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O60729

- CC14B_HUMAN

UniProt

O60729 - CC14B_HUMAN

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Protein

Dual specificity protein phosphatase CDC14B

Gene
CDC14B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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). Dephosphorylates SIRT2 around early anaphase. 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.2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei314 – 3141Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein serine/threonine phosphatase activity Source: UniProtKB
  3. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  4. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. activation of anaphase-promoting complex activity Source: UniProtKB
  2. DNA repair Source: UniProtKB-KW
  3. G2 DNA damage checkpoint Source: UniProtKB
  4. peptidyl-tyrosine dephosphorylation Source: GOC
  5. protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDC14B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:1719. CDC14B.

Subcellular locationi

Nucleusnucleolus. Nucleusnucleoplasm
Note: Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1.4 Publications

GO - Cellular componenti

  1. nuclear membrane Source: HPA
  2. nucleolus Source: UniProtKB
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26255.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Dual specificity protein phosphatase CDC14BPRO_0000094878Add
BLAST

Proteomic databases

PaxDbiO60729.
PRIDEiO60729.

PTM databases

PhosphoSiteiO60729.

Expressioni

Gene expression databases

ArrayExpressiO60729.
BgeeiO60729.
CleanExiHS_CDC14B.
GenevestigatoriO60729.

Organism-specific databases

HPAiHPA013312.

Interactioni

Subunit structurei

Interacts with FZR1/CDH1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SIRT2Q8IXJ62EBI-970231,EBI-477232

Protein-protein interaction databases

BioGridi114125. 3 interactions.
IntActiO60729. 2 interactions.
MINTiMINT-4778030.
STRINGi9606.ENSP00000364389.

Structurei

Secondary structure

1
498
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 463
Beta strandi48 – 6013
Beta strandi71 – 755
Turni77 – 793
Beta strandi85 – 873
Helixi94 – 10916
Helixi111 – 1133
Beta strandi116 – 1227
Helixi126 – 14318
Helixi148 – 1558
Turni156 – 1594
Beta strandi168 – 1725
Helixi179 – 19113
Beta strandi197 – 1993
Helixi202 – 2098
Helixi211 – 2133
Beta strandi216 – 2205
Turni221 – 2233
Beta strandi224 – 2274
Beta strandi237 – 2393
Helixi246 – 2549
Beta strandi257 – 2626
Helixi271 – 2744
Turni275 – 2773
Beta strandi279 – 2824
Helixi293 – 30412
Beta strandi307 – 3137
Beta strandi315 – 3184
Helixi319 – 33315
Helixi337 – 34711
Helixi355 – 37723

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OHCX-ray2.50A39-386[»]
1OHDX-ray2.60A39-386[»]
1OHEX-ray2.20A39-386[»]
ProteinModelPortaliO60729.
SMRiO60729. Positions 42-379.

Miscellaneous databases

EvolutionaryTraceiO60729.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 198155AAdd
BLAST
Regioni199 – 21214LinkerAdd
BLAST
Regioni213 – 379167BAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1 – 5454Nucleolar localization signal InferredAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000198341.
HOVERGENiHBG050818.
InParanoidiO60729.
KOiK06639.
OMAiYIPYFKN.
OrthoDBiEOG776SPM.
PhylomeDBiO60729.
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.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
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 2 (identifier: O60729-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL    50
DITDRLCFAI LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY 100
CCKINKKLKS ITMLRKKIVH FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE 150
AYRILIFGET SYIPFRDAAY GSCNFYITLL DCFHAVKKAM QYGFLNFNSF 200
NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY HQHSPETYIQ 250
YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 300
DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG 350
SVIGPQQQFL VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI 400
SINGVENQDQ QEPEPYSDDD EINGVTQGDR LRALKSRRQS KTNAIPLTVI 450
LQSSVQSCKT SEPNISGSAG ITKRTTRSAS RKSSVKSLSI SRTKTVLR 498
Length:498
Mass (Da):56,802
Last modified:August 1, 1998 - v1
Checksum:iCEE15EC4DC3B1DC7
GO
Isoform 1 (identifier: O60729-2) [UniParc]FASTAAdd to Basket

Also known as: CDC14B1

The sequence of this isoform differs from the canonical sequence as follows:
     449-487: Missing.

Show »
Length:459
Mass (Da):52,752
Checksum:i7E5057E7677B2E61
GO
Isoform 3 (identifier: O60729-3) [UniParc]FASTAAdd to Basket

Also known as: CDC14B3

The sequence of this isoform differs from the canonical sequence as follows:
     449-498: VILQSSVQSCKTSEPNISGSAGITKRTTRSASRKSSVKSLSISRTKTVLR → DGWLSQAVTFLDRLLIWLGIHKD

Show »
Length:471
Mass (Da):54,176
Checksum:i7E55AF3DF2B39475
GO
Isoform 4 (identifier: O60729-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     449-498: VILQSSVQSC...SISRTKTVLR → CPLAVLTSAL...LFCLDGFRTQ

Show »
Length:485
Mass (Da):55,665
Checksum:i72641340642F981F
GO
Isoform 5 (identifier: O60729-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:461
Mass (Da):52,311
Checksum:i94244A208280B2CB
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021I → T.1 Publication
Corresponds to variant rs16911114 [ dbSNP | Ensembl ].
VAR_019959
Natural varianti341 – 3411I → T.1 Publication
Corresponds to variant rs16911075 [ dbSNP | Ensembl ].
VAR_019960

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353MKRKS…YLDIT → MSREGAGAALVAEVIK in isoform 5. VSP_043576Add
BLAST
Alternative sequencei449 – 49850VILQS…KTVLR → DGWLSQAVTFLDRLLIWLGI HKD in isoform 3. VSP_012039Add
BLAST
Alternative sequencei449 – 49850VILQS…KTVLR → CPLAVLTSALCSVVIWWIVC DYILPILLFCLDGFRTQ in isoform 4. VSP_030720Add
BLAST
Alternative sequencei449 – 48739Missing in isoform 1. VSP_012038Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43853.1. [O60729-5]
CCDS6721.1. [O60729-2]
CCDS6722.1. [O60729-1]
RefSeqiNP_001070649.1. NM_001077181.1. [O60729-5]
NP_003662.1. NM_003671.3. [O60729-2]
NP_201588.1. NM_033331.2. [O60729-1]
XP_005252343.1. XM_005252286.1. [O60729-4]
XP_005252344.1. XM_005252287.1. [O60729-4]
UniGeneiHs.40582.

Genome annotation databases

EnsembliENST00000265659; 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]
GeneIDi8555.
KEGGihsa:8555.
UCSCiuc004awi.3. human. [O60729-5]
uc004awj.3. human. [O60729-1]
uc004awk.3. human. [O60729-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43853.1. [O60729-5 ]
CCDS6721.1. [O60729-2 ]
CCDS6722.1. [O60729-1 ]
RefSeqi NP_001070649.1. NM_001077181.1. [O60729-5 ]
NP_003662.1. NM_003671.3. [O60729-2 ]
NP_201588.1. NM_033331.2. [O60729-1 ]
XP_005252343.1. XM_005252286.1. [O60729-4 ]
XP_005252344.1. XM_005252287.1. [O60729-4 ]
UniGenei Hs.40582.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OHC X-ray 2.50 A 39-386 [» ]
1OHD X-ray 2.60 A 39-386 [» ]
1OHE X-ray 2.20 A 39-386 [» ]
ProteinModelPortali O60729.
SMRi O60729. Positions 42-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114125. 3 interactions.
IntActi O60729. 2 interactions.
MINTi MINT-4778030.
STRINGi 9606.ENSP00000364389.

PTM databases

PhosphoSitei O60729.

Proteomic databases

PaxDbi O60729.
PRIDEi O60729.

Protocols and materials databases

DNASUi 8555.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265659 ; 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 ]
GeneIDi 8555.
KEGGi hsa:8555.
UCSCi uc004awi.3. human. [O60729-5 ]
uc004awj.3. human. [O60729-1 ]
uc004awk.3. human. [O60729-2 ]

Organism-specific databases

CTDi 8555.
GeneCardsi GC09M099252.
HGNCi HGNC:1719. CDC14B.
HPAi HPA013312.
MIMi 603505. gene.
neXtProti NX_O60729.
PharmGKBi PA26255.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000198341.
HOVERGENi HBG050818.
InParanoidi O60729.
KOi K06639.
OMAi YIPYFKN.
OrthoDBi EOG776SPM.
PhylomeDBi O60729.
TreeFami TF101053.

Miscellaneous databases

EvolutionaryTracei O60729.
GeneWikii CDC14B.
GenomeRNAii 8555.
NextBioi 32057.
PROi O60729.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60729.
Bgeei O60729.
CleanExi HS_CDC14B.
Genevestigatori O60729.

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.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
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. 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.
    , 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.
    , 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. 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. "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.
  12. "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.
  13. "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.

Entry informationi

Entry nameiCC14B_HUMAN
AccessioniPrimary (citable) accession number: O60729
Secondary accession number(s): A6N5X8
, A8MQ20, B1AL31, B1AL32, O43183, O60730, Q5JU08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 119 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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