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Database: UniProt
Entry: P41223
LinkDB: P41223
Original site: P41223 
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   29-SEP-2021, entry version 175.
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   SMR; P41223; -.
DR   BioGRID; 114413; 74.
DR   CORUM; P41223; -.
DR   IntAct; P41223; 41.
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; 241 antibodies.
DR   DNASU; 8896; -.
DR   Ensembl; ENST00000222969; ENSP00000222969; ENSG00000106245. [P41223-1]
DR   Ensembl; ENST00000403633; ENSP00000386023; ENSG00000106245. [P41223-1]
DR   GeneID; 8896; -.
DR   KEGG; hsa:8896; -.
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; CIQSRDM; -.
DR   OrthoDB; 1236198at2759; -.
DR   PhylomeDB; P41223; -.
DR   TreeFam; TF105609; -.
DR   PathwayCommons; P41223; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 8896; 774 hits in 994 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 testis and 246 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
//
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