ID   NOC2L_HUMAN             Reviewed;         749 AA.
AC   Q9Y3T9; Q5SVA3; Q9BTN6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Nucleolar complex protein 2 homolog;
DE            Short=Protein NOC2 homolog;
DE   AltName: Full=NOC2-like protein;
DE   AltName: Full=Novel INHAT repressor;
GN   Name=NOC2L; Synonyms=NIR;
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], FUNCTION IN INHIBITION OF HISTONE ACETYLATION,
RP   INTERACTION WITH TP53, AND ASSOCIATION WITH CORE HISTONES AND NUCLEOSOMES.
RX   PubMed=16322561; DOI=10.1101/gad.351205;
RA   Hublitz P., Kunowska N., Mayer U.P., Muller J.M., Heyne K., Yin N.,
RA   Fritzsche C., Poli C., Miguet L., Schupp I.W., van Grunsven L.A.,
RA   Potiers N., van Dorsselaer A., Metzger E., Roemer K., Schule R.;
RT   "NIR is a novel INHAT repressor that modulates the transcriptional activity
RT   of p53.";
RL   Genes Dev. 19:2912-2924(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-300.
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-300.
RC   TISSUE=Placenta;
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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-672; SER-673 AND
RP   THR-678, 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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-673, AND
RP   IDENTIFICATION BY 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   [11]
RP   FUNCTION, INTERACTION WITH TP53 AND TP63, AND SUBCELLULAR LOCATION.
RX   PubMed=20123734; DOI=10.1093/nar/gkq016;
RA   Heyne K., Willnecker V., Schneider J., Conrad M., Raulf N., Schule R.,
RA   Roemer K.;
RT   "NIR, an inhibitor of histone acetyltransferases, regulates transcription
RT   factor TAp63 and is controlled by the cell cycle.";
RL   Nucleic Acids Res. 38:3159-3171(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-672, AND
RP   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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   FUNCTION, INTERACTION WITH AURKB AND TP53, INDUCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=20959462; DOI=10.1074/jbc.m110.174755;
RA   Wu L., Ma C.A., Zhao Y., Jain A.;
RT   "Aurora B interacts with NIR-p53, leading to p53 phosphorylation in its
RT   DNA-binding domain and subsequent functional suppression.";
RL   J. Biol. Chem. 286:2236-2244(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-56 AND SER-672, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-56; SER-672 AND
RP   SER-673, 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-746, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Acts as an inhibitor of histone acetyltransferase activity;
CC       prevents acetylation of all core histones by the EP300/p300 histone
CC       acetyltransferase at p53/TP53-regulated target promoters in a histone
CC       deacetylases (HDAC)-independent manner. Acts as a transcription
CC       corepressor of p53/TP53- and TP63-mediated transactivation of the
CC       p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent
CC       apoptosis. Associates together with TP63 isoform TA*-gamma to the
CC       p21/CDKN1A promoter. {ECO:0000269|PubMed:16322561,
CC       ECO:0000269|PubMed:20123734, ECO:0000269|PubMed:20959462}.
CC   -!- SUBUNIT: Interacts with p53/TP53. Interacts (via the N- and C-terminus
CC       domains) with AURKB (via the middle kinase domain). Interacts with TP63
CC       isoform TA*-gamma (via activation domain). Interacts with histone H3
CC       (via N-terminus and non-acetylated form preferentially). Associates
CC       with core histones and nucleosomes. {ECO:0000269|PubMed:16322561,
CC       ECO:0000269|PubMed:20123734, ECO:0000269|PubMed:20959462}.
CC   -!- INTERACTION:
CC       Q9Y3T9; O15265: ATXN7; NbExp=2; IntAct=EBI-751547, EBI-708350;
CC       Q9Y3T9; P04637: TP53; NbExp=8; IntAct=EBI-751547, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, nucleolus.
CC       Note=Translocates from the nucleoli to the nucleoplasm in presence of
CC       several stressors like ultraviolet irradiation and actinomycin-D.
CC       Predominantly detected in the nucleoli in non-mitotic cells.
CC       Predominantly detected in nucleoplasma in cells undergoing mitosis.
CC   -!- INDUCTION: Up-regulated by IL4 and CD40L in B-cells.
CC       {ECO:0000269|PubMed:20959462}.
CC   -!- SIMILARITY: Belongs to the NOC2 family. {ECO:0000305}.
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DR   EMBL; AL050019; CAB43240.2; -; mRNA.
DR   EMBL; AL645608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003555; AAH03555.1; -; mRNA.
DR   CCDS; CCDS3.1; -.
DR   RefSeq; NP_056473.2; NM_015658.3.
DR   PDB; 8FKV; EM; 2.47 A; NA=1-749.
DR   PDB; 8FKW; EM; 2.50 A; NA=1-749.
DR   PDB; 8FKX; EM; 2.59 A; NA=1-749.
DR   PDB; 8FKY; EM; 2.67 A; NA=1-749.
DR   PDBsum; 8FKV; -.
DR   PDBsum; 8FKW; -.
DR   PDBsum; 8FKX; -.
DR   PDBsum; 8FKY; -.
DR   AlphaFoldDB; Q9Y3T9; -.
DR   EMDB; EMD-29258; -.
DR   EMDB; EMD-29259; -.
DR   EMDB; EMD-29260; -.
DR   EMDB; EMD-29261; -.
DR   SMR; Q9Y3T9; -.
DR   BioGRID; 117586; 302.
DR   IntAct; Q9Y3T9; 72.
DR   MINT; Q9Y3T9; -.
DR   STRING; 9606.ENSP00000317992; -.
DR   GlyCosmos; Q9Y3T9; 1 site, 1 glycan.
DR   GlyGen; Q9Y3T9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y3T9; -.
DR   MetOSite; Q9Y3T9; -.
DR   PhosphoSitePlus; Q9Y3T9; -.
DR   SwissPalm; Q9Y3T9; -.
DR   BioMuta; NOC2L; -.
DR   DMDM; 317373580; -.
DR   CPTAC; CPTAC-1744; -.
DR   EPD; Q9Y3T9; -.
DR   jPOST; Q9Y3T9; -.
DR   MassIVE; Q9Y3T9; -.
DR   MaxQB; Q9Y3T9; -.
DR   PaxDb; 9606-ENSP00000317992; -.
DR   PeptideAtlas; Q9Y3T9; -.
DR   ProteomicsDB; 86078; -.
DR   Pumba; Q9Y3T9; -.
DR   Antibodypedia; 26026; 139 antibodies from 25 providers.
DR   DNASU; 26155; -.
DR   Ensembl; ENST00000327044.7; ENSP00000317992.6; ENSG00000188976.11.
DR   GeneID; 26155; -.
DR   KEGG; hsa:26155; -.
DR   MANE-Select; ENST00000327044.7; ENSP00000317992.6; NM_015658.4; NP_056473.3.
DR   UCSC; uc001abz.5; human.
DR   AGR; HGNC:24517; -.
DR   CTD; 26155; -.
DR   DisGeNET; 26155; -.
DR   GeneCards; NOC2L; -.
DR   HGNC; HGNC:24517; NOC2L.
DR   HPA; ENSG00000188976; Low tissue specificity.
DR   MIM; 610770; gene.
DR   neXtProt; NX_Q9Y3T9; -.
DR   OpenTargets; ENSG00000188976; -.
DR   PharmGKB; PA142671261; -.
DR   VEuPathDB; HostDB:ENSG00000188976; -.
DR   eggNOG; KOG2256; Eukaryota.
DR   GeneTree; ENSGT00390000010057; -.
DR   HOGENOM; CLU_011272_1_2_1; -.
DR   InParanoid; Q9Y3T9; -.
DR   OMA; GCLRYYL; -.
DR   OrthoDB; 152110at2759; -.
DR   PhylomeDB; Q9Y3T9; -.
DR   TreeFam; TF314829; -.
DR   PathwayCommons; Q9Y3T9; -.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   SignaLink; Q9Y3T9; -.
DR   BioGRID-ORCS; 26155; 671 hits in 1166 CRISPR screens.
DR   ChiTaRS; NOC2L; human.
DR   GeneWiki; NOC2L; -.
DR   GenomeRNAi; 26155; -.
DR   Pharos; Q9Y3T9; Tbio.
DR   PRO; PR:Q9Y3T9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9Y3T9; Protein.
DR   Bgee; ENSG00000188976; Expressed in lower esophagus mucosa and 169 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030690; C:Noc1p-Noc2p complex; IBA:GO_Central.
DR   GO; GO:0030691; C:Noc2p-Noc3p complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR   GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR   GO; GO:0002903; P:negative regulation of B cell apoptotic process; IMP:UniProtKB.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IDA:GO_Central.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR005343; Noc2.
DR   PANTHER; PTHR12687; NUCLEOLAR COMPLEX 2 AND RAD4-RELATED; 1.
DR   PANTHER; PTHR12687:SF10; NUCLEOLAR COMPLEX PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF03715; Noc2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SWISS-2DPAGE; Q9Y3T9; -.
DR   Genevisible; Q9Y3T9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..749
FT                   /note="Nucleolar complex protein 2 homolog"
FT                   /id="PRO_0000121048"
FT   REGION          21..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..716
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   MOD_RES         672
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         678
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         746
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VARIANT         271
FT                   /note="A -> V (in dbSNP:rs3828049)"
FT                   /id="VAR_028145"
FT   VARIANT         300
FT                   /note="I -> V (in dbSNP:rs3748597)"
FT                   /evidence="ECO:0000269|PubMed:11230166,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028146"
FT   VARIANT         556
FT                   /note="S -> L (in dbSNP:rs35471880)"
FT                   /id="VAR_050289"
FT   CONFLICT        178
FT                   /note="R -> Q (in Ref. 2; CAB43240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="K -> E (in Ref. 2; CAB43240)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   749 AA;  84919 MW;  B178FE65E711CFDB CRC64;
     MAAAGSRKRR LAELTVDEFL ASGFDSESES ESENSPQAET REAREAARSP DKPGGSPSAS
     RRKGRASEHK DQLSRLKDRD PEFYKFLQEN DQSLLNFSDS DSSEEEEGPF HSLPDVLEEA
     SEEEDGAEEG EDGDRVPRGL KGKKNSVPVT VAMVERWKQA AKQRLTPKLF HEVVQAFRAA
     VATTRGDQES AEANKFQVTD SAAFNALVTF CIRDLIGCLQ KLLFGKVAKD SSRMLQPSSS
     PLWGKLRVDI KAYLGSAIQL VSCLSETTVL AAVLRHISVL VPCFLTFPKQ CRMLLKRMVI
     VWSTGEESLR VLAFLVLSRV CRHKKDTFLG PVLKQMYITY VRNCKFTSPG ALPFISFMQW
     TLTELLALEP GVAYQHAFLY IRQLAIHLRN AMTTRKKETY QSVYNWQYVH CLFLWCRVLS
     TAGPSEALQP LVYPLAQVII GCIKLIPTAR FYPLRMHCIR ALTLLSGSSG AFIPVLPFIL
     EMFQQVDFNR KPGRMSSKPI NFSVILKLSN VNLQEKAYRD GLVEQLYDLT LEYLHSQAHC
     IGFPELVLPV VLQLKSFLRE CKVANYCRQV QQLLGKVQEN SAYICSRRQR VSFGVSEQQA
     VEAWEKLTRE EGTPLTLYYS HWRKLRDREI QLEISGKERL EDLNFPEIKR RKMADRKDED
     RKQFKDLFDL NSSEEDDTEG FSERGILRPL STRHGVEDDE EDEEEGEEDS SNSEDGDPDA
     EAGLAPGELQ QLAQGPEDEL EDLQLSEDD
//