Reviewed, UniProtKB/Swiss-Prot Q6GQT0 (CC14A_MOUSE)

Names and origin

Protein names

Recommended name:
    Dual specificity protein phosphatase CDC14A
    EC=3.1.3.48
    EC=3.1.3.16
Alternative name(s):
    CDC14 cell division cycle 14 homolog A

Gene names

Name:

Cdc14a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle 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 process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 603	603	Dual specificity protein phosphatase CDC14A		PRO_0000094877
Regions
	Region	7 – 162	156	A
	Region	163 – 176	14	Linker
	Region	177 – 343	167	B
	Compositional bias	539 – 549	11	Poly-Ser
	Compositional bias	580 – 585	6	Poly-Ser
Sites
	Active site	278	1	Phosphocysteine intermediate By similarity
Natural variations
	Alternative sequence	104 – 152	49	Missing in isoform 2.		VSP_012324

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: 496676322A54C078	FASTA	603	67,634
	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
	Isoform 2. Checksum: D63622E867C09338	FASTA	554	62,115
	10 20 30 40 50 60 MAAESGELIG ACEFMKDRLY FATLRNRPKS TINIHYFSID EELVYENFYA DFGPLNLAMV 70 80 90 100 110 120 YRYCCKLNKK LKSYSLSRKK IVHYTSFDQR KRANAAFLIG AYAGLQHGFF DFETFDAEEY 130 140 150 160 170 180 EHYERVENGD FNWIVPGKFL AFSGPHPKSK IENGYPLHAP EAYFPYFKKN NVTTIVRLNK 190 200 210 220 230 240 KIYEAKRFTD AGFEHYDLFF IDGSTPSDNI VRRFLNICEN TEGAIAVHCK AGLGRTGTLI 250 260 270 280 290 300 ACYVMKHYRF THAEIIAWIR ICRPGSIIGP QQHFLKEKQA SLWVQGDIFR SKLKNRPSSE 310 320 330 340 350 360 GSITKIISTL DDMSIGANLS KLQSTERIGE NNFEDEDMEI KNNVTQGDKL RALKSQRHPR 370 380 390 400 410 420 SSPSCAFRSD DMKGHQRAMA QTFRLSSSPQ PTMSTMKTSK VCLSPSVTAK KISRGSLSSG 430 440 450 460 470 480 ANIRSFSINS RLASSLGNLN AGTEEPETKK TTSLTKAAFI ASPFTSFLNG STQTPGRNYP 490 500 510 520 530 540 ELNNNQYTRS SNSNSSSSSS GLGGNLNSSP VPQSAKPEEH TTILRPSFPG SLSSSSVRFL 550 SRSIPSLQSE YVHY

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: 15489334] [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. , 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: 16141072] [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.
IPI	IPI00345371. IPI00462566.
RefSeq	NP_001074287.1.
UniGene	Mm.17647
3D structure databases
SMR	Q6GQT0. Positions 15-343.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GQT0.
Proteomic databases
PRIDE	Q6GQT0.
Genome annotation databases
Ensembl	ENSMUST00000090464; ENSMUSP00000087950; ENSMUSG00000033502; Mus musculus. [Genome view] ENSMUST00000106491; ENSMUSP00000102100; ENSMUSG00000033502; Mus musculus. [Genome view]
GeneID	229776.
KEGG	mmu:229776.
UCSC	uc008rca.1. mouse.
Organism-specific databases
CTD	229776.
MGI	MGI:2442676. Cdc14a.
Phylogenomic databases
eggNOG	roNOG05149.
HOGENOM	HBG507028.
HOVERGEN	Q6GQT0.
InParanoid	Q6GQT0.
OMA	GENNLEE.
OrthoDB	EOG93N9ZT.
PhylomeDB	Q6GQT0.
Enzyme and pathway databases
BRENDA	3.1.3.16. 244. 3.1.3.48. 244.
Gene expression databases
ArrayExpress	Q6GQT0.
Bgee	Q6GQT0.
Genevestigator	Q6GQT0.
GermOnline	ENSMUSG00000033502. Mus musculus.
Family and domain databases
InterPro	IPR000387. Dual-sp/Tyr_phosphatase. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR016130. Tyr_Pase_AS. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	379667.
SOURCE	Search...

Entry information

Entry name

CC14A_MOUSE

Accession

Primary (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:	February 9, 2010
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)