BUD31_HUMAN
ID BUD31_HUMAN Reviewed; 144 AA.
AC P41223; A4D274; B7Z4S9; D6W5S6; Q6IB53; Q9UDV1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein BUD31 homolog {ECO:0000303|PubMed:25091737};
DE AltName: Full=Protein EDG-2 {ECO:0000303|PubMed:7841202};
DE AltName: Full=Protein G10 homolog {ECO:0000303|PubMed:7841202};
GN Name=BUD31; Synonyms=EDG2;
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).
RX PubMed=7841202; DOI=10.1016/0167-4781(94)00219-s;
RA Hla T., Jackson A.Q., Appleby S.B., Maciag T.;
RT "Characterization of edg-2, a human homologue of the Xenopus maternal
RT transcript G10 from endothelial cells.";
RL Biochim. Biophys. Acta 1260:227-229(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(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] {ECO:0007744|PDB:4OED, ECO:0007744|PDB:4OH6, ECO:0007744|PDB:4OKB}
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 56-70 IN COMPLEX WITH AR,
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AR, DOMAIN, AND TISSUE
RP SPECIFICITY.
RX PubMed=25091737; DOI=10.1016/j.molonc.2014.06.009;
RA Hsu C.L., Liu J.S., Wu P.L., Guan H.H., Chen Y.L., Lin A.C., Ting H.J.,
RA Pang S.T., Yeh S.D., Ma W.L., Chen C.J., Wu W.G., Chang C.;
RT "Identification of a new androgen receptor (AR) co-regulator BUD31 and
RT related peptides to suppress wild-type and mutated AR-mediated prostate
RT cancer growth via peptide screening and X-ray structure analysis.";
RL Mol. Oncol. 8:1575-1587(2014).
RN [11] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [12] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
CC -!- FUNCTION: Involved in the pre-mRNA splicing process (PubMed:28502770,
CC PubMed:28076346). May play a role as regulator of AR transcriptional
CC activity; may increase AR transcriptional activity (PubMed:25091737).
CC {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000305|PubMed:25091737}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:28502770,
CC PubMed:28076346). May interact with AR (PubMed:25091737).
CC {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000305|PubMed:25091737}.
CC -!- INTERACTION:
CC P41223; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-3904603, EBI-724373;
CC P41223; P49639: HOXA1; NbExp=3; IntAct=EBI-3904603, EBI-740785;
CC P41223; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-3904603, EBI-10172290;
CC P41223; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3904603, EBI-16439278;
CC P41223; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3904603, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25091737,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC Note=Detected in chromatin at the promoter of AR target genes.
CC {ECO:0000305|PubMed:25091737}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41223-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41223-2; Sequence=VSP_055558;
CC -!- TISSUE SPECIFICITY: Detected in epithelial and stromal cells in benign
CC prostate hyperplasia tissue (at protein level).
CC {ECO:0000269|PubMed:25091737}.
CC -!- DOMAIN: Contains a short sequence motif (Phe-Xaa-Xaa-Phe-Tyr) that can
CC bind to AR and may modulate AR activity. {ECO:0000305|PubMed:25091737}.
CC -!- SIMILARITY: Belongs to the BUD31 (G10) family. {ECO:0000305}.
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DR EMBL; U11861; AAA20008.1; -; mRNA.
DR EMBL; S77329; AAB33291.1; -; mRNA.
DR EMBL; AK297784; BAH12665.1; -; mRNA.
DR EMBL; AK316477; BAH14848.1; -; mRNA.
DR EMBL; CR456951; CAG33232.1; -; mRNA.
DR EMBL; AC004922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23881.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76670.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76671.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76672.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76673.1; -; Genomic_DNA.
DR EMBL; BC022821; AAH22821.1; -; mRNA.
DR EMBL; BC104670; AAI04671.1; -; mRNA.
DR CCDS; CCDS5663.1; -. [P41223-1]
DR PIR; S52131; S52131.
DR RefSeq; NP_003901.2; NM_003910.3. [P41223-1]
DR RefSeq; XP_005250727.1; XM_005250670.4. [P41223-2]
DR RefSeq; XP_005250728.1; XM_005250671.4. [P41223-2]
DR RefSeq; XP_005250731.1; XM_005250674.3.
DR RefSeq; XP_016868249.1; XM_017012760.1. [P41223-2]
DR RefSeq; XP_016868250.1; XM_017012761.1. [P41223-2]
DR RefSeq; XP_016868251.1; XM_017012762.1.
DR PDB; 4OED; X-ray; 2.79 A; B=56-70.
DR PDB; 4OH6; X-ray; 3.56 A; B=56-70.
DR PDB; 4OKB; X-ray; 2.95 A; B=56-70.
DR PDB; 5MQF; EM; 5.90 A; Q=1-144.
DR PDB; 5XJC; EM; 3.60 A; N=1-144.
DR PDB; 5YZG; EM; 4.10 A; N=1-144.
DR PDB; 5Z56; EM; 5.10 A; N=1-144.
DR PDB; 5Z57; EM; 6.50 A; N=1-144.
DR PDB; 6FF4; EM; 16.00 A; Q=1-144.
DR PDB; 6FF7; EM; 4.50 A; Q=1-144.
DR PDB; 6ICZ; EM; 3.00 A; N=1-144.
DR PDB; 6ID0; EM; 2.90 A; N=1-144.
DR PDB; 6ID1; EM; 2.86 A; N=1-144.
DR PDB; 6QDV; EM; 3.30 A; L=1-144.
DR PDB; 6ZYM; EM; 3.40 A; Q=1-144.
DR PDB; 7AAV; EM; 4.20 A; Q=1-144.
DR PDB; 7ABF; EM; 3.90 A; Q=1-144.
DR PDB; 7ABG; EM; 7.80 A; Q=1-144.
DR PDB; 7ABI; EM; 8.00 A; Q=1-144.
DR PDBsum; 4OED; -.
DR PDBsum; 4OH6; -.
DR PDBsum; 4OKB; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; P41223; -.
DR SMR; P41223; -.
DR BioGRID; 114413; 95.
DR CORUM; P41223; -.
DR IntAct; P41223; 42.
DR MINT; P41223; -.
DR STRING; 9606.ENSP00000386023; -.
DR GlyGen; P41223; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P41223; -.
DR PhosphoSitePlus; P41223; -.
DR SwissPalm; P41223; -.
DR BioMuta; BUD31; -.
DR EPD; P41223; -.
DR jPOST; P41223; -.
DR MassIVE; P41223; -.
DR MaxQB; P41223; -.
DR PaxDb; P41223; -.
DR PeptideAtlas; P41223; -.
DR PRIDE; P41223; -.
DR ProteomicsDB; 55432; -. [P41223-1]
DR Antibodypedia; 16150; 244 antibodies from 29 providers.
DR DNASU; 8896; -.
DR Ensembl; ENST00000222969.10; ENSP00000222969.5; ENSG00000106245.11. [P41223-1]
DR Ensembl; ENST00000403633.6; ENSP00000386023.2; ENSG00000106245.11. [P41223-1]
DR GeneID; 8896; -.
DR KEGG; hsa:8896; -.
DR MANE-Select; ENST00000222969.10; ENSP00000222969.5; NM_003910.4; NP_003901.2.
DR UCSC; uc003uqf.4; human. [P41223-1]
DR CTD; 8896; -.
DR DisGeNET; 8896; -.
DR GeneCards; BUD31; -.
DR HGNC; HGNC:29629; BUD31.
DR HPA; ENSG00000106245; Low tissue specificity.
DR MIM; 603477; gene.
DR neXtProt; NX_P41223; -.
DR OpenTargets; ENSG00000106245; -.
DR PharmGKB; PA144596513; -.
DR VEuPathDB; HostDB:ENSG00000106245; -.
DR eggNOG; KOG3404; Eukaryota.
DR GeneTree; ENSGT00390000014300; -.
DR InParanoid; P41223; -.
DR OMA; VRCIQSR; -.
DR OrthoDB; 1236198at2759; -.
DR PhylomeDB; P41223; -.
DR TreeFam; TF105609; -.
DR PathwayCommons; P41223; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P41223; -.
DR BioGRID-ORCS; 8896; 782 hits in 1052 CRISPR screens.
DR ChiTaRS; BUD31; human.
DR GenomeRNAi; 8896; -.
DR Pharos; P41223; Tbio.
DR PRO; PR:P41223; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P41223; protein.
DR Bgee; ENSG00000106245; Expressed in olfactory segment of nasal mucosa and 209 other tissues.
DR ExpressionAtlas; P41223; baseline and differential.
DR Genevisible; P41223; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:2000825; P:positive regulation of androgen receptor activity; IDA:UniProtKB.
DR InterPro; IPR018230; BUD31/G10-rel_CS.
DR InterPro; IPR001748; G10.
DR PANTHER; PTHR19411; PTHR19411; 1.
DR Pfam; PF01125; G10; 1.
DR PRINTS; PR00322; G10.
DR PROSITE; PS00997; G10_1; 1.
DR PROSITE; PS00998; G10_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Spliceosome; Transcription;
KW Transcription regulation.
FT CHAIN 1..144
FT /note="Protein BUD31 homolog"
FT /id="PRO_0000193897"
FT REGION 59..67
FT /note="Interaction with AR"
FT /evidence="ECO:0000269|PubMed:28076346"
FT MOTIF 2..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 129..144
FT /note="GRIIECTHCGCRGCSG -> VMSDTQAWCCFQLKILP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055558"
FT CONFLICT 12
FT /note="P -> Q (in Ref. 1; AAA20008/AAB33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="E -> Q (in Ref. 1; AAA20008/AAB33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="I -> Y (in Ref. 1; AAA20008/AAB33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..79
FT /note="YEYCI -> LDICY (in Ref. 1; AAA20008)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="Y -> L (in Ref. 1; AAA20008/AAB33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="I -> L (in Ref. 1; AAA20008/AAB33291)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..98
FT /note="YE -> IG (in Ref. 1; AAA20008/AAB33291)"
FT /evidence="ECO:0000305"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:4OED"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6ID0"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:6ID1"
SQ SEQUENCE 144 AA; 17000 MW; 520B8E74C97D0926 CRC64;
MPKVKRSRKA PPDGWELIEP TLDELDQKMR EAETEPHEGK RKVESLWPIF RIHHQKTRYI
FDLFYKRKAI SRELYEYCIK EGYADKNLIA KWKKQGYENL CCLRCIQTRD TNFGTNCICR
VPKSKLEVGR IIECTHCGCR GCSG
