BLM10_YEAST - dbPTM
BLM10_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLM10_YEAST
UniProt AC P43583
Protein Name Proteasome activator BLM10
Gene Name BLM10
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 2143
Subcellular Localization Nucleus. Cytoplasm.
Protein Description 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..
Protein Sequence MTANNDDDIKSPIPITNKTLSQLKRFERSPGRPSSSQGEIKRKKSRLYAADGRPHSPLRARSATPTLQDQKLFNGMDSTSLLNERLQHYTLDYVSDRAQHMKNIYDPSSRWFSRSVRPEFPIEEFLPYKTESHEDQAKYLCHVLVNLYIAISSLDIQGLISISSKDLADLKKEVDDLALKTDLFRLSNNTAENDLLGNDIADYDDAEGLEDELDEYFDLAGPDFNATGKITAKSATIVNVNHWTNELKNCLHFDFPVALRKSLATVYYYLSLVQGQKVYRQMHVDMFERLVSLDDDRTNFTELLQKQGLLLDHQIMLNFLCEFLPYPDPDYARYELSSKEDLQLFRLLLKHAHNAKPFFDKSKESLLVDTMNFLLSSLAPSTMMAVMPIVTSVVPYHYHIHSKIIDYFPFCYSIWSSVSANVAIDTHMYDFVGSISKDVHNKILSSEHEKDVVGVEFGEFGIFTDDQMTFMFNRLQGHLRTDGQIHSYSRTVKPFVYAINGSKKDRFFEKLVSLAKAIETFIHPSNNGFWTKPNAKFVHAFIKSYHGRVKYEEDICARGVTNGICLTSFCHEEIVEIFLNIISLGSQNKNPDIANYYISCFAYLLELDPSNAYLIYDKILIDLYDTLADQFINSRHRIISSLKQFTRVIRFIVMDKLYRVHITNVLSMLVSKLDMNDTNLTSNLINGIVSIAAFIPIQDLTGEDDYISFESDTLPLVQQHFYHIKCGESSKTFRVDDELLNNAFKASTTVFQSMLKVYVEKIFQLVDVDLEDSLVTKINQTTMILQESMDDKIFNYFASLLQRNFWSNDSFKEKDPNYELVTIPLAALVRRNNGLSKELVRTLLFHIKEQIKRGAGSVRSTSEIQQRDVKLVLYLTALNDVLRQCHESLLEYSDELITFMKYLYDNVTNPPLDVITSIVIHSALATLCTTEITDCRLFPEDSKIPEKDRWGGLQFDPRRFDKQHLSFQWHVPSSDEITLSISILESLSEYCINNVEELMKAPRHDSEYGDMIQKYVLVMTHTLSGSSLLFDPDFNKYRTQSNLSYREKLILLKNIRENNCDPQELDIDIEQIRSGKDDEDYIESKDIEAGLNAGVSDVVQLRDEFPDELIVDEEVVSEMPSGVNTPIAGTHGTDNSAMSSDLAFRDLDIYTCNYYFGNTTEEKLQNPQYLQVHRVRARIGHFFHKLYVFLSTNFENNTNMFQILLHGLKVWFTDLGQETVFNEDPNAFIDVDFLENVQSLSHVNEPFTRTNFAIRANSLHQSRVLLHSTNRKASKLENLLLVDIIQLATSLYPDIYKPAQGTLVHCMKQLVGSYGVVINKIIPSLEKAIKDHDYMKIQVILNVLLIKKIHRKLMTDYKDIGRLIFLLIECCRVNELEIGMYADKILTDIVIGIKIPSSVCVISDQAFLPLAPPDGTINLQVEAVKLAKKKKREYYLSLLVDLQDKLLDKLDNEKDMGWKIRMFILRFVTQIQSNLESKPDKRAVFSIISQISTKHPEIIHLVVKSLLSTCNKIISLSDYEYDITRAYKNEFNPSFVEILDTSTTSFPKTFTEEMNNFDNPKYFIDLRAYVGWLCWGRLMYVMSPKALKLNLRENELEVLKTAGHLLTREFLRDVTMNLVQDNETRGVFSSGNVSFFSLVILLISSGFCELNMSDLFELCESYYNKDDKASMIMSVEIVAGLVCGSKFMSVSDLDKRDTFIENFLAKCLDYELNHDAFEIWSTLAWWLPAVVDLRRSKTFFCHFINADGMFDRESDAATHQTSKIYMLRSILMSMEFRAPDVGKLFDELVFDHPYDQVRQAVAKLLTTLVQNQSNPSISDPTTLLEAERNDPDGLGLPLKSVPEKVDAYIKKQFEIIKNLEDSVVGLNPQQFIKTDYFYRTSTIFYWIKEMARGPNKVLLVPYLVDYVLPFLIGLVKHKDVCALASLDPVRLYAGLGYMPIRKNHVAAIVDYVCSSNVALSSNQTKLQLAFIQHFLSAELLQLTEEEKNKILEFVVSNLYNEQFVEVRVRAASILSDIVHNWKEEQPLLSLIERFAKGLDVNKYTSKERQKLSKTDIKIHGNVLGLGAIISAFPYVFPLPPWIPKQLSNLSSWARTSGMTGQAAKNTISEFKKVRADTWKFDRASFNTEELEDLEGVLWRSYYA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MTANNDDDI
------CCCCCCCCC		49.7719823750
11PhosphorylationNNDDDIKSPIPITNK
CCCCCCCCCCCCCCC		28.5322369663
16PhosphorylationIKSPIPITNKTLSQL
CCCCCCCCCCHHHHH		25.8819823750
18AcetylationSPIPITNKTLSQLKR
CCCCCCCCHHHHHHH		42.0422865919
21PhosphorylationPITNKTLSQLKRFER
CCCCCHHHHHHHHHC		38.4030377154
24AcetylationNKTLSQLKRFERSPG
CCHHHHHHHHHCCCC		47.6125381059
29PhosphorylationQLKRFERSPGRPSSS
HHHHHHCCCCCCCCC		25.2222369663
34PhosphorylationERSPGRPSSSQGEIK
HCCCCCCCCCHHHHH		41.0622369663
35PhosphorylationRSPGRPSSSQGEIKR
CCCCCCCCCHHHHHH		29.3922369663
36PhosphorylationSPGRPSSSQGEIKRK
CCCCCCCCHHHHHHH		46.6822369663
45PhosphorylationGEIKRKKSRLYAADG
HHHHHHHCCEEECCC		30.4722369663
48PhosphorylationKRKKSRLYAADGRPH
HHHHCCEEECCCCCC		9.9122369663
56PhosphorylationAADGRPHSPLRARSA
ECCCCCCCCCCCCCC		28.4522369663
62PhosphorylationHSPLRARSATPTLQD
CCCCCCCCCCCCHHH		35.1922369663
64PhosphorylationPLRARSATPTLQDQK
CCCCCCCCCCHHHHH		20.3222369663
66PhosphorylationRARSATPTLQDQKLF
CCCCCCCCHHHHHHH		32.4722369663
180AcetylationEVDDLALKTDLFRLS
HHHHHHHHHHHHHCC		34.0924489116
233UbiquitinationATGKITAKSATIVNV
CCCCEEECEEEEEEC		31.7917644757
248UbiquitinationNHWTNELKNCLHFDF
CHHHHHHHHHHCCCC		39.1617644757
261UbiquitinationDFPVALRKSLATVYY
CCCHHHHHHHHHHHH		51.1517644757
277UbiquitinationLSLVQGQKVYRQMHV
HHHHCCHHHHHHHCH		48.3217644757
306UbiquitinationNFTELLQKQGLLLDH
CHHHHHHHCCCCCCH		46.4317644757
493AcetylationHSYSRTVKPFVYAIN
EECCCCCCCEEEEEC		31.9324489116
532AcetylationSNNGFWTKPNAKFVH
CCCCCCCCCCHHHHH		27.2022865919
1037PhosphorylationFDPDFNKYRTQSNLS
ECCCHHHCCCCCCCC		21.7219823750
1039PhosphorylationPDFNKYRTQSNLSYR
CCHHHCCCCCCCCHH		33.0122369663
1041PhosphorylationFNKYRTQSNLSYREK
HHHCCCCCCCCHHHH		38.8422369663
1044PhosphorylationYRTQSNLSYREKLIL
CCCCCCCCHHHHHHH		26.7922369663
1053AcetylationREKLILLKNIRENNC
HHHHHHHHHHHHCCC		47.0524489116
1076UbiquitinationIEQIRSGKDDEDYIE
HHHHHCCCCCHHHHH		64.3523749301
1355PhosphorylationKIHRKLMTDYKDIGR
HHHHHHCCCHHHHHH		46.7619795423
1357PhosphorylationHRKLMTDYKDIGRLI
HHHHCCCHHHHHHHH		11.0319795423
1486PhosphorylationPDKRAVFSIISQIST
CCHHHHHHHHHHHHC		16.6523749301
1489PhosphorylationRAVFSIISQISTKHP
HHHHHHHHHHHCCCH		21.5723749301
1492PhosphorylationFSIISQISTKHPEII
HHHHHHHHCCCHHHH		24.6223749301
1493PhosphorylationSIISQISTKHPEIIH
HHHHHHHCCCHHHHH		34.6923749301
1600AcetylationENELEVLKTAGHLLT
HHHHHHHHHHHHHHH		41.3224489116
2022UbiquitinationSDIVHNWKEEQPLLS
HHHHCCCCHHCHHHH		57.6017644757
2042UbiquitinationAKGLDVNKYTSKERQ
HHCCCHHHCCHHHHH		50.1623749301
2053AcetylationKERQKLSKTDIKIHG
HHHHHCCCCCCEECC		61.7325381059
2087PhosphorylationPWIPKQLSNLSSWAR
CCCCHHHHCHHHHHH		32.9830377154
2119AcetylationKVRADTWKFDRASFN
HHCCCCCCCCHHHCC		39.2122865919
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BLM10_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLM10_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BLM10_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECM29_YEASTECM29genetic
15778719
RPN4_YEASTRPN4genetic
15778719
BLM10_YEASTBLM10physical
16554755
PBP4_YEASTPBP4physical
16554755
ZUO1_YEASTZUO1physical
16554755
SSZ1_YEASTSSZ1physical
16554755
HS104_YEASTHSP104physical
16554755
HSC82_YEASTHSC82physical
16554755
TPA1_YEASTTPA1genetic
17314980
EAF1_YEASTEAF1genetic
17314980
CIN8_YEASTCIN8genetic
17314980
RPN2_YEASTRPN2genetic
17911101
HSP71_YEASTSSA1physical
19536198
RPN4_YEASTRPN4genetic
22025621
YPK9_YEASTYPK9genetic
22457822
BLM10_YEASTBLM10physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
KPYK1_YEASTCDC19physical
22940862
DYHC_YEASTDYN1physical
22875988
DNM1_YEASTDNM1genetic
24604417
RTC1_YEASTRTC1genetic
27708008
SEC66_YEASTSEC66genetic
27708008
HPC2_YEASTHPC2genetic
27708008
AGP1_YEASTAGP1genetic
27708008
RV161_YEASTRVS161genetic
27708008
YD241_YEASTYDL241Wgenetic
27708008
OCA6_YEASTOCA6genetic
27708008
VPS41_YEASTVPS41genetic
27708008
ALAT_YEASTALT2genetic
27708008
RPA14_YEASTRPA14genetic
27708008
MTHR2_YEASTMET13genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
BYE1_YEASTBYE1genetic
27708008
BLI1_YEASTBLI1genetic
27708008
YKK0_YEASTYPF1genetic
27708008
UBR2_YEASTUBR2genetic
27708008
ADY4_YEASTADY4genetic
27708008
TSL1_YEASTTSL1genetic
27708008
NAB6_YEASTNAB6genetic
27708008
GCSP_YEASTGCV2genetic
27708008
RAD14_YEASTRAD14genetic
27708008
TPM1_YEASTTPM1genetic
27708008
MSO1_YEASTMSO1genetic
27708008
IZH2_YEASTIZH2genetic
27708008
INO4_YEASTINO4genetic
27708008
BUB3_YEASTBUB3genetic
27708008
CYC2_YEASTCYC2genetic
27708008
RUP1_YEASTRUP1genetic
27708008
YO268_YEASTYOR268Cgenetic
27708008
SNX3_YEASTSNX3genetic
27708008
SYH1_YEASTSYH1genetic
27708008
VPS1_YEASTVPS1genetic
27453043
DCOR_YEASTSPE1genetic
27453043
CYPC_YEASTCPR3genetic
27453043
SERB_YEASTSER2genetic
27453043
PVH1_YEASTYVH1genetic
27453043
IMDH4_YEASTIMD4genetic
27453043
APC10_YEASTDOC1genetic
27453043
MSH1_YEASTMSH1genetic
27453043
ARP8_YEASTARP8genetic
27453043
COQ6_YEASTCOQ6genetic
27453043
TPM1_YEASTTPM1genetic
27453043
ASF1_YEASTASF1genetic
27453043
DUN1_YEASTDUN1genetic
27453043
RPD3_YEASTRPD3genetic
27453043
SWI5_YEASTSWI5genetic
27453043
SODC_YEASTSOD1genetic
27453043
DBF2_YEASTDBF2genetic
27453043
DCAM_YEASTSPE2genetic
27453043
YL422_YEASTYLR422Wgenetic
27453043
AIM33_YEASTAIM33genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BLM10_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-29; SER-56;SER-62; THR-64; THR-66 AND SER-1041, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-62 AND THR-64,AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-34; SER-35;SER-56; SER-62; THR-64 AND SER-1041, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-1041, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-64, AND MASSSPECTROMETRY.

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