CC14B_MOUSE
ID CC14B_MOUSE Reviewed; 485 AA.
AC Q6PFY9; Q80WC4; Q8BLV5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Dual specificity protein phosphatase CDC14B;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDC14 cell division cycle 14 homolog B;
GN Name=Cdc14b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Dual-specificity phosphatase involved in DNA damage response.
CC Essential regulator of the G2 DNA damage checkpoint: following DNA
CC damage, translocates to the nucleus and dephosphorylates FZR1/CDH1, a
CC key activator of the anaphase promoting complex/cyclosome (APC/C).
CC Dephosphorylates SIRT2 around early anaphase. Dephosphorylation of
CC FZR1/CDH1 activates the APC/C, leading to the ubiquitination of PLK1,
CC preventing entry into mitosis. Preferentially dephosphorylates proteins
CC modified by proline-directed kinases (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with FZR1/CDH1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}. Note=Following DNA damage, translocates from
CC the nucleolus to the nucleoplasm and interacts with FZR1/CDH1.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PFY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PFY9-2; Sequence=VSP_012325;
CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that
CC adopt a dual specificity protein phosphatase (DSP) fold.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK041155; BAC30842.1; -; mRNA.
DR EMBL; BC049794; AAH49794.1; -; mRNA.
DR EMBL; BC057357; AAH57357.1; -; mRNA.
DR CCDS; CCDS26598.1; -. [Q6PFY9-1]
DR CCDS; CCDS49292.1; -. [Q6PFY9-2]
DR RefSeq; NP_001116461.1; NM_001122989.1. [Q6PFY9-2]
DR RefSeq; NP_766175.3; NM_172587.3. [Q6PFY9-1]
DR AlphaFoldDB; Q6PFY9; -.
DR SMR; Q6PFY9; -.
DR STRING; 10090.ENSMUSP00000046003; -.
DR PhosphoSitePlus; Q6PFY9; -.
DR PaxDb; Q6PFY9; -.
DR PeptideAtlas; Q6PFY9; -.
DR PRIDE; Q6PFY9; -.
DR ProteomicsDB; 265696; -. [Q6PFY9-1]
DR ProteomicsDB; 265697; -. [Q6PFY9-2]
DR DNASU; 218294; -.
DR Ensembl; ENSMUST00000039318; ENSMUSP00000046003; ENSMUSG00000033102. [Q6PFY9-1]
DR Ensembl; ENSMUST00000109769; ENSMUSP00000105391; ENSMUSG00000033102. [Q6PFY9-2]
DR Ensembl; ENSMUST00000109770; ENSMUSP00000105392; ENSMUSG00000033102. [Q6PFY9-1]
DR Ensembl; ENSMUST00000221139; ENSMUSP00000152843; ENSMUSG00000033102. [Q6PFY9-1]
DR GeneID; 218294; -.
DR KEGG; mmu:218294; -.
DR UCSC; uc007qym.2; mouse. [Q6PFY9-1]
DR UCSC; uc007qyo.2; mouse. [Q6PFY9-2]
DR CTD; 8555; -.
DR MGI; MGI:2441808; Cdc14b.
DR VEuPathDB; HostDB:ENSMUSG00000033102; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00940000155950; -.
DR HOGENOM; CLU_017787_2_0_1; -.
DR InParanoid; Q6PFY9; -.
DR OMA; GRENGPH; -.
DR OrthoDB; 1357618at2759; -.
DR PhylomeDB; Q6PFY9; -.
DR TreeFam; TF101053; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR BioGRID-ORCS; 218294; 1 hit in 108 CRISPR screens.
DR ChiTaRS; Cdc14b; mouse.
DR PRO; PR:Q6PFY9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6PFY9; protein.
DR Bgee; ENSMUSG00000033102; Expressed in manus and 222 other tissues.
DR ExpressionAtlas; Q6PFY9; baseline and differential.
DR Genevisible; Q6PFY9; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA repair; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..485
FT /note="Dual specificity protein phosphatase CDC14B"
FT /id="PRO_0000094879"
FT DOMAIN 215..374
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..198
FT /note="A"
FT REGION 199..212
FT /note="Linker"
FT REGION 213..379
FT /note="B"
FT REGION 402..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..54
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..53
FT /note="MKRKSERRSAWATAPPCSRRSSSSSPGVKKSRSSTPQELHRLEQQDDLYLDI
FT T -> MRREGAGTPLMAEVIR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012325"
FT CONFLICT 136
FT /note="V -> I (in Ref. 2; AAH49794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55661 MW; 8963E14648FC89DA CRC64;
MKRKSERRSA WATAPPCSRR SSSSSPGVKK SRSSTPQELH RLEQQDDLYL DITDRLCFAI
LYSRPKSATN EHYFSIDNEL EYENFYADFG PLNLAMVYRY CCKINKKLKS ITMLRKKIIH
FTGTDQRKQA NAAFLVGCYM VIYLGRTPED AYRTLIFGDT AYIPFRDAAY GSCSFYITLL
DCFHAVKKAM QYGFFNFNSF NLDEYEHYEK AENGDFNWII PERFLAFCGP HSRSRLESGY
HQHSPETYIP YFKNHNVTTI IRLNKRMYDA KRFTDAGFDH HDLFFPDGST PAESIVQEFL
DICENVKGAI AVHCKAGLGR TGTLIGCYLM KHYRMTAAES IAWLRICRPG SVIGPQQQFL
VMKQSSLWLE GDYFRQKLRG QENGPLREAF SKHLSDADDL SLNGLENQDN QEPEPYSDDD
EVSGMTQGDR LRALKSRRQP KASAIPLTCP LAVLTSALCS VAIWWIVCDY ILPTLLFCLD
GFRTQ
