PSMD1_MOUSE - dbPTM
PSMD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSMD1_MOUSE
UniProt AC Q3TXS7
Protein Name 26S proteasome non-ATPase regulatory subunit 1
Gene Name Psmd1
Organism Mus musculus (Mouse).
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 MITSAAGIISLLDEEEPQLKEFALHKLNAVVNDFWAEISESVDKIEVLYEDEGFRSRQFAALVASKVFYHLGAFEESLNYALGAGDLFNVNDNSEYVETIIAKCIDHYTKQCVENADLPEGEKKPIDQRLEGIVNKMFQRCLDDHKYKQAIGIALETRRLDVFEKTILESNDVPGMLAYSLKLCMSLMQNKQFRNKVLRVLVKIYMNLEKPDFINVCQCLIFLDDPQAVSDILEKLVKEDNLLMAYQICFDLYESASQQFLSSVIQNLRTVGTPIASVPGSTNTGTVPGSEKDSDPMETEEKTASAVAGKTPDASPEPKDQTLKMIKILSGEMAIELHLQFLIRNNNTDLMILKNTKDAVRNSVCHTATVIANSFMHCGTTSDQFLRDNLEWLARATNWAKFTATASLGVIHKGHEKEALQLMATYLPKDTSPGSAYQEGGGLYALGLIHANHGGDIIDYLLNQLKNASNDIVRHGGSLGLGLAAMGTARQDVYDLLKTNLYQDDAVTGEAAGLALGLVMLGSKNAQAIEDMVGYAQETQHEKILRGLAVGIALVMYGRMEEADALIESLCRDKDPILRRSGMYTVAMAYCGSGNNKAIRRLLHVAVSDVNDDVRRAAVESLGFILFRTPEQCPSVVSLLSESYNPHVRYGAAMALGICCAGTGNKEAINLLEPMTNDPVNYVRQGALIASALIMIQQTEITCPKVNQFRQLYSKVINDKHDDVMAKFGAILAQGILDAGGHNVTISLQSRTGHTHMPSVVGVLVFTQFWFWFPLSHFLSLAYTPTCVIGLNKDLKMPKVQYKSNCKPSTFAYPAPLEVPKEKEKEKVSTAVLSITAKAKKKEKEKEKKEEEKMEVDEAEKKEEKEKKKEPEPNFQLLDNPARVMPAQLKVLSMTETCRYQPFKPLSIGGIIILKDTSEDVEELVEPVAAHGPKIEEEEQEPEPPEPFEYIDD
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		7.32-
136AcetylationRLEGIVNKMFQRCLD
HHHHHHHHHHHHHHC		30.1423954790
136UbiquitinationRLEGIVNKMFQRCLD
HHHHHHHHHHHHHHC		30.1422790023
184S-palmitoylationLAYSLKLCMSLMQNK
HHHHHHHHHHHHCCH		1.3428526873
270PhosphorylationSVIQNLRTVGTPIAS
HHHHHHHCCCCCCCC		26.8425521595
273PhosphorylationQNLRTVGTPIASVPG
HHHHCCCCCCCCCCC		13.7425521595
277PhosphorylationTVGTPIASVPGSTNT
CCCCCCCCCCCCCCC		29.5724925903
281PhosphorylationPIASVPGSTNTGTVP
CCCCCCCCCCCCCCC		16.6525619855
282PhosphorylationIASVPGSTNTGTVPG
CCCCCCCCCCCCCCC		42.5925619855
284PhosphorylationSVPGSTNTGTVPGSE
CCCCCCCCCCCCCCC		34.0325619855
286PhosphorylationPGSTNTGTVPGSEKD
CCCCCCCCCCCCCCC		22.8425619855
290PhosphorylationNTGTVPGSEKDSDPM
CCCCCCCCCCCCCCC		35.0925619855
292UbiquitinationGTVPGSEKDSDPMET
CCCCCCCCCCCCCCC		65.32-
294PhosphorylationVPGSEKDSDPMETEE
CCCCCCCCCCCCCHH		55.4725619855
299PhosphorylationKDSDPMETEEKTASA
CCCCCCCCHHHHHHH		43.1025619855
302UbiquitinationDPMETEEKTASAVAG
CCCCCHHHHHHHHCC		43.0622790023
303PhosphorylationPMETEEKTASAVAGK
CCCCHHHHHHHHCCC		29.1725619855
305PhosphorylationETEEKTASAVAGKTP
CCHHHHHHHHCCCCC		28.6224925903
310MalonylationTASAVAGKTPDASPE
HHHHHCCCCCCCCCC		47.3426320211
310UbiquitinationTASAVAGKTPDASPE
HHHHHCCCCCCCCCC		47.3427667366
310AcetylationTASAVAGKTPDASPE
HHHHHCCCCCCCCCC		47.3423806337
311PhosphorylationASAVAGKTPDASPEP
HHHHCCCCCCCCCCC		26.0324925903
315PhosphorylationAGKTPDASPEPKDQT
CCCCCCCCCCCCHHH		36.8624925903
319UbiquitinationPDASPEPKDQTLKMI
CCCCCCCCHHHHHHH		61.8927667366
322PhosphorylationSPEPKDQTLKMIKIL
CCCCCHHHHHHHHHH		38.1828609623
354UbiquitinationNTDLMILKNTKDAVR
CCCEEEEECHHHHHH		52.2022790023
354AcetylationNTDLMILKNTKDAVR
CCCEEEEECHHHHHH		52.2022826441
367PhosphorylationVRNSVCHTATVIANS
HHHCHHHHHHHHHHC		20.9222802335
494PhosphorylationGTARQDVYDLLKTNL
HHHHHHHHHHHHCCC		14.79-
498UbiquitinationQDVYDLLKTNLYQDD
HHHHHHHHCCCCCCC		42.54-
571S-palmitoylationDALIESLCRDKDPIL
HHHHHHHCCCCCHHH		8.0228526873
574UbiquitinationIESLCRDKDPILRRS
HHHHCCCCCHHHHHC		46.1622790023
584PhosphorylationILRRSGMYTVAMAYC
HHHHCCCEEEEEEEC		11.11-
585PhosphorylationLRRSGMYTVAMAYCG
HHHCCCEEEEEEECC		7.90-
633S-palmitoylationLFRTPEQCPSVVSLL
EECCHHHCCCHHHHH		2.3028526873
633GlutathionylationLFRTPEQCPSVVSLL
EECCHHHCCCHHHHH		2.3024333276
676PhosphorylationINLLEPMTNDPVNYV
HHHHHCCCCCCCHHH		47.3823140645
682PhosphorylationMTNDPVNYVRQGALI
CCCCCCHHHHHHHHH		9.3923140645
691PhosphorylationRQGALIASALIMIQQ
HHHHHHHHHHHHHHC		19.3323140645
699PhosphorylationALIMIQQTEITCPKV
HHHHHHCCCCCCCCH		16.9923140645
702PhosphorylationMIQQTEITCPKVNQF
HHHCCCCCCCCHHHH		19.2723140645
720AcetylationYSKVINDKHDDVMAK
HHHHHCCCHHHHHHH		44.4323806337
720UbiquitinationYSKVINDKHDDVMAK
HHHHHCCCHHHHHHH		44.4327667366
720MalonylationYSKVINDKHDDVMAK
HHHHHCCCHHHHHHH		44.4326320211
750PhosphorylationNVTISLQSRTGHTHM
EEEEEEECCCCCCCC		36.7824759943
803UbiquitinationKMPKVQYKSNCKPST
CCCCCCCCCCCCCCC		20.3622790023
806GlutathionylationKVQYKSNCKPSTFAY
CCCCCCCCCCCCCCC		9.8924333276
807UbiquitinationVQYKSNCKPSTFAYP
CCCCCCCCCCCCCCC		46.3722790023
821UbiquitinationPAPLEVPKEKEKEKV
CCCCCCCCHHHHHCC		83.2222790023
830PhosphorylationKEKEKVSTAVLSITA
HHHHCCHHHHHHHHH		24.6322942356
834PhosphorylationKVSTAVLSITAKAKK
CCHHHHHHHHHHHHH		15.9928066266
836PhosphorylationSTAVLSITAKAKKKE
HHHHHHHHHHHHHHH		20.8028066266
838UbiquitinationAVLSITAKAKKKEKE
HHHHHHHHHHHHHHH		52.6822790023
861UbiquitinationMEVDEAEKKEEKEKK
HHHHHHHHHHHHHHH		72.9627667366
868UbiquitinationKKEEKEKKKEPEPNF
HHHHHHHHCCCCCCC		64.5627667366
890UbiquitinationRVMPAQLKVLSMTET
HHCHHHHEEECCCCC		29.1122790023
897PhosphorylationKVLSMTETCRYQPFK
EEECCCCCCCCCCCC		7.9726643407
898GlutathionylationVLSMTETCRYQPFKP
EECCCCCCCCCCCCC		2.8824333276
898S-nitrosocysteineVLSMTETCRYQPFKP
EECCCCCCCCCCCCC		2.88-
898S-nitrosylationVLSMTETCRYQPFKP
EECCCCCCCCCCCCC		2.8821278135
900PhosphorylationSMTETCRYQPFKPLS
CCCCCCCCCCCCCCE		23.7626643407
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 PSMD1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSMD1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PSMD1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSMD1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, ANDMASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273, AND MASSSPECTROMETRY.

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