PSMD1_HUMAN - dbPTM
PSMD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSMD1_HUMAN
UniProt AC Q99460
Protein Name 26S proteasome non-ATPase regulatory subunit 1
Gene Name PSMD1
Organism Homo sapiens (Human).
Sequence Length 953
Subcellular Localization
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..
Protein Sequence MITSAAGIISLLDEDEPQLKEFALHKLNAVVNDFWAEISESVDKIEVLYEDEGFRSRQFAALVASKVFYHLGAFEESLNYALGAGDLFNVNDNSEYVETIIAKCIDHYTKQCVENADLPEGEKKPIDQRLEGIVNKMFQRCLDDHKYKQAIGIALETRRLDVFEKTILESNDVPGMLAYSLKLCMSLMQNKQFRNKVLRVLVKIYMNLEKPDFINVCQCLIFLDDPQAVSDILEKLVKEDNLLMAYQICFDLYESASQQFLSSVIQNLRTVGTPIASVPGSTNTGTVPGSEKDSDSMETEEKTSSAFVGKTPEASPEPKDQTLKMIKILSGEMAIELHLQFLIRNNNTDLMILKNTKDAVRNSVCHTATVIANSFMHCGTTSDQFLRDNLEWLARATNWAKFTATASLGVIHKGHEKEALQLMATYLPKDTSPGSAYQEGGGLYALGLIHANHGGDIIDYLLNQLKNASNDIVRHGGSLGLGLAAMGTARQDVYDLLKTNLYQDDAVTGEAAGLALGLVMLGSKNAQAIEDMVGYAQETQHEKILRGLAVGIALVMYGRMEEADALIESLCRDKDPILRRSGMYTVAMAYCGSGNNKAIRRLLHVAVSDVNDDVRRAAVESLGFILFRTPEQCPSVVSLLSESYNPHVRYGAAMALGICCAGTGNKEAINLLEPMTNDPVNYVRQGALIASALIMIQQTEITCPKVNQFRQLYSKVINDKHDDVMAKFGAILAQGILDAGGHNVTISLQSRTGHTHMPSVVGVLVFTQFWFWFPLSHFLSLAYTPTCVIGLNKDLKMPKVQYKSNCKPSTFAYPAPLEVPKEKEKEKVSTAVLSITAKAKKKEKEKEKKEEEKMEVDEAEKKEEKEKKKEPEPNFQLLDNPARVMPAQLKVLTMPETCRYQPFKPLSIGGIIILKDTSEDIEELVEPVAAHGPKIEEEEQEPEPPEPFEYIDD
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
1Acetylation-------MITSAAGI
-------CCCCHHHH
7.3222223895
20UbiquitinationDEDEPQLKEFALHKL
CCCCHHHHHHHHHHH
45.6021906983
20 (in isoform 1)Ubiquitination-45.6021890473
20 (in isoform 2)Ubiquitination-45.6021890473
26UbiquitinationLKEFALHKLNAVVND
HHHHHHHHHHHHHHH
44.2623503661
49PhosphorylationVDKIEVLYEDEGFRS
CCEEEEEECCCCCCH
26.8916097034
110AcetylationKCIDHYTKQCVENAD
HHHHHHHHHHHHCCC
34.2426051181
110UbiquitinationKCIDHYTKQCVENAD
HHHHHHHHHHHHCCC
34.2421963094
110 (in isoform 2)Ubiquitination-34.24-
123UbiquitinationADLPEGEKKPIDQRL
CCCCCCCCCCHHHHH
74.7722817900
124UbiquitinationDLPEGEKKPIDQRLE
CCCCCCCCCHHHHHH
42.7921906983
124 (in isoform 1)Ubiquitination-42.7921890473
124 (in isoform 2)Ubiquitination-42.7921890473
136AcetylationRLEGIVNKMFQRCLD
HHHHHHHHHHHHHHC
30.1425953088
136UbiquitinationRLEGIVNKMFQRCLD
HHHHHHHHHHHHHHC
30.1423000965
136 (in isoform 1)Ubiquitination-30.1421890473
136 (in isoform 2)Ubiquitination-30.1421890473
146AcetylationQRCLDDHKYKQAIGI
HHHHCCHHHHHHHHH
62.2225953088
146UbiquitinationQRCLDDHKYKQAIGI
HHHHCCHHHHHHHHH
62.2229967540
147PhosphorylationRCLDDHKYKQAIGIA
HHHCCHHHHHHHHHH
12.62-
1482-HydroxyisobutyrylationCLDDHKYKQAIGIAL
HHCCHHHHHHHHHHH
37.75-
157PhosphorylationAIGIALETRRLDVFE
HHHHHHHHHCCCCHH
23.1820068231
166PhosphorylationRLDVFEKTILESNDV
CCCCHHHHHHHCCCC
24.4820068231
170PhosphorylationFEKTILESNDVPGML
HHHHHHHCCCCCHHH
34.5820068231
179PhosphorylationDVPGMLAYSLKLCMS
CCCHHHHHHHHHHHH
15.5820068231
180PhosphorylationVPGMLAYSLKLCMSL
CCHHHHHHHHHHHHH
17.2724719451
191UbiquitinationCMSLMQNKQFRNKVL
HHHHHCCHHHHHHHH
33.6423000965
196UbiquitinationQNKQFRNKVLRVLVK
CCHHHHHHHHHHHHH
38.0923000965
199DimethylationQFRNKVLRVLVKIYM
HHHHHHHHHHHHHHH
23.78-
199MethylationQFRNKVLRVLVKIYM
HHHHHHHHHHHHHHH
23.7830762955
205PhosphorylationLRVLVKIYMNLEKPD
HHHHHHHHHCCCCCC
3.6827067055
210UbiquitinationKIYMNLEKPDFINVC
HHHHCCCCCCCEEEE
53.7216196087
235UbiquitinationAVSDILEKLVKEDNL
HHHHHHHHHHHHCCH
55.9516196087
270PhosphorylationSVIQNLRTVGTPIAS
HHHHHHHCCCCCCCC
26.8429255136
273PhosphorylationQNLRTVGTPIASVPG
HHHHCCCCCCCCCCC
13.7419664994
277PhosphorylationTVGTPIASVPGSTNT
CCCCCCCCCCCCCCC
29.5730266825
281PhosphorylationPIASVPGSTNTGTVP
CCCCCCCCCCCCCCC
16.6530266825
282PhosphorylationIASVPGSTNTGTVPG
CCCCCCCCCCCCCCC
42.5930266825
284PhosphorylationSVPGSTNTGTVPGSE
CCCCCCCCCCCCCCC
34.0330266825
286PhosphorylationPGSTNTGTVPGSEKD
CCCCCCCCCCCCCCC
22.8423927012
290PhosphorylationNTGTVPGSEKDSDSM
CCCCCCCCCCCCCCC
35.0930278072
292AcetylationGTVPGSEKDSDSMET
CCCCCCCCCCCCCCC
65.3223236377
292UbiquitinationGTVPGSEKDSDSMET
CCCCCCCCCCCCCCC
65.3221906983
292 (in isoform 1)Ubiquitination-65.3221890473
292 (in isoform 2)Ubiquitination-65.3221890473
294PhosphorylationVPGSEKDSDSMETEE
CCCCCCCCCCCCCCC
42.5329255136
296PhosphorylationGSEKDSDSMETEEKT
CCCCCCCCCCCCCHH
23.5929255136
297SulfoxidationSEKDSDSMETEEKTS
CCCCCCCCCCCCHHH
9.9130846556
299PhosphorylationKDSDSMETEEKTSSA
CCCCCCCCCCHHHHH
40.5829255136
302UbiquitinationDSMETEEKTSSAFVG
CCCCCCCHHHHHCCC
47.6927667366
302 (in isoform 1)Ubiquitination-47.6921890473
302 (in isoform 2)Ubiquitination-47.6921890473
303PhosphorylationSMETEEKTSSAFVGK
CCCCCCHHHHHCCCC
31.0630266825
304PhosphorylationMETEEKTSSAFVGKT
CCCCCHHHHHCCCCC
30.6430266825
305PhosphorylationETEEKTSSAFVGKTP
CCCCHHHHHCCCCCC
30.8430266825
310AcetylationTSSAFVGKTPEASPE
HHHHCCCCCCCCCCC
56.4519608861
310MalonylationTSSAFVGKTPEASPE
HHHHCCCCCCCCCCC
56.4526320211
310SumoylationTSSAFVGKTPEASPE
HHHHCCCCCCCCCCC
56.4519608861
310UbiquitinationTSSAFVGKTPEASPE
HHHHCCCCCCCCCCC
56.4527667366
310 (in isoform 1)Ubiquitination-56.4521890473
310 (in isoform 2)Ubiquitination-56.4521890473
311PhosphorylationSSAFVGKTPEASPEP
HHHCCCCCCCCCCCC
22.0419664994
315PhosphorylationVGKTPEASPEPKDQT
CCCCCCCCCCCCHHH
28.3019664994
319UbiquitinationPEASPEPKDQTLKMI
CCCCCCCCHHHHHHH
61.8921906983
319 (in isoform 1)Ubiquitination-61.8921890473
319 (in isoform 2)Ubiquitination-61.8921890473
322PhosphorylationSPEPKDQTLKMIKIL
CCCCCHHHHHHHHHH
38.1823403867
324UbiquitinationEPKDQTLKMIKILSG
CCCHHHHHHHHHHCC
41.8021906983
324 (in isoform 1)Ubiquitination-41.8021890473
324 (in isoform 2)Ubiquitination-41.8021890473
327UbiquitinationDQTLKMIKILSGEMA
HHHHHHHHHHCCHHH
33.8122817900
348PhosphorylationFLIRNNNTDLMILKN
HHHHCCCCCEEEEEC
32.41-
351SulfoxidationRNNNTDLMILKNTKD
HCCCCCEEEEECHHH
3.6221406390
354AcetylationNTDLMILKNTKDAVR
CCCEEEEECHHHHHH
52.2027452117
354UbiquitinationNTDLMILKNTKDAVR
CCCEEEEECHHHHHH
52.2021906983
354 (in isoform 1)Ubiquitination-52.2021890473
354 (in isoform 2)Ubiquitination-52.2021890473
357UbiquitinationLMILKNTKDAVRNSV
EEEEECHHHHHHHCH
53.7522817900
363PhosphorylationTKDAVRNSVCHTATV
HHHHHHHCHHHHHHH
18.6328348404
367PhosphorylationVRNSVCHTATVIANS
HHHCHHHHHHHHHHC
20.9227251275
401AcetylationARATNWAKFTATASL
HHHCCHHHHHHEEEE
34.567467763
407PhosphorylationAKFTATASLGVIHKG
HHHHHEEEEEEEECC
22.6920068231
413AcetylationASLGVIHKGHEKEAL
EEEEEEECCCHHHHH
51.337467775
413UbiquitinationASLGVIHKGHEKEAL
EEEEEEECCCHHHHH
51.3316196087
417AcetylationVIHKGHEKEALQLMA
EEECCCHHHHHHHHH
42.487467787
417UbiquitinationVIHKGHEKEALQLMA
EEECCCHHHHHHHHH
42.4829967540
425PhosphorylationEALQLMATYLPKDTS
HHHHHHHHHCCCCCC
16.1828851738
426PhosphorylationALQLMATYLPKDTSP
HHHHHHHHCCCCCCC
16.0928851738
429UbiquitinationLMATYLPKDTSPGSA
HHHHHCCCCCCCCCC
71.6716196087
488PhosphorylationLGLAAMGTARQDVYD
HHHHHHHHHHHHHHH
12.9422817900
494PhosphorylationGTARQDVYDLLKTNL
HHHHHHHHHHHHCCC
14.79-
498UbiquitinationQDVYDLLKTNLYQDD
HHHHHHHHCCCCCCC
42.5416196087
524UbiquitinationGLVMLGSKNAQAIED
HHHHHCCCCHHHHHH
55.2816196087
5432-HydroxyisobutyrylationAQETQHEKILRGLAV
HHHHHHHHHHHHHHH
44.94-
543AcetylationAQETQHEKILRGLAV
HHHHHHHHHHHHHHH
44.9425953088
543UbiquitinationAQETQHEKILRGLAV
HHHHHHHHHHHHHHH
44.9421906983
543 (in isoform 1)Ubiquitination-44.9421890473
543 (in isoform 2)Ubiquitination-44.9421890473
560SulfoxidationALVMYGRMEEADALI
HHHHHCCHHHHHHHH
4.7921406390
571GlutathionylationDALIESLCRDKDPIL
HHHHHHHCCCCCHHH
8.0222555962
5742-HydroxyisobutyrylationIESLCRDKDPILRRS
HHHHCCCCCHHHHHC
46.16-
574AcetylationIESLCRDKDPILRRS
HHHHCCCCCHHHHHC
46.1625953088
574UbiquitinationIESLCRDKDPILRRS
HHHHCCCCCHHHHHC
46.1624816145
597UbiquitinationYCGSGNNKAIRRLLH
ECCCCCHHHHHHHHH
49.5521963094
608PhosphorylationRLLHVAVSDVNDDVR
HHHHHHHHCCCHHHH
26.55-
633GlutathionylationLFRTPEQCPSVVSLL
EECCHHHCCCHHHHH
2.3022555962
633S-palmitoylationLFRTPEQCPSVVSLL
EECCHHHCCCHHHHH
2.3029575903
641PhosphorylationPSVVSLLSESYNPHV
CCHHHHHCCCCCCCC
29.7728152594
643PhosphorylationVVSLLSESYNPHVRY
HHHHHCCCCCCCCCH
27.1728152594
644PhosphorylationVSLLSESYNPHVRYG
HHHHCCCCCCCCCHH
28.7628152594
666UbiquitinationCCAGTGNKEAINLLE
HCCCCCCHHHHHHHH
50.2816196087
675SulfoxidationAINLLEPMTNDPVNY
HHHHHHCCCCCCCHH
3.9030846556
713PhosphorylationVNQFRQLYSKVINDK
HHHHHHHHHHHHCCC
9.7122461510
715UbiquitinationQFRQLYSKVINDKHD
HHHHHHHHHHCCCHH
33.3132015554
720AcetylationYSKVINDKHDDVMAK
HHHHHCCCHHHHHHH
44.4325825284
720UbiquitinationYSKVINDKHDDVMAK
HHHHHCCCHHHHHHH
44.4321906983
720 (in isoform 1)Ubiquitination-44.4321890473
720 (in isoform 2)Ubiquitination-44.4321890473
725SulfoxidationNDKHDDVMAKFGAIL
CCCHHHHHHHHHHHH
4.2830846556
727UbiquitinationKHDDVMAKFGAILAQ
CHHHHHHHHHHHHHC
26.6616196087
796UbiquitinationIGLNKDLKMPKVQYK
EECCCCCCCCCCCCC
64.3927667366
799UbiquitinationNKDLKMPKVQYKSNC
CCCCCCCCCCCCCCC
38.1729967540
803AcetylationKMPKVQYKSNCKPST
CCCCCCCCCCCCCCC
20.3625953088
803UbiquitinationKMPKVQYKSNCKPST
CCCCCCCCCCCCCCC
20.3633845483
806GlutathionylationKVQYKSNCKPSTFAY
CCCCCCCCCCCCCCC
9.8922555962
806S-palmitoylationKVQYKSNCKPSTFAY
CCCCCCCCCCCCCCC
9.8929575903
807AcetylationVQYKSNCKPSTFAYP
CCCCCCCCCCCCCCC
46.3726051181
807UbiquitinationVQYKSNCKPSTFAYP
CCCCCCCCCCCCCCC
46.3727667366
807 (in isoform 2)Ubiquitination-46.3721890473
809PhosphorylationYKSNCKPSTFAYPAP
CCCCCCCCCCCCCCC
22.9628152594
809UbiquitinationYKSNCKPSTFAYPAP
CCCCCCCCCCCCCCC
22.9622817900
810PhosphorylationKSNCKPSTFAYPAPL
CCCCCCCCCCCCCCC
22.3228152594
810UbiquitinationKSNCKPSTFAYPAPL
CCCCCCCCCCCCCCC
22.3222817900
811UbiquitinationSNCKPSTFAYPAPLE
CCCCCCCCCCCCCCC
7.8122817900
813PhosphorylationCKPSTFAYPAPLEVP
CCCCCCCCCCCCCCC
8.8528152594
813UbiquitinationCKPSTFAYPAPLEVP
CCCCCCCCCCCCCCC
8.8523503661
817UbiquitinationTFAYPAPLEVPKEKE
CCCCCCCCCCCCHHH
12.9222817900
818UbiquitinationFAYPAPLEVPKEKEK
CCCCCCCCCCCHHHH
56.5733845483
821AcetylationPAPLEVPKEKEKEKV
CCCCCCCCHHHHHCC
83.2226051181
821UbiquitinationPAPLEVPKEKEKEKV
CCCCCCCCHHHHHCC
83.2221890473
821 (in isoform 1)Ubiquitination-83.2221890473
822UbiquitinationAPLEVPKEKEKEKVS
CCCCCCCHHHHHCCH
61.4533845483
822 (in isoform 2)Ubiquitination-61.4521890473
823UbiquitinationPLEVPKEKEKEKVST
CCCCCCHHHHHCCHH
79.0022817900
825UbiquitinationEVPKEKEKEKVSTAV
CCCCHHHHHCCHHHH
74.1122817900
8272-HydroxyisobutyrylationPKEKEKEKVSTAVLS
CCHHHHHCCHHHHHH
53.18-
827UbiquitinationPKEKEKEKVSTAVLS
CCHHHHHCCHHHHHH
53.1821906983
827 (in isoform 1)Ubiquitination-53.1821890473
829PhosphorylationEKEKEKVSTAVLSIT
HHHHHCCHHHHHHHH
23.0120068231
830PhosphorylationKEKEKVSTAVLSITA
HHHHCCHHHHHHHHH
24.6325159151
830UbiquitinationKEKEKVSTAVLSITA
HHHHCCHHHHHHHHH
24.6327667366
830 (in isoform 2)Ubiquitination-24.6321890473
831UbiquitinationEKEKVSTAVLSITAK
HHHCCHHHHHHHHHH
7.8622817900
831 (in isoform 2)Ubiquitination-7.8621890473
834PhosphorylationKVSTAVLSITAKAKK
CCHHHHHHHHHHHHH
15.9923879269
834UbiquitinationKVSTAVLSITAKAKK
CCHHHHHHHHHHHHH
15.9922817900
834 (in isoform 2)Ubiquitination-15.9921890473
836PhosphorylationSTAVLSITAKAKKKE
HHHHHHHHHHHHHHH
20.8020068231
836UbiquitinationSTAVLSITAKAKKKE
HHHHHHHHHHHHHHH
20.8022817900
837UbiquitinationTAVLSITAKAKKKEK
HHHHHHHHHHHHHHH
14.2422817900
838AcetylationAVLSITAKAKKKEKE
HHHHHHHHHHHHHHH
52.6825953088
838UbiquitinationAVLSITAKAKKKEKE
HHHHHHHHHHHHHHH
52.6821906983
838 (in isoform 1)Ubiquitination-52.6821890473
838 (in isoform 2)Ubiquitination-52.6821890473
840UbiquitinationLSITAKAKKKEKEKE
HHHHHHHHHHHHHHH
64.7722817900
841UbiquitinationSITAKAKKKEKEKEK
HHHHHHHHHHHHHHH
71.6522817900
842UbiquitinationITAKAKKKEKEKEKK
HHHHHHHHHHHHHHH
73.6222817900
844UbiquitinationAKAKKKEKEKEKKEE
HHHHHHHHHHHHHHH
80.9123503661
848UbiquitinationKKEKEKEKKEEEKME
HHHHHHHHHHHHHHH
76.2522817900
849AcetylationKEKEKEKKEEEKMEV
HHHHHHHHHHHHHHH
72.027851319
849UbiquitinationKEKEKEKKEEEKMEV
HHHHHHHHHHHHHHH
72.0233845483
853UbiquitinationKEKKEEEKMEVDEAE
HHHHHHHHHHHHHHH
43.5721906983
853 (in isoform 1)Ubiquitination-43.5721890473
859UbiquitinationEKMEVDEAEKKEEKE
HHHHHHHHHHHHHHH
29.4623000965
859 (in isoform 2)Ubiquitination-29.4621890473
861UbiquitinationMEVDEAEKKEEKEKK
HHHHHHHHHHHHHHH
72.9621906983
861 (in isoform 1)Ubiquitination-72.9621890473
862UbiquitinationEVDEAEKKEEKEKKK
HHHHHHHHHHHHHHC
63.7121906983
862 (in isoform 1)Ubiquitination-63.7121890473
865UbiquitinationEAEKKEEKEKKKEPE
HHHHHHHHHHHCCCC
75.7622817900
865 (in isoform 1)Ubiquitination-75.7621890473
867UbiquitinationEKKEEKEKKKEPEPN
HHHHHHHHHCCCCCC
79.0022817900
868UbiquitinationKKEEKEKKKEPEPNF
HHHHHHHHCCCCCCC
64.5627667366
869UbiquitinationKEEKEKKKEPEPNFQ
HHHHHHHCCCCCCCC
84.9421906983
869 (in isoform 1)Ubiquitination-84.9421890473
873UbiquitinationEKKKEPEPNFQLLDN
HHHCCCCCCCCCCCC
58.6233845483
884UbiquitinationLLDNPARVMPAQLKV
CCCCHHHCCHHHCEE
6.1433845483
890UbiquitinationRVMPAQLKVLTMPET
HCCHHHCEEECCCCC
24.1023000965
890 (in isoform 1)Ubiquitination-24.1021890473
898GlutathionylationVLTMPETCRYQPFKP
EECCCCCCCCCCCCC
3.4822555962
900PhosphorylationTMPETCRYQPFKPLS
CCCCCCCCCCCCCCE
23.76-
903UbiquitinationETCRYQPFKPLSIGG
CCCCCCCCCCCEEEE
8.2122817900
903 (in isoform 2)Ubiquitination-8.2121890473
904UbiquitinationTCRYQPFKPLSIGGI
CCCCCCCCCCEEEEE
52.2933845483
915UbiquitinationIGGIIILKDTSEDIE
EEEEEEEECCCHHHH
48.8533845483
934SumoylationPVAAHGPKIEEEEQE
HHHHHCCCCCHHCCC
68.30-
934UbiquitinationPVAAHGPKIEEEEQE
HHHHHCCCCCHHCCC
68.3022817900
934 (in isoform 1)Ubiquitination-68.3021890473
950PhosphorylationEPPEPFEYIDD----
CCCCCCCCCCC----
15.2728796482

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
273TPhosphorylationKinaseMAPK14P47811
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSMD1_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 PSMD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS8_HUMANPSMC5physical
11361004
ADRM1_HUMANADRM1physical
16990800
PRS4_HUMANPSMC1physical
19589775
PSMD5_HUMANPSMD5physical
19589775
PRS7_HUMANPSMC2physical
19589775
PSMD6_HUMANPSMD6physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSMD5_HUMANPSMD5physical
22939629
PSME1_HUMANPSME1physical
22939629
PSME2_HUMANPSME2physical
22939629
PSME3_HUMANPSME3physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
TBA4A_HUMANTUBA4Aphysical
22939629
ECD_HUMANECDphysical
22939629
SF3A1_HUMANSF3A1physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
PYR1_HUMANCADphysical
22939629
TBA1B_HUMANTUBA1Bphysical
22939629
RBM12_HUMANRBM12physical
22939629
SC24C_HUMANSEC24Cphysical
22939629
TPM4_HUMANTPM4physical
22939629
TBA1A_HUMANTUBA1Aphysical
22939629
ADRM1_HUMANADRM1physical
22863883
LIPA1_HUMANPPFIA1physical
22863883
PRS4_HUMANPSMC1physical
22863883
PRS7_HUMANPSMC2physical
22863883
PRS6B_HUMANPSMC4physical
22863883
PRS8_HUMANPSMC5physical
22863883
PRS10_HUMANPSMC6physical
22863883
PSD11_HUMANPSMD11physical
22863883
PSMD3_HUMANPSMD3physical
22863883
PSMD4_HUMANPSMD4physical
22863883
PSMD6_HUMANPSMD6physical
22863883
PSMD7_HUMANPSMD7physical
22863883
RS15A_HUMANRPS15Aphysical
22863883
RS28_HUMANRPS28physical
22863883
RS8_HUMANRPS8physical
22863883
UBC_HUMANUBCphysical
24743594
ADRM1_MOUSEAdrm1physical
25666615
ADRM1_HUMANADRM1physical
26344197
PSA1_HUMANPSMA1physical
26344197
PSA2_HUMANPSMA2physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSA5_HUMANPSMA5physical
26344197
PSA7_HUMANPSMA7physical
26344197
PSA7L_HUMANPSMA8physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB4_HUMANPSMB4physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB6_HUMANPSMB6physical
26344197
PSB7_HUMANPSMB7physical
26344197
PSB8_HUMANPSMB8physical
26344197
PRS4_HUMANPSMC1physical
26344197
PRS7_HUMANPSMC2physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS6B_HUMANPSMC4physical
26344197
PRS8_HUMANPSMC5physical
26344197
PRS10_HUMANPSMC6physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD12_HUMANPSMD12physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD3_HUMANPSMD3physical
26344197
PSMD6_HUMANPSMD6physical
26344197
PSMD7_HUMANPSMD7physical
26344197
PSMD9_HUMANPSMD9physical
26344197
RD23A_HUMANRAD23Aphysical
26344197
RD23B_HUMANRAD23Bphysical
26344197
ADRM1_HUMANADRM1physical
26466095

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
DB00188Bortezomib
Regulatory Network of PSMD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-273; THR-311 AND SER-315, 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 THR-311 AND SER-315,ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
"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-310, 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 THR-311 AND SER-315, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-273; THR-311 AND SER-315, 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 THR-273; SER-296; THR-311AND SER-315, AND MASS SPECTROMETRY.
"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 THR-311 AND SER-315,ACETYLATION AT MET-1, 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 THR-311 AND SER-315, ANDMASS SPECTROMETRY.
"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 THR-273; THR-311 ANDSER-315, AND MASS SPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49, AND MASSSPECTROMETRY.

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