PSA3_HUMAN - dbPTM
PSA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSA3_HUMAN
UniProt AC P25788
Protein Name Proteasome subunit alpha type-3
Gene Name PSMA3
Organism Homo sapiens (Human).
Sequence Length 255
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2..
Protein Sequence MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM
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------MSSIGTGYD
------CCCCCCCCC
30.5712376572
2Phosphorylation------MSSIGTGYD
------CCCCCCCCC
30.5728464451
2 (in isoform 2)Acetylation-30.57-
3Phosphorylation-----MSSIGTGYDL
-----CCCCCCCCCC
24.6030576142
6Phosphorylation--MSSIGTGYDLSAS
--CCCCCCCCCCCCC
30.7926074081
8NitrationMSSIGTGYDLSASTF
CCCCCCCCCCCCCEE
17.35-
8PhosphorylationMSSIGTGYDLSASTF
CCCCCCCCCCCCCEE
17.3526074081
8 (in isoform 2)Phosphorylation-17.35-
11PhosphorylationIGTGYDLSASTFSPD
CCCCCCCCCCEECCC
19.7820068231
13PhosphorylationTGYDLSASTFSPDGR
CCCCCCCCEECCCCC
26.9825159151
14PhosphorylationGYDLSASTFSPDGRV
CCCCCCCEECCCCCE
28.0522199227
16PhosphorylationDLSASTFSPDGRVFQ
CCCCCEECCCCCEEE
23.3625159151
16 (in isoform 2)Phosphorylation-23.36-
26PhosphorylationGRVFQVEYAMKAVEN
CCEEEEEEHHHHHHC
17.0926074081
28SulfoxidationVFQVEYAMKAVENSS
EEEEEEHHHHHHCCC
2.5421406390
29UbiquitinationFQVEYAMKAVENSST
EEEEEHHHHHHCCCC
40.9021906983
29 (in isoform 1)Ubiquitination-40.9021890473
29 (in isoform 2)Ubiquitination-40.9021890473
34PhosphorylationAMKAVENSSTAIGIR
HHHHHHCCCCEEEEE
18.6326074081
35PhosphorylationMKAVENSSTAIGIRC
HHHHHCCCCEEEEEE
33.1826074081
36PhosphorylationKAVENSSTAIGIRCK
HHHHCCCCEEEEEEC
23.3221712546
43AcetylationTAIGIRCKDGVVFGV
CEEEEEECCCEEEEE
47.9026051181
43UbiquitinationTAIGIRCKDGVVFGV
CEEEEEECCCEEEEE
47.9021906983
43 (in isoform 1)Ubiquitination-47.9021890473
43 (in isoform 2)Ubiquitination-47.9021890473
522-HydroxyisobutyrylationGVVFGVEKLVLSKLY
CEEEEEEHHHHHHHH
41.30-
52UbiquitinationGVVFGVEKLVLSKLY
CEEEEEEHHHHHHHH
41.30-
57UbiquitinationVEKLVLSKLYEEGSN
EEHHHHHHHHHCCCC
51.4321890473
572-HydroxyisobutyrylationVEKLVLSKLYEEGSN
EEHHHHHHHHHCCCC
51.43-
57AcetylationVEKLVLSKLYEEGSN
EEHHHHHHHHHCCCC
51.4319608861
57MalonylationVEKLVLSKLYEEGSN
EEHHHHHHHHHCCCC
51.4326320211
57UbiquitinationVEKLVLSKLYEEGSN
EEHHHHHHHHHCCCC
51.4321890473
57 (in isoform 1)Ubiquitination-51.4321890473
57 (in isoform 2)Acetylation-51.43-
57 (in isoform 2)Ubiquitination-51.4321890473
59PhosphorylationKLVLSKLYEEGSNKR
HHHHHHHHHCCCCCC
18.7028152594
652-HydroxyisobutyrylationLYEEGSNKRLFNVDR
HHHCCCCCCCCEECH
52.77-
65AcetylationLYEEGSNKRLFNVDR
HHHCCCCCCCCEECH
52.7723749302
65UbiquitinationLYEEGSNKRLFNVDR
HHHCCCCCCCCEECH
52.7721906983
65 (in isoform 1)Ubiquitination-52.7721890473
65 (in isoform 2)Ubiquitination-52.7721890473
97PhosphorylationDIAREEASNFRSNFG
HHHHHHHHHHHHCCC
39.52-
101PhosphorylationEEASNFRSNFGYNIP
HHHHHHHHCCCCCCC
32.1621712546
105PhosphorylationNFRSNFGYNIPLKHL
HHHHCCCCCCCHHHH
13.0420090780
110UbiquitinationFGYNIPLKHLADRVA
CCCCCCHHHHHHHHH
31.0821890473
110AcetylationFGYNIPLKHLADRVA
CCCCCCHHHHHHHHH
31.0819608861
110UbiquitinationFGYNIPLKHLADRVA
CCCCCCHHHHHHHHH
31.0821890473
110 (in isoform 1)Ubiquitination-31.0821890473
110 (in isoform 2)Acetylation-31.08-
110 (in isoform 2)Ubiquitination-31.0821890473
154 (in isoform 2)Phosphorylation-23.27-
161PhosphorylationPSGVSYGYWGCAIGK
CCCCCCCCHHHHHHH
7.1522817900
172 (in isoform 2)Ubiquitination-12.8421890473
174UbiquitinationGKARQAAKTEIEKLQ
HHHHHHHHHHHHHHH
50.10-
175PhosphorylationKARQAAKTEIEKLQM
HHHHHHHHHHHHHHH
37.1528258704
176 (in isoform 2)Ubiquitination-48.7421890473
1792-HydroxyisobutyrylationAAKTEIEKLQMKEMT
HHHHHHHHHHHHHCC
50.08-
179AcetylationAAKTEIEKLQMKEMT
HHHHHHHHHHHHHCC
50.0826822725
179UbiquitinationAAKTEIEKLQMKEMT
HHHHHHHHHHHHHCC
50.0821906983
179 (in isoform 1)Ubiquitination-50.0821890473
183AcetylationEIEKLQMKEMTCRDI
HHHHHHHHHCCHHHH
31.2225953088
183UbiquitinationEIEKLQMKEMTCRDI
HHHHHHHHHCCHHHH
31.2221906983
183 (in isoform 1)Ubiquitination-31.2221890473
186PhosphorylationKLQMKEMTCRDIVKE
HHHHHHCCHHHHHHH
12.8928258704
192AcetylationMTCRDIVKEVAKIIY
CCHHHHHHHHHHHHE
46.9725953088
192UbiquitinationMTCRDIVKEVAKIIY
CCHHHHHHHHHHHHE
46.97-
199AcetylationKEVAKIIYIVHDEVK
HHHHHHHEEECHHHC
10.6019608861
199PhosphorylationKEVAKIIYIVHDEVK
HHHHHHHEEECHHHC
10.6028152594
199UbiquitinationKEVAKIIYIVHDEVK
HHHHHHHEEECHHHC
10.6019608861
199 (in isoform 2)Acetylation-10.60-
199 (in isoform 2)Ubiquitination-10.6021890473
2062-HydroxyisobutyrylationYIVHDEVKDKAFELE
EEECHHHCCCCEEEE
52.01-
206AcetylationYIVHDEVKDKAFELE
EEECHHHCCCCEEEE
52.0119608861
206UbiquitinationYIVHDEVKDKAFELE
EEECHHHCCCCEEEE
52.0121906983
206 (in isoform 1)Ubiquitination-52.0121890473
208UbiquitinationVHDEVKDKAFELELS
ECHHHCCCCEEEEEE
49.62-
223AcetylationWVGELTNGRHEIVPK
EEEECCCCCCEECCH
27.3819608861
223UbiquitinationWVGELTNGRHEIVPK
EEEECCCCCCEECCH
27.3819608861
223 (in isoform 2)Acetylation-27.38-
223 (in isoform 2)Ubiquitination-27.3821890473
230UbiquitinationGRHEIVPKDIREEAE
CCCEECCHHHHHHHH
55.6921890473
2302-HydroxyisobutyrylationGRHEIVPKDIREEAE
CCCEECCHHHHHHHH
55.69-
230AcetylationGRHEIVPKDIREEAE
CCCEECCHHHHHHHH
55.6919608861
230UbiquitinationGRHEIVPKDIREEAE
CCCEECCHHHHHHHH
55.6921890473
230 (in isoform 1)Ubiquitination-55.6921890473
231AcetylationRHEIVPKDIREEAEK
CCEECCHHHHHHHHH
38.8219608861
231UbiquitinationRHEIVPKDIREEAEK
CCEECCHHHHHHHHH
38.8219608861
231 (in isoform 2)Acetylation-38.82-
231 (in isoform 2)Ubiquitination-38.8221890473
236 (in isoform 2)Phosphorylation-17.52-
238UbiquitinationDIREEAEKYAKESLK
HHHHHHHHHHHHHHH
58.5221890473
238AcetylationDIREEAEKYAKESLK
HHHHHHHHHHHHHHH
58.5223749302
238UbiquitinationDIREEAEKYAKESLK
HHHHHHHHHHHHHHH
58.5221890473
238 (in isoform 1)Ubiquitination-58.5221890473
238 (in isoform 2)Ubiquitination-58.5221890473
241UbiquitinationEEAEKYAKESLKEED
HHHHHHHHHHHHHCC
44.75-
243PhosphorylationAEKYAKESLKEEDES
HHHHHHHHHHHCCCC
43.9919664994
243 (in isoform 2)Phosphorylation-43.99-
245UbiquitinationKYAKESLKEEDESDD
HHHHHHHHHCCCCCC
69.232190698
245 (in isoform 1)Ubiquitination-69.2321890473
250PhosphorylationSLKEEDESDDDNM--
HHHHCCCCCCCCC--
59.6719664994

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
243SPhosphorylationKinaseCK2-FAMILY-GPS
243SPhosphorylationKinaseCK2_GROUP-PhosphoELM
250SPhosphorylationKinaseCK2-FAMILY-GPS
250SPhosphorylationKinaseCK2_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSA3_HUMAN !!

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 PSA3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA1_HUMANPSMA1physical
9451443
PSA6_HUMANPSMA6physical
9451443
PLK1_HUMANPLK1physical
11205743
EGR1_HUMANEGR1physical
12379479
CDN1A_HUMANCDKN1Aphysical
11350925
PRS6A_HUMANPSMC3physical
22079093
UBP5_HUMANUSP5physical
22079093
WDR48_HUMANWDR48physical
22079093
UBP14_HUMANUSP14physical
22079093
PAF1_HUMANPAF1physical
22079093
HDAC2_HUMANHDAC2physical
22079093
TBL1R_HUMANTBL1XR1physical
22079093
RBBP5_HUMANRBBP5physical
22079093
ENOA_HUMANENO1physical
22079093
WDR5_HUMANWDR5physical
22079093
NUCL_HUMANNCLphysical
22079093
SF3A3_HUMANSF3A3physical
22079093
PUF60_HUMANPUF60physical
22079093
U5S1_HUMANEFTUD2physical
22079093
CPSF2_HUMANCPSF2physical
22079093
TADBP_HUMANTARDBPphysical
22079093
HNRPF_HUMANHNRNPFphysical
22079093
HNRLL_HUMANHNRNPLLphysical
22079093
ROA2_HUMANHNRNPA2B1physical
22079093
HNRPC_HUMANHNRNPCphysical
22079093
FUBP2_HUMANKHSRPphysical
22079093
NONO_HUMANNONOphysical
22079093
PTBP1_HUMANPTBP1physical
22079093
DDX1_HUMANDDX1physical
22079093
DDX5_HUMANDDX5physical
22079093
SRRT_HUMANSRRTphysical
22079093
CALR_HUMANCALRphysical
22079093
PDIA1_HUMANP4HBphysical
22079093
GRP75_HUMANHSPA9physical
22079093
CH60_HUMANHSPD1physical
22079093
HSP7C_HUMANHSPA8physical
22079093
HS71L_HUMANHSPA1Lphysical
22079093
HS90B_HUMANHSP90AB1physical
22079093
HS90A_HUMANHSP90AA1physical
22079093
DNJA1_HUMANDNAJA1physical
22079093
TCPB_HUMANCCT2physical
22079093
ACTB_HUMANACTBphysical
22079093
ACTN2_HUMANACTN2physical
22079093
ACTN4_HUMANACTN4physical
22079093
TBA1B_HUMANTUBA1Bphysical
22079093
TBB2A_HUMANTUBB2Aphysical
22079093
PRP19_HUMANPRPF19physical
22079093
XRCC6_HUMANXRCC6physical
22079093
XRCC5_HUMANXRCC5physical
22079093
RUVB1_HUMANRUVBL1physical
22079093
GRP78_HUMANHSPA5physical
22079093
ATPB_HUMANATP5Bphysical
22079093
ALDOA_HUMANALDOAphysical
22079093
FETUA_HUMANAHSGphysical
22079093
KCRB_HUMANCKBphysical
22079093
G3P_HUMANGAPDHphysical
22079093
MDHM_HUMANMDH2physical
22079093
MCM3_HUMANMCM3physical
22079093
MCM6_HUMANMCM6physical
22079093
PPM1F_HUMANPPM1Fphysical
22079093
PRS6B_HUMANPSMC4physical
22079093
RD23B_HUMANRAD23Bphysical
22079093
TF2B_HUMANGTF2Bphysical
22079093
ROA1_HUMANHNRNPA1physical
22079093
PCBP2_HUMANPCBP2physical
22079093
IREB2_HUMANIREB2physical
22079093
EF1A1_HUMANEEF1A1physical
22079093
EF2_HUMANEEF2physical
22079093
SYWC_HUMANWARSphysical
22079093
GARS_HUMANGARSphysical
22079093
SYK_HUMANKARSphysical
22079093
ENPL_HUMANHSP90B1physical
22079093
HSP72_HUMANHSPA2physical
22079093
TCPQ_HUMANCCT8physical
22079093
TCPD_HUMANCCT4physical
22079093
TCPG_HUMANCCT3physical
22079093
TCPZ_HUMANCCT6Aphysical
22079093
STIP1_HUMANSTIP1physical
22079093
TPIS_HUMANTPI1physical
22079093
ECHB_HUMANHADHBphysical
22079093
PGAM1_HUMANPGAM1physical
22079093
AACT_HUMANSERPINA3physical
22079093
KPYM_HUMANPKMphysical
22079093
PGK1_HUMANPGK1physical
22079093
LDHA_HUMANLDHAphysical
22079093
ODP2_HUMANDLATphysical
22079093
C1TC_HUMANMTHFD1physical
22079093
PYRG1_HUMANCTPS1physical
22079093
LONM_HUMANLONP1physical
22079093
GANAB_HUMANGANABphysical
22079093
ASAH1_HUMANASAH1physical
22079093
DONS_HUMANDONSONphysical
22079093
ALBU_HUMANALBphysical
22079093
TRFE_HUMANTFphysical
22079093
SPB3_HUMANSERPINB3physical
22079093
PSA1_HUMANPSMA1physical
22079093
PSMD1_HUMANPSMD1physical
22079093
NCOA3_HUMANNCOA3physical
18313384
CFTR_HUMANCFTRphysical
16390870
PSA7_HUMANPSMA7physical
15225636
PSA4_HUMANPSMA4physical
15225636
PSA2_HUMANPSMA2physical
14733938
PSA4_HUMANPSMA4physical
14733938
PAI1_HUMANSERPINE1physical
21135093
AURKB_HUMANAURKBphysical
14674694
PSA1_HUMANPSMA1physical
9311996
PSA2_HUMANPSMA2physical
9311996
PSA4_HUMANPSMA4physical
9311996
PSA5_HUMANPSMA5physical
9311996
PSA6_HUMANPSMA6physical
9311996
PSA7_HUMANPSMA7physical
9311996
1433T_HUMANYWHAQphysical
20086099
CDN1A_HUMANCDKN1Aphysical
20086099
MDM2_HUMANMDM2physical
20308078
CDN1A_HUMANCDKN1Aphysical
20308078
PSB10_HUMANPSMB10physical
17948026
PSA7_HUMANPSMA7physical
17948026
PRS6A_HUMANPSMC3physical
11139393
PSB9_HUMANPSMB9physical
11139393
PSA6_HUMANPSMA6physical
22939629
PSA7_HUMANPSMA7physical
22939629
PSA4_HUMANPSMA4physical
22939629
PSB5_HUMANPSMB5physical
22939629
PSD13_HUMANPSMD13physical
22939629
PSA5_HUMANPSMA5physical
22939629
PSB1_HUMANPSMB1physical
22939629
PSB2_HUMANPSMB2physical
22939629
PSB3_HUMANPSMB3physical
22939629
PSB4_HUMANPSMB4physical
22939629
PSB6_HUMANPSMB6physical
22939629
PSB7_HUMANPSMB7physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSD11_HUMANPSMD11physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSB8_HUMANPSMB8physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PSME2_HUMANPSME2physical
22939629
PSME1_HUMANPSME1physical
22939629
PSA7L_HUMANPSMA8physical
22939629
PSA6_HUMANPSMA6physical
16169070
PSA7_HUMANPSMA7physical
21988832
TF7L2_HUMANTCF7L2physical
21988832
HXA2_HUMANHOXA2physical
24244684
AP3M1_HUMANAP3M1physical
22863883
PSA2_HUMANPSMA2physical
22863883
PSA4_HUMANPSMA4physical
22863883
PSA5_HUMANPSMA5physical
22863883
PSA7_HUMANPSMA7physical
22863883
PSB1_HUMANPSMB1physical
22863883
PSB2_HUMANPSMB2physical
22863883
PSB3_HUMANPSMB3physical
22863883
PSB5_HUMANPSMB5physical
22863883
PSB6_HUMANPSMB6physical
22863883
PSB7_HUMANPSMB7physical
22863883
PSA3_HUMANPSMA3physical
25416956
PSA6_HUMANPSMA6physical
25416956
PSB4_HUMANPSMB4physical
25416956
R3GEF_HUMANRAB3IL1physical
25416956
RSMB_HUMANSNRPBphysical
25416956
RU1C_HUMANSNRPCphysical
25416956
STX4_HUMANSTX4physical
25416956
SF01_HUMANSF1physical
25416956
APEL_HUMANAPLNphysical
25416956
SERF2_HUMANSERF2physical
25416956
STX6_HUMANSTX6physical
25416956
BT2A2_HUMANBTN2A2physical
25416956
PLD3A_HUMANSLMO1physical
25416956
DMC1_HUMANDMC1physical
25416956
AGRL1_HUMANLPHN1physical
25416956
ARIP4_HUMANRAD54L2physical
25416956
IQCE_HUMANIQCEphysical
25416956
RFOX2_HUMANRBFOX2physical
25416956
FBX7_HUMANFBXO7physical
25416956
PTN23_HUMANPTPN23physical
25416956
GORS2_HUMANGORASP2physical
25416956
CCD69_HUMANCCDC69physical
25416956
SH3K1_HUMANSH3KBP1physical
25416956
PRR13_HUMANPRR13physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
CCL28_HUMANCCL28physical
25416956
DMRT3_HUMANDMRT3physical
25416956
S22AN_HUMANSLC22A23physical
25416956
RBM42_HUMANRBM42physical
25416956
GLUCM_HUMANC14orf159physical
25416956
FXL18_HUMANFBXL18physical
25416956
PRR3_HUMANPRR3physical
25416956
RAM_HUMANFAM103A1physical
25416956
YPEL3_HUMANYPEL3physical
25416956
KIRR2_HUMANKIRREL2physical
25416956
MUM1_HUMANMUM1physical
25416956
RFT1_HUMANRFT1physical
25416956
CA105_HUMANC1orf105physical
25416956
CRUM3_HUMANCRB3physical
25416956
OSR2_HUMANOSR2physical
25416956
SLAI1_HUMANSLAIN1physical
25416956
TBC16_HUMANTBC1D16physical
25416956
NEUR4_HUMANNEU4physical
25416956
SPAT8_HUMANSPATA8physical
25416956
F218A_HUMANFAM218Aphysical
25416956
ZN366_HUMANZNF366physical
25416956
PWP2B_HUMANPWWP2Bphysical
25416956
PATL1_HUMANPATL1physical
25416956
F1712_HUMANFAM171A2physical
25416956
RUAS1_HUMANRUSC1-AS1physical
25416956
RTP5_HUMANRTP5physical
25416956
KRA81_HUMANKRTAP8-1physical
25416956
KR195_HUMANKRTAP19-5physical
25416956
KR261_HUMANKRTAP26-1physical
25416956
CI106_HUMANC9orf106physical
25416956
PCOTH_HUMANC1QTNF9B-AS1physical
25416956
ELP6_HUMANELP6physical
26344197
EXOS4_HUMANEXOSC4physical
26344197
EXOS6_HUMANEXOSC6physical
26344197
NELFE_HUMANNELFEphysical
26344197
PRS7_HUMANPSMC2physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS6B_HUMANPSMC4physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD3_HUMANPSMD3physical
26344197
PSMD7_HUMANPSMD7physical
26344197
PSME3_HUMANPSME3physical
26344197
PSMG2_HUMANPSMG2physical
26344197
TERA_HUMANVCPphysical
26344197
PSA3_HUMANPSMA3physical
21516116
PSA6_HUMANPSMA6physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSA3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex.";
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
Biochemistry 46:3553-3565(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, ACETYLATION ATSER-2, AND MASS SPECTROMETRY.
"Mapping and structural dissection of human 20 s proteasome usingproteomic approaches.";
Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E.,Monsarrat B.;
Mol. Cell. Proteomics 1:567-578(2002).
Cited for: ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-250.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-110; LYS-206;LYS-230 AND LYS-238, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, ANDMASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex.";
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
Biochemistry 46:3553-3565(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, ACETYLATION ATSER-2, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.
"Mapping and structural dissection of human 20 s proteasome usingproteomic approaches.";
Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E.,Monsarrat B.;
Mol. Cell. Proteomics 1:567-578(2002).
Cited for: ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-250.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, AND MASSSPECTROMETRY.

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