PHF23_HUMAN
ID PHF23_HUMAN Reviewed; 403 AA.
AC Q9BUL5; A1DZ74; B3KVH8; B4DLK6; D3DTN4; Q8IZK0; Q96HG7; Q9H5X0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=PHD finger protein 23 {ECO:0000303|PubMed:25484098};
DE AltName: Full=PDH-containing protein JUNE-1 {ECO:0000250|UniProtKB:Q8BSN5};
GN Name=PHF23 {ECO:0000303|PubMed:25484098};
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), AND CHROMOSOMAL REARRANGEMENT.
RC TISSUE=Peripheral blood;
RX PubMed=17287853; DOI=10.1038/sj.leu.2404579;
RA Reader J.C., Meekins J.S., Gojo I., Ning Y.;
RT "A novel NUP98-PHF23 fusion resulting from a cryptic translocation
RT t(11;17)(p15;p13) in acute myeloid leukemia.";
RL Leukemia 21:842-844(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Yuan Z.Q., McCann T., Lappin T.R.J.;
RT "Identification of JUNE-1, a novel gene encoding a PHD-containing
RT protein.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Esophagus, Signet-ring cell carcinoma, Teratocarcinoma, and
RC Umbilical cord blood;
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-150; THR-165;
RP SER-315; SER-316 AND SER-317, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, 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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-400, AND
RP 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 [12]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH LRSAM1, DOMAIN,
RP AND FUNCTION.
RX PubMed=25484098; DOI=10.4161/auto.36439;
RA Wang Z., Hu J., Li G., Qu L., He Q., Lou Y., Song Q., Ma D., Chen Y.;
RT "PHF23 (plant homeodomain finger protein 23) negatively regulates cell
RT autophagy by promoting ubiquitination and degradation of E3 ligase
RT LRSAM1.";
RL Autophagy 10:2158-2170(2014).
RN [13]
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 a negative regulator of autophagy, through promoting
CC ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that
CC promotes autophagy in response to starvation or infecting bacteria.
CC {ECO:0000269|PubMed:25484098}.
CC -!- SUBUNIT: Interacts with LRSAM1. {ECO:0000269|PubMed:25484098}.
CC -!- INTERACTION:
CC Q9BUL5; P55212: CASP6; NbExp=3; IntAct=EBI-722852, EBI-718729;
CC Q9BUL5; P99999: CYCS; NbExp=3; IntAct=EBI-722852, EBI-446479;
CC Q9BUL5; P22607: FGFR3; NbExp=3; IntAct=EBI-722852, EBI-348399;
CC Q9BUL5; P06396: GSN; NbExp=3; IntAct=EBI-722852, EBI-351506;
CC Q9BUL5; P01112: HRAS; NbExp=3; IntAct=EBI-722852, EBI-350145;
CC Q9BUL5; O14901: KLF11; NbExp=3; IntAct=EBI-722852, EBI-948266;
CC Q9BUL5; P13473-2: LAMP2; NbExp=3; IntAct=EBI-722852, EBI-21591415;
CC Q9BUL5; P62826: RAN; NbExp=3; IntAct=EBI-722852, EBI-286642;
CC Q9BUL5; Q96ST3: SIN3A; NbExp=2; IntAct=EBI-722852, EBI-347218;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25484098}. Cytoplasm
CC {ECO:0000269|PubMed:25484098}. Note=Mainly present in the nucleus and
CC part in the cytoplasm. {ECO:0000269|PubMed:25484098}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BUL5-1; Sequence=Displayed;
CC Name=2; Synonyms=JUNE1B;
CC IsoId=Q9BUL5-2; Sequence=VSP_027962, VSP_027963;
CC Name=3;
CC IsoId=Q9BUL5-3; Sequence=VSP_056058;
CC Name=4;
CC IsoId=Q9BUL5-4; Sequence=VSP_057218;
CC -!- TISSUE SPECIFICITY: Widely expressed in human tissues and various cell
CC lines. {ECO:0000269|PubMed:25484098}.
CC -!- DOMAIN: The PHD-type zinc-finger domain is required for interaction
CC with LRSAM1 and negative regulation of autophagy.
CC {ECO:0000269|PubMed:25484098}.
CC -!- DISEASE: Note=A chromosomal aberration involving PHF23 is found in a
CC patient with acute myeloid leukemia (AML). Translocation
CC t(11;17)(p15;p13) with NUP98.
CC -!- SIMILARITY: Belongs to the PHF23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK59096.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15498.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EF071958; ABK59096.1; ALT_INIT; mRNA.
DR EMBL; EF071959; ABK59097.1; -; mRNA.
DR EMBL; AY099328; AAM44129.1; -; mRNA.
DR EMBL; AK026537; BAB15498.1; ALT_FRAME; mRNA.
DR EMBL; AK074766; BAC11192.1; -; mRNA.
DR EMBL; AK122901; BAG53790.1; -; mRNA.
DR EMBL; AK297040; BAG59568.1; -; mRNA.
DR EMBL; AC120057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90241.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90242.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90243.1; -; Genomic_DNA.
DR EMBL; BC002509; AAH02509.1; -; mRNA.
DR EMBL; BC008630; AAH08630.1; -; mRNA.
DR CCDS; CCDS42250.1; -. [Q9BUL5-1]
DR CCDS; CCDS67143.1; -. [Q9BUL5-4]
DR CCDS; CCDS67144.1; -. [Q9BUL5-3]
DR RefSeq; NP_001271446.1; NM_001284517.1. [Q9BUL5-3]
DR RefSeq; NP_001271447.1; NM_001284518.1. [Q9BUL5-4]
DR RefSeq; NP_077273.2; NM_024297.2. [Q9BUL5-1]
DR PDB; 6WXK; X-ray; 2.90 A; A/B/C/D/E=338-393.
DR PDBsum; 6WXK; -.
DR AlphaFoldDB; Q9BUL5; -.
DR SMR; Q9BUL5; -.
DR BioGRID; 122561; 24.
DR IntAct; Q9BUL5; 25.
DR MINT; Q9BUL5; -.
DR STRING; 9606.ENSP00000322579; -.
DR BindingDB; Q9BUL5; -.
DR ChEMBL; CHEMBL2424508; -.
DR iPTMnet; Q9BUL5; -.
DR PhosphoSitePlus; Q9BUL5; -.
DR BioMuta; PHF23; -.
DR DMDM; 74733231; -.
DR EPD; Q9BUL5; -.
DR jPOST; Q9BUL5; -.
DR MassIVE; Q9BUL5; -.
DR MaxQB; Q9BUL5; -.
DR PaxDb; Q9BUL5; -.
DR PeptideAtlas; Q9BUL5; -.
DR PRIDE; Q9BUL5; -.
DR ProteomicsDB; 3757; -.
DR ProteomicsDB; 4541; -.
DR ProteomicsDB; 79106; -. [Q9BUL5-1]
DR ProteomicsDB; 79107; -. [Q9BUL5-2]
DR Antibodypedia; 23960; 58 antibodies from 14 providers.
DR DNASU; 79142; -.
DR Ensembl; ENST00000320316.8; ENSP00000322579.3; ENSG00000040633.13. [Q9BUL5-1]
DR Ensembl; ENST00000454255.6; ENSP00000414607.2; ENSG00000040633.13. [Q9BUL5-4]
DR Ensembl; ENST00000571362.5; ENSP00000460738.1; ENSG00000040633.13. [Q9BUL5-3]
DR GeneID; 79142; -.
DR KEGG; hsa:79142; -.
DR MANE-Select; ENST00000320316.8; ENSP00000322579.3; NM_024297.3; NP_077273.2.
DR UCSC; uc002gfa.3; human. [Q9BUL5-1]
DR CTD; 79142; -.
DR DisGeNET; 79142; -.
DR GeneCards; PHF23; -.
DR HGNC; HGNC:28428; PHF23.
DR HPA; ENSG00000040633; Low tissue specificity.
DR MIM; 612910; gene.
DR neXtProt; NX_Q9BUL5; -.
DR OpenTargets; ENSG00000040633; -.
DR PharmGKB; PA142671175; -.
DR VEuPathDB; HostDB:ENSG00000040633; -.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00530000063882; -.
DR HOGENOM; CLU_047981_1_0_1; -.
DR InParanoid; Q9BUL5; -.
DR OMA; SGHKKDP; -.
DR OrthoDB; 982722at2759; -.
DR PhylomeDB; Q9BUL5; -.
DR TreeFam; TF331373; -.
DR PathwayCommons; Q9BUL5; -.
DR SignaLink; Q9BUL5; -.
DR BioGRID-ORCS; 79142; 87 hits in 1089 CRISPR screens.
DR ChiTaRS; PHF23; human.
DR GenomeRNAi; 79142; -.
DR Pharos; Q9BUL5; Tbio.
DR PRO; PR:Q9BUL5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BUL5; protein.
DR Bgee; ENSG00000040633; Expressed in granulocyte and 177 other tissues.
DR ExpressionAtlas; Q9BUL5; baseline and differential.
DR Genevisible; Q9BUL5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:GO_Central.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; IMP:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autophagy;
KW Chromosomal rearrangement; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..403
FT /note="PHD finger protein 23"
FT /id="PRO_0000302830"
FT ZN_FING 339..387
FT /note="PHD-type"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 120..121
FT /note="Breakpoint for translocation to form NUP98-PHF23
FT oncogene"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..11
FT /note="MLEAMAEPSPE -> MPGDCRR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057218"
FT VAR_SEQ 54..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056058"
FT VAR_SEQ 150..158
FT /note="SPTSLTHTS -> SRPCAANTP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027962"
FT VAR_SEQ 159..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027963"
FT CONFLICT 390
FT /note="E -> D (in Ref. 3; BAB15498)"
FT /evidence="ECO:0000305"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6WXK"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6WXK"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6WXK"
FT TURN 365..369
FT /evidence="ECO:0007829|PDB:6WXK"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:6WXK"
SQ SEQUENCE 403 AA; 43818 MW; 7C9DA0FA8D72C8D0 CRC64;
MLEAMAEPSP EDPPPTLKPE TQPPEKRRRT IEDFNKFCSF VLAYAGYIPP SKEESDWPAS
GSSSPLRGES AADSDGWDSA PSDLRTIQTF VKKAKSSKRR AAQAGPTQPG PPRSTFSRLQ
APDSATLLEK MKLKDSLFDL DGPKVASPLS PTSLTHTSRP PAALTPVPLS QGDLSHPPRK
KDRKNRKLGP GAGAGFGVLR RPRPTPGDGE KRSRIKKSKK RKLKKAERGD RLPPPGPPQA
PPSDTDSEEE EEEEEEEEEE EMATVVGGEA PVPVLPTPPE APRPPATVHP EGVPPADSES
KEVGSTETSQ DGDASSSEGE MRVMDEDIMV ESGDDSWDLI TCYCRKPFAG RPMIECSLCG
TWIHLSCAKI KKTNVPDFFY CQKCKELRPE ARRLGGPPKS GEP
