O60729 (CC14B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CDC14B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	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). 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. Ref.1 Ref.11
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.9 A phosphoprotein + H2O = a protein + phosphate. Ref.9
Subunit structure	Interacts with FZR1/CDH1. Ref.11
Subcellular location	Nucleus › nucleolus. Nucleus › nucleoplasm. Note: Following DNA damage, translocates from the nucleolus to the nucleoplasm and interacts with FZR1/CDH1. Ref.1 Ref.9 Ref.10 Ref.11
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.
Sequence caution	The sequence CAI40539.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW G2 DNA damage checkpoint Inferred from direct assay Ref.11. Source: UniProtKB activation of anaphase-promoting complex activity Inferred from mutant phenotype Ref.11. Source: UniProtKB
Cellular_component	nuclear membrane Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay Ref.11. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	protein serine/threonine phosphatase activity Inferred from direct assay Ref.11Ref.1. Source: UniProtKB protein tyrosine phosphatase activity Inferred from direct assay Ref.1. Source: UniProtKB protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 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

Isoform 5 (identifier: O60729-5)

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

Note: No experimental confirmation available.

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

1 – 53

53

MKRKS…YLDIT → MSREGAGAALVAEVIK in isoform 5.

VSP_043576

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. Ref.6
Corresponds to variant rs16911114 [ dbSNP | Ensembl ].

VAR_019959

Natural variant

341

1

I → T. Ref.6
Corresponds to variant rs16911075 [ dbSNP | Ensembl ].

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

Beta strand

168 – 172

5

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

Beta strand

237 – 239

3

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) [UniParc]. 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) [UniParc]. 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 [UniParc]. 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
	Isoform 5 [UniParc]. Checksum: 94244A208280B2CB	FASTA	461	52,311
	10 20 30 40 50 60 MSREGAGAAL VAEVIKDRLC FAILYSRPKS ASNVHYFSID NELEYENFYA DFGPLNLAMV 70 80 90 100 110 120 YRYCCKINKK LKSITMLRKK IVHFTGSDQR KQANAAFLVG CYMVIYLGRT PEEAYRILIF 130 140 150 160 170 180 GETSYIPFRD AAYGSCNFYI TLLDCFHAVK KAMQYGFLNF NSFNLDEYEH YEKAENGDLN 190 200 210 220 230 240 WIIPDRFIAF CGPHSRARLE SGYHQHSPET YIQYFKNHNV TTIIRLNKRM YDAKRFTDAG 250 260 270 280 290 300 FDHHDLFFAD GSTPTDAIVK EFLDICENAE GAIAVHCKAG LGRTGTLIAC YIMKHYRMTA 310 320 330 340 350 360 AETIAWVRIC RPGSVIGPQQ QFLVMKQTNL WLEGDYFRQK LKGQENGQHR AAFSKLLSGV 370 380 390 400 410 420 DDISINGVEN QDQQEPEPYS DDDEINGVTQ GDRLRALKSR RQSKTNAIPL TVILQSSVQS 430 440 450 460 CKTSEPNISG SAGITKRTTR SASRKSSVKS LSISRTKTVL R

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] [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]	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].
[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]	"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.
[12]	"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.

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.
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.

IPI

IPI00026976.
IPI00026977.
IPI00103560.
IPI00552176.
IPI00798000.

RefSeq

NP_001070649.1. NM_001077181.1.
NP_003662.1. NM_003671.3.
NP_201588.1. NM_033331.2.

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	[»]

ProteinModelPortal

O60729.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60729. 1 interaction.

STRING

9606.ENSP00000364389.

PTM databases

PhosphoSite

O60729.

Proteomic databases

PaxDb

O60729.

PRIDE

O60729.

Protocols and materials databases

DNASU

8555.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265659; ENSP00000265659; ENSG00000081377.
ENST00000375236; ENSP00000364384; ENSG00000081377.
ENST00000375240; ENSP00000364388; ENSG00000081377.
ENST00000375241; ENSP00000364389; ENSG00000081377.
ENST00000375242; ENSP00000364390; ENSG00000081377.
ENST00000463569; ENSP00000420572; ENSG00000081377.
ENST00000474602; ENSP00000417897; ENSG00000081377.

GeneID

8555.

KEGG

hsa:8555.

UCSC

uc004awj.3. human.
uc004awk.3. human.

Organism-specific databases

CTD

8555.

GeneCards

GC09M099252.

HGNC

HGNC:1719. CDC14B.

HPA

HPA013312.

MIM

603505. gene.

neXtProt

NX_O60729.

PharmGKB

PA26255.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000198341.

HOVERGEN

HBG050818.

InParanoid

O60729.

KO

K06639.

OMA

YIPYFKN.

OrthoDB

EOG4QVCBW.

PhylomeDB

O60729.

Gene expression databases

ArrayExpress

O60729.

Bgee

O60729.

CleanEx

HS_CDC14B.

Genevestigator

O60729.

GermOnline

ENSG00000081377. Homo sapiens.

Family and domain databases

InterPro

IPR000340. 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]

PANTHER

PTHR23339:SF27. PTHR23339:SF27. 1 hit.

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

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Other

EvolutionaryTrace

O60729.

GenomeRNAi

8555.

NextBio

32057.

SOURCE

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Entry information

Entry name

CC14B_HUMAN

Accession

Primary (citable) accession number: O60729
Secondary accession number(s): A6N5X8 , A8MQ20, B1AL31, B1AL32, O43183, O60730, Q5JU08

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.