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

Q6PFY9 (CC14B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Interacts with FZR1/CDH1 By similarity.

Subcellular location

Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Note: Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1 By similarity.

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PFY9-1)

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 2 (identifier: Q6PFY9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MKRKSERRSAWATAPPCSRRSSSSSPGVKKSRSSTPQELHRLEQQDDLYLDIT → MRREGAGTPLMAEVIR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Dual specificity protein phosphatase CDC14B
PRO_0000094879

Regions

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

Sites

Active site3141Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence1 – 5353MKRKS…YLDIT → MRREGAGTPLMAEVIR in isoform 2.
VSP_012325

Experimental info

Sequence conflict1361V → I in AAH49794. Ref.2

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 8963E14648FC89DA

FASTA48555,661
        10         20         30         40         50         60 
MKRKSERRSA WATAPPCSRR SSSSSPGVKK SRSSTPQELH RLEQQDDLYL DITDRLCFAI 

        70         80         90        100        110        120 
LYSRPKSATN EHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIIH 

       130        140        150        160        170        180 
FTGTDQRKQA NAAFLVGCYM VIYLGRTPED AYRTLIFGDT AYIPFRDAAY GSCSFYITLL 

       190        200        210        220        230        240 
DCFHAVKKAM QYGFFNFNSF NLDEYEHYEK AENGDFNWII PERFLAFCGP HSRSRLESGY 

       250        260        270        280        290        300 
HQHSPETYIP YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFPDGST PAESIVQEFL 

       310        320        330        340        350        360 
DICENVKGAI AVHCKAGLGR TGTLIGCYLM KHYRMTAAES IAWLRICRPG SVIGPQQQFL 

       370        380        390        400        410        420 
VMKQSSLWLE GDYFRQKLRG QENGPLREAF SKHLSDADDL SLNGLENQDN QEPEPYSDDD 

       430        440        450        460        470        480 
EVSGMTQGDR LRALKSRRQP KASAIPLTCP LAVLTSALCS VAIWWIVCDY ILPTLLFCLD 


GFRTQ 

« Hide

Isoform 2 [UniParc].

Checksum: C18E8112A217EBE6
Show »

FASTA44851,402

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Aorta and Vein.
[2]"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 1).
Strain: C57BL/6.
Tissue: Brain and Limb.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK041155 mRNA. Translation: BAC30842.1.
BC049794 mRNA. Translation: AAH49794.1.
BC057357 mRNA. Translation: AAH57357.1.
RefSeqNP_001116461.1. NM_001122989.1.
NP_766175.3. NM_172587.3.
XP_006517287.1. XM_006517224.1.
UniGeneMm.25335.

3D structure databases

ProteinModelPortalQ6PFY9.
SMRQ6PFY9. Positions 43-379.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6PFY9.

Proteomic databases

PRIDEQ6PFY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039318; ENSMUSP00000046003; ENSMUSG00000033102. [Q6PFY9-1]
ENSMUST00000109769; ENSMUSP00000105391; ENSMUSG00000033102. [Q6PFY9-2]
ENSMUST00000109770; ENSMUSP00000105392; ENSMUSG00000033102. [Q6PFY9-1]
GeneID218294.
KEGGmmu:218294.
UCSCuc007qym.2. mouse. [Q6PFY9-1]
uc007qyo.2. mouse. [Q6PFY9-2]

Organism-specific databases

CTD8555.
MGIMGI:2441808. Cdc14b.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00390000010254.
HOGENOMHOG000198341.
HOVERGENHBG050818.
InParanoidQ6PFY9.
KOK06639.
OMAYIPYFKN.
OrthoDBEOG776SPM.
PhylomeDBQ6PFY9.
TreeFamTF101053.

Gene expression databases

BgeeQ6PFY9.
GenevestigatorQ6PFY9.

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

NextBio376235.
PROQ6PFY9.
SOURCESearch...

Entry information

Entry nameCC14B_MOUSE
AccessionPrimary (citable) accession number: Q6PFY9
Secondary accession number(s): Q80WC4, Q8BLV5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot