PSMG1_HUMAN - dbPTM
PSMG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSMG1_HUMAN
UniProt AC O95456
Protein Name Proteasome assembly chaperone 1
Gene Name PSMG1
Organism Homo sapiens (Human).
Sequence Length 288
Subcellular Localization Cytoplasm. Endoplasmic reticulum.
Protein Description Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization..
Protein Sequence MAATFFGEVVKAPCRAGTEDEEEEEEGRRETPEDREVRLQLARKREVRLLRRQTKTSLEVSLLEKYPCSKFIIAIGNNAVAFLSSFVMNSGVWEEVGCAKLWNEWCRTTDTTHLSSTEAFCVFYHLKSNPSVFLCQCSCYVAEDQQYQWLEKVFGSCPRKNMQITILTCRHVTDYKTSESTGSLPSPFLRALKTQNFKDSACCPLLEQPNIVHDLPAAVLSYCQVWKIPAILYLCYTDVMKLDLITVEAFKPILSTRSLKGLVKNIPQSTEILKKLMTTNEIQSNIYT
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------MAATFFGEV
------CCCCCCCCC		18.4022223895
4Phosphorylation----MAATFFGEVVK
----CCCCCCCCCCC		15.2320068231
11UbiquitinationTFFGEVVKAPCRAGT
CCCCCCCCCCCCCCC		52.3524816145
11AcetylationTFFGEVVKAPCRAGT
CCCCCCCCCCCCCCC		52.3527452117
15MethylationEVVKAPCRAGTEDEE
CCCCCCCCCCCCCHH		34.69-
18PhosphorylationKAPCRAGTEDEEEEE
CCCCCCCCCCHHHHH		39.0023401153
31PhosphorylationEEEGRRETPEDREVR
HHHHCCCCHHHHHHH		30.1125159151
35MethylationRRETPEDREVRLQLA
CCCCHHHHHHHHHHH		42.52-
54PhosphorylationVRLLRRQTKTSLEVS
HHHHHHHCCCCCHHH		34.1823911959
55UbiquitinationRLLRRQTKTSLEVSL
HHHHHHCCCCCHHHH		27.9829967540
56PhosphorylationLLRRQTKTSLEVSLL
HHHHHCCCCCHHHHH		41.7629978859
57PhosphorylationLRRQTKTSLEVSLLE
HHHHCCCCCHHHHHH		24.8826074081
61PhosphorylationTKTSLEVSLLEKYPC
CCCCCHHHHHHHCCC		20.1924719451
65AcetylationLEVSLLEKYPCSKFI
CHHHHHHHCCCCCEE		55.2325038526
65UbiquitinationLEVSLLEKYPCSKFI
CHHHHHHHCCCCCEE		55.2332015554
68UbiquitinationSLLEKYPCSKFIIAI
HHHHHCCCCCEEEEE		6.6621963094
85UbiquitinationNAVAFLSSFVMNSGV
CHHHHHHHHHHCCCC		24.8122817900
89UbiquitinationFLSSFVMNSGVWEEV
HHHHHHHCCCCHHCH		30.2521963094
90UbiquitinationLSSFVMNSGVWEEVG
HHHHHHCCCCHHCHH		19.3421963094
106UbiquitinationAKLWNEWCRTTDTTH
HHHHHHHHCCCCCCC		1.9522817900
111UbiquitinationEWCRTTDTTHLSSTE
HHHCCCCCCCCCCCC		17.6421963094
135 (in isoform 2)Phosphorylation-2.32-
143UbiquitinationQCSCYVAEDQQYQWL
EEEEEEECHHHHHHH		46.4321890473
152UbiquitinationQQYQWLEKVFGSCPR
HHHHHHHHHHCCCCC		40.4723000965
155UbiquitinationQWLEKVFGSCPRKNM
HHHHHHHCCCCCCCC		31.1821963094
155 (in isoform 2)Ubiquitination-31.1821890473
156UbiquitinationWLEKVFGSCPRKNMQ
HHHHHHCCCCCCCCE		14.9621890473
160UbiquitinationVFGSCPRKNMQITIL
HHCCCCCCCCEEEEE		41.75-
164UbiquitinationCPRKNMQITILTCRH
CCCCCCEEEEEEEEE		1.4721890473
166UbiquitinationRKNMQITILTCRHVT
CCCCEEEEEEEEEEC		2.9922817900
167UbiquitinationKNMQITILTCRHVTD
CCCEEEEEEEEEECC		2.5021963094
171UbiquitinationITILTCRHVTDYKTS
EEEEEEEEECCCCCC		29.0421963094
172UbiquitinationTILTCRHVTDYKTSE
EEEEEEEECCCCCCC		1.9422817900
172 (in isoform 2)Ubiquitination-1.9421890473
173UbiquitinationILTCRHVTDYKTSES
EEEEEEECCCCCCCC		27.7323000965
176 (in isoform 1)Ubiquitination-48.6721890473
176UbiquitinationCRHVTDYKTSESTGS
EEEECCCCCCCCCCC		48.6721906983
177UbiquitinationRHVTDYKTSESTGSL
EEECCCCCCCCCCCC		31.3423000965
177PhosphorylationRHVTDYKTSESTGSL
EEECCCCCCCCCCCC		31.3423312004
178PhosphorylationHVTDYKTSESTGSLP
EECCCCCCCCCCCCC		25.9523312004
180PhosphorylationTDYKTSESTGSLPSP
CCCCCCCCCCCCCHH		37.5223917254
181PhosphorylationDYKTSESTGSLPSPF
CCCCCCCCCCCCHHH		27.0923917254
183PhosphorylationKTSESTGSLPSPFLR
CCCCCCCCCCHHHHH		36.8828985074
186PhosphorylationESTGSLPSPFLRALK
CCCCCCCHHHHHHHH		33.3123186163
187UbiquitinationSTGSLPSPFLRALKT
CCCCCCHHHHHHHHH		30.2827667366
188UbiquitinationTGSLPSPFLRALKTQ
CCCCCHHHHHHHHHC		9.4021963094
193UbiquitinationSPFLRALKTQNFKDS
HHHHHHHHHCCCCCC		47.2621906983
193 (in isoform 1)Ubiquitination-47.2621890473
193MethylationSPFLRALKTQNFKDS
HHHHHHHHHCCCCCC		47.26-
198UbiquitinationALKTQNFKDSACCPL
HHHHCCCCCCCCCHH		59.3221963094
230UbiquitinationCQVWKIPAILYLCYT
HHHHCCCHHHHHHHC		14.1121890473
230 (in isoform 2)Ubiquitination-14.1121890473
239UbiquitinationLYLCYTDVMKLDLIT
HHHHHCCCHHCCEEE		2.5523000965
243UbiquitinationYTDVMKLDLITVEAF
HCCCHHCCEEEHHHH		30.4323000965
243AcetylationYTDVMKLDLITVEAF
HCCCHHCCEEEHHHH		30.4319608861
243 (in isoform 2)Ubiquitination-30.4321890473
246UbiquitinationVMKLDLITVEAFKPI
CHHCCEEEHHHHHHH		21.4221890473
251UbiquitinationLITVEAFKPILSTRS
EEEHHHHHHHHCCCC		37.8921963094
251AcetylationLITVEAFKPILSTRS
EEEHHHHHHHHCCCC		37.8923954790
251 (in isoform 1)Ubiquitination-37.8921890473
253UbiquitinationTVEAFKPILSTRSLK
EHHHHHHHHCCCCHH		4.9727667366
254UbiquitinationVEAFKPILSTRSLKG
HHHHHHHHCCCCHHH		6.0821963094
254 (in isoform 2)Ubiquitination-6.0821890473
255PhosphorylationEAFKPILSTRSLKGL
HHHHHHHCCCCHHHH		23.6124719451
255UbiquitinationEAFKPILSTRSLKGL
HHHHHHHCCCCHHHH		23.6123000965
256O-linked_GlycosylationAFKPILSTRSLKGLV
HHHHHHCCCCHHHHH		22.3430059200
259UbiquitinationPILSTRSLKGLVKNI
HHHCCCCHHHHHHCC		4.6123000965
260AcetylationILSTRSLKGLVKNIP
HHCCCCHHHHHHCCC		51.9825953088
260UbiquitinationILSTRSLKGLVKNIP
HHCCCCHHHHHHCCC		51.9823000965
264MalonylationRSLKGLVKNIPQSTE
CCHHHHHHCCCCHHH		54.9526320211
264AcetylationRSLKGLVKNIPQSTE
CCHHHHHHCCCCHHH		54.9519608861
264UbiquitinationRSLKGLVKNIPQSTE
CCHHHHHHCCCCHHH		54.9523000965
264 (in isoform 1)Ubiquitination-54.9521890473
269UbiquitinationLVKNIPQSTEILKKL
HHHCCCCHHHHHHHH		23.7427667366
270UbiquitinationVKNIPQSTEILKKLM
HHCCCCHHHHHHHHH		23.0721963094
274UbiquitinationPQSTEILKKLMTTNE
CCHHHHHHHHHCHHH		49.9027667366
275UbiquitinationQSTEILKKLMTTNEI
CHHHHHHHHHCHHHH		39.7921963094
275 (in isoform 1)Ubiquitination-39.7921890473
287PhosphorylationNEIQSNIYT------
HHHHHHCCC------		15.6227642862
288PhosphorylationEIQSNIYT-------
HHHHHCCC-------		28.4729978859
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 PSMG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSMG1_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 PSMG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPARD_HUMANPPARDphysical
18793612
PSMG2_HUMANPSMG2physical
22939629
APEX1_HUMANAPEX1physical
22863883
CAZA1_HUMANCAPZA1physical
22863883
CAZA2_HUMANCAPZA2physical
22863883
EHD4_HUMANEHD4physical
22863883
NOL3_HUMANNOL3physical
22863883
SC23A_HUMANSEC23Aphysical
22863883
PSMG3_HUMANPSMG3physical
17189198
PSMG1_HUMANPSMG1physical
17189198
PSMG2_HUMANPSMG2physical
17189198
PSA7_HUMANPSMA7physical
17189198
PSA6_HUMANPSMA6physical
17189198
PSA5_HUMANPSMA5physical
17189198
PSA2_HUMANPSMA2physical
17189198
POMP_HUMANPOMPphysical
17189198
PSMG2_HUMANPSMG2physical
26109405
RHDF1_HUMANRHBDF1physical
26109405
POMP_HUMANPOMPphysical
27173435
CE120_HUMANCEP120physical
27173435
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSMG1_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 ALA-2, 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-264, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-56 AND SER-57, AND MASSSPECTROMETRY.

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