ID NLE1_HUMAN Reviewed; 485 AA.
AC Q9NVX2; O60868; Q59GJ8; Q9BU54;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 27-MAR-2024, entry version 193.
DE RecName: Full=Notchless protein homolog 1;
GN Name=NLE1; ORFNames=HUSSY-07;
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 MRNA] (ISOFORM 1), AND VARIANTS ALA-6 AND
RP LYS-169.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-6 AND
RP LYS-169.
RC TISSUE=Lung, and 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 PROTEIN SEQUENCE OF 2-12 AND 87-99, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND VARIANT ALA-6.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 400-485.
RC TISSUE=Brain;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP ALA-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
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 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP ALA-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP ALA-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP INTERACTION WITH MDN1.
RX PubMed=26601951; DOI=10.1074/jbc.m115.693259;
RA Romes E.M., Sobhany M., Stanley R.E.;
RT "The crystal structure of the ubiquitin-like domain of ribosome assembly
RT factor Ytm1 and characterization of its interaction with the AAA-ATPase
RT Midasin.";
RL J. Biol. Chem. 291:882-893(2016).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-319.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in regulating Notch activity. Plays a role in
CC regulating the expression of CDKN1A and several members of the Wnt
CC pathway, probably via its effects on Notch activity. Required during
CC embryogenesis for inner mass cell survival (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associates with the pre-60S ribosomal particle. Interacts (via
CC WD repeats) with uL18 (By similarity). Interacts (via UBL domain) with
CC MDN1 (via VWFA/MIDAS domain) (PubMed:26601951).
CC {ECO:0000250|UniProtKB:P25382, ECO:0000269|PubMed:26601951}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|Ref.5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVX2-2; Sequence=VSP_040555;
CC -!- SIMILARITY: Belongs to the NLE1/RSA4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92348.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK001320; BAA91621.1; -; mRNA.
DR EMBL; AB209111; BAD92348.1; ALT_INIT; mRNA.
DR EMBL; AC022916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002884; AAH02884.2; -; mRNA.
DR EMBL; BC012075; AAH12075.1; -; mRNA.
DR EMBL; AJ005257; CAA06444.1; -; mRNA.
DR CCDS; CCDS11291.1; -. [Q9NVX2-1]
DR CCDS; CCDS45647.1; -. [Q9NVX2-2]
DR RefSeq; NP_001014445.1; NM_001014445.2. [Q9NVX2-2]
DR RefSeq; NP_060566.2; NM_018096.4. [Q9NVX2-1]
DR RefSeq; XP_016880266.1; XM_017024777.1. [Q9NVX2-2]
DR PDB; 6WAJ; X-ray; 1.90 A; A=1-97.
DR PDB; 8FL0; EM; 2.91 A; NJ=1-485.
DR PDB; 8FL2; EM; 2.67 A; NJ=1-485.
DR PDB; 8FL3; EM; 2.53 A; NJ=1-485.
DR PDB; 8FL4; EM; 2.89 A; NJ=1-485.
DR PDB; 8INK; EM; 3.20 A; W=1-485.
DR PDB; 8IPD; EM; 3.20 A; W=1-485.
DR PDB; 8IPX; EM; 4.30 A; W=1-485.
DR PDB; 8IPY; EM; 3.20 A; W=1-485.
DR PDB; 8IR1; EM; 3.30 A; N=1-485.
DR PDB; 8IR3; EM; 3.50 A; N=1-485.
DR PDBsum; 6WAJ; -.
DR PDBsum; 8FL0; -.
DR PDBsum; 8FL2; -.
DR PDBsum; 8FL3; -.
DR PDBsum; 8FL4; -.
DR PDBsum; 8INK; -.
DR PDBsum; 8IPD; -.
DR PDBsum; 8IPX; -.
DR PDBsum; 8IPY; -.
DR PDBsum; 8IR1; -.
DR PDBsum; 8IR3; -.
DR AlphaFoldDB; Q9NVX2; -.
DR EMDB; EMD-29263; -.
DR EMDB; EMD-29265; -.
DR EMDB; EMD-29266; -.
DR EMDB; EMD-29267; -.
DR EMDB; EMD-35599; -.
DR EMDB; EMD-35639; -.
DR EMDB; EMD-35649; -.
DR EMDB; EMD-35651; -.
DR EMDB; EMD-35672; -.
DR EMDB; EMD-35673; -.
DR SMR; Q9NVX2; -.
DR BioGRID; 119980; 234.
DR IntAct; Q9NVX2; 22.
DR MINT; Q9NVX2; -.
DR STRING; 9606.ENSP00000413572; -.
DR GlyGen; Q9NVX2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVX2; -.
DR PhosphoSitePlus; Q9NVX2; -.
DR SwissPalm; Q9NVX2; -.
DR BioMuta; NLE1; -.
DR DMDM; 296439488; -.
DR SWISS-2DPAGE; Q9NVX2; -.
DR EPD; Q9NVX2; -.
DR jPOST; Q9NVX2; -.
DR MassIVE; Q9NVX2; -.
DR MaxQB; Q9NVX2; -.
DR PaxDb; 9606-ENSP00000413572; -.
DR PeptideAtlas; Q9NVX2; -.
DR ProteomicsDB; 82876; -. [Q9NVX2-1]
DR ProteomicsDB; 82877; -. [Q9NVX2-2]
DR Pumba; Q9NVX2; -.
DR Antibodypedia; 15565; 270 antibodies from 31 providers.
DR DNASU; 54475; -.
DR Ensembl; ENST00000442241.9; ENSP00000413572.3; ENSG00000073536.18. [Q9NVX2-1]
DR Ensembl; ENST00000586869.5; ENSP00000466588.1; ENSG00000073536.18. [Q9NVX2-2]
DR GeneID; 54475; -.
DR KEGG; hsa:54475; -.
DR MANE-Select; ENST00000442241.9; ENSP00000413572.3; NM_018096.5; NP_060566.2.
DR UCSC; uc002hiy.3; human. [Q9NVX2-1]
DR AGR; HGNC:19889; -.
DR CTD; 54475; -.
DR DisGeNET; 54475; -.
DR GeneCards; NLE1; -.
DR HGNC; HGNC:19889; NLE1.
DR HPA; ENSG00000073536; Low tissue specificity.
DR neXtProt; NX_Q9NVX2; -.
DR OpenTargets; ENSG00000073536; -.
DR PharmGKB; PA142671263; -.
DR VEuPathDB; HostDB:ENSG00000073536; -.
DR eggNOG; KOG0271; Eukaryota.
DR GeneTree; ENSGT00940000157881; -.
DR HOGENOM; CLU_000288_57_16_1; -.
DR InParanoid; Q9NVX2; -.
DR OMA; AWEPYHR; -.
DR OrthoDB; 859at2759; -.
DR PhylomeDB; Q9NVX2; -.
DR TreeFam; TF300668; -.
DR PathwayCommons; Q9NVX2; -.
DR SignaLink; Q9NVX2; -.
DR BioGRID-ORCS; 54475; 779 hits in 1159 CRISPR screens.
DR ChiTaRS; NLE1; human.
DR GeneWiki; NLE1; -.
DR GenomeRNAi; 54475; -.
DR Pharos; Q9NVX2; Tbio.
DR PRO; PR:Q9NVX2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NVX2; Protein.
DR Bgee; ENSG00000073536; Expressed in primordial germ cell in gonad and 99 other cell types or tissues.
DR ExpressionAtlas; Q9NVX2; baseline and differential.
DR Genevisible; Q9NVX2; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0001826; P:inner cell mass cell differentiation; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR012972; NLE.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19848:SF0; NOTCHLESS PROTEIN HOMOLOG 1; 1.
DR PANTHER; PTHR19848; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF08154; NLE; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Notch signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..485
FT /note="Notchless protein homolog 1"
FT /id="PRO_0000051098"
FT REPEAT 112..151
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 154..193
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 197..241
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 244..282
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 325..366
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 370..409
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 412..451
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 454..485
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 14..96
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000250|UniProtKB:P25382"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040555"
FT VARIANT 6
FT /note="P -> A (in dbSNP:rs1471615)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT /id="VAR_060327"
FT VARIANT 169
FT /note="R -> K (in dbSNP:rs7215209)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060328"
FT VARIANT 319
FT /note="Q -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs75635495)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035886"
FT VARIANT 406
FT /note="Y -> H (in dbSNP:rs2306513)"
FT /id="VAR_057616"
FT VARIANT 434
FT /note="S -> N (in dbSNP:rs2306512)"
FT /id="VAR_057617"
FT CONFLICT 321
FT /note="S -> F (in Ref. 2; BAD92348)"
FT /evidence="ECO:0000305"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:6WAJ"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:6WAJ"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:6WAJ"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6WAJ"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:6WAJ"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6WAJ"
SQ SEQUENCE 485 AA; 53320 MW; E2E638B13884BC07 CRC64;
MAAAVPDEAV ARDVQRLLVQ FQDEGGQLLG SPFDVPVDIT PDRLQLVCNA LLAQEDPLPL
AFFVHDAEIV SSLGKTLESQ AVETEKVLDI IYQPQAIFRV RAVTRCTSSL EGHSEAVISV
AFSPTGKYLA SGSGDTTVRF WDLSTETPHF TCKGHRHWVL SISWSPDGRK LASGCKNGQI
LLWDPSTGKQ VGRTLAGHSK WITGLSWEPL HANPECRYVA SSSKDGSVRI WDTTAGRCER
ILTGHTQSVT CLRWGGDGLL YSASQDRTIK VWRAHDGVLC RTLQGHGHWV NTMALSTDYA
LRTGAFEPAE ASVNPQDLQG SLQELKERAL SRYNLVRGQG PERLVSGSDD FTLFLWSPAE
DKKPLTRMTG HQALINQVLF SPDSRIVASA SFDKSIKLWD GRTGKYLASL RGHVAAVYQI
AWSADSRLLV SGSSDSTLKV WDVKAQKLAM DLPGHADEVY AVDWSPDGQR VASGGKDKCL
RIWRR
//
