PSME4_HUMAN - dbPTM
PSME4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSME4_HUMAN
UniProt AC Q14997
Protein Name Proteasome activator complex subunit 4
Gene Name PSME4
Organism Homo sapiens (Human).
Sequence Length 1843
Subcellular Localization Cytoplasm, cytosol. Nucleus . Nucleus speckle. Found in nuclear foci following treatment with ionizing radiation, but not with ultraviolet irradiation or H(2)O(2).
Protein Description Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradation of histones following DNA double-strand breaks..
Protein Sequence MEPAERAGVGEPPEPGGRPEPGPRGFVPQKEIVYNKLLPYAERLDAESDLQLAQIKCNLGRAVQLQELWPGGLFWTRKLSTYIRLYGRKFSKEDHVLFIKLLYELVSIPKLEISMMQGFARLLINLLKKKELLSRADLELPWRPLYDMVERILYSKTEHLGLNWFPNSVENILKTLVKSCRPYFPADATAEMLEEWRPLMCPFDVTMQKAITYFEIFLPTSLPPELHHKGFKLWFDELIGLWVSVQNLPQWEGQLVNLFARLATDNIGYIDWDPYVPKIFTRILRSLNLPVGSSQVLVPRFLTNAYDIGHAVIWITAMMGGPSKLVQKHLAGLFNSITSFYHPSNNGRWLNKLMKLLQRLPNSVVRRLHRERYKKPSWLTPVPDSHKLTDQDVTDFVQCIIQPVLLAMFSKTGSLEAAQALQNLALMRPELVIPPVLERTYPALETLTEPHQLTATLSCVIGVARSLVSGGRWFPEGPTHMLPLLMRALPGVDPNDFSKCMITFQFIATFSTLVPLVDCSSVLQERNDLTEVERELCSATAEFEDFVLQFMDRCFGLIESSTLEQTREETETEKMTHLESLVELGLSSTFSTILTQCSKEIFMVALQKVFNFSTSHIFETRVAGRMVADMCRAAVKCCPEESLKLFVPHCCSVITQLTMNDDVLNDEELDKELLWNLQLLSEITRVDGRKLLLYREQLVKILQRTLHLTCKQGYTLSCNLLHHLLRSTTLIYPTEYCSVPGGFDKPPSEYFPIKDWGKPGDLWNLGIQWHVPSSEEVSFAFYLLDSFLQPELVKLQHCGDGKLEMSRDDILQSLTIVHNCLIGSGNLLPPLKGEPVTNLVPSMVSLEETKLYTGLEYDLSRENHREVIATVIRKLLNHILDNSEDDTKSLFLIIKIIGDLLQFQGSHKHEFDSRWKSFNLVKKSMENRLHGKKQHIRALLIDRVMLQHELRTLTVEGCEYKKIHQDMIRDLLRLSTSSYSQVRNKAQQTFFAALGAYNFCCRDIIPLVLEFLRPDRQGVTQQQFKGALYCLLGNHSGVCLANLHDWDCIVQTWPAIVSSGLSQAMSLEKPSIVRLFDDLAEKIHRQYETIGLDFTIPKSCVEIAELLQQSKNPSINQILLSPEKIKEGIKRQQEKNADALRNYENLVDTLLDGVEQRNLPWKFEHIGIGLLSLLLRDDRVLPLRAIRFFVENLNHDAIVVRKMAISAVAGILKQLKRTHKKLTINPCEISGCPKPTQIIAGDRPDNHWLHYDSKTIPRTKKEWESSCFVEKTHWGYYTWPKNMVVYAGVEEQPKLGRSREDMTEAEQIIFDHFSDPKFVEQLITFLSLEDRKGKDKFNPRRFCLFKGIFRNFDDAFLPVLKPHLEHLVADSHESTQRCVAEIIAGLIRGSKHWTFEKVEKLWELLCPLLRTALSNITVETYNDWGACIATSCESRDPRKLHWLFELLLESPLSGEGGSFVDACRLYVLQGGLAQQEWRVPELLHRLLKYLEPKLTQVYKNVRERIGSVLTYIFMIDVSLPNTTPTISPHVPEFTARILEKLKPLMDVDEEIQNHVMEENGIGEEDERTQGIKLLKTILKWLMASAGRSFSTAVTEQLQLLPLFFKIAPVENDNSYDELKRDAKLCLSLMSQGLLYPHQVPLVLQVLKQTARSSSWHARYTVLTYLQTMVFYNLFIFLNNEDAVKDIRWLVISLLEDEQLEVREMAATTLSGLLQCNFLTMDSPMQIHFEQLCKTKLPKKRKRDPGSVGDTIPSAELVKRHAGVLGLGACVLSSPYDVPTWMPQLLMNLSAHLNDPQPIEMTVKKTLSNFRRTHHDNWQEHKQQFTDDQLLVLTDLLVSPCYYA
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
30AcetylationPRGFVPQKEIVYNKL
CCCCCCHHHHHHHHH		43.2523236377
36UbiquitinationQKEIVYNKLLPYAER
HHHHHHHHHHHHHHH		33.4429967540
48PhosphorylationAERLDAESDLQLAQI
HHHCCCCCCHHHHHH		45.3925693802
56UbiquitinationDLQLAQIKCNLGRAV
CHHHHHHHCCCCCCC		12.6521963094
60 (in isoform 3)Ubiquitination-11.0821890473
74UbiquitinationELWPGGLFWTRKLST
HHCCCCCHHHHHHHH		7.6721890473
80UbiquitinationLFWTRKLSTYIRLYG
CHHHHHHHHHHHHHC		23.3823000965
81PhosphorylationFWTRKLSTYIRLYGR
HHHHHHHHHHHHHCC		33.14-
82PhosphorylationWTRKLSTYIRLYGRK
HHHHHHHHHHHHCCC		4.8121394647
130 (in isoform 4)Ubiquitination-52.5921906983
134PhosphorylationLKKKELLSRADLELP
HHHHHHHCCCCCCCC		37.7424719451
155PhosphorylationMVERILYSKTEHLGL
HHHHHHHCCCCCCCC		29.6529759185
164 (in isoform 2)Ubiquitination-18.3421890473
213PhosphorylationTMQKAITYFEIFLPT
CHHHHCCEEEEECCC		7.97-
278UbiquitinationDWDPYVPKIFTRILR
CCCCHHHHHHHHHHH		40.1722817900
278 (in isoform 1)Ubiquitination-40.1721890473
293PhosphorylationSLNLPVGSSQVLVPR
HCCCCCCCCCCHHHH		20.1725693802
294PhosphorylationLNLPVGSSQVLVPRF
CCCCCCCCCCHHHHH		20.5525693802
300UbiquitinationSSQVLVPRFLTNAYD
CCCCHHHHHHCCCHH		31.5622817900
336PhosphorylationHLAGLFNSITSFYHP
HHHHHHHHHHHCCCC		21.65-
338PhosphorylationAGLFNSITSFYHPSN
HHHHHHHHHCCCCCC		16.77-
339PhosphorylationGLFNSITSFYHPSNN
HHHHHHHHCCCCCCC		23.34-
355AcetylationRWLNKLMKLLQRLPN
HHHHHHHHHHHHCCH		57.3825953088
355MalonylationRWLNKLMKLLQRLPN
HHHHHHHHHHHHCCH		57.3826320211
374MalonylationRLHRERYKKPSWLTP
HHHHHHHCCCCCCCC		65.5126320211
494UbiquitinationRALPGVDPNDFSKCM
HHCCCCCCCCHHHHH		39.6224816145
504UbiquitinationFSKCMITFQFIATFS
HHHHHHHHHHHHCHH		3.7521963094
572PhosphorylationQTREETETEKMTHLE
HHHHHHHHHHHHHHH		48.61-
580PhosphorylationEKMTHLESLVELGLS
HHHHHHHHHHHHCCC		44.04-
636AcetylationDMCRAAVKCCPEESL
HHHHHHHHHCCHHHH		25.9525953088
636UbiquitinationDMCRAAVKCCPEESL
HHHHHHHHHCCHHHH		25.9533845483
642PhosphorylationVKCCPEESLKLFVPH
HHHCCHHHHHHHHHH		29.1920068231
714PhosphorylationHLTCKQGYTLSCNLL
CCCCCCCCCHHHHHH		11.3029083192
715PhosphorylationLTCKQGYTLSCNLLH
CCCCCCCCHHHHHHH		21.0129083192
717PhosphorylationCKQGYTLSCNLLHHL
CCCCCCHHHHHHHHH		7.9929083192
763 (in isoform 3)Ubiquitination-11.6221890473
777UbiquitinationHVPSSEEVSFAFYLL
ECCCHHHHHHHHHHH		5.1122817900
781UbiquitinationSEEVSFAFYLLDSFL
HHHHHHHHHHHHHHH		4.0922817900
802 (in isoform 2)Ubiquitination-46.1121890473
883PhosphorylationLNHILDNSEDDTKSL
HHHHHCCCCCCHHHH		41.91-
895UbiquitinationKSLFLIIKIIGDLLQ
HHHHHHHHHHHHHHH		22.6832015554
902 (in isoform 3)Ubiquitination-35.5921890473
906PhosphorylationDLLQFQGSHKHEFDS
HHHHHCCCCCCCCCH		20.6922468782
908UbiquitinationLQFQGSHKHEFDSRW
HHHCCCCCCCCCHHH		46.6729967540
916UbiquitinationHEFDSRWKSFNLVKK
CCCCHHHHHHHHHHH		44.0223000965
916 (in isoform 1)Ubiquitination-44.0221890473
922UbiquitinationWKSFNLVKKSMENRL
HHHHHHHHHHHHHCC		42.1523000965
938UbiquitinationGKKQHIRALLIDRVM
CCHHHHHHHHHHHHH		13.2021890473
944UbiquitinationRALLIDRVMLQHELR
HHHHHHHHHHHHHHH		3.8923000965
952PhosphorylationMLQHELRTLTVEGCE
HHHHHHHHEECCCCC		39.1327251275
954PhosphorylationQHELRTLTVEGCEYK
HHHHHHEECCCCCHH		18.8527251275
961AcetylationTVEGCEYKKIHQDMI
ECCCCCHHHHCHHHH		23.9826051181
1082UbiquitinationLFDDLAEKIHRQYET
HHHHHHHHHHHHHHH		37.9033845483
10822-HydroxyisobutyrylationLFDDLAEKIHRQYET
HHHHHHHHHHHHHHH		37.90-
1082AcetylationLFDDLAEKIHRQYET
HHHHHHHHHHHHHHH		37.9025953088
1087PhosphorylationAEKIHRQYETIGLDF
HHHHHHHHHHCCCCC		18.26-
1099PhosphorylationLDFTIPKSCVEIAEL
CCCCCCHHHHHHHHH		20.3130622161
1114PhosphorylationLQQSKNPSINQILLS
HHHCCCCCHHHHHCC		43.4923312004
1121PhosphorylationSINQILLSPEKIKEG
CHHHHHCCHHHHHHH		27.8019664994
1124UbiquitinationQILLSPEKIKEGIKR
HHHCCHHHHHHHHHH		63.5629967540
1206PhosphorylationVVRKMAISAVAGILK
HHHHHHHHHHHHHHH		13.7320071362
1234AcetylationCEISGCPKPTQIIAG
CCCCCCCCCCEEEEC		65.8526051181
1261UbiquitinationKTIPRTKKEWESSCF
CCCCCCHHHHHHCCE		68.4029967540
1294UbiquitinationAGVEEQPKLGRSRED
ECCCCCCCCCCCHHH		64.3729967540
1298PhosphorylationEQPKLGRSREDMTEA
CCCCCCCCHHHCHHH		37.9224719451
1336UbiquitinationEDRKGKDKFNPRRFC
CCCCCCCCCCHHHHH		50.9924816145
1346UbiquitinationPRRFCLFKGIFRNFD
HHHHHHHHHHHCCCC		37.8421963094
1358UbiquitinationNFDDAFLPVLKPHLE
CCCCCHHHHHHHHHH		23.9624816145
1368UbiquitinationKPHLEHLVADSHEST
HHHHHHHHCCCHHHH		6.3221963094
1394PhosphorylationIRGSKHWTFEKVEKL
HHCCCCCCHHHHHHH		22.95-
1397AcetylationSKHWTFEKVEKLWEL
CCCCCHHHHHHHHHH		52.0520167786
1411PhosphorylationLLCPLLRTALSNITV
HHHHHHHHHHHCCEE		31.74-
1434PhosphorylationCIATSCESRDPRKLH
CCHHHCCCCCHHHHH		46.4317081983
1489PhosphorylationLLHRLLKYLEPKLTQ
HHHHHHHHHCHHHHH		19.1022817900
1493UbiquitinationLLKYLEPKLTQVYKN
HHHHHCHHHHHHHHH		55.5829967540
1499UbiquitinationPKLTQVYKNVRERIG
HHHHHHHHHHHHHHH		50.5433845483
1505 (in isoform 2)Ubiquitination-4.0621890473
1572UbiquitinationDERTQGIKLLKTILK
CHHHHHHHHHHHHHH		55.3729967540
1605UbiquitinationQLLPLFFKIAPVEND
HHHHHHHEECCCCCC		30.53-
1614PhosphorylationAPVENDNSYDELKRD
CCCCCCCCHHHHHHH		36.5025159151
1615PhosphorylationPVENDNSYDELKRDA
CCCCCCCHHHHHHHH		21.4927642862
1619UbiquitinationDNSYDELKRDAKLCL
CCCHHHHHHHHHHHH		46.3021906983
1619 (in isoform 1)Ubiquitination-46.3021890473
1623UbiquitinationDELKRDAKLCLSLMS
HHHHHHHHHHHHHHH		43.9822817900
1630PhosphorylationKLCLSLMSQGLLYPH
HHHHHHHHCCCCCCC		26.7924043423
1635PhosphorylationLMSQGLLYPHQVPLV
HHHCCCCCCCHHHHH		12.0524043423
1641UbiquitinationLYPHQVPLVLQVLKQ
CCCCHHHHHHHHHHH		6.7122817900
1644 (in isoform 2)Ubiquitination-30.9021890473
1645UbiquitinationQVPLVLQVLKQTARS
HHHHHHHHHHHHHHC		6.7022817900
1649PhosphorylationVLQVLKQTARSSSWH
HHHHHHHHHHCCCHH		23.5824043423
1652PhosphorylationVLKQTARSSSWHARY
HHHHHHHCCCHHHHH		26.6824043423
1653PhosphorylationLKQTARSSSWHARYT
HHHHHHCCCHHHHHH		31.7124043423
1654PhosphorylationKQTARSSSWHARYTV
HHHHHCCCHHHHHHH		24.9124043423
1746PhosphorylationKRKRDPGSVGDTIPS
CCCCCCCCCCCCCCH		28.4521712546
1750PhosphorylationDPGSVGDTIPSAELV
CCCCCCCCCCHHHHH		28.9422199227
1753PhosphorylationSVGDTIPSAELVKRH
CCCCCCCHHHHHHHH		30.4421406692
1758 (in isoform 1)Ubiquitination-51.6021890473
1758UbiquitinationIPSAELVKRHAGVLG
CCHHHHHHHHCCCCC		51.6022817900
1780UbiquitinationSPYDVPTWMPQLLMN
CCCCCCCHHHHHHHH		7.1522817900
1804UbiquitinationPIEMTVKKTLSNFRR
CCEEHHHHHHHCHHH		50.8129967540
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
-KUbiquitinationE3 ubiquitin ligaseXP03165
PMID:32235678
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSME4_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 PSME4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA7_HUMANPSMA7physical
22863883
NUTM1_HUMANNUTM1physical
25416956
DDX3X_HUMANDDX3Xphysical
26344197
PSA1_HUMANPSMA1physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA5_HUMANPSMA5physical
26344197
PSB6_HUMANPSMB6physical
26344197
PSMD3_HUMANPSMD3physical
26344197
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 PSME4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1121, AND MASSSPECTROMETRY.

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