Reviewed, UniProtKB/Swiss-Prot O60729 (CC14B_HUMAN)

Names and origin

Protein names

Recommended name:
    Dual specificity protein phosphatase CDC14B
    EC=3.1.3.48
    EC=3.1.3.16
Alternative name(s):
    CDC14 cell division cycle 14 homolog B

Gene names

Name:

CDC14B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases. Ref.1
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.8 A phosphoprotein + H2O = a protein + phosphate. Ref.8
Subcellular location	Nucleus › nucleolus By similarity. Note: Nucleolar during interphase. Ref.1 Ref.8 Ref.9
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine phosphatase activity Ref.1 Inferred from direct assay. Source: UniProtKB protein tyrosine phosphatase activity Ref.1 Inferred from direct assay. Source: UniProtKB protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FZR1	Q9UM11	1	EBI-970231,EBI-724997

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: O60729-1)

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.

Isoform 1 (identifier: O60729-2)

Also known as: CDC14B1;

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

Isoform 3 (identifier: O60729-3)

Also known as: CDC14B3;

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

Isoform 4 (identifier: O60729-4)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 498

498

Dual specificity protein phosphatase CDC14B

PRO_0000094878

Regions

Region

44 – 198

155

A

Region

199 – 212

14

Linker

Region

213 – 379

167

B

Motif

1 – 54

54

Nucleolar localization signal Probable

Sites

Active site

314

1

Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence

449 – 498

50

VILQS…KTVLR → DGWLSQAVTFLDRLLIWLGI HKD in isoform 3.

VSP_012039

Alternative sequence

449 – 498

50

VILQS…KTVLR → CPLAVLTSALCSVVIWWIVC DYILPILLFCLDGFRTQ in isoform 4.

VSP_030720

Alternative sequence

449 – 487

39

Missing in isoform 1.

VSP_012038

Natural variant

302

1

I → T: dbSNP rs16911114. Ref.5

VAR_019959

Natural variant

341

1

I → T: dbSNP rs16911075. Ref.5

VAR_019960

Secondary structure

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498

Helix Strand Turn

Details...

Helix

44 – 46

3

Beta strand

48 – 60

13

Beta strand

71 – 75

5

Turn

77 – 79

3

Beta strand

85 – 87

3

Helix

94 – 109

16

Helix

111 – 113

3

Beta strand

116 – 122

7

Helix

126 – 143

18

Helix

148 – 155

8

Turn

156 – 159

4

Helix

179 – 191

13

Beta strand

197 – 199

3

Helix

202 – 209

8

Helix

211 – 213

3

Beta strand

216 – 220

5

Turn

221 – 223

3

Beta strand

224 – 227

4

Helix

246 – 254

9

Beta strand

257 – 262

6

Helix

271 – 274

4

Turn

275 – 277

3

Beta strand

279 – 282

4

Helix

293 – 304

12

Beta strand

307 – 313

7

Beta strand

315 – 318

4

Helix

319 – 333

15

Helix

337 – 347

11

Helix

355 – 377

23

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (CDC14B2) [UniParc]. Last modified August 1, 1998. Version 1. Checksum: CEE15EC4DC3B1DC7	FASTA	498	56,802
	10 20 30 40 50 60 MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL DITDRLCFAI 70 80 90 100 110 120 LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIVH 130 140 150 160 170 180 FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE AYRILIFGET SYIPFRDAAY GSCNFYITLL 190 200 210 220 230 240 DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY 250 260 270 280 290 300 HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 310 320 330 340 350 360 DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG SVIGPQQQFL 370 380 390 400 410 420 VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI SINGVENQDQ QEPEPYSDDD 430 440 450 460 470 480 EINGVTQGDR LRALKSRRQS KTNAIPLTVI LQSSVQSCKT SEPNISGSAG ITKRTTRSAS 490 RKSSVKSLSI SRTKTVLR
	Isoform 1 (CDC14B1). Checksum: 7E5057E7677B2E61	FASTA	459	52,752
	10 20 30 40 50 60 MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL DITDRLCFAI 70 80 90 100 110 120 LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIVH 130 140 150 160 170 180 FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE AYRILIFGET SYIPFRDAAY GSCNFYITLL 190 200 210 220 230 240 DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY 250 260 270 280 290 300 HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 310 320 330 340 350 360 DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG SVIGPQQQFL 370 380 390 400 410 420 VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI SINGVENQDQ QEPEPYSDDD 430 440 450 EINGVTQGDR LRALKSRRQS KTNAIPLTLS ISRTKTVLR
	Isoform 3 (CDC14B3). Checksum: 7E55AF3DF2B39475	FASTA	471	54,176
	10 20 30 40 50 60 MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL DITDRLCFAI 70 80 90 100 110 120 LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIVH 130 140 150 160 170 180 FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE AYRILIFGET SYIPFRDAAY GSCNFYITLL 190 200 210 220 230 240 DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY 250 260 270 280 290 300 HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 310 320 330 340 350 360 DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG SVIGPQQQFL 370 380 390 400 410 420 VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI SINGVENQDQ QEPEPYSDDD 430 440 450 460 470 EINGVTQGDR LRALKSRRQS KTNAIPLTDG WLSQAVTFLD RLLIWLGIHK D
	Isoform 4. Checksum: 72641340642F981F	FASTA	485	55,665
	10 20 30 40 50 60 MKRKSERRSS WAAAPPCSRR CSSTSPGVKK IRSSTQQDPR RRDPQDDVYL DITDRLCFAI 70 80 90 100 110 120 LYSRPKSASN VHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIVH 130 140 150 160 170 180 FTGSDQRKQA NAAFLVGCYM VIYLGRTPEE AYRILIFGET SYIPFRDAAY GSCNFYITLL 190 200 210 220 230 240 DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK AENGDLNWII PDRFIAFCGP HSRARLESGY 250 260 270 280 290 300 HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFADGST PTDAIVKEFL 310 320 330 340 350 360 DICENAEGAI AVHCKAGLGR TGTLIACYIM KHYRMTAAET IAWVRICRPG SVIGPQQQFL 370 380 390 400 410 420 VMKQTNLWLE GDYFRQKLKG QENGQHRAAF SKLLSGVDDI SINGVENQDQ QEPEPYSDDD 430 440 450 460 470 480 EINGVTQGDR LRALKSRRQS KTNAIPLTCP LAVLTSALCS VVIWWIVCDY ILPILLFCLD GFRTQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9367992] [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]	NIEHS SNPs program Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-302 AND THR-341.
[6]	"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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 12134069] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[9]	"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: 11901424] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"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: 12853468] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-386.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF023158 mRNA. Translation: AAB88293.1.
AF064104 mRNA. Translation: AAC16661.1.
AF064105 mRNA. Translation: AAC16662.2.
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.

IPI

IPI00026976.
IPI00026977.
IPI00103560.
IPI00552176.

RefSeq

NP_003662.1.
NP_201588.1.

UniGene

Hs.40582

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O60729. 2 interactions.

STRING

O60729.

Proteomic databases

PRIDE

O60729.

Genome annotation databases

Ensembl

ENST00000375241; ENSP00000364389; ENSG00000081377; Homo sapiens. [Genome view]

GeneID

8555.

UCSC

uc004awj.1. human.
uc004awk.1. human.

Organism-specific databases

CTD

8555.

GeneCards

GC09M098292.

H-InvDB

HIX0025700.
HIX0033628.
HIX0058430.

HGNC

HGNC:1719. CDC14B.

HPA

HPA013312.

MIM

603505. gene.

PharmGKB

PA26255.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11234.

HOGENOM

HBG507028.

HOVERGEN

O60729.

InParanoid

O60729.

OMA

YIPYFKN.

PhylomeDB

O60729.

Enzyme and pathway databases

BRENDA

3.1.3.16. 247.
3.1.3.48. 247.

Gene expression databases

ArrayExpress

O60729.

Bgee

O60729.

CleanEx

HS_CDC14B.

Genevestigator

O60729.

GermOnline

ENSG00000081377. Homo sapiens.

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

32057.

SOURCE

Search...

Entry information

Entry name

CC14B_HUMAN

Accession

Primary (citable) accession number: O60729
Secondary accession number(s): A6N5X8 , B1AL31, B1AL32, O43183, O60730, Q5JU08

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	August 1, 1998
Last modified:	February 9, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.