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Q6GQT0 (CC14A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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 KIF20A. Interaction is required to localize CDC14 to the midzone of the mitotic spindle By similarity.

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity. Note: Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the midzone of the mitotic spindle By similarity.

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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6GQT0-1)

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: Q6GQT0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     104-152: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Dual specificity protein phosphatase CDC14A
PRO_0000094877

Regions

Region7 – 162156A
Region163 – 17614Linker
Region177 – 343167B
Compositional bias539 – 54911Poly-Ser
Compositional bias580 – 5856Poly-Ser

Sites

Active site2781Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence104 – 15249Missing in isoform 2.
VSP_012324

Sequences

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

Last modified December 21, 2004. Version 2.
Checksum: 496676322A54C078

FASTA60367,634
        10         20         30         40         50         60 
MAAESGELIG ACEFMKDRLY FATLRNRPKS TINIHYFSID EELVYENFYA DFGPLNLAMV 

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

       130        140        150        160        170        180 
GSNPPYLPFR DASFGNCTYN LTVLDCLQGI RKGLQHGFFD FETFDAEEYE HYERVENGDF 

       190        200        210        220        230        240 
NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKNN VTTIVRLNKK IYEAKRFTDA 

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

       310        320        330        340        350        360 
HAEIIAWIRI CRPGSIIGPQ QHFLKEKQAS LWVQGDIFRS KLKNRPSSEG SITKIISTLD 

       370        380        390        400        410        420 
DMSIGANLSK LQSTERIGEN NFEDEDMEIK NNVTQGDKLR ALKSQRHPRS SPSCAFRSDD 

       430        440        450        460        470        480 
MKGHQRAMAQ TFRLSSSPQP TMSTMKTSKV CLSPSVTAKK ISRGSLSSGA NIRSFSINSR 

       490        500        510        520        530        540 
LASSLGNLNA GTEEPETKKT TSLTKAAFIA SPFTSFLNGS TQTPGRNYPE LNNNQYTRSS 

       550        560        570        580        590        600 
NSNSSSSSSG LGGNLNSSPV PQSAKPEEHT TILRPSFPGS LSSSSVRFLS RSIPSLQSEY 


VHY 

« Hide

Isoform 2 [UniParc].

Checksum: D63622E867C09338
Show »

FASTA55462,115

References

[1]"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 2).
Strain: C57BL/6.
Tissue: Brain.
[2]"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] OF 72-603 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC072644 mRNA. Translation: AAH72644.1.
AK036556 mRNA. Translation: BAC29476.1.
RefSeqNP_001074287.1. NM_001080818.2.
NP_001167024.1. NM_001173553.1.
UniGeneMm.17647.

3D structure databases

ProteinModelPortalQ6GQT0.
SMRQ6GQT0. Positions 15-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000087950.

PTM databases

PhosphoSiteQ6GQT0.

Proteomic databases

PRIDEQ6GQT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090464; ENSMUSP00000087950; ENSMUSG00000033502. [Q6GQT0-1]
ENSMUST00000106491; ENSMUSP00000102100; ENSMUSG00000033502. [Q6GQT0-2]
GeneID229776.
KEGGmmu:229776.
UCSCuc008rca.1. mouse. [Q6GQT0-1]
uc012cwq.1. mouse. [Q6GQT0-2]

Organism-specific databases

CTD8556.
MGIMGI:2442676. Cdc14a.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00390000010254.
HOGENOMHOG000198341.
HOVERGENHBG050818.
InParanoidQ6GQT0.
KOK06639.
OMAACEFMKD.
OrthoDBEOG776SPM.
PhylomeDBQ6GQT0.
TreeFamTF101053.

Gene expression databases

BgeeQ6GQT0.
GenevestigatorQ6GQT0.

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

NextBio379667.
PROQ6GQT0.
SOURCESearch...

Entry information

Entry nameCC14A_MOUSE
AccessionPrimary (citable) accession number: Q6GQT0
Secondary accession number(s): Q8BZ66
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 88 of the entry and version 2 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