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Q9UNH5

- CC14A_HUMAN

UniProt

Q9UNH5 - CC14A_HUMAN

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Protein

Dual specificity protein phosphatase CDC14A

Gene

CDC14A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis.4 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei278 – 2781Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: ProtInc
  2. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  3. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. cell proliferation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiREACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDC14A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1718. CDC14A.

Subcellular locationi

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.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi251 – 2511D → A: Loss of phosphatase activity. 1 Publication
Mutagenesisi278 – 2781C → S: Loss of phosphatase activity. 2 Publications
Mutagenesisi284 – 2841R → A: Loss of phosphatase activity. 1 Publication
Mutagenesisi362 – 3621M → A: Inappropriate nucleolar localization; when associated with A-364. 1 Publication
Mutagenesisi364 – 3641I → A: Inappropriate nucleolar localization; when associated with A-362. 1 Publication

Organism-specific databases

PharmGKBiPA26254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Dual specificity protein phosphatase CDC14APRO_0000094876Add
BLAST

Proteomic databases

PaxDbiQ9UNH5.
PRIDEiQ9UNH5.

PTM databases

PhosphoSiteiQ9UNH5.

Expressioni

Gene expression databases

BgeeiQ9UNH5.
CleanExiHS_CDC14A.
ExpressionAtlasiQ9UNH5. baseline and differential.
GenevestigatoriQ9UNH5.

Organism-specific databases

HPAiHPA023783.

Interactioni

Subunit structurei

Interacts with KIF20A, which is required to localize CDC14 to the midzone of the mitotic spindle.1 Publication

Protein-protein interaction databases

BioGridi114126. 10 interactions.
IntActiQ9UNH5. 1 interaction.
MINTiMINT-8330048.
STRINGi9606.ENSP00000354916.

Structurei

3D structure databases

ProteinModelPortaliQ9UNH5.
SMRiQ9UNH5. Positions 15-343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 162156AAdd
BLAST
Regioni163 – 17614LinkerAdd
BLAST
Regioni177 – 343167BAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00390000010254.
HOVERGENiHBG050818.
InParanoidiQ9UNH5.
KOiK06639.
OMAiNNQYSRS.
OrthoDBiEOG776SPM.
PhylomeDBiQ9UNH5.
TreeFamiTF101053.

Family and domain databases

Gene3Di3.90.190.10. 2 hits.
InterProiIPR029260. 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]
PANTHERiPTHR23339:SF62. PTHR23339:SF62. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UNH5-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA
60 70 80 90 100
DFGPLNLAMV YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG
110 120 130 140 150
AYAVIYLKKT PEEAYRALLS GSNPPYLPFR DASFGNCTYN LTILDCLQGI
160 170 180 190 200
RKGLQHGFFD FETFDVDEYE HYERVENGDF NWIVPGKFLA FSGPHPKSKI
210 220 230 240 250
ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA GFEHYDLFFI
260 270 280 290 300
DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT
310 320 330 340 350
HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG
360 370 380 390 400
SINKILSGLD DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR
410 420 430 440 450
ALKSQRQPRT SPSCAFRSDD TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM
460 470 480 490 500
ALSPSATAKR INRTSLSSGA TVRSFSINSR LASSLGNLNA ATDDPENKKT
510 520 530 540 550
SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS NSNGGNLNSP
560 570 580 590
PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY
Length:594
Mass (Da):66,574
Last modified:May 1, 2000 - v1
Checksum:iD5552E2BAEEA84DF
GO
Isoform 2 (identifier: Q9UNH5-2) [UniParc]FASTAAdd to Basket

Also known as: CDC14A2

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

Show »
Length:623
Mass (Da):69,543
Checksum:iCAB2041A59DB3350
GO
Isoform 3 (identifier: Q9UNH5-3) [UniParc]FASTAAdd to Basket

Also known as: CDC14A3

The sequence of this isoform differs from the canonical sequence as follows:
     380-383: DNLE → VSFP
     384-594: Missing.

Show »
Length:383
Mass (Da):43,908
Checksum:i28295D04793D00B7
GO
Isoform 4 (identifier: Q9UNH5-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:191
Mass (Da):22,175
Checksum:i14E97BCF291E4D81
GO
Isoform 5 (identifier: Q9UNH5-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:610
Mass (Da):68,203
Checksum:iCA0AC7B44CAE4947
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641F → I in AAB88277. (PubMed:9367992)Curated
Sequence conflicti182 – 1821W → C in AAB88277. (PubMed:9367992)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti345 – 3451R → Q.1 Publication
Corresponds to variant rs28364897 [ dbSNP | Ensembl ].
VAR_019957
Natural varianti493 – 4931D → Y in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035655
Natural varianti589 – 5891S → F.1 Publication
Corresponds to variant rs28364923 [ dbSNP | Ensembl ].
VAR_019958

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 19118RVENG…KFLAF → VILFTPLKPTFLISKSIM in isoform 4. 1 PublicationVSP_012322Add
BLAST
Alternative sequencei192 – 594403Missing in isoform 4. 1 PublicationVSP_012323Add
BLAST
Alternative sequencei380 – 3834DNLE → VSFP in isoform 3. 2 PublicationsVSP_012035
Alternative sequencei384 – 594211Missing in isoform 3. 2 PublicationsVSP_012036Add
BLAST
Alternative sequencei586 – 5949SLQSEYVHY → VSAQTPPPGPQNPECNFCAL PSQPRLPPKKFNSAKEAF in isoform 2. 1 PublicationVSP_012037
Alternative sequencei586 – 5949SLQSEYVHY → CSCLLLVFRKPFLGSPLLSL PISHL in isoform 5. 1 PublicationVSP_047597

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS769.1. [Q9UNH5-1]
CCDS770.1. [Q9UNH5-2]
CCDS771.1. [Q9UNH5-3]
RefSeqiNP_003663.2. NM_003672.3. [Q9UNH5-1]
NP_201569.1. NM_033312.2. [Q9UNH5-2]
NP_201570.1. NM_033313.2. [Q9UNH5-3]
UniGeneiHs.127411.

Genome annotation databases

EnsembliENST00000336454; ENSP00000336739; ENSG00000079335. [Q9UNH5-1]
ENST00000361544; ENSP00000354916; ENSG00000079335. [Q9UNH5-2]
ENST00000370124; ENSP00000359142; ENSG00000079335. [Q9UNH5-3]
GeneIDi8556.
KEGGihsa:8556.
UCSCiuc001dte.4. human. [Q9UNH5-3]
uc001dtf.2. human. [Q9UNH5-2]
uc001dtg.4. human. [Q9UNH5-1]
uc009wec.1. human. [Q9UNH5-4]
uc009wee.3. human.

Polymorphism databases

DMDMi55976620.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS769.1. [Q9UNH5-1 ]
CCDS770.1. [Q9UNH5-2 ]
CCDS771.1. [Q9UNH5-3 ]
RefSeqi NP_003663.2. NM_003672.3. [Q9UNH5-1 ]
NP_201569.1. NM_033312.2. [Q9UNH5-2 ]
NP_201570.1. NM_033313.2. [Q9UNH5-3 ]
UniGenei Hs.127411.

3D structure databases

ProteinModelPortali Q9UNH5.
SMRi Q9UNH5. Positions 15-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114126. 10 interactions.
IntActi Q9UNH5. 1 interaction.
MINTi MINT-8330048.
STRINGi 9606.ENSP00000354916.

Chemistry

BindingDBi Q9UNH5.
ChEMBLi CHEMBL1772926.

PTM databases

PhosphoSitei Q9UNH5.

Polymorphism databases

DMDMi 55976620.

Proteomic databases

PaxDbi Q9UNH5.
PRIDEi Q9UNH5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336454 ; ENSP00000336739 ; ENSG00000079335 . [Q9UNH5-1 ]
ENST00000361544 ; ENSP00000354916 ; ENSG00000079335 . [Q9UNH5-2 ]
ENST00000370124 ; ENSP00000359142 ; ENSG00000079335 . [Q9UNH5-3 ]
GeneIDi 8556.
KEGGi hsa:8556.
UCSCi uc001dte.4. human. [Q9UNH5-3 ]
uc001dtf.2. human. [Q9UNH5-2 ]
uc001dtg.4. human. [Q9UNH5-1 ]
uc009wec.1. human. [Q9UNH5-4 ]
uc009wee.3. human.

Organism-specific databases

CTDi 8556.
GeneCardsi GC01P100817.
HGNCi HGNC:1718. CDC14A.
HPAi HPA023783.
MIMi 603504. gene.
neXtProti NX_Q9UNH5.
PharmGKBi PA26254.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00390000010254.
HOVERGENi HBG050818.
InParanoidi Q9UNH5.
KOi K06639.
OMAi NNQYSRS.
OrthoDBi EOG776SPM.
PhylomeDBi Q9UNH5.
TreeFami TF101053.

Enzyme and pathway databases

Reactomei REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.

Miscellaneous databases

GeneWikii CDC14A.
GenomeRNAii 8556.
NextBioi 32065.
PROi Q9UNH5.
SOURCEi Search...

Gene expression databases

Bgeei Q9UNH5.
CleanExi HS_CDC14A.
ExpressionAtlasi Q9UNH5. baseline and differential.
Genevestigatori Q9UNH5.

Family and domain databases

Gene3Di 3.90.190.10. 2 hits.
InterProi IPR029260. 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 ]
PANTHERi PTHR23339:SF62. PTHR23339:SF62. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 2 hits.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation."
    North B.J., Verdin E.
    J. Biol. Chem. 282:19546-19555(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SIRT2 PHOSPHATASE.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-493.

Entry informationi

Entry nameiCC14A_HUMAN
AccessioniPrimary (citable) accession number: Q9UNH5
Secondary accession number(s): A6MA65
, B1AQ14, B1AQ15, O43171, O60727, O60728, Q52LH9, Q8IXX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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