Full text data of BROX
BROX
(BROFTI, C1orf58)
[Confidence: low (only semi-automatic identification from reviews)]
BRO1 domain-containing protein BROX (BRO1 domain- and CAAX motif-containing protein; Flags: Precursor)
BRO1 domain-containing protein BROX (BRO1 domain- and CAAX motif-containing protein; Flags: Precursor)
UniProt
Q5VW32
ID BROX_HUMAN Reviewed; 411 AA.
AC Q5VW32; Q96MG1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 73.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-408, AND INTERACTION
RP 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
RT associates with charged multivesicular body protein 4 (CHMP4).";
RL FEBS J. 275:682-692(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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
RT proteins.";
RL PLoS Comput. Biol. 3:634-648(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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
RT release.";
RL Structure 19:1485-1495(2011).
CC -!- SUBUNIT: Interacts with CHMP4B.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC -!- SIMILARITY: Belongs to the BROX family.
CC -!- SIMILARITY: Contains 1 BRO1 domain.
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DR EMBL; AB276123; BAF56045.1; -; mRNA.
DR EMBL; AK056983; BAB71331.1; -; mRNA.
DR EMBL; AL392172; CAH73932.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93265.1; -; Genomic_DNA.
DR EMBL; BC113635; AAI13636.1; -; mRNA.
DR EMBL; BC113637; AAI13638.1; -; mRNA.
DR RefSeq; NP_653296.2; NM_144695.2.
DR UniGene; Hs.552608; -.
DR PDB; 3R9M; X-ray; 1.95 A; A=2-374.
DR PDB; 3ULY; X-ray; 2.60 A; A=2-411.
DR PDB; 3UM0; X-ray; 3.10 A; A=2-411.
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 ProteinModelPortal; Q5VW32; -.
DR SMR; Q5VW32; 2-374.
DR DIP; DIP-59406N; -.
DR IntAct; Q5VW32; 1.
DR STRING; 9606.ENSP00000343742; -.
DR PhosphoSite; Q5VW32; -.
DR DMDM; 74747339; -.
DR PaxDb; Q5VW32; -.
DR PeptideAtlas; Q5VW32; -.
DR PRIDE; Q5VW32; -.
DR Ensembl; ENST00000340934; ENSP00000343742; ENSG00000162819.
DR GeneID; 148362; -.
DR KEGG; hsa:148362; -.
DR UCSC; uc001hnq.1; human.
DR CTD; 148362; -.
DR GeneCards; GC01P222886; -.
DR H-InvDB; HIX0001617; -.
DR H-InvDB; HIX0001618; -.
DR HGNC; HGNC:26512; BROX.
DR HPA; HPA031445; -.
DR neXtProt; NX_Q5VW32; -.
DR PharmGKB; PA142672509; -.
DR eggNOG; NOG150121; -.
DR HOGENOM; HOG000007224; -.
DR HOVERGEN; HBG107541; -.
DR InParanoid; Q5VW32; -.
DR OMA; EAKDVHR; -.
DR OrthoDB; EOG7X3QQZ; -.
DR PhylomeDB; Q5VW32; -.
DR ChiTaRS; BROX; human.
DR GenomeRNAi; 148362; -.
DR NextBio; 85919; -.
DR PRO; PR:Q5VW32; -.
DR ArrayExpress; Q5VW32; -.
DR Bgee; Q5VW32; -.
DR CleanEx; HS_C1orf58; -.
DR Genevestigator; Q5VW32; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR004328; BRO1_dom.
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; Complete proteome; Lipoprotein; Membrane;
KW Methylation; Prenylation; Reference proteome.
FT CHAIN 1 408 BRO1 domain-containing protein BROX.
FT /FTId=PRO_0000304612.
FT PROPEP 409 411 Removed in mature form (Probable).
FT /FTId=PRO_0000396736.
FT DOMAIN 90 408 BRO1.
FT MOD_RES 283 283 N6-acetyllysine.
FT MOD_RES 408 408 Cysteine methyl ester (Probable).
FT LIPID 408 408 S-farnesyl cysteine.
FT CONFLICT 335 335 I -> T (in Ref. 1; BAF56045 and 2;
FT BAB71331).
FT HELIX 21 23
FT HELIX 27 46
FT HELIX 54 68
FT HELIX 69 71
FT STRAND 75 81
FT TURN 83 86
FT STRAND 90 92
FT STRAND 95 97
FT STRAND 102 105
FT HELIX 107 130
FT HELIX 137 160
FT HELIX 162 164
FT STRAND 173 176
FT HELIX 177 201
FT HELIX 206 227
FT HELIX 232 263
FT HELIX 267 292
FT STRAND 298 301
FT HELIX 303 305
FT HELIX 307 329
FT STRAND 347 349
FT HELIX 367 371
FT HELIX 375 377
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
//
ID BROX_HUMAN Reviewed; 411 AA.
AC Q5VW32; Q96MG1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 73.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ISOPRENYLATION AT CYS-408, AND INTERACTION
RP 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
RT associates with charged multivesicular body protein 4 (CHMP4).";
RL FEBS J. 275:682-692(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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
RT proteins.";
RL PLoS Comput. Biol. 3:634-648(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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
RT release.";
RL Structure 19:1485-1495(2011).
CC -!- SUBUNIT: Interacts with CHMP4B.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC -!- SIMILARITY: Belongs to the BROX family.
CC -!- SIMILARITY: Contains 1 BRO1 domain.
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DR EMBL; AB276123; BAF56045.1; -; mRNA.
DR EMBL; AK056983; BAB71331.1; -; mRNA.
DR EMBL; AL392172; CAH73932.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93265.1; -; Genomic_DNA.
DR EMBL; BC113635; AAI13636.1; -; mRNA.
DR EMBL; BC113637; AAI13638.1; -; mRNA.
DR RefSeq; NP_653296.2; NM_144695.2.
DR UniGene; Hs.552608; -.
DR PDB; 3R9M; X-ray; 1.95 A; A=2-374.
DR PDB; 3ULY; X-ray; 2.60 A; A=2-411.
DR PDB; 3UM0; X-ray; 3.10 A; A=2-411.
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 ProteinModelPortal; Q5VW32; -.
DR SMR; Q5VW32; 2-374.
DR DIP; DIP-59406N; -.
DR IntAct; Q5VW32; 1.
DR STRING; 9606.ENSP00000343742; -.
DR PhosphoSite; Q5VW32; -.
DR DMDM; 74747339; -.
DR PaxDb; Q5VW32; -.
DR PeptideAtlas; Q5VW32; -.
DR PRIDE; Q5VW32; -.
DR Ensembl; ENST00000340934; ENSP00000343742; ENSG00000162819.
DR GeneID; 148362; -.
DR KEGG; hsa:148362; -.
DR UCSC; uc001hnq.1; human.
DR CTD; 148362; -.
DR GeneCards; GC01P222886; -.
DR H-InvDB; HIX0001617; -.
DR H-InvDB; HIX0001618; -.
DR HGNC; HGNC:26512; BROX.
DR HPA; HPA031445; -.
DR neXtProt; NX_Q5VW32; -.
DR PharmGKB; PA142672509; -.
DR eggNOG; NOG150121; -.
DR HOGENOM; HOG000007224; -.
DR HOVERGEN; HBG107541; -.
DR InParanoid; Q5VW32; -.
DR OMA; EAKDVHR; -.
DR OrthoDB; EOG7X3QQZ; -.
DR PhylomeDB; Q5VW32; -.
DR ChiTaRS; BROX; human.
DR GenomeRNAi; 148362; -.
DR NextBio; 85919; -.
DR PRO; PR:Q5VW32; -.
DR ArrayExpress; Q5VW32; -.
DR Bgee; Q5VW32; -.
DR CleanEx; HS_C1orf58; -.
DR Genevestigator; Q5VW32; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR004328; BRO1_dom.
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; Complete proteome; Lipoprotein; Membrane;
KW Methylation; Prenylation; Reference proteome.
FT CHAIN 1 408 BRO1 domain-containing protein BROX.
FT /FTId=PRO_0000304612.
FT PROPEP 409 411 Removed in mature form (Probable).
FT /FTId=PRO_0000396736.
FT DOMAIN 90 408 BRO1.
FT MOD_RES 283 283 N6-acetyllysine.
FT MOD_RES 408 408 Cysteine methyl ester (Probable).
FT LIPID 408 408 S-farnesyl cysteine.
FT CONFLICT 335 335 I -> T (in Ref. 1; BAF56045 and 2;
FT BAB71331).
FT HELIX 21 23
FT HELIX 27 46
FT HELIX 54 68
FT HELIX 69 71
FT STRAND 75 81
FT TURN 83 86
FT STRAND 90 92
FT STRAND 95 97
FT STRAND 102 105
FT HELIX 107 130
FT HELIX 137 160
FT HELIX 162 164
FT STRAND 173 176
FT HELIX 177 201
FT HELIX 206 227
FT HELIX 232 263
FT HELIX 267 292
FT STRAND 298 301
FT HELIX 303 305
FT HELIX 307 329
FT STRAND 347 349
FT HELIX 367 371
FT HELIX 375 377
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
//