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O60729 (CC14B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase CDC14B

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
CDC14 cell division cycle 14 homolog B
Gene names
Name:CDC14B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual-specificity phosphatase involved in DNA damage response. Essential regulator of the G2 DNA damage checkpoint: following DNA damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a key activator of the anaphase promoting complex/cyclosome (APC/C). Dephosphorylation of FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1, preventing entry into mitosis. Preferentially dephosphorylates proteins modified by proline-directed kinases. Ref.1 Ref.11

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.9

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.9

Subunit structure

Interacts with FZR1/CDH1. Ref.11

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm. Note: Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1. Ref.1 Ref.9 Ref.10 Ref.11

Domain

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

Sequence similarities

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

Sequence caution

The sequence CAI40539.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIRT2Q8IXJ62EBI-970231,EBI-477232

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: O60729-1)

Also known as: CDC14B2;

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 1 (identifier: O60729-2)

Also known as: CDC14B1;

The sequence of this isoform differs from the canonical sequence as follows:
     449-487: Missing.
Isoform 3 (identifier: O60729-3)

Also known as: CDC14B3;

The sequence of this isoform differs from the canonical sequence as follows:
     449-498: VILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR → DGWLSQAVTFLDRLLIWLGIHKD
Isoform 4 (identifier: O60729-4)

The sequence of this isoform differs from the canonical sequence as follows:
     449-498: VILQSSVQSC...SISRTKTVLR → CPLAVLTSAL...LFCLDGFRTQ
Isoform 5 (identifier: O60729-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MKRKSERRSSWAAAPPCSRRCSSTSPGVKKIRSSTQQDPRRRDPQDDVYLDIT → MSREGAGAALVAEVIK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Dual specificity protein phosphatase CDC14B
PRO_0000094878

Regions

Region44 – 198155A
Region199 – 21214Linker
Region213 – 379167B
Motif1 – 5454Nucleolar localization signal Probable

Sites

Active site3141Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence1 – 5353MKRKS…YLDIT → MSREGAGAALVAEVIK in isoform 5.
VSP_043576
Alternative sequence449 – 49850VILQS…KTVLR → DGWLSQAVTFLDRLLIWLGI HKD in isoform 3.
VSP_012039
Alternative sequence449 – 49850VILQS…KTVLR → CPLAVLTSALCSVVIWWIVC DYILPILLFCLDGFRTQ in isoform 4.
VSP_030720
Alternative sequence449 – 48739Missing in isoform 1.
VSP_012038
Natural variant3021I → T. Ref.6
Corresponds to variant rs16911114 [ dbSNP | Ensembl ].
VAR_019959
Natural variant3411I → T. Ref.6
Corresponds to variant rs16911075 [ dbSNP | Ensembl ].
VAR_019960

Secondary structure

.......................................................... 498
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (CDC14B2) [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: CEE15EC4DC3B1DC7

FASTA49856,802
        10         20         30         40         50         60 
MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL DITDRLCFAI 

        70         80         90        100        110        120 
LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIVH 

       130        140        150        160        170        180 
FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE AYRILIFGET SYIPFRDAAY GSCNFYITLL 

       190        200        210        220        230        240 
DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY 

       250        260        270        280        290        300 
HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 

       310        320        330        340        350        360 
DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG SVIGPQQQFL 

       370        380        390        400        410        420 
VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI SINGVENQDQ QEPEPYSDDD 

       430        440        450        460        470        480 
EINGVTQGDR LRALKSRRQS KTNAIPLTVI LQSSVQSCKT SEPNISGSAG ITKRTTRSAS 

       490 
RKSSVKSLSI SRTKTVLR 

« Hide

Isoform 1 (CDC14B1) [UniParc].

Checksum: 7E5057E7677B2E61
Show »

FASTA45952,752
Isoform 3 (CDC14B3) [UniParc].

Checksum: 7E55AF3DF2B39475
Show »

FASTA47154,176
Isoform 4 [UniParc].

Checksum: 72641340642F981F
Show »

FASTA48555,665
Isoform 5 [UniParc].

Checksum: 94244A208280B2CB
Show »

FASTA46152,311

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]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.
[3]Hao L., Baskerville C., Charbonneau H.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION (ISOFORM 3).
[4]"Subcellular adaptation of a hominoid cell cycle protein expressed in the brain."
Rosso L., Marques A.C., Kaessmann H.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Uterus.
[6]NIEHS SNPs program
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-302 AND THR-341.
[7]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[10]"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: SUBCELLULAR LOCATION.
[11]"The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint."
Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M.
Cell 134:256-267(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZR1.
[12]"The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase."
Gray C.H., Good V.M., Tonks N.K., Barford D.
EMBO J. 22:3524-3535(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-386.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF023158 mRNA. Translation: AAB88293.1.
AF064104 mRNA. Translation: AAC16661.1.
AF064105 mRNA. Translation: AAC16662.2.
AK126388 mRNA. Translation: BAG54321.1.
EF611343 mRNA. Translation: ABR12627.1.
AY675321 Genomic DNA. Translation: AAT70726.1.
AL133477, AL353578 Genomic DNA. Translation: CAI39616.1.
AL133477, AL353578 Genomic DNA. Translation: CAI39617.1.
AL133477, AL353578 Genomic DNA. Translation: CAI39619.1.
AL353578, AL133477 Genomic DNA. Translation: CAI40536.1.
AL353578, AL133477 Genomic DNA. Translation: CAI40537.1.
AL353578 Genomic DNA. Translation: CAI40539.1. Different initiation.
CH471174 Genomic DNA. Translation: EAW92658.1.
CH471174 Genomic DNA. Translation: EAW92659.1.
RefSeqNP_001070649.1. NM_001077181.1.
NP_003662.1. NM_003671.3.
NP_201588.1. NM_033331.2.
XP_005252343.1. XM_005252286.1.
XP_005252344.1. XM_005252287.1.
UniGeneHs.40582.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OHCX-ray2.50A39-386[»]
1OHDX-ray2.60A39-386[»]
1OHEX-ray2.20A39-386[»]
ProteinModelPortalO60729.
SMRO60729. Positions 42-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114125. 3 interactions.
IntActO60729. 2 interactions.
MINTMINT-4778030.
STRING9606.ENSP00000364389.

PTM databases

PhosphoSiteO60729.

Proteomic databases

PaxDbO60729.
PRIDEO60729.

Protocols and materials databases

DNASU8555.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265659; ENSP00000265659; ENSG00000081377. [O60729-3]
ENST00000375236; ENSP00000364384; ENSG00000081377. [O60729-4]
ENST00000375240; ENSP00000364388; ENSG00000081377. [O60729-2]
ENST00000375241; ENSP00000364389; ENSG00000081377. [O60729-1]
ENST00000375242; ENSP00000364390; ENSG00000081377. [O60729-5]
ENST00000463569; ENSP00000420572; ENSG00000081377. [O60729-4]
ENST00000474602; ENSP00000417897; ENSG00000081377. [O60729-3]
GeneID8555.
KEGGhsa:8555.
UCSCuc004awi.3. human. [O60729-5]
uc004awj.3. human. [O60729-1]
uc004awk.3. human. [O60729-2]

Organism-specific databases

CTD8555.
GeneCardsGC09M099252.
HGNCHGNC:1719. CDC14B.
HPAHPA013312.
MIM603505. gene.
neXtProtNX_O60729.
PharmGKBPA26255.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000198341.
HOVERGENHBG050818.
InParanoidO60729.
KOK06639.
OMAYIPYFKN.
OrthoDBEOG776SPM.
PhylomeDBO60729.
TreeFamTF101053.

Gene expression databases

ArrayExpressO60729.
BgeeO60729.
CleanExHS_CDC14B.
GenevestigatorO60729.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR026068. Dual_Pase_CDC14.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR23339:SF27. PTHR23339:SF27. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60729.
GeneWikiCDC14B.
GenomeRNAi8555.
NextBio32057.
PROO60729.
SOURCESearch...

Entry information

Entry nameCC14B_HUMAN
AccessionPrimary (citable) accession number: O60729
Secondary accession number(s): A6N5X8 expand/collapse secondary AC list , A8MQ20, B1AL31, B1AL32, O43183, O60730, Q5JU08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 115 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

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 9

Human chromosome 9: entries, gene names and cross-references to MIM