MPLKI_HUMAN
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 03-AUG-2022, entry version 140.
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; 34.
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; Q8TAP9; -.
DR PeptideAtlas; Q8TAP9; -.
DR PRIDE; Q8TAP9; -.
DR ProteomicsDB; 73905; -.
DR Antibodypedia; 53252; 60 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 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; WSGQFRR; -.
DR OrthoDB; 1543160at2759; -.
DR PhylomeDB; Q8TAP9; -.
DR TreeFam; TF335586; -.
DR PathwayCommons; Q8TAP9; -.
DR SignaLink; Q8TAP9; -.
DR SIGNOR; Q8TAP9; -.
DR BioGRID-ORCS; 136647; 24 hits in 1086 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 199 other tissues.
DR ExpressionAtlas; Q8TAP9; baseline and differential.
DR Genevisible; Q8TAP9; HS.
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; PTHR22446; 1.
DR Pfam; PF15502; MPLKIP; 1.
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
