TEX14_MOUSE
ID TEX14_MOUSE Reviewed; 1450 AA.
AC Q7M6U3; B2KGL0; Q3UT36; Q5NC10; Q5NC11; Q8CGK1; Q8CGK2; Q99MV8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Inactive serine/threonine-protein kinase TEX14;
DE AltName: Full=Testis-expressed sequence 14;
DE AltName: Full=Testis-expressed sequence 14 protein;
GN Name=Tex14;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-227 (ISOFORM 1), IDENTIFICATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=12711554; DOI=10.1016/s1567-133x(03)00036-x;
RA Wu M.-H., Rajkovic A., Burns K.H., Yan W., Lin Y.-N., Matzuk M.M.;
RT "Sequence and expression of testis-expressed gene 14 (Tex14): a gene
RT encoding a protein kinase preferentially expressed during
RT spermatogenesis.";
RL Gene Expr. Patterns 3:231-236(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-1396.
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [5]
RP FUNCTION, ABSENCE OF PROTEIN KINASE ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16549803; DOI=10.1073/pnas.0505123103;
RA Greenbaum M.P., Yan W., Wu M.H., Lin Y.N., Agno J.E., Sharma M.,
RA Braun R.E., Rajkovic A., Matzuk M.M.;
RT "TEX14 is essential for intercellular bridges and fertility in male mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4982-4987(2006).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KIF23.
RX PubMed=17383626; DOI=10.1016/j.ydbio.2007.02.025;
RA Greenbaum M.P., Ma L., Matzuk M.M.;
RT "Conversion of midbodies into germ cell intercellular bridges.";
RL Dev. Biol. 305:389-396(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19020301; DOI=10.1095/biolreprod.108.070649;
RA Greenbaum M.P., Iwamori N., Agno J.E., Matzuk M.M.;
RT "Mouse TEX14 is required for embryonic germ cell intercellular bridges but
RT not female fertility.";
RL Biol. Reprod. 80:449-457(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-1060; SER-1221;
RP SER-1357; SER-1358; SER-1412 AND SER-1449, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP55, AND MUTAGENESIS OF
RP GLY-791; PRO-792 AND TYR-797.
RX PubMed=20176808; DOI=10.1128/mcb.01392-09;
RA Iwamori T., Iwamori N., Ma L., Edson M.A., Greenbaum M.P., Matzuk M.M.;
RT "TEX14 interacts with CEP55 to block cell abscission.";
RL Mol. Cell. Biol. 30:2280-2292(2010).
RN [10]
RP INTERACTION WITH RBM44.
RX PubMed=21364893; DOI=10.1371/journal.pone.0017066;
RA Iwamori T., Lin Y.N., Ma L., Iwamori N., Matzuk M.M.;
RT "Identification and characterization of RBM44 as a novel intercellular
RT bridge protein.";
RL PLoS ONE 6:E17066-E17066(2011).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22245112; DOI=10.1016/j.mod.2011.12.005;
RA Mork L., Tang H., Batchvarov I., Capel B.;
RT "Mouse germ cell clusters form by aggregation as well as clonal
RT divisions.";
RL Mech. Dev. 128:591-596(2012).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-431, AND MUTAGENESIS
RP OF SER-431 AND 889-ARG--ASN-897.
RX PubMed=22405274; DOI=10.1016/j.molcel.2012.01.013;
RA Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.;
RT "Tex14, a plk1-regulated protein, is required for kinetochore-microtubule
RT attachment and regulation of the spindle assembly checkpoint.";
RL Mol. Cell 45:680-695(2012).
CC -!- FUNCTION: Required both for the formation of intercellular bridges
CC during meiosis and for kinetochore-microtubule attachment during
CC mitosis. Intercellular bridges are evolutionarily conserved structures
CC that connect differentiating germ cells and are required for
CC spermatogenesis and male fertility. Acts by promoting the conversion of
CC midbodies into intercellular bridges via its interaction with CEP55:
CC interaction with CEP55 inhibits the interaction between CEP55 and
CC PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to
CC transform midbodies into intercellular bridges. Also plays a role
CC during mitosis: recruited to kinetochores by PLK1 during early mitosis
CC and regulates the maturation of the outer kinetochores and microtubule
CC attachment. Has no protein kinase activity in vitro.
CC {ECO:0000269|PubMed:16549803, ECO:0000269|PubMed:19020301,
CC ECO:0000269|PubMed:20176808, ECO:0000269|PubMed:22405274}.
CC -!- SUBUNIT: Interacts with KIF23 and RBM44. Interacts with CEP55;
CC inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101.
CC {ECO:0000269|PubMed:17383626, ECO:0000269|PubMed:20176808,
CC ECO:0000269|PubMed:21364893}.
CC -!- INTERACTION:
CC Q7M6U3; Q8BT07: Cep55; NbExp=11; IntAct=EBI-6674575, EBI-2552328;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Midbody. Chromosome, centromere,
CC kinetochore. Note=Detected in the intercellular bridges that connect
CC male germ cell daughter cells after cell division.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7M6U3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7M6U3-2; Sequence=VSP_019870;
CC -!- TISSUE SPECIFICITY: Detected in testis and spermatogonia. Not
CC detectable in the other tissues tested. {ECO:0000269|PubMed:11279525,
CC ECO:0000269|PubMed:12711554, ECO:0000269|PubMed:16549803}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in developing testis at 5
CC and 10 days after birth. Highly expressed in testis 15 and 20 days
CC after birth. Highly expressed in pachytene, diplotene and meiotically
CC dividing spermatocytes and in early round spermatids.
CC {ECO:0000269|PubMed:12711554}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DOMAIN: The GPPX3Y motif mediates interaction with CEP55.
CC {ECO:0000269|PubMed:20176808}.
CC -!- PTM: Phosphorylated on Thr residues by CDK1 during early phases of
CC mitosis, promoting the interaction with PLK1 and recruitment to
CC kinetochores. Phosphorylated on Ser-431 by PLK1 during late
CC prometaphase promotes the rapid depletion from kinetochores and its
CC subsequent degradation by the APC/C complex.
CC {ECO:0000269|PubMed:22405274}.
CC -!- DISRUPTION PHENOTYPE: Male mice are sterile, due to the absence of
CC intercellular bridges. Intercellular bridges do not form during
CC spermatogenesis, and male mice are sterile. In females, embryonic
CC intercellular bridges are also absent, mice have fewer oocytes, but
CC they are fertile. {ECO:0000269|PubMed:16549803,
CC ECO:0000269|PubMed:19020301}.
CC -!- MISCELLANEOUS: Used as a marker for intercellular bridges.
CC {ECO:0000305|PubMed:22245112}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Ser-370 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI35965.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF285584; AAK31963.1; -; mRNA.
DR EMBL; AL596086; CAI35127.1; -; Genomic_DNA.
DR EMBL; AL669902; CAI35127.1; JOINED; Genomic_DNA.
DR EMBL; AL669902; CAI35965.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL669902; CAI35966.1; -; Genomic_DNA.
DR EMBL; AL596086; CAI35966.1; JOINED; Genomic_DNA.
DR EMBL; CU406969; CAQ52018.1; -; Genomic_DNA.
DR EMBL; CU406988; CAQ52018.1; JOINED; Genomic_DNA.
DR EMBL; CU406988; CAQ52278.1; -; Genomic_DNA.
DR EMBL; CU406969; CAQ52278.1; JOINED; Genomic_DNA.
DR EMBL; AY193717; AAN86761.1; -; mRNA.
DR EMBL; AY193718; AAN86762.1; -; mRNA.
DR EMBL; BK000966; DAA01357.1; -; mRNA.
DR EMBL; BK000967; DAA01358.1; -; mRNA.
DR EMBL; AK139808; BAE24144.1; -; mRNA.
DR CCDS; CCDS48877.1; -. [Q7M6U3-1]
DR RefSeq; NP_001186222.1; NM_001199293.1.
DR RefSeq; NP_113563.2; NM_031386.2. [Q7M6U3-1]
DR AlphaFoldDB; Q7M6U3; -.
DR SMR; Q7M6U3; -.
DR BioGRID; 219946; 7.
DR ELM; Q7M6U3; -.
DR IntAct; Q7M6U3; 2.
DR STRING; 10090.ENSMUSP00000054444; -.
DR iPTMnet; Q7M6U3; -.
DR PhosphoSitePlus; Q7M6U3; -.
DR MaxQB; Q7M6U3; -.
DR PaxDb; Q7M6U3; -.
DR PeptideAtlas; Q7M6U3; -.
DR PRIDE; Q7M6U3; -.
DR ProteomicsDB; 259004; -. [Q7M6U3-1]
DR ProteomicsDB; 259005; -. [Q7M6U3-2]
DR Antibodypedia; 31015; 89 antibodies from 25 providers.
DR DNASU; 83560; -.
DR Ensembl; ENSMUST00000060835; ENSMUSP00000054444; ENSMUSG00000010342. [Q7M6U3-1]
DR GeneID; 83560; -.
DR KEGG; mmu:83560; -.
DR UCSC; uc007ktr.2; mouse. [Q7M6U3-1]
DR CTD; 56155; -.
DR MGI; MGI:1933227; Tex14.
DR VEuPathDB; HostDB:ENSMUSG00000010342; -.
DR eggNOG; ENOG502QSZN; Eukaryota.
DR GeneTree; ENSGT00390000015123; -.
DR HOGENOM; CLU_004733_0_0_1; -.
DR InParanoid; Q7M6U3; -.
DR OMA; LCFQFYL; -.
DR OrthoDB; 92703at2759; -.
DR PhylomeDB; Q7M6U3; -.
DR TreeFam; TF328704; -.
DR BioGRID-ORCS; 83560; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Tex14; mouse.
DR PRO; PR:Q7M6U3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7M6U3; protein.
DR Bgee; ENSMUSG00000010342; Expressed in spermatocyte and 61 other tissues.
DR ExpressionAtlas; Q7M6U3; baseline and differential.
DR Genevisible; Q7M6U3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0043063; P:intercellular bridge organization; IDA:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IDA:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR039339; Tex14.
DR PANTHER; PTHR23060; PTHR23060; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; ATP-binding; Cell cycle; Cell division;
KW Centromere; Chromosome; Cytoplasm; Kinetochore; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1450
FT /note="Inactive serine/threonine-protein kinase TEX14"
FT /id="PRO_0000246996"
FT REPEAT 27..54
FT /note="ANK 1"
FT REPEAT 55..84
FT /note="ANK 2"
FT REPEAT 88..117
FT /note="ANK 3"
FT DOMAIN 199..512
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 700..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 791..797
FT /note="GPPX3Y"
FT MOTIF 889..897
FT /note="D-box"
FT COMPBIAS 854..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 431
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:22405274"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11279525"
FT /id="VSP_019870"
FT MUTAGEN 431
FT /note="S->A: Reduced phosphorylation by PLK1 and abolishes
FT depletion from kinetochores and subsequent degradation by
FT the APC/C complex."
FT /evidence="ECO:0000269|PubMed:22405274"
FT MUTAGEN 431
FT /note="S->D,E: Mimicks phosphorylation state; inducing
FT early depletion from kinetochores and subsequent
FT degradation by the APC/C complex."
FT /evidence="ECO:0000269|PubMed:22405274"
FT MUTAGEN 791
FT /note="G->A: Does not affect interaction with CEP55."
FT /evidence="ECO:0000269|PubMed:20176808"
FT MUTAGEN 792
FT /note="P->A: Abolishes interaction with CEP55."
FT /evidence="ECO:0000269|PubMed:20176808"
FT MUTAGEN 797
FT /note="Y->A: Abolishes interaction with CEP55."
FT /evidence="ECO:0000269|PubMed:20176808"
FT MUTAGEN 889..897
FT /note="Missing: Prevents degradation during metaphase."
FT /evidence="ECO:0000269|PubMed:22405274"
FT CONFLICT 324
FT /note="T -> A (in Ref. 1; AAK31963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1450 AA; 162541 MW; 0628605EBE0FF0A4 CRC64;
MSRGAPFPVP CPVLLGTFTD DSLEAQLHEY AKQGNCVKLK KILKKGVCVD AVNTQGQSAL
FVAALLGHVK LVDVLVDYGS DPNHRCFDGS TPVHAAAFSG NQWILSKLLT AGGDLRLHDE
KGRNPQAWAL TAGKDRSTQM VEFMQRCTSH MKAIIQGFSY DLLKKIDSPQ RLIGSPPWFG
SLIQGSPNSS PNRQLKPGII SAQNIYSFGF GKFYLTSGMQ LTYPGSLPVI GEKEVVQADD
EPTFSFFSGP YMVMTNLVWN RSRVTVKELN LPTRPHCSRL RLADLLIAEQ EHSSNLRHPN
LLQLMAVCLS RDLEKIRLVY ERITVGTLFS VLHERRSQFP VLHMEVIVHL LLQVADALIY
LHSRGFIHRS LSSYAVHIVS AGEARLTNLE YLTESQDSGA HRNVTRMPLP TQLYNWAAPE
VVLQKAATVK SDIYSFSVII QEILTDSIPW NGLDGSLVKE TIALGNYLEA DVRLPEPYYD
IVKSGIHAKQ KNRTMNLQDI RYILKNDLKE FIGAQKTQPT ESPRGQSYEP HPDVNICLGL
TSEYQKDPPD LDIKELKEMG SQPHSPTDHS FLTVKPTLAP QTLDSSLSAQ KPDNANVPSP
PAACLAEEVR SPTASQDSLC SFEINEIYSG CLTLGTDKEE ECLGTAASPE GDRPNQGDEL
PSLEEELDKM ERELHCFCEE DKSISEVDTD LLFEDDDWQS DSLGSLNLPE PTREAKGKTS
SWSKTDEYVS KCVLNLKISQ VMMQQSAEWL RKLEQEVEEL EWAQKELDSQ CSSLRDASLK
FANAKFQPAV GPPSLAYLPP VMQLPGLKQP ENGGTWLTLA RSPGNEREFQ EGHFSKKPEK
LSACGWKPFT QVSEESRGDC SELNNQLPTL RGPGKQSTGE QLPSTQEARE SLEKNTNQNS
RSMASVSSEI YATKSRNNED NGEAHLKWRL AVKEMAEKAV SGQLLLPPWN PQSSAPFESK
VENESTPLPR PPIRGPESTE WQHILEYQRE NDEPKGNTKF GKMDNSDCDK NKHSRWTGLQ
RFTGIRYPFF RNHEQPEQNE ASQASCDTSV GTEKFYSTSS PIGDDFERFQ DSFAQRQGYV
EENFQIREIF EKNAEILTKP QFQAIQCAED KQDETLGETP KELKEKNTSL TDIQDLSSIT
YDQDGYFKET SYKTPKLKHA PTSASTPLSP ESISSAASHY EDCLENTTFH VKRGSTFCWN
GQEAMRTLSA KFTTVRERAK SLESLLASSK SLPAKLTDSK RLCMLSETGS SNVSAAFVTS
THATKRKSLP RELAEATSQQ HLDELPPPAQ ELLDEIEQLK QQQVSSLASH ENTARDLSVT
NKDKKHLEEQ ETNSSKDSSF LSSREIQDLE DTERAHSSLD EDLERFLQSP EENTALLDPT
KGSTREKKNK DQDVVEQKRK KKESIKPERR ESDSSLGTLE EDELKPCFWK RLGWSEPSRI
IVLDQSDLSD
