5.

Family and domain databases

Gene3D3.90.190.10. 2 hits.
InterProIPR029260. DSPn.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR026068. Dual_Pase_CDC14A.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR23339:SF62. PTHR23339:SF62. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 2 hits.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCDC14A.
GenomeRNAi8556.
NextBio32065.
PROQ9UNH5.
SOURCESearch...

Entry information

Entry nameCC14A_HUMAN
AccessionPrimary (citable) accession number: Q9UNH5
Secondary accession number(s): A6MA65 expand/collapse secondary AC list , B1AQ14, B1AQ15, O43171, O60727, O60728, Q52LH9, Q8IXX0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 119 of the entry and version 1 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM