ID   MPLKI_HUMAN             Reviewed;         179 AA.
AC   Q8TAP9;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=M-phase-specific PLK1-interacting protein;
DE   AltName: Full=TTD non-photosensitive 1 protein;
GN   Name=MPLKIP; Synonyms=C7orf11, TTDN1;
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 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   [2]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=11829489; DOI=10.1006/geno.2002.6695;
RA   Nakabayashi K., Fernandez B.A., Teshima I., Shuman C., Proud V.K.,
RA   Curry C.J., Chitayat D., Grebe T., Ming J., Oshimura M., Meguro M.,
RA   Mitsuya K., Deb-Rinker P., Herbrick J.A., Weksberg R., Scherer S.W.;
RT   "Molecular genetic studies of human chromosome 7 in Russell-Silver
RT   syndrome.";
RL   Genomics 79:186-196(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [4]
RP   FUNCTION, INTERACTION WITH PLK1, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   SER-93; SER-104 AND THR-120, AND PHOSPHORYLATION AT SER-93 AND SER-104.
RX   PubMed=17310276; DOI=10.1007/s00018-007-6501-8;
RA   Zhang Y., Tian Y., Chen Q., Chen D., Zhai Z., Shu H.-B.;
RT   "TTDN1 is a Plk1-interacting protein involved in maintenance of cell cycle
RT   integrity.";
RL   Cell. Mol. Life Sci. 64:632-640(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-133, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-51; SER-80; SER-93;
RP   SER-104; THR-120 AND SER-124, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-80; SER-82 AND
RP   SER-133, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-47; THR-51; SER-80;
RP   SER-115 AND SER-124, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-57; ARG-59; ARG-68; ARG-77 AND
RP   ARG-117, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [10]
RP   VARIANT TTD4 VAL-144, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15645389; DOI=10.1086/428141;
RA   Nakabayashi K., Amann D., Ren Y., Saarialho-Kere U., Avidan N., Gentles S.,
RA   MacDonald J.R., Puffenberger E.G., Christiano A.M., Martinez-Mir A.,
RA   Salas-Alanis J.C., Rizzo R., Vamos E., Raams A., Les C., Seboun E.,
RA   Jaspers N.G.J., Beckmann J.S., Jackson C.E., Scherer S.W.;
RT   "Identification of C7orf11 (TTDN1) gene mutations and genetic heterogeneity
RT   in nonphotosensitive trichothiodystrophy.";
RL   Am. J. Hum. Genet. 76:510-516(2005).
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-29.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May play a role in maintenance of cell cycle integrity by
CC       regulating mitosis or cytokinesis. {ECO:0000269|PubMed:17310276}.
CC   -!- SUBUNIT: Interacts with PLK1; phosphorylation-dependent.
CC       {ECO:0000269|PubMed:17310276}.
CC   -!- INTERACTION:
CC       Q8TAP9; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11603426, EBI-357530;
CC       Q8TAP9; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-11603426, EBI-739467;
CC       Q8TAP9; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11603426, EBI-741158;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome. Note=The subcellular
CC       location is regulated during cell cycle. During interphase located in
CC       the nucleus. During mitosis located at the centrosome and dispersed in
CC       the cytoplasm. During telophase located in the midbody. Colocalizes
CC       with PLK1 at the centrosome in M phase.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in liver and kidney;
CC       intermediate expression in skeletal muscle, pancreas, heart and
CC       placenta; low expression in brain and lung. Expressed in epidermis and
CC       hair follicles. {ECO:0000269|PubMed:11829489,
CC       ECO:0000269|PubMed:15645389}.
CC   -!- PTM: Phosphorylated during mitosis in the cell cycle probably by CDK1.
CC       {ECO:0000269|PubMed:17310276}.
CC   -!- DISEASE: Trichothiodystrophy 4, non-photosensitive (TTD4) [MIM:234050]:
CC       A form of trichothiodystrophy, an autosomal recessive disease
CC       characterized by sulfur-deficient brittle hair and multisystem variable
CC       abnormalities. The spectrum of clinical features varies from mild
CC       disease with only hair involvement to severe disease with cutaneous,
CC       neurologic and profound developmental defects. Ichthyosis, intellectual
CC       and developmental disabilities, decreased fertility, abnormal
CC       characteristics at birth, ocular abnormalities, short stature, and
CC       infections are common manifestations. There are both photosensitive and
CC       non-photosensitive forms of the disorder. TTD4 patients do not manifest
CC       cutaneous photosensitivity. {ECO:0000269|PubMed:15645389}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
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DR   EMBL; BC026265; AAH26265.1; -; mRNA.
DR   CCDS; CCDS5463.1; -.
DR   RefSeq; NP_619646.1; NM_138701.3.
DR   AlphaFoldDB; Q8TAP9; -.
DR   BioGRID; 126463; 36.
DR   IntAct; Q8TAP9; 6.
DR   STRING; 9606.ENSP00000304553; -.
DR   iPTMnet; Q8TAP9; -.
DR   PhosphoSitePlus; Q8TAP9; -.
DR   BioMuta; MPLKIP; -.
DR   DMDM; 71153365; -.
DR   EPD; Q8TAP9; -.
DR   jPOST; Q8TAP9; -.
DR   MassIVE; Q8TAP9; -.
DR   MaxQB; Q8TAP9; -.
DR   PaxDb; 9606-ENSP00000304553; -.
DR   PeptideAtlas; Q8TAP9; -.
DR   ProteomicsDB; 73905; -.
DR   Pumba; Q8TAP9; -.
DR   Antibodypedia; 53252; 62 antibodies from 14 providers.
DR   DNASU; 136647; -.
DR   Ensembl; ENST00000306984.8; ENSP00000304553.5; ENSG00000168303.9.
DR   GeneID; 136647; -.
DR   KEGG; hsa:136647; -.
DR   MANE-Select; ENST00000306984.8; ENSP00000304553.5; NM_138701.4; NP_619646.1.
DR   UCSC; uc003thl.5; human.
DR   AGR; HGNC:16002; -.
DR   CTD; 136647; -.
DR   DisGeNET; 136647; -.
DR   GeneCards; MPLKIP; -.
DR   HGNC; HGNC:16002; MPLKIP.
DR   HPA; ENSG00000168303; Low tissue specificity.
DR   MalaCards; MPLKIP; -.
DR   MIM; 234050; phenotype.
DR   MIM; 609188; gene.
DR   neXtProt; NX_Q8TAP9; -.
DR   OpenTargets; ENSG00000168303; -.
DR   Orphanet; 33364; Trichothiodystrophy.
DR   PharmGKB; PA25943; -.
DR   VEuPathDB; HostDB:ENSG00000168303; -.
DR   eggNOG; ENOG502S6ND; Eukaryota.
DR   GeneTree; ENSGT00390000002582; -.
DR   HOGENOM; CLU_1510143_0_0_1; -.
DR   InParanoid; Q8TAP9; -.
DR   OMA; QTTCTGK; -.
DR   OrthoDB; 4496402at2759; -.
DR   PhylomeDB; Q8TAP9; -.
DR   TreeFam; TF335586; -.
DR   PathwayCommons; Q8TAP9; -.
DR   SignaLink; Q8TAP9; -.
DR   SIGNOR; Q8TAP9; -.
DR   BioGRID-ORCS; 136647; 28 hits in 1161 CRISPR screens.
DR   ChiTaRS; MPLKIP; human.
DR   GeneWiki; C7orf11; -.
DR   GeneWiki; MPLKIP; -.
DR   GenomeRNAi; 136647; -.
DR   Pharos; Q8TAP9; Tbio.
DR   PRO; PR:Q8TAP9; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q8TAP9; Protein.
DR   Bgee; ENSG00000168303; Expressed in kidney epithelium and 201 other cell types or tissues.
DR   ExpressionAtlas; Q8TAP9; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR026618; MPLKIP-like_vertebrate.
DR   InterPro; IPR028265; TTDN1/SICKLE.
DR   PANTHER; PTHR22446:SF3; M-PHASE-SPECIFIC PLK1-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR22446; UNCHARACTERIZED; 1.
DR   Pfam; PF15502; MPLKIP; 1.
DR   Genevisible; Q8TAP9; HS.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Disease variant;
KW   Methylation; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..179
FT                   /note="M-phase-specific PLK1-interacting protein"
FT                   /id="PRO_0000065674"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D011"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         51
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         57
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         59
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         68
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         77
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17310276,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17310276,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         117
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         120
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT   VARIANT         29
FT                   /note="G -> E (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs565833937)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036273"
FT   VARIANT         144
FT                   /note="M -> V (in TTD4; dbSNP:rs137853117)"
FT                   /evidence="ECO:0000269|PubMed:15645389"
FT                   /id="VAR_022940"
FT   MUTAGEN         93
FT                   /note="S->A: Partially prevents phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17310276"
FT   MUTAGEN         104
FT                   /note="S->A: Has no effect on interaction with PLK1 in
FT                   mitosis. Partially prevents phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:17310276"
FT   MUTAGEN         120
FT                   /note="T->A: Abolishes interaction with PLK1 in mitosis."
FT                   /evidence="ECO:0000269|PubMed:17310276"
SQ   SEQUENCE   179 AA;  19147 MW;  77DBA4FBDF9C70CC CRC64;
     MQRQNFRPPT PPYPGPGGGG WGSGSSFRGT PGGGGPRPPS PRDGYGSPHH TPPYGPRSRP
     YGSSHSPRHG GSFPGGRFGS PSPGGYPGSY SRSPAGSQQQ FGYSPGQQQT HPQGSPRTST
     PFGSGRVREK RMSNELENYF KPSMLEDPWA GLEPVSVVDI SQQYSNTQTF TGKKGRYFC
//