NOC2L_HUMAN
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 03-AUG-2022, entry version 187.
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 AlphaFoldDB; Q9Y3T9; -.
DR BioGRID; 117586; 272.
DR IntAct; Q9Y3T9; 68.
DR MINT; Q9Y3T9; -.
DR STRING; 9606.ENSP00000317992; -.
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 SWISS-2DPAGE; Q9Y3T9; -.
DR CPTAC; CPTAC-1744; -.
DR EPD; Q9Y3T9; -.
DR jPOST; Q9Y3T9; -.
DR MassIVE; Q9Y3T9; -.
DR MaxQB; Q9Y3T9; -.
DR PaxDb; Q9Y3T9; -.
DR PeptideAtlas; Q9Y3T9; -.
DR PRIDE; Q9Y3T9; -.
DR ProteomicsDB; 86078; -.
DR Antibodypedia; 26026; 129 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 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; FPLRFHC; -.
DR OrthoDB; 1194328at2759; -.
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; 645 hits in 1087 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 167 other tissues.
DR Genevisible; Q9Y3T9; HS.
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:0031497; P:chromatin assembly; IDA:UniProtKB.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IDA: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 InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005343; Noc2.
DR PANTHER; PTHR12687; PTHR12687; 1.
DR Pfam; PF03715; Noc2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW 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
