CC14C_HUMAN
ID CC14C_HUMAN Reviewed; 447 AA.
AC A4D256; Q2VIP7; Q6NUS3; Q8NCT2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Dual specificity protein phosphatase CDC14C {ECO:0000305};
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDC14 cell division cycle 14 homolog C;
GN Name=CDC14C {ECO:0000312|HGNC:HGNC:22427};
GN Synonyms=CDC14B2 {ECO:0000303|PubMed:16201836}, CDC14Bretro;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-429.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18547142; DOI=10.1371/journal.pbio.0060140;
RA Rosso L., Marques A.C., Weier M., Lambert N., Lambot M.A.,
RA Vanderhaeghen P., Kaessmann H.;
RT "Birth and rapid subcellular adaptation of a hominoid-specific CDC14
RT protein.";
RL PLoS Biol. 6:E140-E140(2008).
CC -!- FUNCTION: Dual-specificity phosphatase. Preferentially dephosphorylates
CC proteins modified by proline-directed kinases (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18547142}; Single-pass membrane protein
CC {ECO:0000255}. Note=Retains its endoplasmic reticulum localization
CC during mitosis. {ECO:0000269|PubMed:18547142}.
CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that
CC adopt a dual specificity protein phosphatase (DSP) fold.
CC -!- MISCELLANEOUS: May act as an autosomal functional substitute.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB92421.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAL23906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236955; EAL23906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC028690; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC068452; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ120635; ABB92421.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A4D256; -.
DR SMR; A4D256; -.
DR IntAct; A4D256; 1.
DR MINT; A4D256; -.
DR DEPOD; CDC14C; -.
DR iPTMnet; A4D256; -.
DR PhosphoSitePlus; A4D256; -.
DR BioMuta; HGNC:22427; -.
DR MassIVE; A4D256; -.
DR PeptideAtlas; A4D256; -.
DR PRIDE; A4D256; -.
DR ProteomicsDB; 639; -.
DR Antibodypedia; 82404; 1 antibodies from 1 providers.
DR Ensembl; ENST00000650262.2; ENSP00000497792.1; ENSG00000218305.5.
DR MANE-Select; ENST00000650262.2; ENSP00000497792.1; NM_152627.3; NP_689840.2.
DR GeneCards; CDC14C; -.
DR HGNC; HGNC:22427; CDC14C.
DR HPA; ENSG00000218305; Group enriched (retina, testis).
DR neXtProt; NX_A4D256; -.
DR VEuPathDB; HostDB:ENSG00000218305; -.
DR GeneTree; ENSGT00940000155950; -.
DR InParanoid; A4D256; -.
DR OMA; GRENGPH; -.
DR PhylomeDB; A4D256; -.
DR PathwayCommons; A4D256; -.
DR ChiTaRS; CDC14C; human.
DR Pharos; A4D256; Tdark.
DR PRO; PR:A4D256; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A4D256; protein.
DR Bgee; ENSG00000218305; Expressed in sperm and 14 other tissues.
DR ExpressionAtlas; A4D256; baseline and differential.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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 Endoplasmic reticulum; Hydrolase; Membrane; Protein phosphatase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..447
FT /note="Dual specificity protein phosphatase CDC14C"
FT /id="PRO_0000315822"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 184..344
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 14..168
FT /note="A"
FT /evidence="ECO:0000250"
FT REGION 169..182
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 183..349
FT /note="B"
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VARIANT 131
FT /note="P -> S (in dbSNP:rs1615556)"
FT /id="VAR_038327"
FT VARIANT 189
FT /note="I -> L (in dbSNP:rs421206)"
FT /id="VAR_038328"
FT CONFLICT 12
FT /note="R -> W (in Ref. 2; EAL23906)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="V -> L (in Ref. 3; BC028690 and 2; EAL23906)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> K (in Ref. 2; EAL23906)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="S -> G (in Ref. 3; BC068452, 4; ABB92421 and 2;
FT EAL23906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 51614 MW; 962ACC30F1C6D3EF CRC64;
MRSSTLQDPR RRDPQDDVYV DITDRLRFAI LYSRPKSASN VHYFSIDNEL EYENFSEDFG
PLNLAMVYRY CCKINKKLKS ITMLRKKIVH FTGSDQRKQA NAAFLVGCYM VIYLGRTPEA
AYRILIFGDT PYIPFRDAAY GSCNFYITLL DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK
AENGDLNWII PDRFIAFCGP HSRARLESGY HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA
KRFTDAGFDH HDLFFADGST PTDAIVKRFL DICENAEGAI AVHCKAGLGR TGTLIACYIM
KHYRMTAAET IAWVRICRPG LVIGPQQQFL VMKQTSLWLE GDYFRQRLKG QENGQHRAAF
SKLLSGVDDI SINGVENQDQ QEPKPYSDDD EINGVTQGDR SRALKRRRQS KTNDILLPSP
LAVLTFTLCS VVIWWIVCDY ILPILLF
