HSP72_YEAST - dbPTM
HSP72_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP72_YEAST
UniProt AC P10592
Protein Name Heat shock protein SSA2
Gene Name SSA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 639
Subcellular Localization Cytoplasm. Secreted, cell wall.
Protein Description May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles..
Protein Sequence MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGDMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDAVTKKAEETIAWLDSNTTATKEEFDDQLKELQEVANPIMSKLYQAGGAPEGAAPGGFPGGAPPAPEAEGPTVEEVD
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
2Acetylation------MSKAVGIDL
------CCCCCCEEC
29.359298649
3Ubiquitination-----MSKAVGIDLG
-----CCCCCCEECC
45.8817644757
12PhosphorylationVGIDLGTTYSCVAHF
CCEECCCCEEEEEEC
16.1928889911
14PhosphorylationIDLGTTYSCVAHFSN
EECCCCEEEEEECCC
10.4628889911
20PhosphorylationYSCVAHFSNDRVDII
EEEEEECCCCCEEEE
28.1417287358
35PhosphorylationANDQGNRTTPSFVGF
ECCCCCCCCCCCCCC
47.2427214570
36PhosphorylationNDQGNRTTPSFVGFT
CCCCCCCCCCCCCCC
17.4425752575
38PhosphorylationQGNRTTPSFVGFTDT
CCCCCCCCCCCCCCH
30.3928889911
45PhosphorylationSFVGFTDTERLIGDA
CCCCCCCHHHHHHHH
21.6811283598
54AcetylationRLIGDAAKNQAAMNP
HHHHHHHHHCHHCCH
51.84-
54UbiquitinationRLIGDAAKNQAAMNP
HHHHHHHHHCHHCCH
51.8423749301
69AcetylationANTVFDAKRLIGRNF
HHHHHHHHHHHCCCC
49.9724489116
69SuccinylationANTVFDAKRLIGRNF
HHHHHHHHHHHCCCC
49.9723954790
69UbiquitinationANTVFDAKRLIGRNF
HHHHHHHHHHHCCCC
49.9717644757
86AcetylationPEVQGDMKHFPFKLI
HHHCCCCCCCCEEEE
47.0024489116
86SuccinylationPEVQGDMKHFPFKLI
HHHCCCCCCCCEEEE
47.0023954790
86UbiquitinationPEVQGDMKHFPFKLI
HHHCCCCCCCCEEEE
47.0023749301
91UbiquitinationDMKHFPFKLIDVDGK
CCCCCCEEEECCCCC
44.7822817900
98UbiquitinationKLIDVDGKPQIQVEF
EEECCCCCEEEEEEE
29.3223749301
106UbiquitinationPQIQVEFKGETKNFT
EEEEEEECCCCCCCC
42.1922817900
109PhosphorylationQVEFKGETKNFTPEQ
EEEECCCCCCCCHHH
39.7021440633
110UbiquitinationVEFKGETKNFTPEQI
EEECCCCCCCCHHHH
45.8423749301
113PhosphorylationKGETKNFTPEQISSM
CCCCCCCCHHHHHHH
35.0021440633
119PhosphorylationFTPEQISSMVLGKMK
CCHHHHHHHHHHHHH
17.9721440633
124UbiquitinationISSMVLGKMKETAES
HHHHHHHHHHHHHHH
42.5122817900
126UbiquitinationSMVLGKMKETAESYL
HHHHHHHHHHHHHHH
56.2323749301
128PhosphorylationVLGKMKETAESYLGA
HHHHHHHHHHHHHCC
30.1521440633
131PhosphorylationKMKETAESYLGAKVN
HHHHHHHHHHCCCCC
24.1621440633
132PhosphorylationMKETAESYLGAKVND
HHHHHHHHHCCCCCC
10.7221440633
136UbiquitinationAESYLGAKVNDAVVT
HHHHHCCCCCCEEEE
39.5123749301
143PhosphorylationKVNDAVVTVPAYFND
CCCCEEEEEEECCCH
17.7428132839
147PhosphorylationAVVTVPAYFNDSQRQ
EEEEEEECCCHHHCC
9.2429734811
151PhosphorylationVPAYFNDSQRQATKD
EEECCCHHHCCHHCC
28.5022369663
156PhosphorylationNDSQRQATKDAGTIA
CHHHCCHHCCCCCCC
22.5621440633
157UbiquitinationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC
48.9023749301
161PhosphorylationQATKDAGTIAGLNVL
CHHCCCCCCCCCHHH
14.9030377154
175PhosphorylationLRIINEPTAAAIAYG
HHHCCCHHHHHHHHC
23.8121440633
185UbiquitinationAIAYGLDKKGKEEHV
HHHHCCCCCCCEEEE
69.3522817900
186UbiquitinationIAYGLDKKGKEEHVL
HHHCCCCCCCEEEEE
74.9222817900
188UbiquitinationYGLDKKGKEEHVLIF
HCCCCCCCEEEEEEE
69.6622817900
217UbiquitinationEDGIFEVKATAGDTH
CCCEEEEEEEECCCC
32.5917644757
219PhosphorylationGIFEVKATAGDTHLG
CEEEEEEEECCCCCC
26.0021440633
223PhosphorylationVKATAGDTHLGGEDF
EEEEECCCCCCCCCH
20.3422369663
243UbiquitinationNHFIQEFKRKNKKDL
HHHHHHHHHHCHHCC
62.8123749301
245UbiquitinationFIQEFKRKNKKDLST
HHHHHHHHCHHCCCH
73.9522817900
247UbiquitinationQEFKRKNKKDLSTNQ
HHHHHHCHHCCCHHH
51.1822817900
248UbiquitinationEFKRKNKKDLSTNQR
HHHHHCHHCCCHHHH
73.6022817900
252PhosphorylationKNKKDLSTNQRALRR
HCHHCCCHHHHHHHH
42.5419779198
268UbiquitinationRTACERAKRTLSSSA
HHHHHHHHHHHCCCC
52.7317644757
316UbiquitinationSTLDPVEKVLRDAKL
HCCCHHHHHHHHCCC
46.9723749301
325UbiquitinationLRDAKLDKSQVDEIV
HHHCCCCHHHCCEEE
53.9024961812
326PhosphorylationRDAKLDKSQVDEIVL
HHCCCCHHHCCEEEE
34.7925521595
337PhosphorylationEIVLVGGSTRIPKVQ
EEEEECCCCCCHHHH
14.4825521595
338PhosphorylationIVLVGGSTRIPKVQK
EEEECCCCCCHHHHH
35.5721440633
342UbiquitinationGGSTRIPKVQKLVTD
CCCCCCHHHHHHHHH
55.7322817900
345UbiquitinationTRIPKVQKLVTDYFN
CCCHHHHHHHHHHHC
48.1624961812
348PhosphorylationPKVQKLVTDYFNGKE
HHHHHHHHHHHCCCC
35.1021440633
350PhosphorylationVQKLVTDYFNGKEPN
HHHHHHHHHCCCCCC
6.9221440633
354UbiquitinationVTDYFNGKEPNRSIN
HHHHHCCCCCCCCCC
71.7223749301
359PhosphorylationNGKEPNRSINPDEAV
CCCCCCCCCCHHHHH
33.1022369663
368PhosphorylationNPDEAVAYGAAVQAA
CHHHHHHHHHHHHHH
10.7422369663
378PhosphorylationAVQAAILTGDESSKT
HHHHHHHHCCCCCCC
36.1522369663
382PhosphorylationAILTGDESSKTQDLL
HHHHCCCCCCCCCEE
41.7021551504
383PhosphorylationILTGDESSKTQDLLL
HHHCCCCCCCCCEEE
37.3622369663
384UbiquitinationLTGDESSKTQDLLLL
HHCCCCCCCCCEEEE
60.5317644757
409UbiquitinationTAGGVMTKLIPRNST
ECCCHHEEEECCCCC
26.7317644757
415PhosphorylationTKLIPRNSTIPTKKS
EEEECCCCCCCCCHH
29.0622369663
416PhosphorylationKLIPRNSTIPTKKSE
EEECCCCCCCCCHHH
34.2322369663
419PhosphorylationPRNSTIPTKKSEVFS
CCCCCCCCCHHHHHE
47.4521440633
420AcetylationRNSTIPTKKSEVFST
CCCCCCCCHHHHHEE
49.2825381059
420UbiquitinationRNSTIPTKKSEVFST
CCCCCCCCHHHHHEE
49.2823749301
421UbiquitinationNSTIPTKKSEVFSTY
CCCCCCCHHHHHEEE
55.0923749301
422PhosphorylationSTIPTKKSEVFSTYA
CCCCCCHHHHHEEEC
40.3225521595
426PhosphorylationTKKSEVFSTYADNQP
CCHHHHHEEECCCCC
26.1922369663
427PhosphorylationKKSEVFSTYADNQPG
CHHHHHEEECCCCCC
15.9722369663
428PhosphorylationKSEVFSTYADNQPGV
HHHHHEEECCCCCCE
15.6825521595
446UbiquitinationVFEGERAKTKDNNLL
EEECCCCCCCCCCCC
63.4322817900
448UbiquitinationEGERAKTKDNNLLGK
ECCCCCCCCCCCCCE
58.7223749301
455UbiquitinationKDNNLLGKFELSGIP
CCCCCCCEEEECCCC
35.3223749301
459PhosphorylationLLGKFELSGIPPAPR
CCCEEEECCCCCCCC
27.7222369663
486PhosphorylationSNGILNVSAVEKGTG
CCCEEEEEEEECCCC
26.0623607784
490UbiquitinationLNVSAVEKGTGKSNK
EEEEEEECCCCCCCC
55.9917644757
492PhosphorylationVSAVEKGTGKSNKIT
EEEEECCCCCCCCEE
53.1322369663
494UbiquitinationAVEKGTGKSNKITIT
EEECCCCCCCCEEEE
51.1722817900
495PhosphorylationVEKGTGKSNKITITN
EECCCCCCCCEEEEC
44.7122369663
497UbiquitinationKGTGKSNKITITNDK
CCCCCCCCEEEECCC
48.6023749301
499PhosphorylationTGKSNKITITNDKGR
CCCCCCEEEECCCCC
24.2922369663
501PhosphorylationKSNKITITNDKGRLS
CCCCEEEECCCCCCC
28.8122369663
504UbiquitinationKITITNDKGRLSKED
CEEEECCCCCCCHHH
48.2623749301
508PhosphorylationTNDKGRLSKEDIEKM
ECCCCCCCHHHHHHH
32.4130377154
509UbiquitinationNDKGRLSKEDIEKMV
CCCCCCCHHHHHHHH
65.0923749301
514UbiquitinationLSKEDIEKMVAEAEK
CCHHHHHHHHHHHHH
38.7224961812
521UbiquitinationKMVAEAEKFKEEDEK
HHHHHHHHHHHHHHH
69.6423749301
523UbiquitinationVAEAEKFKEEDEKES
HHHHHHHHHHHHHHH
71.8623793018
528UbiquitinationKFKEEDEKESQRIAS
HHHHHHHHHHHHHHH
75.0024961812
530PhosphorylationKEEDEKESQRIASKN
HHHHHHHHHHHHHHH
35.5128889911
535PhosphorylationKESQRIASKNQLESI
HHHHHHHHHHHHHHH
29.7523749301
536UbiquitinationESQRIASKNQLESIA
HHHHHHHHHHHHHHH
39.4323749301
541PhosphorylationASKNQLESIAYSLKN
HHHHHHHHHHHHHHH
22.5522369663
545PhosphorylationQLESIAYSLKNTISE
HHHHHHHHHHHHHHH
24.6822369663
547UbiquitinationESIAYSLKNTISEAG
HHHHHHHHHHHHHHH
46.2124961812
549PhosphorylationIAYSLKNTISEAGDK
HHHHHHHHHHHHHHH
25.0520377248
551PhosphorylationYSLKNTISEAGDKLE
HHHHHHHHHHHHHHH
21.2522369663
556UbiquitinationTISEAGDKLEQADKD
HHHHHHHHHHHHCHH
53.6723749301
562AcetylationDKLEQADKDAVTKKA
HHHHHHCHHHHHHHH
51.0724489116
562UbiquitinationDKLEQADKDAVTKKA
HHHHHHCHHHHHHHH
51.0717644757
566PhosphorylationQADKDAVTKKAEETI
HHCHHHHHHHHHHHH
28.6621440633
567UbiquitinationADKDAVTKKAEETIA
HCHHHHHHHHHHHHH
43.3017644757
568UbiquitinationDKDAVTKKAEETIAW
CHHHHHHHHHHHHHH
52.2217644757
584AcetylationDSNTTATKEEFDDQL
CCCCCCCHHHHHHHH
53.4324489116
584UbiquitinationDSNTTATKEEFDDQL
CCCCCCCHHHHHHHH
53.4324961812
592AcetylationEEFDDQLKELQEVAN
HHHHHHHHHHHHHHH
51.2324489116
592UbiquitinationEEFDDQLKELQEVAN
HHHHHHHHHHHHHHH
51.2317644757
603PhosphorylationEVANPIMSKLYQAGG
HHHHHHHHHHHHCCC
21.8928152593
604UbiquitinationVANPIMSKLYQAGGA
HHHHHHHHHHHCCCC
33.5617644757
634PhosphorylationAPEAEGPTVEEVD--
CCCCCCCCCCCCC--
51.9427017623

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 HSP72_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP72_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 HSP72_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP73_YEASTSSA3genetic
3302682
UBP3_YEASTUBP3genetic
9644204
HSP74_YEASTSSA4genetic
3302682
SPT2_YEASTSPT2genetic
1644272
HSF_YEASTHSF1genetic
1644272
SPT2_YEASTSPT2genetic
9851990
HSP73_YEASTSSA3genetic
17947402
HSP74_YEASTSSA4genetic
17947402
ERF3_YEASTSUP35physical
18353968
FRA1_YEASTFRA1physical
19536198
MED14_YEASTRGR1physical
19536198
METK1_YEASTSAM1physical
19536198
SKG3_YEASTSKG3physical
19536198
ATG26_YEASTATG26physical
19536198
NMT_YEASTNMT1physical
19536198
PNPH_YEASTPNP1physical
19536198
ELP1_YEASTIKI3physical
19536198
VAC14_YEASTVAC14physical
19536198
SKI2_YEASTSKI2physical
19536198
VIP1_YEASTVIP1physical
19536198
CDC73_YEASTCDC73physical
19536198
SIR3_YEASTSIR3physical
19536198
MFT1_YEASTMFT1physical
19536198
ARMT1_YEASTYMR027Wphysical
19536198
DHR1_YEASTECM16physical
19536198
PO152_YEASTPOM152physical
19536198
RRP5_YEASTRRP5physical
19536198
BCH1_YEASTBCH1physical
19536198
ZDS1_YEASTZDS1physical
19536198
HRB1_YEASTHRB1physical
19536198
DPOA_YEASTPOL1physical
19536198
NOG2_YEASTNOG2physical
19536198
TOP1_YEASTTOP1physical
19536198
RRP44_YEASTDIS3physical
19536198
SYEM_YEASTMSE1physical
19536198
CTR9_YEASTCTR9physical
19536198
STI1_YEASTSTI1physical
19536198
WHI2_YEASTWHI2physical
19536198
SGT1_YEASTSGT1physical
19536198
PDP1_YEASTPTC5physical
19536198
ULS1_YEASTULS1physical
19536198
RPA1_YEASTRPA190physical
19536198
RRP12_YEASTRRP12physical
19536198
RAD1_YEASTRAD1physical
19536198
SYDM_YEASTMSD1physical
19536198
GDE1_YEASTGDE1physical
19536198
DPOZ_YEASTREV3physical
19536198
CTI6_YEASTCTI6physical
19536198
NSL1_YEASTNSL1physical
19536198
RPA2_YEASTRPA135physical
19536198
CCL1_YEASTCCL1physical
19536198
CTF4_YEASTCTF4physical
19536198
TAZ1_YEASTTAZ1physical
19536198
NOC4_YEASTNOC4physical
19536198
BSP1_YEASTBSP1physical
19536198
HSC82_YEASTHSC82physical
19536198
HSP71_YEASTSSA1physical
19536198
HSP26_YEASTHSP26physical
19536198
SSB1_YEASTSSB1physical
19536198
HSP42_YEASTHSP42physical
19536198
HSP74_YEASTSSA4physical
19536198
SIS1_YEASTSIS1physical
19536198
HSP7F_YEASTSSE1physical
19536198
HSP71_YEASTSSA1genetic
20093466
FTH1_YEASTFTH1genetic
20093466
UGX2_YEASTUGX2genetic
20093466
ODO2_YEASTKGD2genetic
20093466
RV167_YEASTRVS167genetic
20093466
GET2_YEASTGET2genetic
20093466
GET1_YEASTGET1genetic
20093466
RE107_YEASTREC107genetic
20093466
PTK2_YEASTPTK2genetic
20093466
DOHH_YEASTLIA1genetic
20093466
MEH1_YEASTMEH1genetic
20093466
NGL2_YEASTNGL2genetic
20093466
MAS5_YEASTYDJ1genetic
20093466
SGT2_YEASTSGT2genetic
20093466
ETFD_YEASTCIR2genetic
20093466
UBI4P_YEASTUBI4physical
20694217
GTS1_YEASTGTS1genetic
21307595
HSP73_YEASTSSA3genetic
22138184
HSP74_YEASTSSA4genetic
22138184
CG13_YEASTCLN3physical
23217712
GET2_YEASTGET2genetic
23891562
PSB5_YEASTPRE2genetic
23891562
DOA10_YEASTSSM4genetic
23637465
MTR10_YEASTMTR10genetic
25853343
TECR_YEASTTSC13genetic
27708008
PRP9_YEASTPRP9genetic
27708008
TIM22_YEASTTIM22genetic
27708008
SC61G_YEASTSSS1genetic
27708008
SP110_YEASTSPC110genetic
27708008
RMRP_YEASTSNM1genetic
27708008
ACT_YEASTACT1genetic
27708008
SWC4_YEASTSWC4genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
MED6_YEASTMED6genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NTR2_YEASTNTR2genetic
27708008
RU1C_YEASTYHC1genetic
27708008
RSC9_YEASTRSC9genetic
27708008
DBP6_YEASTDBP6genetic
27708008
CLP1_YEASTCLP1genetic
27708008
DIB1_YEASTDIB1genetic
27708008
HSP71_YEASTSSA1genetic
27708008
H4_YEASTHHF1genetic
27708008
FTH1_YEASTFTH1genetic
27708008
ATG20_YEASTATG20genetic
27708008
UGX2_YEASTUGX2genetic
27708008
TPS2_YEASTTPS2genetic
27708008
PEX5_YEASTPEX5genetic
27708008
HPRT_YEASTHPT1genetic
27708008
PEX8_YEASTPEX8genetic
27708008
COX23_YEASTCOX23genetic
27708008
RE107_YEASTREC107genetic
27708008
PTK2_YEASTPTK2genetic
27708008
DOHH_YEASTLIA1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
COA4_YEASTCOA4genetic
27708008
EAF7_YEASTEAF7genetic
27708008
PMP1_YEASTPMP1physical
26404137
PSA3_YEASTPRE9genetic
28322792
SEM1_YEASTSEM1genetic
28322792
RPN12_YEASTRPN12genetic
28322792
KAPB_YEASTTPK2genetic
26209979
DSK2_YEASTDSK2physical
29507114
HSF_YEASTHSF1physical
29393852

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP72_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2, AND PHOSPHORYLATION.
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-20; THR-35; THR-36 ANDSER-551, 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-551, AND MASSSPECTROMETRY.
"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-426, AND MASSSPECTROMETRY.
"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-551, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, AND MASSSPECTROMETRY.

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