PRS4_HUMAN - dbPTM
PRS4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRS4_HUMAN
UniProt AC P62191
Protein Name 26S proteasome regulatory subunit 4
Gene Name PSMC1
Organism Homo sapiens (Human).
Sequence Length 440
Subcellular Localization Cytoplasm. Nucleus. Membrane
Lipid-anchor .
Protein Description Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides..
Protein Sequence MGQSQSGGHGPGGGKKDDKDKKKKYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL
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
2N-myristoyl glycine------MGQSQSGGH
------CCCCCCCCC
35.53-
2Myristoylation------MGQSQSGGH
------CCCCCCCCC
35.5322223895
4Phosphorylation----MGQSQSGGHGP
----CCCCCCCCCCC
22.1519362540
6Phosphorylation--MGQSQSGGHGPGG
--CCCCCCCCCCCCC
52.5726546556
13UbiquitinationSGGHGPGGGKKDDKD
CCCCCCCCCCCCCCC
48.13-
18UbiquitinationPGGGKKDDKDKKKKY
CCCCCCCCCCHHHCC
70.68-
23UbiquitinationKDDKDKKKKYEPPVP
CCCCCHHHCCCCCCC
67.34-
24AcetylationDDKDKKKKYEPPVPT
CCCCHHHCCCCCCCC
64.8225825284
24MalonylationDDKDKKKKYEPPVPT
CCCCHHHCCCCCCCC
64.8226320211
24UbiquitinationDDKDKKKKYEPPVPT
CCCCHHHCCCCCCCC
64.82-
25UbiquitinationDKDKKKKYEPPVPTR
CCCHHHCCCCCCCCC
42.41-
25PhosphorylationDKDKKKKYEPPVPTR
CCCHHHCCCCCCCCC
42.4127273156
40PhosphorylationVGKKKKKTKGPDAAS
CCCCCCCCCCCCHHH
50.5423312004
41UbiquitinationGKKKKKTKGPDAASK
CCCCCCCCCCCHHHC
76.85-
47PhosphorylationTKGPDAASKLPLVTP
CCCCCHHHCCCCCCC
36.1223312004
48UbiquitinationKGPDAASKLPLVTPH
CCCCHHHCCCCCCCC
49.7721890473
48UbiquitinationKGPDAASKLPLVTPH
CCCCHHHCCCCCCCC
49.7721906983
48UbiquitinationKGPDAASKLPLVTPH
CCCCHHHCCCCCCCC
49.7721890473
53PhosphorylationASKLPLVTPHTQCRL
HHCCCCCCCCCHHHH
19.6230266825
56PhosphorylationLPLVTPHTQCRLKLL
CCCCCCCCHHHHHHH
30.4830266825
58GlutathionylationLVTPHTQCRLKLLKL
CCCCCCHHHHHHHHH
6.0622555962
61UbiquitinationPHTQCRLKLLKLERI
CCCHHHHHHHHHHHH
32.21-
64UbiquitinationQCRLKLLKLERIKDY
HHHHHHHHHHHHHHH
59.75-
69UbiquitinationLLKLERIKDYLLMEE
HHHHHHHHHHHHHHH
46.6821890473
69AcetylationLLKLERIKDYLLMEE
HHHHHHHHHHHHHHH
46.6826051181
69UbiquitinationLLKLERIKDYLLMEE
HHHHHHHHHHHHHHH
46.6821906983
69UbiquitinationLLKLERIKDYLLMEE
HHHHHHHHHHHHHHH
46.6821890473
71PhosphorylationKLERIKDYLLMEEEF
HHHHHHHHHHHHHHH
9.2027642862
74SulfoxidationRIKDYLLMEEEFIRN
HHHHHHHHHHHHHHC
5.8630846556
85SulfoxidationFIRNQEQMKPLEEKQ
HHHCHHHCCCHHHHH
4.8030846556
86UbiquitinationIRNQEQMKPLEEKQE
HHCHHHCCCHHHHHH
46.2621906983
91AcetylationQMKPLEEKQEEERSK
HCCCHHHHHHHHHHC
54.3426051181
91UbiquitinationQMKPLEEKQEEERSK
HCCCHHHHHHHHHHC
54.3421906983
98UbiquitinationKQEEERSKVDDLRGT
HHHHHHHCHHHHCCC
56.7721890473
98SumoylationKQEEERSKVDDLRGT
HHHHHHHCHHHHCCC
56.77-
98UbiquitinationKQEEERSKVDDLRGT
HHHHHHHCHHHHCCC
56.7721906983
98UbiquitinationKQEEERSKVDDLRGT
HHHHHHHCHHHHCCC
56.7721890473
105UbiquitinationKVDDLRGTPMSVGTL
CHHHHCCCCCCHHHH
14.91-
144UbiquitinationSFVDKDLLEPGCSVL
HCCCHHHCCCCCEEH
12.23-
147UbiquitinationDKDLLEPGCSVLLNH
CHHHCCCCCEEHHCC
13.63-
149PhosphorylationDLLEPGCSVLLNHKV
HHCCCCCEEHHCCCC
23.0129978859
155UbiquitinationCSVLLNHKVHAVIGV
CEEHHCCCCCEEEEE
34.34-
159UbiquitinationLNHKVHAVIGVLMDD
HCCCCCEEEEEECCC
2.06-
164UbiquitinationHAVIGVLMDDTDPLV
CEEEEEECCCCCCCE
3.99-
175SumoylationDPLVTVMKVEKAPQE
CCCEEEEEEEECCCC
42.79-
178AcetylationVTVMKVEKAPQETYA
EEEEEEEECCCCHHH
69.2425953088
178UbiquitinationVTVMKVEKAPQETYA
EEEEEEEECCCCHHH
69.2421906983
183PhosphorylationVEKAPQETYADIGGL
EEECCCCHHHCCCCC
20.8229978859
184PhosphorylationEKAPQETYADIGGLD
EECCCCHHHCCCCCH
11.0928796482
185AcetylationKAPQETYADIGGLDN
ECCCCHHHCCCCCHH
14.90-
185UbiquitinationKAPQETYADIGGLDN
ECCCCHHHCCCCCHH
14.90-
192AcetylationADIGGLDNQIQEIKE
HCCCCCHHHHHHHHH
45.99-
192UbiquitinationADIGGLDNQIQEIKE
HCCCCCHHHHHHHHH
45.99-
198UbiquitinationDNQIQEIKESVELPL
HHHHHHHHHHCCCCC
43.09-
200PhosphorylationQIQEIKESVELPLTH
HHHHHHHHCCCCCCC
18.8528796482
206PhosphorylationESVELPLTHPEYYEE
HHCCCCCCCHHHHHH
33.1828796482
210PhosphorylationLPLTHPEYYEEMGIK
CCCCCHHHHHHCCCC
22.1928796482
211PhosphorylationPLTHPEYYEEMGIKP
CCCCHHHHHHCCCCC
12.0728796482
217UbiquitinationYYEEMGIKPPKGVIL
HHHHCCCCCCCEEEE
49.9221906983
220UbiquitinationEMGIKPPKGVILYGP
HCCCCCCCEEEEECC
74.47-
220UbiquitinationEMGIKPPKGVILYGP
HCCCCCCCEEEEECC
74.47-
225PhosphorylationPPKGVILYGPPGTGK
CCCEEEEECCCCCCH
19.2323917254
230PhosphorylationILYGPPGTGKTLLAK
EEECCCCCCHHHHHH
41.0829083192
232UbiquitinationYGPPGTGKTLLAKAV
ECCCCCCHHHHHHHH
35.5221890473
2322-HydroxyisobutyrylationYGPPGTGKTLLAKAV
ECCCCCCHHHHHHHH
35.52-
232AcetylationYGPPGTGKTLLAKAV
ECCCCCCHHHHHHHH
35.5225953088
232UbiquitinationYGPPGTGKTLLAKAV
ECCCCCCHHHHHHHH
35.5221906983
232UbiquitinationYGPPGTGKTLLAKAV
ECCCCCCHHHHHHHH
35.5221890473
233PhosphorylationGPPGTGKTLLAKAVA
CCCCCCHHHHHHHHH
28.4829083192
237AcetylationTGKTLLAKAVANQTS
CCHHHHHHHHHCCCC
43.2825953088
237UbiquitinationTGKTLLAKAVANQTS
CCHHHHHHHHHCCCC
43.2817370265
243PhosphorylationAKAVANQTSATFLRV
HHHHHCCCCHHHHHH
21.8220873877
244PhosphorylationKAVANQTSATFLRVV
HHHHCCCCHHHHHHH
18.6230624053
246PhosphorylationVANQTSATFLRVVGS
HHCCCCHHHHHHHCH
23.9920873877
253UbiquitinationTFLRVVGSELIQKYL
HHHHHHCHHHHHHHH
20.02-
258UbiquitinationVGSELIQKYLGDGPK
HCHHHHHHHHCCCHH
35.1321890473
2582-HydroxyisobutyrylationVGSELIQKYLGDGPK
HCHHHHHHHHCCCHH
35.13-
258AcetylationVGSELIQKYLGDGPK
HCHHHHHHHHCCCHH
35.1319608861
258UbiquitinationVGSELIQKYLGDGPK
HCHHHHHHHHCCCHH
35.1321890473
258UbiquitinationVGSELIQKYLGDGPK
HCHHHHHHHHCCCHH
35.1321890473
265AcetylationKYLGDGPKLVRELFR
HHHCCCHHHHHHHHH
66.2123749302
265UbiquitinationKYLGDGPKLVRELFR
HHHCCCHHHHHHHHH
66.21265
277UbiquitinationLFRVAEEHAPSIVFI
HHHHHHHHCCCEEEE
34.15-
286UbiquitinationPSIVFIDEIDAIGTK
CCEEEEEECCCCCCC
37.64-
293AcetylationEIDAIGTKRYDSNSG
ECCCCCCCCCCCCCC
43.6925953088
293UbiquitinationEIDAIGTKRYDSNSG
ECCCCCCCCCCCCCC
43.6921906983
295PhosphorylationDAIGTKRYDSNSGGE
CCCCCCCCCCCCCCH
25.8622964224
297PhosphorylationIGTKRYDSNSGGERE
CCCCCCCCCCCCHHH
24.78-
308PhosphorylationGEREIQRTMLELLNQ
CHHHHHHHHHHHHHH
15.1028176443
309SulfoxidationEREIQRTMLELLNQL
HHHHHHHHHHHHHHC
2.7430846556
314UbiquitinationRTMLELLNQLDGFDS
HHHHHHHHHCCCCCC
53.66-
321PhosphorylationNQLDGFDSRGDVKVI
HHCCCCCCCCCEEEE
35.5828176443
322MethylationQLDGFDSRGDVKVIM
HCCCCCCCCCEEEEE
47.37115492847
323UbiquitinationLDGFDSRGDVKVIMA
CCCCCCCCCEEEEEE
48.27-
326UbiquitinationFDSRGDVKVIMATNR
CCCCCCEEEEEECCC
30.6821906983
340UbiquitinationRIETLDPALIRPGRI
CCEECCHHHCCCCCC
18.45-
347UbiquitinationALIRPGRIDRKIEFP
HHCCCCCCCCEEECC
8.13-
348UbiquitinationLIRPGRIDRKIEFPL
HCCCCCCCCEEECCC
44.45-
350UbiquitinationRPGRIDRKIEFPLPD
CCCCCCCEEECCCCC
42.72-
350UbiquitinationRPGRIDRKIEFPLPD
CCCCCCCEEECCCCC
42.72-
357UbiquitinationKIEFPLPDEKTKKRI
EEECCCCCHHHHHHE
77.14-
359UbiquitinationEFPLPDEKTKKRIFQ
ECCCCCHHHHHHEEE
73.3835966
369PhosphorylationKRIFQIHTSRMTLAD
HHEEEEECCCCCCCC
21.4730001349
370PhosphorylationRIFQIHTSRMTLADD
HEEEEECCCCCCCCC
13.0923312004
372SulfoxidationFQIHTSRMTLADDVT
EEEECCCCCCCCCCC
3.4530846556
373PhosphorylationQIHTSRMTLADDVTL
EEECCCCCCCCCCCH
20.0622985185
385SulfoxidationVTLDDLIMAKDDLSG
CCHHHHHHCCCCCCC
5.0130846556
387UbiquitinationLDDLIMAKDDLSGAD
HHHHHHCCCCCCCCC
34.1021906983
391PhosphorylationIMAKDDLSGADIKAI
HHCCCCCCCCCHHHH
38.6421712546
3962-HydroxyisobutyrylationDLSGADIKAICTEAG
CCCCCCHHHHHHHHH
32.04-
396UbiquitinationDLSGADIKAICTEAG
CCCCCCHHHHHHHHH
32.04-
399GlutathionylationGADIKAICTEAGLMA
CCCHHHHHHHHHHHH
3.1722555962
405SulfoxidationICTEAGLMALRERRM
HHHHHHHHHHHHHHH
3.0221406390
413UbiquitinationALRERRMKVTNEDFK
HHHHHHHCCCHHHHH
44.0621906983
420UbiquitinationKVTNEDFKKSKENVL
CCCHHHHHHHHHHCE
69.3421890473
4202-HydroxyisobutyrylationKVTNEDFKKSKENVL
CCCHHHHHHHHHHCE
69.34-
420UbiquitinationKVTNEDFKKSKENVL
CCCHHHHHHHHHHCE
69.3421890473
420UbiquitinationKVTNEDFKKSKENVL
CCCHHHHHHHHHHCE
69.3421890473
421UbiquitinationVTNEDFKKSKENVLY
CCHHHHHHHHHHCEE
67.75-
423UbiquitinationNEDFKKSKENVLYKK
HHHHHHHHHHCEEEC
63.29-
429AcetylationSKENVLYKKQEGTPE
HHHHCEEECCCCCCC
43.767396815
429UbiquitinationSKENVLYKKQEGTPE
HHHHCEEECCCCCCC
43.76-
430SumoylationKENVLYKKQEGTPEG
HHHCEEECCCCCCCC
39.77-
430SumoylationKENVLYKKQEGTPEG
HHHCEEECCCCCCCC
39.77-
430UbiquitinationKENVLYKKQEGTPEG
HHHCEEECCCCCCCC
39.772190698
434PhosphorylationLYKKQEGTPEGLYL-
EEECCCCCCCCCCC-
19.8822617229
439PhosphorylationEGTPEGLYL------
CCCCCCCCC------
22.6325807930

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 PRS4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRS4_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 PRS4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
PSMD2_HUMANPSMD2physical
16189514
PSMD5_HUMANPSMD5physical
10625621
PRS7_HUMANPSMC2physical
10625621
ATX7_HUMANATXN7physical
11734547
PRS7_HUMANPSMC2physical
19490896
PSME1_HUMANPSME1physical
12419264
TAT_HV1H2tatphysical
12419264
PRS6B_HUMANPSMC4physical
20810900
PAAF1_HUMANPAAF1physical
15831487
FKBP8_HUMANFKBP8physical
17573772
PSA2_HUMANPSMA2physical
15837734
PSA3_HUMANPSMA3physical
15837734
PRS8_HUMANPSMC5physical
21628461
PSMD8_HUMANPSMD8physical
21628461
PSB5_HUMANPSMB5physical
21628461
PSMD6_HUMANPSMD6physical
22275368
PSMD8_HUMANPSMD8physical
22275368
A4_HUMANAPPphysical
21832049
PSMD2_HUMANPSMD2physical
22939629
PRS7_HUMANPSMC2physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PRS8_HUMANPSMC5physical
22939629
PSD13_HUMANPSMD13physical
22939629
PSDE_HUMANPSMD14physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSD10_HUMANPSMD10physical
22939629
PRS6B_HUMANPSMC4physical
22939629
PSMD5_HUMANPSMD5physical
22939629
PRS6A_HUMANPSMC3physical
22939629
PSD11_HUMANPSMD11physical
22939629
PSD12_HUMANPSMD12physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSA7_HUMANPSMA7physical
22939629
PSA1_HUMANPSMA1physical
22939629
PSA3_HUMANPSMA3physical
22939629
PSA6_HUMANPSMA6physical
22939629
PSB5_HUMANPSMB5physical
22939629
PSA5_HUMANPSMA5physical
22939629
PSB1_HUMANPSMB1physical
22939629
PSB7_HUMANPSMB7physical
22939629
PSB2_HUMANPSMB2physical
22939629
PSB3_HUMANPSMB3physical
22939629
PSB6_HUMANPSMB6physical
22939629
PSA4_HUMANPSMA4physical
22939629
PSME2_HUMANPSME2physical
22939629
PSB8_HUMANPSMB8physical
22939629
PSA7L_HUMANPSMA8physical
22939629
RT16_HUMANMRPS16physical
22939629
SF3A1_HUMANSF3A1physical
22939629
UGGG1_HUMANUGGT1physical
22939629
SNX12_HUMANSNX12physical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
JHD2C_HUMANJMJD1Cphysical
23455924
JMJD6_HUMANJMJD6physical
23455924
ADRM1_HUMANADRM1physical
22863883
PSDE_HUMANPSMD14physical
22863883
PSMD4_HUMANPSMD4physical
22863883
PSMD2_HUMANPSMD2physical
25416956
PSMD5_HUMANPSMD5physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
PRS10_HUMANPSMC6physical
26186194
PRS6A_HUMANPSMC3physical
26186194
PRS8_HUMANPSMC5physical
26186194
PSD10_HUMANPSMD10physical
26186194
BAG1_HUMANBAG1physical
26186194
CCAR2_HUMANCCAR2physical
26344197
DPY30_HUMANDPY30physical
26344197
RT16_HUMANMRPS16physical
26344197
MTCH1_HUMANMTCH1physical
26344197
PSA1_HUMANPSMA1physical
26344197
PSA2_HUMANPSMA2physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSA5_HUMANPSMA5physical
26344197
PSA6_HUMANPSMA6physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB4_HUMANPSMB4physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB7_HUMANPSMB7physical
26344197
PSB8_HUMANPSMB8physical
26344197
PSB9_HUMANPSMB9physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS8_HUMANPSMC5physical
26344197
PSD10_HUMANPSMD10physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD3_HUMANPSMD3physical
26344197
PSMD4_HUMANPSMD4physical
26344197
PSMD6_HUMANPSMD6physical
26344197
PSMD7_HUMANPSMD7physical
26344197
PSMD8_HUMANPSMD8physical
26344197
RD23A_HUMANRAD23Aphysical
26344197
RD23B_HUMANRAD23Bphysical
26344197
RPN1_HUMANRPN1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
1433E_HUMANYWHAEphysical
26344197
BAG1_HUMANBAG1physical
26496610
CBL_HUMANCBLphysical
26496610
PRS7_HUMANPSMC2physical
26496610
PRS6A_HUMANPSMC3physical
26496610
PRS6B_HUMANPSMC4physical
26496610
PRS8_HUMANPSMC5physical
26496610
PRS10_HUMANPSMC6physical
26496610
PSMD1_HUMANPSMD1physical
26496610
PSMD2_HUMANPSMD2physical
26496610
PSMD3_HUMANPSMD3physical
26496610
PSMD4_HUMANPSMD4physical
26496610
PSMD5_HUMANPSMD5physical
26496610
PSMD7_HUMANPSMD7physical
26496610
PSMD8_HUMANPSMD8physical
26496610
PSD10_HUMANPSMD10physical
26496610
PSD11_HUMANPSMD11physical
26496610
PSD12_HUMANPSMD12physical
26496610
PSD13_HUMANPSMD13physical
26496610
PTN2_HUMANPTPN2physical
26496610
UBE3A_HUMANUBE3Aphysical
26496610
NCOA4_HUMANNCOA4physical
26496610
HERC2_HUMANHERC2physical
26496610
UBP14_HUMANUSP14physical
26496610
TXNL1_HUMANTXNL1physical
26496610
PSMD6_HUMANPSMD6physical
26496610
PSDE_HUMANPSMD14physical
26496610
CEPT1_HUMANCEPT1physical
26496610
ADRM1_HUMANADRM1physical
26496610
CEP83_HUMANCEP83physical
26496610
UCHL5_HUMANUCHL5physical
26496610
VATD_HUMANATP6V1Dphysical
26496610
XRN1_HUMANXRN1physical
26496610
MI4GD_HUMANMIF4GDphysical
26496610
PAAF1_HUMANPAAF1physical
26496610
NEUL4_HUMANNEURL4physical
26496610
MIDN_HUMANMIDNphysical
26496610
ZN561_HUMANZNF561physical
26496610
PSD12_HUMANPSMD12physical
28514442
PRS6B_HUMANPSMC4physical
28514442
PSD10_HUMANPSMD10physical
28514442
BAG1_HUMANBAG1physical
28514442
PRS6A_HUMANPSMC3physical
28514442
PSMD1_HUMANPSMD1physical
28514442
PRS10_HUMANPSMC6physical
28514442
PSMD2_HUMANPSMD2physical
28514442

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 PRS4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-258, AND MASS SPECTROMETRY.
Myristoylation
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: MYRISTOYLATION [LARGE SCALE ANALYSIS] AT GLY-2, 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-4, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, AND MASSSPECTROMETRY.

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