NEK4_HUMAN
ID NEK4_HUMAN Reviewed; 841 AA.
AC P51957; A5YM70; B2R633; B7Z200; Q6P576;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Serine/threonine-protein kinase Nek4;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9Z1J2};
DE AltName: Full=Never in mitosis A-related kinase 4;
DE Short=NimA-related protein kinase 4;
DE AltName: Full=Serine/threonine-protein kinase 2;
DE AltName: Full=Serine/threonine-protein kinase NRK2;
GN Name=NEK4; Synonyms=STK2;
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 [MRNA] (ISOFORM 1), VARIANT ALA-225, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Mammary gland;
RX PubMed=8208544;
RA Levedakou E.N., He M., Baptist E.W., Craven R.J., Cance W.G., Welcsh P.L.,
RA Simmons A., Naylor S.L., Leach R.J., Lewis T.B., Bowcock A., Liu E.T.;
RT "Two novel human serine/threonine kinases with homologies to the cell cycle
RT regulating Xenopus MO15, and NIMA kinases: cloning and characterization of
RT their expression pattern.";
RL Oncogene 9:1977-1988(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-225.
RA Schupp I.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Amygdala, and Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-225.
RC TISSUE=Brain;
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 [6]
RP 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-563, 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 INTERACTION WITH RPGRIP1 AND RPGRIP1L, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21685204; DOI=10.1093/hmg/ddr280;
RA Coene K.L., Mans D.A., Boldt K., Gloeckner C.J., van Reeuwijk J., Bolat E.,
RA Roosing S., Letteboer S.J., Peters T.A., Cremers F.P., Ueffing M.,
RA Roepman R.;
RT "The ciliopathy-associated protein homologs RPGRIP1 and RPGRIP1L are linked
RT to cilium integrity through interaction with Nek4 serine/threonine
RT kinase.";
RL Hum. Mol. Genet. 20:3592-3605(2011).
RN [9]
RP FUNCTION.
RX PubMed=22851694; DOI=10.1128/mcb.00436-12;
RA Nguyen C.L., Possemato R., Bauerlein E.L., Xie A., Scully R., Hahn W.C.;
RT "Nek4 regulates entry into replicative senescence and the response to DNA
RT damage in human fibroblasts.";
RL Mol. Cell. Biol. 32:3963-3977(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-343; SER-461 AND
RP SER-563, AND IDENTIFICATION BY MASS 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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-622, AND IDENTIFICATION BY MASS
RP 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 [12]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-225; GLY-239; LEU-250; ILE-357;
RP GLU-456; LEU-567 AND LYS-777.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Protein kinase that seems to act exclusively upon threonine
CC residues (By similarity). Required for normal entry into proliferative
CC arrest after a limited number of cell divisions, also called
CC replicative senescence. Required for normal cell cycle arrest in
CC response to double-stranded DNA damage. {ECO:0000250|UniProtKB:Q9Z1J2,
CC ECO:0000269|PubMed:22851694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1J2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9Z1J2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1J2};
CC -!- SUBUNIT: Interacts with RPGRIP1 and RPGRIP1L.
CC {ECO:0000269|PubMed:21685204}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:21685204}. Cytoplasm {ECO:0000269|PubMed:21685204}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51957-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51957-2; Sequence=VSP_037123, VSP_037124;
CC Name=3;
CC IsoId=P51957-3; Sequence=VSP_043334;
CC -!- TISSUE SPECIFICITY: Highest expression in adult heart, followed by
CC pancreas, skeletal muscle, brain, testis, retina, liver, kidney, lung
CC and placenta. Present in most primary carcinomas.
CC {ECO:0000269|PubMed:21685204, ECO:0000269|PubMed:8208544}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; L20321; AAA36658.1; -; mRNA.
DR EMBL; EF560744; ABQ59054.1; -; mRNA.
DR EMBL; AK294165; BAH11686.1; -; mRNA.
DR EMBL; AK312420; BAG35330.1; -; mRNA.
DR EMBL; AC006254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063044; AAH63044.1; -; mRNA.
DR CCDS; CCDS2863.1; -. [P51957-1]
DR CCDS; CCDS54593.1; -. [P51957-3]
DR CCDS; CCDS87089.1; -. [P51957-2]
DR PIR; I78885; I78885.
DR RefSeq; NP_001180462.1; NM_001193533.2. [P51957-3]
DR RefSeq; NP_001335342.1; NM_001348413.1. [P51957-2]
DR RefSeq; NP_003148.2; NM_003157.5. [P51957-1]
DR AlphaFoldDB; P51957; -.
DR SMR; P51957; -.
DR BioGRID; 112663; 564.
DR IntAct; P51957; 554.
DR MINT; P51957; -.
DR STRING; 9606.ENSP00000233027; -.
DR BindingDB; P51957; -.
DR ChEMBL; CHEMBL5819; -.
DR DrugBank; DB12010; Fostamatinib.
DR GlyGen; P51957; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51957; -.
DR PhosphoSitePlus; P51957; -.
DR BioMuta; NEK4; -.
DR DMDM; 229462924; -.
DR EPD; P51957; -.
DR jPOST; P51957; -.
DR MassIVE; P51957; -.
DR MaxQB; P51957; -.
DR PaxDb; P51957; -.
DR PeptideAtlas; P51957; -.
DR PRIDE; P51957; -.
DR ProteomicsDB; 56459; -. [P51957-1]
DR ProteomicsDB; 56460; -. [P51957-2]
DR ProteomicsDB; 56461; -. [P51957-3]
DR Antibodypedia; 14725; 223 antibodies from 29 providers.
DR DNASU; 6787; -.
DR Ensembl; ENST00000233027.10; ENSP00000233027.5; ENSG00000114904.13. [P51957-1]
DR Ensembl; ENST00000383721.8; ENSP00000373227.4; ENSG00000114904.13. [P51957-2]
DR Ensembl; ENST00000535191.5; ENSP00000437703.1; ENSG00000114904.13. [P51957-3]
DR GeneID; 6787; -.
DR KEGG; hsa:6787; -.
DR MANE-Select; ENST00000233027.10; ENSP00000233027.5; NM_003157.6; NP_003148.2.
DR UCSC; uc003dfq.5; human. [P51957-1]
DR CTD; 6787; -.
DR DisGeNET; 6787; -.
DR GeneCards; NEK4; -.
DR HGNC; HGNC:11399; NEK4.
DR HPA; ENSG00000114904; Tissue enhanced (testis).
DR MIM; 601959; gene.
DR neXtProt; NX_P51957; -.
DR OpenTargets; ENSG00000114904; -.
DR PharmGKB; PA31548; -.
DR VEuPathDB; HostDB:ENSG00000114904; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000157448; -.
DR HOGENOM; CLU_017439_0_0_1; -.
DR InParanoid; P51957; -.
DR OMA; SRQRWQK; -.
DR OrthoDB; 70360at2759; -.
DR PhylomeDB; P51957; -.
DR TreeFam; TF106472; -.
DR PathwayCommons; P51957; -.
DR SignaLink; P51957; -.
DR BioGRID-ORCS; 6787; 13 hits in 1113 CRISPR screens.
DR ChiTaRS; NEK4; human.
DR GenomeRNAi; 6787; -.
DR Pharos; P51957; Tchem.
DR PRO; PR:P51957; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P51957; protein.
DR Bgee; ENSG00000114904; Expressed in bronchial epithelial cell and 198 other tissues.
DR ExpressionAtlas; P51957; baseline and differential.
DR Genevisible; P51957; HS.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; IMP:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:CACAO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Cytoplasm; Kinase; Magnesium; Metal-binding; Methylation;
KW Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..841
FT /note="Serine/threonine-protein kinase Nek4"
FT /id="PRO_0000086425"
FT DOMAIN 6..261
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 517..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 165
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 622
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1J2"
FT VAR_SEQ 32..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043334"
FT VAR_SEQ 457..502
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037123"
FT VAR_SEQ 813..841
FT /note="RLREHMGEKYTTYSVKARQLKFFEENMNF -> SVSLTVSRCLCYRIF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037124"
FT VARIANT 225
FT /note="P -> A (in dbSNP:rs1029871)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:8208544,
FT ECO:0000269|Ref.2"
FT /id="VAR_040915"
FT VARIANT 239
FT /note="R -> G (in dbSNP:rs35778416)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040916"
FT VARIANT 250
FT /note="P -> L (in dbSNP:rs56408749)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040917"
FT VARIANT 357
FT /note="T -> I (in dbSNP:rs2230537)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040918"
FT VARIANT 456
FT /note="Q -> E (in dbSNP:rs56019351)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040919"
FT VARIANT 567
FT /note="F -> L (in dbSNP:rs34986855)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040920"
FT VARIANT 777
FT /note="R -> K (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040921"
FT CONFLICT 63
FT /note="P -> L (in Ref. 3; BAG35330)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="N -> D (in Ref. 2; ABQ59054)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> K (in Ref. 3; BAG35330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 841 AA; 94597 MW; 43E8F11BA4007263 CRC64;
MPLAAYCYLR VVGKGSYGEV TLVKHRRDGK QYVIKKLNLR NASSRERRAA EQEAQLLSQL
KHPNIVTYKE SWEGGDGLLY IVMGFCEGGD LYRKLKEQKG QLLPENQVVE WFVQIAMALQ
YLHEKHILHR DLKTQNVFLT RTNIIKVGDL GIARVLENHC DMASTLIGTP YYMSPELFSN
KPYNYKSDVW ALGCCVYEMA TLKHAFNAKD MNSLVYRIIE GKLPPMPRDY SPELAELIRT
MLSKRPEERP SVRSILRQPY IKRQISFFLE ATKIKTSKNN IKNGDSQSKP FATVVSGEAE
SNHEVIHPQP LSSEGSQTYI MGEGKCLSQE KPRASGLLKS PASLKAHTCK QDLSNTTELA
TISSVNIDIL PAKGRDSVSD GFVQENQPRY LDASNELGGI CSISQVEEEM LQDNTKSSAQ
PENLIPMWSS DIVTGEKNEP VKPLQPLIKE QKPKDQSLAL SPKLECSGTI LAHSNLRLLG
SSDSPASASR VAGITGVCHH AQDQVAGECI IEKQGRIHPD LQPHNSGSEP SLSRQRRQKR
REQTEHRGEK RQVRRDLFAF QESPPRFLPS HPIVGKVDVT STQKEAENQR RVVTGSVSSS
RSSEMSSSKD RPLSARERRR LKQSQEEMSS SGPSVRKASL SVAGPGKPQE EDQPLPARRL
SSDCSVTQER KQIHCLSEDE LSSSTSSTDK SDGDYGEGKG QTNEINALVQ LMTQTLKLDS
KESCEDVPVA NPVSEFKLHR KYRDTLILHG KVAEEAEEIH FKELPSAIMP GSEKIRRLVE
VLRTDVIRGL GVQLLEQVYD LLEEEDEFDR EVRLREHMGE KYTTYSVKAR QLKFFEENMN
F
