BROX_HUMAN
ID BROX_HUMAN Reviewed; 411 AA.
AC Q5VW32; B7Z9G5; Q96MG1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=BRO1 domain-containing protein BROX;
DE AltName: Full=BRO1 domain- and CAAX motif-containing protein;
DE Flags: Precursor;
GN Name=BROX; Synonyms=BROFTI, C1orf58;
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), ISOPRENYLATION AT CYS-408,
RP METHYLATION AT CYS-408, AND INTERACTION WITH CHMP4B.
RC TISSUE=Cervix carcinoma;
RX PubMed=18190528; DOI=10.1111/j.1742-4658.2007.06230.x;
RA Ichioka F., Kobayashi R., Katoh K., Shibata H., Maki M.;
RT "Brox, a novel farnesylated Bro1 domain-containing protein that associates
RT with charged multivesicular body protein 4 (CHMP4).";
RL FEBS J. 275:682-692(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Skeletal muscle;
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 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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [6]
RP ISOPRENYLATION AT CYS-408.
RX PubMed=17411337; DOI=10.1371/journal.pcbi.0030066;
RA Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,
RA Eisenhaber F.;
RT "Towards complete sets of farnesylated and geranylgeranylated proteins.";
RL PLoS Comput. Biol. 3:634-648(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, 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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-374.
RX PubMed=21889351; DOI=10.1016/j.str.2011.07.016;
RA Sette P., Mu R., Dussupt V., Jiang J., Snyder G., Smith P., Xiao T.S.,
RA Bouamr F.;
RT "The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release.";
RL Structure 19:1485-1495(2011).
CC -!- SUBUNIT: Interacts with CHMP4B. {ECO:0000269|PubMed:18190528}.
CC -!- INTERACTION:
CC Q5VW32; Q9H444: CHMP4B; NbExp=5; IntAct=EBI-6286053, EBI-749627;
CC Q5VW32; Q9NZZ3-1: CHMP5; NbExp=6; IntAct=EBI-6286053, EBI-15979532;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VW32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VW32-2; Sequence=VSP_055551;
CC -!- SIMILARITY: Belongs to the BROX family. {ECO:0000305}.
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DR EMBL; AB276123; BAF56045.1; -; mRNA.
DR EMBL; AK056983; BAB71331.1; -; mRNA.
DR EMBL; AK315930; BAH14301.1; -; mRNA.
DR EMBL; AL392172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93265.1; -; Genomic_DNA.
DR EMBL; BC113635; AAI13636.1; -; mRNA.
DR EMBL; BC113637; AAI13638.1; -; mRNA.
DR EMBL; BC143811; AAI43812.1; -; mRNA.
DR CCDS; CCDS1534.1; -. [Q5VW32-1]
DR CCDS; CCDS73037.1; -. [Q5VW32-2]
DR RefSeq; NP_001275508.1; NM_001288579.1. [Q5VW32-2]
DR RefSeq; NP_001275509.1; NM_001288580.1. [Q5VW32-2]
DR RefSeq; NP_001275510.1; NM_001288581.1.
DR RefSeq; NP_653296.2; NM_144695.3. [Q5VW32-1]
DR RefSeq; XP_005273122.2; XM_005273065.2.
DR RefSeq; XP_011507516.1; XM_011509214.2. [Q5VW32-1]
DR RefSeq; XP_016855863.1; XM_017000374.1. [Q5VW32-1]
DR PDB; 3R9M; X-ray; 1.95 A; A=2-374.
DR PDB; 3ULY; X-ray; 2.60 A; A=2-408.
DR PDB; 3UM0; X-ray; 3.10 A; A=2-408.
DR PDB; 3UM1; X-ray; 2.71 A; A/D=2-377.
DR PDB; 3UM2; X-ray; 2.59 A; A/D=2-377.
DR PDB; 3UM3; X-ray; 3.80 A; A=2-411.
DR PDB; 3ZXP; X-ray; 2.50 A; A/B/C=1-401.
DR PDBsum; 3R9M; -.
DR PDBsum; 3ULY; -.
DR PDBsum; 3UM0; -.
DR PDBsum; 3UM1; -.
DR PDBsum; 3UM2; -.
DR PDBsum; 3UM3; -.
DR PDBsum; 3ZXP; -.
DR AlphaFoldDB; Q5VW32; -.
DR SMR; Q5VW32; -.
DR BioGRID; 127145; 22.
DR DIP; DIP-59406N; -.
DR IntAct; Q5VW32; 13.
DR MINT; Q5VW32; -.
DR STRING; 9606.ENSP00000343742; -.
DR GlyGen; Q5VW32; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VW32; -.
DR PhosphoSitePlus; Q5VW32; -.
DR SwissPalm; Q5VW32; -.
DR BioMuta; BROX; -.
DR DMDM; 74747339; -.
DR EPD; Q5VW32; -.
DR jPOST; Q5VW32; -.
DR MassIVE; Q5VW32; -.
DR MaxQB; Q5VW32; -.
DR PaxDb; Q5VW32; -.
DR PeptideAtlas; Q5VW32; -.
DR PRIDE; Q5VW32; -.
DR ProteomicsDB; 65514; -. [Q5VW32-1]
DR ProteomicsDB; 7028; -.
DR Antibodypedia; 34631; 31 antibodies from 14 providers.
DR DNASU; 148362; -.
DR Ensembl; ENST00000340934.10; ENSP00000343742.5; ENSG00000162819.12. [Q5VW32-1]
DR Ensembl; ENST00000539697.5; ENSP00000441080.1; ENSG00000162819.12. [Q5VW32-2]
DR Ensembl; ENST00000612948.4; ENSP00000478496.1; ENSG00000162819.12. [Q5VW32-2]
DR GeneID; 148362; -.
DR KEGG; hsa:148362; -.
DR MANE-Select; ENST00000340934.10; ENSP00000343742.5; NM_144695.4; NP_653296.2.
DR UCSC; uc001hns.2; human. [Q5VW32-1]
DR CTD; 148362; -.
DR GeneCards; BROX; -.
DR HGNC; HGNC:26512; BROX.
DR HPA; ENSG00000162819; Low tissue specificity.
DR neXtProt; NX_Q5VW32; -.
DR OpenTargets; ENSG00000162819; -.
DR PharmGKB; PA142672509; -.
DR VEuPathDB; HostDB:ENSG00000162819; -.
DR eggNOG; ENOG502QQBR; Eukaryota.
DR GeneTree; ENSGT00390000006681; -.
DR HOGENOM; CLU_056561_0_0_1; -.
DR InParanoid; Q5VW32; -.
DR OMA; HTCLRRA; -.
DR OrthoDB; 614228at2759; -.
DR PhylomeDB; Q5VW32; -.
DR TreeFam; TF314743; -.
DR PathwayCommons; Q5VW32; -.
DR SignaLink; Q5VW32; -.
DR BioGRID-ORCS; 148362; 6 hits in 1079 CRISPR screens.
DR ChiTaRS; BROX; human.
DR GenomeRNAi; 148362; -.
DR Pharos; Q5VW32; Tbio.
DR PRO; PR:Q5VW32; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VW32; protein.
DR Bgee; ENSG00000162819; Expressed in ileal mucosa and 187 other tissues.
DR ExpressionAtlas; Q5VW32; baseline and differential.
DR Genevisible; Q5VW32; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR InterPro; IPR038898; BROX.
DR PANTHER; PTHR23032; PTHR23032; 1.
DR Pfam; PF03097; BRO1; 1.
DR SMART; SM01041; BRO1; 1.
DR PROSITE; PS51180; BRO1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Lipoprotein; Membrane;
KW Methylation; Prenylation; Reference proteome.
FT CHAIN 1..408
FT /note="BRO1 domain-containing protein BROX"
FT /id="PRO_0000304612"
FT PROPEP 409..411
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396736"
FT DOMAIN 90..408
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REGION 372..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 408
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305|PubMed:18190528"
FT LIPID 408
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:17411337,
FT ECO:0000269|PubMed:18190528"
FT VAR_SEQ 103..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_055551"
FT CONFLICT 335
FT /note="I -> T (in Ref. 1; BAF56045 and 2; BAB71331)"
FT /evidence="ECO:0000305"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 27..46
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3R9M"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3ZXP"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3R9M"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3R9M"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3ULY"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 107..130
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 137..160
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3R9M"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3ZXP"
FT HELIX 177..201
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 206..227
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 232..263
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 267..292
FT /evidence="ECO:0007829|PDB:3R9M"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:3ZXP"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 307..329
FT /evidence="ECO:0007829|PDB:3R9M"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:3ULY"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:3R9M"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3ULY"
SQ SEQUENCE 411 AA; 46476 MW; 6ED03F79BE1514C6 CRC64;
MTHWFHRNPL KATAPVSFNY YGVVTGPSAS KICNDLRSSR ARLLELFTDL SCNPEMMKNA
ADSYFSLLQG FINSLDESTQ ESKLRYIQNF KWTDTLQGQV PSAQQDAVFE LISMGFNVAL
WYTKYASRLA GKENITEDEA KEVHRSLKIA AGIFKHLKES HLPKLITPAE KGRDLESRLI
EAYVIQCQAE AQEVTIARAI ELKHAPGLIA ALAYETANFY QKADHTLSSL EPAYSAKWRK
YLHLKMCFYT AYAYCYHGET LLASDKCGEA IRSLQEAEKL YAKAEALCKE YGETKGPGPT
VKPSGHLFFR KLGNLVKNTL EKCQRENGFI YFQKIPTEAP QLELKANYGL VEPIPFEFPP
TSVQWTPETL AAFDLTKRPK DDSTKPKPEE EVKPVKEPDI KPQKDTGCYI S
