Reviewed, UniProtKB/Swiss-Prot P43583 (BLM10_YEAST)

Names and origin

Protein names

Recommended name:
    Proteasome activator BLM10
Alternative name(s):
    Bleomycin resistance protein BLM10

Gene names

Name:	BLM10
Synonyms:	BLM3
Ordered Locus Names:	YFL007W/YFL006W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2143 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	According to Ref.8, involved in the late stage of nuclear proteasome assembly by preventing premature activation of proteasomal core particles (CPs). According to Ref.7, regulates proteasome by capping the proteolytically active CP and activates CP by opening the axial channel into its proteolytic chamber. May be involved in protection against oxidative damage.
Subunit structure	According to Ref.8, colocalizes with nascent proteasome. According to Ref.7, associates with proteasome core particles and also forms a complex with regulatory particle-core particle (RP-CP).
Subcellular location	Nucleus. Cytoplasm.
Miscellaneous	Present with 2600 molecules/cell in log phase SD medium.
Sequence similarities	Contains 4 HEAT repeats.
Sequence caution	BAA09231.1 sequence differs from that shown. Reason: Frameshift at position 1800. Produces 2 separate ORFs. BAA09232.1 sequence differs from that shown. Reason: Frameshift at position 1800. Produces 2 separate ORFs. Ref.5 sequence differs from that shown. Reason: Frameshift at position 1800.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteasome assembly Ref.9 Inferred from mutant phenotype. Source: SGD protein catabolic process Ref.7 Ref.9 Inferred from mutant phenotype. Source: SGD
Cellular component	nucleus Ref.7 Ref.9 Inferred from direct assay. Source: SGD
Molecular function	proteasome activator activity Ref.7 Ref.9 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SSA2	P10592	1	EBI-22761,EBI-8603
SSB1	P11484	1	EBI-22761,EBI-8627

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 2143	2143	Proteasome activator BLM10
Regions
	Repeat	1316 – 1355	40	HEAT 1
	Repeat	1779 – 1814	36	HEAT 2
	Repeat	1902 – 1941	40	HEAT 3
	Repeat	1985 – 2023	39	HEAT 4
Amino acid modifications
	Modified residue	11	1	Phosphoserine
	Modified residue	29	1	Phosphoserine
	Modified residue	34	1	Phosphoserine
	Modified residue	35	1	Phosphoserine
	Modified residue	56	1	Phosphoserine
	Modified residue	62	1	Phosphoserine
	Modified residue	64	1	Phosphothreonine
	Modified residue	66	1	Phosphothreonine
	Modified residue	1041	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	P43583-1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: A195A4455C687644	FASTA	2,143	245,996
	10 20 30 40 50 60 MTANNDDDIK SPIPITNKTL SQLKRFERSP GRPSSSQGEI KRKKSRLYAA DGRPHSPLRA 70 80 90 100 110 120 RSATPTLQDQ KLFNGMDSTS LLNERLQHYT LDYVSDRAQH MKNIYDPSSR WFSRSVRPEF 130 140 150 160 170 180 PIEEFLPYKT ESHEDQAKYL CHVLVNLYIA ISSLDIQGLI SISSKDLADL KKEVDDLALK 190 200 210 220 230 240 TDLFRLSNNT AENDLLGNDI ADYDDAEGLE DELDEYFDLA GPDFNATGKI TAKSATIVNV 250 260 270 280 290 300 NHWTNELKNC LHFDFPVALR KSLATVYYYL SLVQGQKVYR QMHVDMFERL VSLDDDRTNF 310 320 330 340 350 360 TELLQKQGLL LDHQIMLNFL CEFLPYPDPD YARYELSSKE DLQLFRLLLK HAHNAKPFFD 370 380 390 400 410 420 KSKESLLVDT MNFLLSSLAP STMMAVMPIV TSVVPYHYHI HSKIIDYFPF CYSIWSSVSA 430 440 450 460 470 480 NVAIDTHMYD FVGSISKDVH NKILSSEHEK DVVGVEFGEF GIFTDDQMTF MFNRLQGHLR 490 500 510 520 530 540 TDGQIHSYSR TVKPFVYAIN GSKKDRFFEK LVSLAKAIET FIHPSNNGFW TKPNAKFVHA 550 560 570 580 590 600 FIKSYHGRVK YEEDICARGV TNGICLTSFC HEEIVEIFLN IISLGSQNKN PDIANYYISC 610 620 630 640 650 660 FAYLLELDPS NAYLIYDKIL IDLYDTLADQ FINSRHRIIS SLKQFTRVIR FIVMDKLYRV 670 680 690 700 710 720 HITNVLSMLV SKLDMNDTNL TSNLINGIVS IAAFIPIQDL TGEDDYISFE SDTLPLVQQH 730 740 750 760 770 780 FYHIKCGESS KTFRVDDELL NNAFKASTTV FQSMLKVYVE KIFQLVDVDL EDSLVTKINQ 790 800 810 820 830 840 TTMILQESMD DKIFNYFASL LQRNFWSNDS FKEKDPNYEL VTIPLAALVR RNNGLSKELV 850 860 870 880 890 900 RTLLFHIKEQ IKRGAGSVRS TSEIQQRDVK LVLYLTALND VLRQCHESLL EYSDELITFM 910 920 930 940 950 960 KYLYDNVTNP PLDVITSIVI HSALATLCTT EITDCRLFPE DSKIPEKDRW GGLQFDPRRF 970 980 990 1000 1010 1020 DKQHLSFQWH VPSSDEITLS ISILESLSEY CINNVEELMK APRHDSEYGD MIQKYVLVMT 1030 1040 1050 1060 1070 1080 HTLSGSSLLF DPDFNKYRTQ SNLSYREKLI LLKNIRENNC DPQELDIDIE QIRSGKDDED 1090 1100 1110 1120 1130 1140 YIESKDIEAG LNAGVSDVVQ LRDEFPDELI VDEEVVSEMP SGVNTPIAGT HGTDNSAMSS 1150 1160 1170 1180 1190 1200 DLAFRDLDIY TCNYYFGNTT EEKLQNPQYL QVHRVRARIG HFFHKLYVFL STNFENNTNM 1210 1220 1230 1240 1250 1260 FQILLHGLKV WFTDLGQETV FNEDPNAFID VDFLENVQSL SHVNEPFTRT NFAIRANSLH 1270 1280 1290 1300 1310 1320 QSRVLLHSTN RKASKLENLL LVDIIQLATS LYPDIYKPAQ GTLVHCMKQL VGSYGVVINK 1330 1340 1350 1360 1370 1380 IIPSLEKAIK DHDYMKIQVI LNVLLIKKIH RKLMTDYKDI GRLIFLLIEC CRVNELEIGM 1390 1400 1410 1420 1430 1440 YADKILTDIV IGIKIPSSVC VISDQAFLPL APPDGTINLQ VEAVKLAKKK KREYYLSLLV 1450 1460 1470 1480 1490 1500 DLQDKLLDKL DNEKDMGWKI RMFILRFVTQ IQSNLESKPD KRAVFSIISQ ISTKHPEIIH 1510 1520 1530 1540 1550 1560 LVVKSLLSTC NKIISLSDYE YDITRAYKNE FNPSFVEILD TSTTSFPKTF TEEMNNFDNP 1570 1580 1590 1600 1610 1620 KYFIDLRAYV GWLCWGRLMY VMSPKALKLN LRENELEVLK TAGHLLTREF LRDVTMNLVQ 1630 1640 1650 1660 1670 1680 DNETRGVFSS GNVSFFSLVI LLISSGFCEL NMSDLFELCE SYYNKDDKAS MIMSVEIVAG 1690 1700 1710 1720 1730 1740 LVCGSKFMSV SDLDKRDTFI ENFLAKCLDY ELNHDAFEIW STLAWWLPAV VDLRRSKTFF 1750 1760 1770 1780 1790 1800 CHFINADGMF DRESDAATHQ TSKIYMLRSI LMSMEFRAPD VGKLFDELVF DHPYDQVRQA 1810 1820 1830 1840 1850 1860 VAKLLTTLVQ NQSNPSISDP TTLLEAERND PDGLGLPLKS VPEKVDAYIK KQFEIIKNLE 1870 1880 1890 1900 1910 1920 DSVVGLNPQQ FIKTDYFYRT STIFYWIKEM ARGPNKVLLV PYLVDYVLPF LIGLVKHKDV 1930 1940 1950 1960 1970 1980 CALASLDPVR LYAGLGYMPI RKNHVAAIVD YVCSSNVALS SNQTKLQLAF IQHFLSAELL 1990 2000 2010 2020 2030 2040 QLTEEEKNKI LEFVVSNLYN EQFVEVRVRA ASILSDIVHN WKEEQPLLSL IERFAKGLDV 2050 2060 2070 2080 2090 2100 NKYTSKERQK LSKTDIKIHG NVLGLGAIIS AFPYVFPLPP WIPKQLSNLS SWARTSGMTG 2110 2120 2130 2140 QAAKNTISEF KKVRADTWKF DRASFNTEEL EDLEGVLWRS YYA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12185839] [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: 15449308] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF FRAMESHIFT. Strain: CM1469-5C.
[3]	"Sequencing of a 23 kb fragment from Saccharomyces cerevisiae chromosome VI." Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H., Shibata T., Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H., Eki T., Murakami Y. Yeast 12:77-84(1996) [PubMed: 8789262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed: 7670463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"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: 11842813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1804, FUNCTION.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1890-2143. Strain: ATCC 204508 / S288c.
[7]	"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: 15778719] [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, MASS SPECTROMETRY.
[8]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-64, 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: 12973301] [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: 12748633] [Abstract] Cited for: IDENTIFICATION OF FRAMESHIFT.
[11]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041, MASS SPECTROMETRY.
[14]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-1041, MASS SPECTROMETRY.
[15]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-34; SER-35; SER-56; SER-62; THR-64 AND SER-1041, MASS SPECTROMETRY.
[16]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-62 AND THR-64, MASS SPECTROMETRY.
[17]	"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 0:0-0(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-29; SER-56; SER-62; THR-64; THR-66 AND SER-1041, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D50617 Genomic DNA. Translation: BAA09231.1. Frameshift. D50617 Genomic DNA. Translation: BAA09232.1. Frameshift. AY693254 Genomic DNA. Translation: AAT93273.1.
PIR	S56247. S56248.
RefSeq	NP_116648.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6358N.
IntAct	P43583.
Proteomic databases
PeptideAtlas	P43583.
Genome annotation databases
Ensembl	YFL007W. Saccharomyces cerevisiae. [Contig view]
GeneID	850541.
GenomeReviews	Gene locus YFL007W in contig D50617_GR.
KEGG	sce:YFL007W.
NMPDR	fig|4932.3.peg.2279.
Organism-specific databases
CYGD	YFL007w.
SGD	S000001887. BLM10.
Phylogenomic databases
HOGENOM	P43583.
Gene expression databases
ArrayExpress	P43583.
GermOnline	YFL007W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000357. HEAT. [Graphical view]
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProDom	P43583. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P43583.
ProtoNet	Search...

Entry information

Entry name

BLM10_YEAST

Accession

Primary (citable) accession number: P43583
Secondary accession number(s): P43584

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 6, 2005
Last modified:	July 22, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)