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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
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi1663 – 1664YN → HD: Abolihes binding to acetylated histones. 1 Publication2
Mutagenesisi2139R → D: Does not affect binding to the proteasome. 1 Publication1
Mutagenesisi2140S → H: Abolishes binding to the proteasome. 1 Publication1
Mutagenesisi2141 – 2143Missing : Loss of function. 1 Publication3
Mutagenesisi2141Y → M: Does not affect viability in the presence of cycloheximide. 1 Publication1
Mutagenesisi2142Y → A or V: Loss of function; abolishes binding to the proteasome. 1 Publication1
Mutagenesisi2142Y → V: Abolishes binding to the proteasome. 1 Publication1
Mutagenesisi2143A → S: Does not affect viability in the presence of cycloheximide. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000761821 – 2143Proteasome activator BLM10Add BLAST2143

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei62PhosphoserineCombined sources1
Modified residuei64PhosphothreonineCombined sources1
Modified residuei66PhosphothreonineCombined sources1
Modified residuei1041PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43583.
PRIDEiP43583.

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 interactors.
DIPiDIP-6344N.
IntActiP43583. 14 interactors.
MINTiMINT-640764.

Structurei

Secondary structure

12143
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi81 – 88Combined sources8
Helixi97 – 103Combined sources7
Helixi122 – 125Combined sources4
Beta strandi126 – 128Combined sources3
Helixi133 – 153Combined sources21
Helixi240 – 248Combined sources9
Helixi249 – 252Combined sources4
Helixi257 – 271Combined sources15
Helixi280 – 290Combined sources11
Helixi300 – 306Combined sources7
Helixi313 – 320Combined sources8
Turni321 – 323Combined sources3
Turni329 – 331Combined sources3
Turni339 – 341Combined sources3
Helixi342 – 354Combined sources13
Helixi364 – 366Combined sources3
Helixi367 – 374Combined sources8
Helixi375 – 377Combined sources3
Turni380 – 382Combined sources3
Helixi383 – 393Combined sources11
Helixi405 – 407Combined sources3
Helixi408 – 414Combined sources7
Turni415 – 417Combined sources3
Helixi422 – 443Combined sources22
Beta strandi444 – 446Combined sources3
Helixi465 – 480Combined sources16
Helixi488 – 496Combined sources9
Turni505 – 507Combined sources3
Helixi508 – 522Combined sources15
Helixi531 – 552Combined sources22
Turni553 – 559Combined sources7
Beta strandi563 – 565Combined sources3
Helixi568 – 586Combined sources19
Helixi591 – 606Combined sources16
Helixi612 – 627Combined sources16
Turni628 – 633Combined sources6
Helixi635 – 646Combined sources12
Helixi649 – 652Combined sources4
Helixi658 – 661Combined sources4
Helixi662 – 671Combined sources10
Helixi678 – 693Combined sources16
Helixi709 – 712Combined sources4
Helixi714 – 725Combined sources12
Beta strandi730 – 732Combined sources3
Helixi739 – 747Combined sources9
Turni748 – 750Combined sources3
Helixi751 – 765Combined sources15
Helixi773 – 787Combined sources15
Helixi791 – 806Combined sources16
Beta strandi813 – 815Combined sources3
Helixi819 – 831Combined sources13
Helixi833 – 835Combined sources3
Helixi836 – 852Combined sources17
Turni853 – 856Combined sources4
Beta strandi861 – 863Combined sources3
Turni866 – 868Combined sources3
Helixi869 – 882Combined sources14
Turni883 – 885Combined sources3
Helixi886 – 890Combined sources5
Helixi893 – 905Combined sources13
Helixi910 – 916Combined sources7
Helixi919 – 928Combined sources10
Beta strandi937 – 941Combined sources5
Beta strandi953 – 956Combined sources4
Helixi957 – 960Combined sources4
Turni962 – 964Combined sources3
Helixi974 – 997Combined sources24
Helixi1009 – 1023Combined sources15
Helixi1026 – 1029Combined sources4
Helixi1032 – 1035Combined sources4
Beta strandi1158 – 1161Combined sources4
Turni1162 – 1165Combined sources4
Helixi1167 – 1193Combined sources27
Helixi1199 – 1211Combined sources13
Beta strandi1215 – 1217Combined sources3
Helixi1231 – 1238Combined sources8
Helixi1249 – 1266Combined sources18
Helixi1276 – 1288Combined sources13
Helixi1293 – 1307Combined sources15
Beta strandi1308 – 1310Combined sources3
Helixi1313 – 1330Combined sources18
Helixi1335 – 1343Combined sources9
Helixi1347 – 1352Combined sources6
Helixi1353 – 1355Combined sources3
Helixi1357 – 1369Combined sources13
Beta strandi1374 – 1377Combined sources4
Turni1378 – 1380Combined sources3
Helixi1381 – 1390Combined sources10
Helixi1404 – 1406Combined sources3
Helixi1408 – 1410Combined sources3
Helixi1420 – 1427Combined sources8
Helixi1430 – 1451Combined sources22
Helixi1460 – 1471Combined sources12
Helixi1481 – 1488Combined sources8
Helixi1489 – 1493Combined sources5
Helixi1496 – 1506Combined sources11
Helixi1508 – 1519Combined sources12
Helixi1523 – 1526Combined sources4
Beta strandi1527 – 1530Combined sources4
Beta strandi1536 – 1541Combined sources6
Turni1544 – 1546Combined sources3
Helixi1547 – 1554Combined sources8
Beta strandi1577 – 1582Combined sources6
Helixi1593 – 1603Combined sources11
Helixi1608 – 1620Combined sources13
Turni1621 – 1625Combined sources5
Helixi1630 – 1643Combined sources14
Helixi1652 – 1654Combined sources3
Helixi1655 – 1661Combined sources7
Helixi1668 – 1681Combined sources14
Turni1690 – 1692Combined sources3
Helixi1693 – 1708Combined sources16
Helixi1716 – 1730Combined sources15
Helixi1733 – 1735Combined sources3
Helixi1737 – 1743Combined sources7
Helixi1764 – 1774Combined sources11
Helixi1782 – 1787Combined sources6
Helixi1795 – 1810Combined sources16
Helixi1820 – 1828Combined sources9
Beta strandi1831 – 1834Combined sources4
Helixi1843 – 1856Combined sources14
Helixi1858 – 1861Combined sources4
Turni1869 – 1873Combined sources5
Helixi1875 – 1890Combined sources16
Helixi1893 – 1895Combined sources3
Helixi1896 – 1899Combined sources4
Helixi1900 – 1902Combined sources3
Helixi1903 – 1907Combined sources5
Turni1908 – 1911Combined sources4
Helixi1919 – 1923Combined sources5
Helixi1929 – 1934Combined sources6
Beta strandi1936 – 1938Combined sources3
Helixi1942 – 1951Combined sources10
Turni1955 – 1958Combined sources4
Beta strandi1961 – 1963Combined sources3
Helixi1964 – 1978Combined sources15
Turni1979 – 1981Combined sources3
Helixi1986 – 1989Combined sources4
Helixi1991 – 1994Combined sources4
Turni1995 – 1999Combined sources5
Helixi2004 – 2019Combined sources16
Helixi2024 – 2034Combined sources11
Turni2039 – 2041Combined sources3
Helixi2045 – 2054Combined sources10
Helixi2056 – 2069Combined sources14
Helixi2081 – 2090Combined sources10
Beta strandi2093 – 2095Combined sources3
Helixi2099 – 2102Combined sources4
Helixi2104 – 2113Combined sources10
Helixi2118 – 2121Combined sources4
Helixi2122 – 2124Combined sources3
Helixi2131 – 2133Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1316 – 1355HEAT 1Add BLAST40
Repeati1779 – 1814HEAT 2Add BLAST36
Repeati1902 – 1941HEAT 3Add BLAST40
Repeati1985 – 2023HEAT 4Add BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1648 – 1732Bromodomain-like (BRDL)Add BLAST85

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2141 – 2143YYX motif3

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.
OrthoDBiEOG092C011F.

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 differs from that shown. Reason: Frameshift at position 1800. Produces 2 separate ORFs.Curated
The sequence BAA09232 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4V7OX-ray3.00A5/A7/B4/B7239-1037[»]
A6/A8/B5/B81147-2143[»]
AE/AF/B3/B679-154[»]
ProteinModelPortaliP43583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP43583.

Proteomic databases

MaxQBiP43583.
PRIDEiP43583.

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.
OrthoDBiEOG092C011F.

Enzyme and pathway databases

BioCyciYEAST:G3O-30449-MONOMER.

Miscellaneous databases

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...

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: November 2, 2016
This is version 153 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.