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Protein

Proteasome activator BLM10

Gene

BLM10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Involved in DNA damage response in somatic cells: binds to acetylated histones and promotes degradation of histones following DNA double-strand breaks.7 Publications

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB
  • peptidase activator activity Source: UniProtKB
  • proteasome binding Source: SGD

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB
  • histone exchange Source: UniProtKB
  • positive regulation of peptidase activity Source: GOC
  • proteasomal ubiquitin-independent protein catabolic process Source: UniProtKB
  • proteasome assembly Source: SGD
  • proteasome core complex import into nucleus Source: SGD
  • regulation of proteasomal protein catabolic process Source: SGD
  • sequestration of proteasome core complex in proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-30449-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome activator BLM10
Alternative name(s):
Bleomycin resistance protein BLM10
Gene namesi
Name:BLM10
Synonyms:BLM3
Ordered Locus Names:YFL007W
ORF Names:YFL006W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL007W.
SGDiS000001887. BLM10.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1663 – 16642YN → HD: Abolihes binding to acetylated histones. 1 Publication
Mutagenesisi2139 – 21391R → D: Does not affect binding to the proteasome. 1 Publication
Mutagenesisi2140 – 21401S → H: Abolishes binding to the proteasome. 1 Publication
Mutagenesisi2141 – 21433Missing : Loss of function. 1 Publication
Mutagenesisi2141 – 21411Y → M: Does not affect viability in the presence of cycloheximide. 1 Publication
Mutagenesisi2142 – 21421Y → A or V: Loss of function; abolishes binding to the proteasome. 1 Publication
Mutagenesisi2142 – 21421Y → V: Abolishes binding to the proteasome. 1 Publication
Mutagenesisi2143 – 21431A → S: Does not affect viability in the presence of cycloheximide. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21432143Proteasome activator BLM10PRO_0000076182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei64 – 641PhosphothreonineCombined sources
Modified residuei66 – 661PhosphothreonineCombined sources
Modified residuei1041 – 10411PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43583.
PeptideAtlasiP43583.

PTM databases

iPTMnetiP43583.

Interactioni

Subunit structurei

According to PubMed:12973301, colocalizes with nascent proteasome. According to PubMed:15778719, associates with proteasome core particles and also forms a complex with regulatory particle-core particle (RP-CP).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GSP1P328352EBI-22761,EBI-7926
PRE2P306563EBI-22761,EBI-14001

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB
  • proteasome binding Source: SGD

Protein-protein interaction databases

BioGridi31140. 114 interactions.
DIPiDIP-6344N.
IntActiP43583. 14 interactions.
MINTiMINT-640764.

Structurei

Secondary structure

1
2143
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 888Combined sources
Helixi97 – 1037Combined sources
Helixi122 – 1254Combined sources
Beta strandi126 – 1283Combined sources
Helixi133 – 15321Combined sources
Helixi240 – 2489Combined sources
Helixi249 – 2524Combined sources
Helixi257 – 27115Combined sources
Helixi280 – 29011Combined sources
Helixi300 – 3067Combined sources
Helixi313 – 3208Combined sources
Turni321 – 3233Combined sources
Turni329 – 3313Combined sources
Turni339 – 3413Combined sources
Helixi342 – 35413Combined sources
Helixi364 – 3663Combined sources
Helixi367 – 3748Combined sources
Helixi375 – 3773Combined sources
Turni380 – 3823Combined sources
Helixi383 – 39311Combined sources
Helixi405 – 4073Combined sources
Helixi408 – 4147Combined sources
Turni415 – 4173Combined sources
Helixi422 – 44322Combined sources
Beta strandi444 – 4463Combined sources
Helixi465 – 48016Combined sources
Helixi488 – 4969Combined sources
Turni505 – 5073Combined sources
Helixi508 – 52215Combined sources
Helixi531 – 55222Combined sources
Turni553 – 5597Combined sources
Beta strandi563 – 5653Combined sources
Helixi568 – 58619Combined sources
Helixi591 – 60616Combined sources
Helixi612 – 62716Combined sources
Turni628 – 6336Combined sources
Helixi635 – 64612Combined sources
Helixi649 – 6524Combined sources
Helixi658 – 6614Combined sources
Helixi662 – 67110Combined sources
Helixi678 – 69316Combined sources
Helixi709 – 7124Combined sources
Helixi714 – 72512Combined sources
Beta strandi730 – 7323Combined sources
Helixi739 – 7479Combined sources
Turni748 – 7503Combined sources
Helixi751 – 76515Combined sources
Helixi773 – 78715Combined sources
Helixi791 – 80616Combined sources
Beta strandi813 – 8153Combined sources
Helixi819 – 83113Combined sources
Helixi833 – 8353Combined sources
Helixi836 – 85217Combined sources
Turni853 – 8564Combined sources
Beta strandi861 – 8633Combined sources
Turni866 – 8683Combined sources
Helixi869 – 88214Combined sources
Turni883 – 8853Combined sources
Helixi886 – 8905Combined sources
Helixi893 – 90513Combined sources
Helixi910 – 9167Combined sources
Helixi919 – 92810Combined sources
Beta strandi937 – 9415Combined sources
Beta strandi953 – 9564Combined sources
Helixi957 – 9604Combined sources
Turni962 – 9643Combined sources
Helixi974 – 99724Combined sources
Helixi1009 – 102315Combined sources
Helixi1026 – 10294Combined sources
Helixi1032 – 10354Combined sources
Beta strandi1158 – 11614Combined sources
Turni1162 – 11654Combined sources
Helixi1167 – 119327Combined sources
Helixi1199 – 121113Combined sources
Beta strandi1215 – 12173Combined sources
Helixi1231 – 12388Combined sources
Helixi1249 – 126618Combined sources
Helixi1276 – 128813Combined sources
Helixi1293 – 130715Combined sources
Beta strandi1308 – 13103Combined sources
Helixi1313 – 133018Combined sources
Helixi1335 – 13439Combined sources
Helixi1347 – 13526Combined sources
Helixi1353 – 13553Combined sources
Helixi1357 – 136913Combined sources
Beta strandi1374 – 13774Combined sources
Turni1378 – 13803Combined sources
Helixi1381 – 139010Combined sources
Helixi1404 – 14063Combined sources
Helixi1408 – 14103Combined sources
Helixi1420 – 14278Combined sources
Helixi1430 – 145122Combined sources
Helixi1460 – 147112Combined sources
Helixi1481 – 14888Combined sources
Helixi1489 – 14935Combined sources
Helixi1496 – 150611Combined sources
Helixi1508 – 151912Combined sources
Helixi1523 – 15264Combined sources
Beta strandi1527 – 15304Combined sources
Beta strandi1536 – 15416Combined sources
Turni1544 – 15463Combined sources
Helixi1547 – 15548Combined sources
Beta strandi1577 – 15826Combined sources
Helixi1593 – 160311Combined sources
Helixi1608 – 162013Combined sources
Turni1621 – 16255Combined sources
Helixi1630 – 164314Combined sources
Helixi1652 – 16543Combined sources
Helixi1655 – 16617Combined sources
Helixi1668 – 168114Combined sources
Turni1690 – 16923Combined sources
Helixi1693 – 170816Combined sources
Helixi1716 – 173015Combined sources
Helixi1733 – 17353Combined sources
Helixi1737 – 17437Combined sources
Helixi1764 – 177411Combined sources
Helixi1782 – 17876Combined sources
Helixi1795 – 181016Combined sources
Helixi1820 – 18289Combined sources
Beta strandi1831 – 18344Combined sources
Helixi1843 – 185614Combined sources
Helixi1858 – 18614Combined sources
Turni1869 – 18735Combined sources
Helixi1875 – 189016Combined sources
Helixi1893 – 18953Combined sources
Helixi1896 – 18994Combined sources
Helixi1900 – 19023Combined sources
Helixi1903 – 19075Combined sources
Turni1908 – 19114Combined sources
Helixi1919 – 19235Combined sources
Helixi1929 – 19346Combined sources
Beta strandi1936 – 19383Combined sources
Helixi1942 – 195110Combined sources
Turni1955 – 19584Combined sources
Beta strandi1961 – 19633Combined sources
Helixi1964 – 197815Combined sources
Turni1979 – 19813Combined sources
Helixi1986 – 19894Combined sources
Helixi1991 – 19944Combined sources
Turni1995 – 19995Combined sources
Helixi2004 – 201916Combined sources
Helixi2024 – 203411Combined sources
Turni2039 – 20413Combined sources
Helixi2045 – 205410Combined sources
Helixi2056 – 206914Combined sources
Helixi2081 – 209010Combined sources
Beta strandi2093 – 20953Combined sources
Helixi2099 – 21024Combined sources
Helixi2104 – 211310Combined sources
Helixi2118 – 21214Combined sources
Helixi2122 – 21243Combined sources
Helixi2131 – 21333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V7OX-ray3.00A5/A7/B4/B7239-1037[»]
A6/A8/B5/B81147-2143[»]
AE/AF/B3/B679-154[»]
ProteinModelPortaliP43583.
SMRiP43583. Positions 79-154, 239-1037, 1147-2143.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1316 – 135540HEAT 1Add
BLAST
Repeati1779 – 181436HEAT 2Add
BLAST
Repeati1902 – 194140HEAT 3Add
BLAST
Repeati1985 – 202339HEAT 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1648 – 173285Bromodomain-like (BRDL)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2141 – 21433YYX motif

Domaini

The bromodomain-like (BRDL) region specifically recognizes and binds acetylated histones.1 Publication
The YYX motif is required for the association with the proteasome.1 Publication

Sequence similaritiesi

Belongs to the BLM10 family.Curated
Contains 4 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000095237.
InParanoidiP43583.
KOiK06699.
OMAiFQILLHG.
OrthoDBiEOG7WMCSR.

Family and domain databases

Gene3Di1.25.10.10. 5 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032430. Blm10_mid.
IPR032372. Blm10_N.
IPR021843. DUF3437.
[Graphical view]
PfamiPF16507. BLM10_mid. 1 hit.
PF16547. BLM10_N. 1 hit.
PF11919. DUF3437. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.

Sequencei

Sequence statusi: Complete.

P43583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTANNDDDIK SPIPITNKTL SQLKRFERSP GRPSSSQGEI KRKKSRLYAA
60 70 80 90 100
DGRPHSPLRA RSATPTLQDQ KLFNGMDSTS LLNERLQHYT LDYVSDRAQH
110 120 130 140 150
MKNIYDPSSR WFSRSVRPEF PIEEFLPYKT ESHEDQAKYL CHVLVNLYIA
160 170 180 190 200
ISSLDIQGLI SISSKDLADL KKEVDDLALK TDLFRLSNNT AENDLLGNDI
210 220 230 240 250
ADYDDAEGLE DELDEYFDLA GPDFNATGKI TAKSATIVNV NHWTNELKNC
260 270 280 290 300
LHFDFPVALR KSLATVYYYL SLVQGQKVYR QMHVDMFERL VSLDDDRTNF
310 320 330 340 350
TELLQKQGLL LDHQIMLNFL CEFLPYPDPD YARYELSSKE DLQLFRLLLK
360 370 380 390 400
HAHNAKPFFD KSKESLLVDT MNFLLSSLAP STMMAVMPIV TSVVPYHYHI
410 420 430 440 450
HSKIIDYFPF CYSIWSSVSA NVAIDTHMYD FVGSISKDVH NKILSSEHEK
460 470 480 490 500
DVVGVEFGEF GIFTDDQMTF MFNRLQGHLR TDGQIHSYSR TVKPFVYAIN
510 520 530 540 550
GSKKDRFFEK LVSLAKAIET FIHPSNNGFW TKPNAKFVHA FIKSYHGRVK
560 570 580 590 600
YEEDICARGV TNGICLTSFC HEEIVEIFLN IISLGSQNKN PDIANYYISC
610 620 630 640 650
FAYLLELDPS NAYLIYDKIL IDLYDTLADQ FINSRHRIIS SLKQFTRVIR
660 670 680 690 700
FIVMDKLYRV HITNVLSMLV SKLDMNDTNL TSNLINGIVS IAAFIPIQDL
710 720 730 740 750
TGEDDYISFE SDTLPLVQQH FYHIKCGESS KTFRVDDELL NNAFKASTTV
760 770 780 790 800
FQSMLKVYVE KIFQLVDVDL EDSLVTKINQ TTMILQESMD DKIFNYFASL
810 820 830 840 850
LQRNFWSNDS FKEKDPNYEL VTIPLAALVR RNNGLSKELV RTLLFHIKEQ
860 870 880 890 900
IKRGAGSVRS TSEIQQRDVK LVLYLTALND VLRQCHESLL EYSDELITFM
910 920 930 940 950
KYLYDNVTNP PLDVITSIVI HSALATLCTT EITDCRLFPE DSKIPEKDRW
960 970 980 990 1000
GGLQFDPRRF DKQHLSFQWH VPSSDEITLS ISILESLSEY CINNVEELMK
1010 1020 1030 1040 1050
APRHDSEYGD MIQKYVLVMT HTLSGSSLLF DPDFNKYRTQ SNLSYREKLI
1060 1070 1080 1090 1100
LLKNIRENNC DPQELDIDIE QIRSGKDDED YIESKDIEAG LNAGVSDVVQ
1110 1120 1130 1140 1150
LRDEFPDELI VDEEVVSEMP SGVNTPIAGT HGTDNSAMSS DLAFRDLDIY
1160 1170 1180 1190 1200
TCNYYFGNTT EEKLQNPQYL QVHRVRARIG HFFHKLYVFL STNFENNTNM
1210 1220 1230 1240 1250
FQILLHGLKV WFTDLGQETV FNEDPNAFID VDFLENVQSL SHVNEPFTRT
1260 1270 1280 1290 1300
NFAIRANSLH QSRVLLHSTN RKASKLENLL LVDIIQLATS LYPDIYKPAQ
1310 1320 1330 1340 1350
GTLVHCMKQL VGSYGVVINK IIPSLEKAIK DHDYMKIQVI LNVLLIKKIH
1360 1370 1380 1390 1400
RKLMTDYKDI GRLIFLLIEC CRVNELEIGM YADKILTDIV IGIKIPSSVC
1410 1420 1430 1440 1450
VISDQAFLPL APPDGTINLQ VEAVKLAKKK KREYYLSLLV DLQDKLLDKL
1460 1470 1480 1490 1500
DNEKDMGWKI RMFILRFVTQ IQSNLESKPD KRAVFSIISQ ISTKHPEIIH
1510 1520 1530 1540 1550
LVVKSLLSTC NKIISLSDYE YDITRAYKNE FNPSFVEILD TSTTSFPKTF
1560 1570 1580 1590 1600
TEEMNNFDNP KYFIDLRAYV GWLCWGRLMY VMSPKALKLN LRENELEVLK
1610 1620 1630 1640 1650
TAGHLLTREF LRDVTMNLVQ DNETRGVFSS GNVSFFSLVI LLISSGFCEL
1660 1670 1680 1690 1700
NMSDLFELCE SYYNKDDKAS MIMSVEIVAG LVCGSKFMSV SDLDKRDTFI
1710 1720 1730 1740 1750
ENFLAKCLDY ELNHDAFEIW STLAWWLPAV VDLRRSKTFF CHFINADGMF
1760 1770 1780 1790 1800
DRESDAATHQ TSKIYMLRSI LMSMEFRAPD VGKLFDELVF DHPYDQVRQA
1810 1820 1830 1840 1850
VAKLLTTLVQ NQSNPSISDP TTLLEAERND PDGLGLPLKS VPEKVDAYIK
1860 1870 1880 1890 1900
KQFEIIKNLE DSVVGLNPQQ FIKTDYFYRT STIFYWIKEM ARGPNKVLLV
1910 1920 1930 1940 1950
PYLVDYVLPF LIGLVKHKDV CALASLDPVR LYAGLGYMPI RKNHVAAIVD
1960 1970 1980 1990 2000
YVCSSNVALS SNQTKLQLAF IQHFLSAELL QLTEEEKNKI LEFVVSNLYN
2010 2020 2030 2040 2050
EQFVEVRVRA ASILSDIVHN WKEEQPLLSL IERFAKGLDV NKYTSKERQK
2060 2070 2080 2090 2100
LSKTDIKIHG NVLGLGAIIS AFPYVFPLPP WIPKQLSNLS SWARTSGMTG
2110 2120 2130 2140
QAAKNTISEF KKVRADTWKF DRASFNTEEL EDLEGVLWRS YYA
Length:2,143
Mass (Da):245,996
Last modified:December 6, 2005 - v2
Checksum:iA195A4455C687644
GO

Sequence cautioni

The sequence BAA09231.1 differs from that shown. Reason: Frameshift at position 1800. Produces 2 separate ORFs.Curated
The sequence BAA09232.1 differs from that shown. Reason: Frameshift at position 1800. Produces 2 separate ORFs.Curated
The sequence described in PubMed:11842813 differs from that shown. Reason: Frameshift at position 1800. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09231.1. Frameshift.
D50617 Genomic DNA. Translation: BAA09232.1. Frameshift.
AY693254 Genomic DNA. Translation: AAT93273.1.
BK006940 Genomic DNA. Translation: DAA12433.1.
PIRiS56247.
S56248.
RefSeqiNP_116648.2. NM_001179959.1.

Genome annotation databases

EnsemblFungiiBAA09231; BAA09231; BAA09231.
BAA09232; BAA09232; BAA09232.
YFL007W; YFL007W; YFL007W.
GeneIDi850541.
KEGGisce:YFL007W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09231.1. Frameshift.
D50617 Genomic DNA. Translation: BAA09232.1. Frameshift.
AY693254 Genomic DNA. Translation: AAT93273.1.
BK006940 Genomic DNA. Translation: DAA12433.1.
PIRiS56247.
S56248.
RefSeqiNP_116648.2. NM_001179959.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V7OX-ray3.00A5/A7/B4/B7239-1037[»]
A6/A8/B5/B81147-2143[»]
AE/AF/B3/B679-154[»]
ProteinModelPortaliP43583.
SMRiP43583. Positions 79-154, 239-1037, 1147-2143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31140. 114 interactions.
DIPiDIP-6344N.
IntActiP43583. 14 interactions.
MINTiMINT-640764.

PTM databases

iPTMnetiP43583.

Proteomic databases

MaxQBiP43583.
PeptideAtlasiP43583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09231; BAA09231; BAA09231.
BAA09232; BAA09232; BAA09232.
YFL007W; YFL007W; YFL007W.
GeneIDi850541.
KEGGisce:YFL007W.

Organism-specific databases

EuPathDBiFungiDB:YFL007W.
SGDiS000001887. BLM10.

Phylogenomic databases

HOGENOMiHOG000095237.
InParanoidiP43583.
KOiK06699.
OMAiFQILLHG.
OrthoDBiEOG7WMCSR.

Enzyme and pathway databases

BioCyciYEAST:G3O-30449-MONOMER.

Miscellaneous databases

NextBioi966304.
PROiP43583.

Family and domain databases

Gene3Di1.25.10.10. 5 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032430. Blm10_mid.
IPR032372. Blm10_N.
IPR021843. DUF3437.
[Graphical view]
PfamiPF16507. BLM10_mid. 1 hit.
PF16547. BLM10_N. 1 hit.
PF11919. DUF3437. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Revisiting the yeast chromosome VI DNA sequence reveals a correction merging YFL007w and YFL006w to a single ORF."
    Robben J., Hertveldt K., Volckaert G.
    Yeast 19:699-702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF FRAMESHIFT.
    Strain: ATCC 201390 / BY4743 and ATCC 96604 / S288c / FY1679.
  2. "Expression of the expanded YFL007w ORF and assignment of the gene name BLM10."
    Doherty K., Pramanik A., Pride L., Lukose J., Moore C.W.
    Yeast 21:1021-1023(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF FRAMESHIFT.
    Strain: CM1469-5C.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "The novel BLM3 gene encodes a protein that protects against lethal effects of oxidative damage."
    Febres D.E., Pramanik A., Caton M., Doherty K., McKoy J., Garcia E., Alejo W., Moore C.W.
    Cell. Mol. Biol. 47:1149-1162(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1804, FUNCTION.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1890-2143.
    Strain: ATCC 204508 / S288c.
  8. "The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle."
    Schmidt M., Haas W., Crosas B., Santamaria P.G., Gygi S.P., Walz T., Finley D.
    Nat. Struct. Mol. Biol. 12:294-303(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 340-346; 481-490; 813-830; 860-867; 950-958; 1039-1046; 1086-1102; 1164-1174; 1250-1271; 1513-1525; 1528-1548; 1562-1567; 1578-1585; 1601-1608; 1687-1706 AND 2123-2139, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly."
    Fehlker M., Wendler P., Lehmann A., Enenkel C.
    EMBO Rep. 4:959-963(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  10. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FRAMESHIFT.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-1041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-62; THR-64 AND SER-1041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Blm10 binds to pre-activated proteasome core particles with open gate conformation."
    Lehmann A., Jechow K., Enenkel C.
    EMBO Rep. 9:1237-1243(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THE PROTEASOME.
  16. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-56 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-64; THR-66 AND SER-1041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism."
    Dange T., Smith D., Noy T., Rommel P.C., Jurzitza L., Cordero R.J., Legendre A., Finley D., Goldberg A.L., Schmidt M.
    J. Biol. Chem. 286:42830-42839(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-2139; SER-2140; TYR-2141; TYR-2142 AND ALA-2143.
  19. Cited for: FUNCTION, MUTAGENESIS OF 1663-TYR-ASN-1664.
  20. "Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes."
    Iwanczyk J., Sadre-Bazzaz K., Ferrell K., Kondrashkina E., Formosa T., Hill C.P., Ortega J.
    J. Mol. Biol. 363:648-659(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF THE PROTEASOME BY ELECTRON MICROSCOPY.
  21. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
    Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
    Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 79-2143 IN COMPLEX WITH THE PROTEASOME, FUNCTION, MUTAGENESIS OF 2141-TYR--ALA-2143.

Entry informationi

Entry nameiBLM10_YEAST
AccessioniPrimary (citable) accession number: P43583
Secondary accession number(s): D6VTM3, P43584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 6, 2005
Last modified: May 11, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.