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M-phase inducer phosphatase 3 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25C)

 MPIP3_HUMAN             Reviewed;         473 AA.
P30307; D3DQB8; Q96PL3; Q9H168; Q9H2E8; Q9H2E9; Q9H2F1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 183.
RecName: Full=M-phase inducer phosphatase 3;
EC=3.1.3.48;
AltName: Full=Dual specificity phosphatase Cdc25C;
Name=CDC25C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-70.
PubMed=2195549; DOI=10.1073/pnas.87.13.5139;
Sadhu K., Reed B.I., Richardson H., Russell P.;
"Human homolog of fission yeast cdc25 mitotic inducer is predominantly
expressed in G2.";
Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=11078813;
Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M.,
Wagner P.;
"An additional transcript of the cdc25C gene from A431 cells encodes a
functional protein.";
Int. J. Oncol. 17:1251-1258(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
CYS-70.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-210 (ISOFORMS 2; 4 AND 5), AND
VARIANT CYS-70.
PubMed=11139144; DOI=10.1078/0171-9335-00115;
Wegener S., Hampe W., Herrmann D., Schaller H.C.;
"Alternative splicing in the regulatory region of the human
phosphatases CDC25A and CDC25C.";
Eur. J. Cell Biol. 79:810-815(2000).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Colon carcinoma;
PubMed=11304565; DOI=10.1038/labinvest.3780254;
Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C.,
Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E.;
"Differential expression of cdc25 cell-cycle-activating phosphatases
in human colorectal carcinoma.";
Lab. Invest. 81:465-473(2001).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-48; THR-67;
SER-122; THR-130; SER-168 AND SER-214.
PubMed=8119945;
Strausfeld U., Fernandez A., Capony J.P., Girard F., Lautredou N.,
Derancourt J., Labbe J.C., Lamb N.J.;
"Activation of p34cdc2 protein kinase by microinjection of human
cdc25C into mammalian cells. Requirement for prior phosphorylation of
cdc25C by p34cdc2 on sites phosphorylated at mitosis.";
J. Biol. Chem. 269:5989-6000(1994).
[9]
PHOSPHORYLATION BY PLK3.
PubMed=10557092; DOI=10.1038/sj.onc.1202983;
Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.;
"The physical association and phosphorylation of Cdc25C protein
phosphatase by Prk.";
Oncogene 18:6029-6036(1999).
[10]
PHOSPHORYLATION BY PLK1.
PubMed=11202906; DOI=10.1016/S0898-6568(00)00080-2;
Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G.,
Marshall L.A.;
"The human polo-like kinase, PLK, regulates cdc2/cyclin B through
phosphorylation and activation of the cdc25C phosphatase.";
Cell. Signal. 12:405-411(2000).
[11]
PHOSPHORYLATION AT SER-216, AND INTERACTION WITH MAPK14 AND 14-3-3
PROTEINS.
PubMed=11333986; DOI=10.1038/35075107;
Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V.,
Potapova O., Appella E., Fornace A.J. Jr.;
"Initiation of a G2/M checkpoint after ultraviolet radiation requires
p38 kinase.";
Nature 411:102-107(2001).
[12]
INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-129 AND THR-130, AND
MUTAGENESIS OF SER-129 AND THR-130.
PubMed=12595692; DOI=10.1126/science.1079079;
Elia A.E., Cantley L.C., Yaffe M.B.;
"Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to
mitotic substrates.";
Science 299:1228-1231(2003).
[13]
PHOSPHORYLATION AT SER-216.
TISSUE=Testis;
PubMed=15150265; DOI=10.1074/jbc.M404728200;
Lu R., Niida H., Nakanishi M.;
"Human SAD1 kinase is involved in UV-induced DNA damage checkpoint
function.";
J. Biol. Chem. 279:31164-31170(2004).
[14]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, AND
MUTAGENESIS OF SER-191.
PubMed=14968113; DOI=10.1038/sj.onc.1207425;
Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.;
"Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear
translocation.";
Oncogene 23:2658-2663(2004).
[15]
INTERACTION WITH HIV-1 VPR, AND MUTAGENESIS OF GLU-352 AND LYS-359.
PubMed=14972559; DOI=10.1016/j.virol.2003.10.007;
Goh W.C., Manel N., Emerman M.;
"The human immunodeficiency virus Vpr protein binds Cdc25C:
implications for G2 arrest.";
Virology 318:337-349(2004).
[16]
PHOSPHORYLATION AT SER-216 BY MAPKAPK2.
PubMed=15629715; DOI=10.1016/j.molcel.2004.11.021;
Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.;
"MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the
G2/M transition and S phase progression in response to UV
irradiation.";
Mol. Cell 17:37-48(2005).
[17]
PHOSPHORYLATION BY PLK4.
PubMed=18239451; DOI=10.4161/cc.7.4.5387;
Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.;
"Human Plk4 phosphorylates Cdc25C.";
Cell Cycle 7:545-547(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-168 AND SER-472,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 (ISOFORMS 4 AND 5),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-48; SER-57;
SER-61; SER-64 AND THR-67, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-64 AND THR-67,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-38 AND SER-216,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Functions as a dosage-dependent inducer in mitotic
control. Tyrosine protein phosphatase required for progression of
the cell cycle. When phosphorylated, highly effective in
activating G2 cells into prophase. Directly dephosphorylates CDK1
and activates its kinase activity. {ECO:0000269|PubMed:8119945}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- SUBUNIT: Interacts with HIV-1 Vpr, thereby inactivating CDC25C
phosphatase activity. Interacts with MAPK14 and 14-3-3 proteins.
When phosphorylated on Ser-129 and/or Thr-130, interacts with
PLK1. {ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:12595692,
ECO:0000269|PubMed:14972559}.
-!- INTERACTION:
P06493:CDK1; NbExp=2; IntAct=EBI-974439, EBI-444308;
O14757:CHEK1; NbExp=2; IntAct=EBI-974439, EBI-974488;
Q9Y250:LZTS1; NbExp=2; IntAct=EBI-974439, EBI-1216080;
P53350:PLK1; NbExp=5; IntAct=EBI-974439, EBI-476768;
P31946:YWHAB; NbExp=4; IntAct=EBI-974439, EBI-359815;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14968113,
ECO:0000269|PubMed:8119945}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=CDC25C1;
IsoId=P30307-1; Sequence=Displayed;
Name=2; Synonyms=CDC25C2;
IsoId=P30307-2; Sequence=VSP_000864;
Name=3; Synonyms=CDC25C3;
IsoId=P30307-5; Sequence=Not described;
Name=4; Synonyms=CDC25C4;
IsoId=P30307-3; Sequence=VSP_000863;
Note=Contains a phosphoserine at position 61.
{ECO:0000244|PubMed:18691976};
Name=5; Synonyms=CDC25C5, Cdc25Cdm;
IsoId=P30307-4; Sequence=VSP_000863, VSP_000864;
Note=Contains a phosphoserine at position 61.
{ECO:0000244|PubMed:18691976};
-!- DEVELOPMENTAL STAGE: Expressed predominantly in G2 phase.
-!- PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-216. This
phosphorylation creates a binding site for 14-3-3 protein and
inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated
by PLK1, leading to activate the phosphatase activity.
Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation.
Ser-198 is a minor phosphorylation site. Was initially reported to
be phosphorylated by PLK3 at Ser-216 (PubMed:10557092). However,
such phosphorylation by PLK3 was not confirmed by other groups.
Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and
Ser-214 occurs at G2 and G2-M transition and is probably catalyzed
by CDK1. Ser-168 phosphorylation levels are lower than those at
the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased
activity. {ECO:0000269|PubMed:10557092,
ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:11333986,
ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:15150265,
ECO:0000269|PubMed:15629715, ECO:0000269|PubMed:18239451,
ECO:0000269|PubMed:8119945}.
-!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc25c/";
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EMBL; M34065; AAA35666.1; -; mRNA.
EMBL; AJ304504; CAC19192.1; -; mRNA.
EMBL; AY497474; AAR32098.1; -; Genomic_DNA.
EMBL; CH471062; EAW62145.1; -; Genomic_DNA.
EMBL; CH471062; EAW62149.1; -; Genomic_DNA.
EMBL; BC019089; AAH19089.1; -; mRNA.
EMBL; AF277723; AAG41885.1; -; mRNA.
EMBL; AF277725; AAG41887.1; -; mRNA.
EMBL; AF277726; AAG41888.1; -; mRNA.
EMBL; AF312681; AAL26835.1; -; mRNA.
CCDS; CCDS4202.1; -. [P30307-1]
CCDS; CCDS4203.1; -. [P30307-4]
PIR; I59168; A38874.
RefSeq; NP_001274511.1; NM_001287582.1. [P30307-1]
RefSeq; NP_001305027.1; NM_001318098.1.
RefSeq; NP_001781.2; NM_001790.4. [P30307-1]
RefSeq; NP_073720.1; NM_022809.3. [P30307-4]
RefSeq; XP_011542064.1; XM_011543762.1. [P30307-4]
UniGene; Hs.656; -.
PDB; 2OJX; X-ray; 2.85 A; E=126-134.
PDB; 3BZI; X-ray; 2.10 A; E=126-134.
PDB; 3OP3; X-ray; 2.63 A; A=270-462.
PDB; 5JIT; X-ray; 2.38 A; C/D=207-244.
PDB; 5JIV; X-ray; 2.45 A; C/D=207-244.
PDBsum; 2OJX; -.
PDBsum; 3BZI; -.
PDBsum; 3OP3; -.
PDBsum; 5JIT; -.
PDBsum; 5JIV; -.
ProteinModelPortal; P30307; -.
SMR; P30307; -.
BioGrid; 107430; 103.
DIP; DIP-24183N; -.
IntAct; P30307; 18.
MINT; MINT-86355; -.
STRING; 9606.ENSP00000321656; -.
BindingDB; P30307; -.
ChEMBL; CHEMBL2378; -.
DEPOD; P30307; -.
iPTMnet; P30307; -.
PhosphoSitePlus; P30307; -.
BioMuta; CDC25C; -.
DMDM; 116242631; -.
PaxDb; P30307; -.
PeptideAtlas; P30307; -.
PRIDE; P30307; -.
DNASU; 995; -.
Ensembl; ENST00000323760; ENSP00000321656; ENSG00000158402. [P30307-1]
Ensembl; ENST00000348983; ENSP00000345205; ENSG00000158402. [P30307-4]
Ensembl; ENST00000415130; ENSP00000392631; ENSG00000158402. [P30307-4]
Ensembl; ENST00000513970; ENSP00000424795; ENSG00000158402. [P30307-1]
Ensembl; ENST00000514555; ENSP00000425470; ENSG00000158402. [P30307-2]
GeneID; 995; -.
KEGG; hsa:995; -.
UCSC; uc003lcp.3; human. [P30307-1]
CTD; 995; -.
DisGeNET; 995; -.
EuPathDB; HostDB:ENSG00000158402.18; -.
GeneCards; CDC25C; -.
HGNC; HGNC:1727; CDC25C.
HPA; CAB003800; -.
HPA; HPA066991; -.
MIM; 157680; gene.
neXtProt; NX_P30307; -.
OpenTargets; ENSG00000158402; -.
PharmGKB; PA100; -.
eggNOG; KOG3772; Eukaryota.
eggNOG; COG5105; LUCA.
GeneTree; ENSGT00390000018747; -.
HOVERGEN; HBG052501; -.
InParanoid; P30307; -.
KO; K05867; -.
OMA; TVSLCDI; -.
OrthoDB; EOG091G0H0D; -.
PhylomeDB; P30307; -.
TreeFam; TF101056; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
SIGNOR; P30307; -.
ChiTaRS; CDC25C; human.
EvolutionaryTrace; P30307; -.
GeneWiki; CDC25C; -.
GenomeRNAi; 995; -.
PRO; PR:P30307; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000158402; -.
CleanEx; HS_CDC25C; -.
ExpressionAtlas; P30307; baseline and differential.
Genevisible; P30307; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; NAS:UniProtKB.
GO; GO:0050699; F:WW domain binding; IPI:BHF-UCL.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IGI:UniProtKB.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:ProtInc.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd01530; Cdc25; 1.
Gene3D; 3.40.250.10; -; 1.
InterPro; IPR000751; MPI_Phosphatase.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
Pfam; PF06617; M-inducer_phosp; 1.
Pfam; PF00581; Rhodanese; 1.
PRINTS; PR00716; MPIPHPHTASE.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Complete proteome; Host-virus interaction; Hydrolase;
Mitosis; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 473 M-phase inducer phosphatase 3.
/FTId=PRO_0000198647.
DOMAIN 321 428 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
REGION 334 379 HIV-1 Vpr binding site.
ACT_SITE 377 377 {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 48 48 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:8119945}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 67 67 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:8119945}.
MOD_RES 122 122 Phosphoserine; by CDK1.
{ECO:0000305|PubMed:8119945}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000269|PubMed:12595692}.
MOD_RES 130 130 Phosphothreonine.
{ECO:0000269|PubMed:12595692}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:8119945}.
MOD_RES 191 191 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:14968113}.
MOD_RES 198 198 Phosphoserine; by PLK3.
{ECO:0000269|PubMed:14968113}.
MOD_RES 214 214 Phosphoserine; by CDK1.
{ECO:0000305|PubMed:8119945}.
MOD_RES 216 216 Phosphoserine; by CHEK1, CHEK2, BRSK1 and
MAPK14. {ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11333986,
ECO:0000269|PubMed:15150265,
ECO:0000269|PubMed:15629715}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 66 123 GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQE
VHLAGMNHDQHLMKCSP -> SPGFFRTSGSAFSWD (in
isoform 4 and isoform 5).
{ECO:0000303|PubMed:11078813,
ECO:0000303|PubMed:11139144}.
/FTId=VSP_000863.
VAR_SEQ 124 153 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:11078813,
ECO:0000303|PubMed:11139144}.
/FTId=VSP_000864.
VARIANT 14 14 S -> N (in dbSNP:rs11567959).
/FTId=VAR_027922.
VARIANT 70 70 R -> C (in dbSNP:rs3734166).
{ECO:0000269|PubMed:11139144,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2195549}.
/FTId=VAR_027923.
VARIANT 78 78 S -> N (in dbSNP:rs11567962).
/FTId=VAR_027924.
VARIANT 297 297 G -> R (in dbSNP:rs11567997).
/FTId=VAR_020146.
MUTAGEN 129 129 S->V: Loss of phosphorylation. Severely
impairs PLK1-binding.
{ECO:0000269|PubMed:12595692}.
MUTAGEN 130 130 T->A: Loss of phosphorylation. Severely
impairs PLK1-binding.
{ECO:0000269|PubMed:12595692}.
MUTAGEN 191 191 S->A: Facilitates nuclear exclusion.
{ECO:0000269|PubMed:14968113}.
MUTAGEN 191 191 S->D: Mimicks phosphorylation state,
leading to enhanced accumulation in the
nucleus. {ECO:0000269|PubMed:14968113}.
MUTAGEN 352 352 E->K: Partial loss of HIV-1 Vpr binding.
{ECO:0000269|PubMed:14972559}.
MUTAGEN 359 359 K->E: No effect on HIV-1 Vpr binding.
{ECO:0000269|PubMed:14972559}.
STRAND 127 129 {ECO:0000244|PDB:3BZI}.
STRAND 286 289 {ECO:0000244|PDB:3OP3}.
STRAND 300 305 {ECO:0000244|PDB:3OP3}.
HELIX 307 314 {ECO:0000244|PDB:3OP3}.
TURN 315 321 {ECO:0000244|PDB:3OP3}.
STRAND 322 329 {ECO:0000244|PDB:3OP3}.
HELIX 333 337 {ECO:0000244|PDB:3OP3}.
STRAND 339 341 {ECO:0000244|PDB:3OP3}.
HELIX 350 357 {ECO:0000244|PDB:3OP3}.
STRAND 369 376 {ECO:0000244|PDB:3OP3}.
HELIX 384 397 {ECO:0000244|PDB:3OP3}.
STRAND 409 412 {ECO:0000244|PDB:3OP3}.
HELIX 415 419 {ECO:0000244|PDB:3OP3}.
TURN 420 422 {ECO:0000244|PDB:3OP3}.
HELIX 424 426 {ECO:0000244|PDB:3OP3}.
STRAND 427 430 {ECO:0000244|PDB:3OP3}.
STRAND 438 440 {ECO:0000244|PDB:3OP3}.
SEQUENCE 473 AA; 53365 MW; 0658A1F1B9B8996A CRC64;
MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL
SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK
CSPAQLLCST PNGLDRGHRK RDAMCSSSAN KENDNGNLVD SEMKYLGSPI TTVPKLDKNP
NLGEDQAEEI SDELMEFSLK DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK
VKKKYFSGQG KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ
DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ EELFNFFLKK
PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ YPALYYPELY ILKGGYRDFF
PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ SKVQEGERQL REQIALLVKD MSP


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