NCK5L_HUMAN
ID NCK5L_HUMAN Reviewed; 1334 AA.
AC Q9HCH0; Q2TB26; Q71RH1; Q8N4W1; Q96HX2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nck-associated protein 5-like;
DE Short=NCKAP5-like {ECO:0000305};
DE AltName: Full=Centrosomal protein of 169 kDa {ECO:0000303|PubMed:26485573};
DE Short=Cep169 {ECO:0000303|PubMed:26485573};
GN Name=NCKAP5L {ECO:0000312|HGNC:HGNC:29321};
GN Synonyms=CEP169 {ECO:0000303|PubMed:26485573}, KIAA1602; ORFNames=FP1193;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 429-1334 (ISOFORM 1).
RC TISSUE=Eye, and Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-1334 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1334 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-496; SER-498 AND
RP SER-571, AND IDENTIFICATION BY MASS SPECTROMETRY [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-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-451; SER-493;
RP SER-496 AND SER-498, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-451; SER-477;
RP SER-493; SER-498; THR-659; SER-767 AND SER-1194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [10]
RP PHOSPHORYLATION AT SER-440; SER-451; SER-470; SER-477; SER-571; SER-577 AND
RP SER-767, AND SUBCELLULAR LOCATION.
RX PubMed=26549230; DOI=10.1016/j.bbrc.2015.11.004;
RA Mori Y., Inoue Y., Taniyama Y., Tanaka S., Terada Y.;
RT "Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its
RT dissociation from centrosomes in mitosis.";
RL Biochem. Biophys. Res. Commun. 468:642-646(2015).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH BETA-TUBULIN,
RP MUTAGENESIS OF 486-ILE-PRO-487; 818-LEU-PRO-819 AND 928-PRO-LEU-929, AND
RP DOMAIN (S/T)X(I/L)P MOTIF.
RX PubMed=26482847; DOI=10.1016/j.bbrc.2015.10.069;
RA Mori Y., Taniyama Y., Tanaka S., Fukuchi H., Terada Y.;
RT "Microtubule-bundling activity of the centrosomal protein, Cep169, and its
RT binding to microtubules.";
RL Biochem. Biophys. Res. Commun. 467:754-759(2015).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK5RAP2 AND MAPRE1,
RP MUTAGENESIS OF 486-ILE-PRO-487; 818-LEU-PRO-819 AND 928-PRO-LEU-929, AND
RP DOMAIN (S/T)X(I/L)P MOTIF.
RX PubMed=26485573; DOI=10.1371/journal.pone.0140968;
RA Mori Y., Inoue Y., Tanaka S., Doda S., Yamanaka S., Fukuchi H., Terada Y.;
RT "Cep169, a novel microtubule plus-end-tracking centrosomal protein, binds
RT to CDK5RAP2 and regulates microtubule stability.";
RL PLoS ONE 10:E0140968-E0140968(2015).
CC -!- FUNCTION: Regulates microtubule organization and stabilization.
CC Promotes microtubule growth and bundling formation and stabilizes
CC microtubules by increasing intense acetylation of microtubules
CC (PubMed:26482847, PubMed:26485573). Both tubulin-binding and homodimer
CC formation are required for NCKAP5L-mediated microtubule bundle
CC formation (PubMed:26485573). {ECO:0000269|PubMed:26482847,
CC ECO:0000269|PubMed:26485573}.
CC -!- SUBUNIT: Homodimer (PubMed:26482847). Interacts with CDK5RAP2
CC (PubMed:26485573). Interacts with MAPRE1 (PubMed:26485573). Interacts
CC with beta-tubulin (PubMed:26482847). {ECO:0000269|PubMed:26482847,
CC ECO:0000269|PubMed:26485573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:26482847,
CC ECO:0000269|PubMed:26485573, ECO:0000269|PubMed:26549230}.
CC Note=Localizes to microtubule plus ends (PubMed:26485573,
CC PubMed:26482847). Associates with centrosomes during interphase, but
CC dissociates from these structures from the onset of mitosis
CC (PubMed:26549230). {ECO:0000269|PubMed:26482847,
CC ECO:0000269|PubMed:26485573, ECO:0000269|PubMed:26549230}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HCH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCH0-2; Sequence=VSP_025678;
CC Name=4;
CC IsoId=Q9HCH0-4; Sequence=VSP_033818, VSP_033819;
CC -!- PTM: CDK1/Cyclin B-dependent phosphorylation mediates its dissociation
CC from centrosomes during mitosis. {ECO:0000269|PubMed:26549230}.
CC -!- MISCELLANEOUS: [Isoform 2]: Dubious isoform produced through intron
CC retention. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Dubious isoform produced through intron
CC retention. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07998.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAQ15202.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC131157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007998; AAH07998.1; ALT_SEQ; mRNA.
DR EMBL; BC033253; AAH33253.1; -; mRNA.
DR EMBL; BC110599; AAI10600.1; -; mRNA.
DR EMBL; AB046822; BAB13428.1; -; mRNA.
DR EMBL; AF370366; AAQ15202.1; ALT_FRAME; mRNA.
DR CCDS; CCDS41781.2; -. [Q9HCH0-1]
DR RefSeq; NP_001032895.2; NM_001037806.3.
DR AlphaFoldDB; Q9HCH0; -.
DR BioGRID; 121726; 99.
DR IntAct; Q9HCH0; 29.
DR MINT; Q9HCH0; -.
DR STRING; 9606.ENSP00000337998; -.
DR iPTMnet; Q9HCH0; -.
DR PhosphoSitePlus; Q9HCH0; -.
DR BioMuta; NCKAP5L; -.
DR DMDM; 156630840; -.
DR EPD; Q9HCH0; -.
DR jPOST; Q9HCH0; -.
DR MassIVE; Q9HCH0; -.
DR MaxQB; Q9HCH0; -.
DR PaxDb; Q9HCH0; -.
DR PeptideAtlas; Q9HCH0; -.
DR PRIDE; Q9HCH0; -.
DR ProteomicsDB; 81713; -. [Q9HCH0-1]
DR ProteomicsDB; 81714; -. [Q9HCH0-2]
DR ProteomicsDB; 81716; -. [Q9HCH0-4]
DR Antibodypedia; 49270; 23 antibodies from 13 providers.
DR DNASU; 57701; -.
DR Ensembl; ENST00000335999.7; ENSP00000337998.6; ENSG00000167566.17. [Q9HCH0-1]
DR GeneID; 57701; -.
DR KEGG; hsa:57701; -.
DR MANE-Select; ENST00000335999.7; ENSP00000337998.6; NM_001037806.4; NP_001032895.2.
DR UCSC; uc009zlk.2; human. [Q9HCH0-1]
DR CTD; 57701; -.
DR GeneCards; NCKAP5L; -.
DR HGNC; HGNC:29321; NCKAP5L.
DR HPA; ENSG00000167566; Low tissue specificity.
DR MIM; 615104; gene.
DR neXtProt; NX_Q9HCH0; -.
DR OpenTargets; ENSG00000167566; -.
DR PharmGKB; PA165513124; -.
DR VEuPathDB; HostDB:ENSG00000167566; -.
DR eggNOG; ENOG502RB0P; Eukaryota.
DR GeneTree; ENSGT00530000063607; -.
DR HOGENOM; CLU_007601_0_0_1; -.
DR InParanoid; Q9HCH0; -.
DR OrthoDB; 29694at2759; -.
DR PhylomeDB; Q9HCH0; -.
DR TreeFam; TF331208; -.
DR PathwayCommons; Q9HCH0; -.
DR SignaLink; Q9HCH0; -.
DR BioGRID-ORCS; 57701; 67 hits in 1075 CRISPR screens.
DR ChiTaRS; NCKAP5L; human.
DR GenomeRNAi; 57701; -.
DR Pharos; Q9HCH0; Tdark.
DR PRO; PR:Q9HCH0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9HCH0; protein.
DR Bgee; ENSG00000167566; Expressed in apex of heart and 112 other tissues.
DR ExpressionAtlas; Q9HCH0; baseline and differential.
DR Genevisible; Q9HCH0; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:UniProtKB.
DR InterPro; IPR032769; NCKAP5_C.
DR InterPro; IPR026163; Nckap5l.
DR PANTHER; PTHR21740; PTHR21740; 1.
DR Pfam; PF15246; NCKAP5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1334
FT /note="Nck-associated protein 5-like"
FT /id="PRO_0000288447"
FT REGION 1..139
FT /note="Mediates interaction with CDK5RAP2 and is required
FT for homodimerization and microtubule bundle formation"
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..1146
FT /note="Mediates interaction with beta-tubulin and is
FT required for microtubule bundle formation"
FT /evidence="ECO:0000269|PubMed:26482847"
FT REGION 782..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..106
FT /evidence="ECO:0000255"
FT COILED 956..994
FT /evidence="ECO:0000255"
FT MOTIF 484..487
FT /note="(S/T)X(I/L)P motif 1"
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT MOTIF 816..819
FT /note="(S/T)X(I/L)P motif 2"
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT MOTIF 926..929
FT /note="(S/T)X(I/L)P motif 3; required for interaction with
FT MAPRE1"
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT COMPBIAS 280..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 451
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230"
FT MOD_RES 477
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 577
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 767
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:26549230,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 66..112
FT /note="ANHVVQALLNQKDLREECIKLKKRVFDLERQNQMLSALFQQKLQLTT -> C
FT GSVVGLGGCGSSAPGRSWGQLMALPRGFLSPGCQPCGTGVAEPEGE (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033818"
FT VAR_SEQ 113..1334
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033819"
FT VAR_SEQ 1265..1334
FT /note="ALPVDRKRSQEPSRPSPTPQGPPFGGSRTPSTSDMAEEGRVASGGPPGLETS
FT ESLSDSLYDSLSSCGSQG -> VRIAAEERERTREQEGVMWGDQFLQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_025678"
FT MUTAGEN 486..487
FT /note="IP->AA: No decrease in localization to microtubule
FT plus ends. Loss of interaction with MAPRE1 and localization
FT to microtubule plus ends; when associated with 818-A-A-819
FT and 928-A-A-929."
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT MUTAGEN 818..819
FT /note="LP->AA: No decrease in localization to microtubule
FT plus ends. Loss of interaction with MAPRE1 and localization
FT to microtubule plus ends; when associated with 486-A-A-487
FT and 928-A-A-929."
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT MUTAGEN 928..929
FT /note="LP->AA: Loss of interaction with MAPRE1 and
FT significantly reduced localization to microtubule plus
FT ends. Loss of interaction with MAPRE1 and localization to
FT microtubule plus ends; when associated with 486-A-A-487 and
FT 818-A-A-819."
FT /evidence="ECO:0000269|PubMed:26482847,
FT ECO:0000269|PubMed:26485573"
FT CONFLICT 1097
FT /note="M -> T (in Ref. 3; BAB13428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1334 AA; 139462 MW; 1D728D7B1906AE48 CRC64;
MSEAMDQPAG GPGNPRPGEG DDGSMEPGTC QELLHRLREL EAENSALAQA NENQRETYER
CLDEVANHVV QALLNQKDLR EECIKLKKRV FDLERQNQML SALFQQKLQL TTGSLPQIPL
TPLQPPSEPP ASPSLSSTEG PAAPLPLGHC AGQREVCWEQ QLRPGGPGPP AAPPPALDAL
SPFLRKKAQI LEVLRALEET DPLLLCSPAT PWRPPGQGPG SPEPINGELC GPPQPEPSPW
APCLLLGPGN LGGLLHWERL LGGLGGEEDT GRPWGPSRGP PQAQGTSSGP NCAPGSSSSS
SSDEAGDPNE APSPDTLLGA LARRQLNLGQ LLEDTESYLQ AFLAGAAGPL NGDHPGPGQS
SSPDQAPPQL SKSKGLPKSA WGGGTPEAHR PGFGATSEGQ GPLPFLSMFM GAGDAPLGSR
PGHPHSSSQV KSKLQIGPPS PGEAQGPLLP SPARGLKFLK LPPTSEKSPS PGGPQLSPQL
PRNSRIPCRN SGSDGSPSPL LARRGLGGGE LSPEGAQGLP TSPSPCYTTP DSTQLRPPQS
ALSTTLSPGP VVSPCYENIL DLSRSTFRGP SPEPPPSPLQ VPTYPQLTLE VPQAPEVLRS
PGVPPSPCLP ESYPYGSPQE KSLDKAGSES PHPGRRTPGN SSKKPSQGSG RRPGDPGSTP
LRDRLAALGK LKTGPEGALG SEKNGVPARP GTEKTRGPGK SGESAGDMVP SIHRPLEQLE
AKGGIRGAVA LGTNSLKQQE PGLMGDPGAR VYSSHSMGAR VDLEPVSPRS CLTKVELAKS
RLAGALCPQV PRTPAKVPTS APSLGKPNKS PHSSPTKLPS KSPTKVVPRP GAPLVTKESP
KPDKGKGPPW ADCGSTTAQS TPLVPGPTDP SQGPEGLAPH SAIEEKVMKG IEENVLRLQG
QERAPGAEVK HRNTSSIASW FGLKKSKLPA LNRRTEATKN KEGAGGGSPL RREVKMEARK
LEAESLNISK LMAKAEDLRR ALEEEKAYLS SRARPRPGGP APGPNTGLGQ VQGQLAGMYQ
GADTFMQQLL NRVDGKELPS KSWREPKPEY GDFQPVSSDP KSPWPACGPR NGLVGPLQGC
GKPPGKPSSE PGRREEMPSE DSLAEPVPTS HFTACGSLTR TLDSGIGTFP PPDHGSSGTP
SKNLPKTKPP RLDPPPGVPP ARPPPLTKVP RRAHTLEREV PGIEELLVSG RHPSMPAFPA
LLPAAPGHRG HETCPDDPCE DPGPTPPVQL AKNWTFPNTR AAGSSSDPLM CPPRQLEGLP
RTPMALPVDR KRSQEPSRPS PTPQGPPFGG SRTPSTSDMA EEGRVASGGP PGLETSESLS
DSLYDSLSSC GSQG
