ADRM1_HUMAN - dbPTM
ADRM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADRM1_HUMAN
UniProt AC Q16186
Protein Name Proteasomal ubiquitin receptor ADRM1
Gene Name ADRM1
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization Cytoplasm . Nucleus .
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. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex..
Protein Sequence MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD
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
2Phosphorylation------MTTSGALFP
------CCCCCCCCC		29.6629255136
2Acetylation------MTTSGALFP
------CCCCCCCCC		29.6620068231
3Phosphorylation-----MTTSGALFPS
-----CCCCCCCCCC		24.7024732914
4Phosphorylation----MTTSGALFPSL
----CCCCCCCCCCC		16.9524732914
10PhosphorylationTSGALFPSLVPGSRG
CCCCCCCCCCCCCCC		34.3624732914
15PhosphorylationFPSLVPGSRGASNKY
CCCCCCCCCCCCCCE		22.8229255136
19PhosphorylationVPGSRGASNKYLVEF
CCCCCCCCCCEEEEE		36.3626074081
21AcetylationGSRGASNKYLVEFRA
CCCCCCCCEEEEEEC		37.1519608861
21UbiquitinationGSRGASNKYLVEFRA
CCCCCCCCEEEEEEC		37.1521890473
212-HydroxyisobutyrylationGSRGASNKYLVEFRA
CCCCCCCCEEEEEEC		37.15-
22PhosphorylationSRGASNKYLVEFRAG
CCCCCCCEEEEEECC		21.8946159931
27MethylationNKYLVEFRAGKMSLK
CCEEEEEECCCCEEE		28.99-
32PhosphorylationEFRAGKMSLKGTTVT
EEECCCCEEECEEEC		30.348656633
34UbiquitinationRAGKMSLKGTTVTPD
ECCCCEEECEEECCC		47.0721890473
34MethylationRAGKMSLKGTTVTPD
ECCCCEEECEEECCC		47.07-
36PhosphorylationGKMSLKGTTVTPDKR
CCCEEECEEECCCCC		19.2629449344
37PhosphorylationKMSLKGTTVTPDKRK
CCEEECEEECCCCCC		30.9325159151
39PhosphorylationSLKGTTVTPDKRKGL
EEECEEECCCCCCCE		24.5521815630
42MethylationGTTVTPDKRKGLVYI
CEEECCCCCCCEEEE		58.16-
42UbiquitinationGTTVTPDKRKGLVYI
CEEECCCCCCCEEEE		58.1621906983
42AcetylationGTTVTPDKRKGLVYI
CEEECCCCCCCEEEE		58.1625953088
422-HydroxyisobutyrylationGTTVTPDKRKGLVYI
CEEECCCCCCCEEEE		58.16-
62UbiquitinationSLIHFCWKDRTSGNV
CEEEEEECCCCCCCC		38.2121906983
80GlutathionylationLIIFPDDCEFKRVPQ
EEEECCCCCCCCCCC		9.6222555962
83AcetylationFPDDCEFKRVPQCPS
ECCCCCCCCCCCCCC		30.1426051181
83UbiquitinationFPDDCEFKRVPQCPS
ECCCCCCCCCCCCCC		30.1421906983
97AcetylationSGRVYVLKFKAGSKR
CCCEEEEEEEECCEE		34.4726051181
97UbiquitinationSGRVYVLKFKAGSKR
CCCEEEEEEEECCEE		34.4721906983
113UbiquitinationFFWMQEPKTDQDEEH
EEEECCCCCCCCHHH		65.07-
127PhosphorylationHCRKVNEYLNNPPMP
HHHHHHHHHCCCCCC		14.9924275569
140PhosphorylationMPGALGASGSSGHEL
CCCCCCCCCCCCCHH		37.0926074081
142PhosphorylationGALGASGSSGHELSA
CCCCCCCCCCCHHHH		30.5626074081
143PhosphorylationALGASGSSGHELSAL
CCCCCCCCCCHHHHC		47.9326074081
211O-linked_GlycosylationSSSSSSRSQSAAVTP
CCCCCCCCCCCCCCC		30.3630059200
211PhosphorylationSSSSSSRSQSAAVTP
CCCCCCCCCCCCCCC		30.3629255136
213O-linked_GlycosylationSSSSRSQSAAVTPSS
CCCCCCCCCCCCCCC		21.3130059200
213PhosphorylationSSSSRSQSAAVTPSS
CCCCCCCCCCCCCCC		21.3129255136
217PhosphorylationRSQSAAVTPSSTTSS
CCCCCCCCCCCCCCC		16.8423927012
217O-linked_GlycosylationRSQSAAVTPSSTTSS
CCCCCCCCCCCCCCC		16.8430059200
219O-linked_GlycosylationQSAAVTPSSTTSSTR
CCCCCCCCCCCCCCC		30.8330059200
219PhosphorylationQSAAVTPSSTTSSTR
CCCCCCCCCCCCCCC		30.8323927012
220O-linked_GlycosylationSAAVTPSSTTSSTRA
CCCCCCCCCCCCCCC		36.5930059200
220PhosphorylationSAAVTPSSTTSSTRA
CCCCCCCCCCCCCCC		36.5923927012
221PhosphorylationAAVTPSSTTSSTRAT
CCCCCCCCCCCCCCC		34.7323927012
221O-linked_GlycosylationAAVTPSSTTSSTRAT
CCCCCCCCCCCCCCC		34.7330059200
222PhosphorylationAVTPSSTTSSTRATP
CCCCCCCCCCCCCCC		23.7223927012
222O-linked_GlycosylationAVTPSSTTSSTRATP
CCCCCCCCCCCCCCC		23.7230059200
223O-linked_GlycosylationVTPSSTTSSTRATPA
CCCCCCCCCCCCCCC		29.7830059200
223PhosphorylationVTPSSTTSSTRATPA
CCCCCCCCCCCCCCC		29.7823927012
224PhosphorylationTPSSTTSSTRATPAP
CCCCCCCCCCCCCCC		21.5923927012
224O-linked_GlycosylationTPSSTTSSTRATPAP
CCCCCCCCCCCCCCC		21.5930059200
225PhosphorylationPSSTTSSTRATPAPS
CCCCCCCCCCCCCCC		24.8823927012
225O-linked_GlycosylationPSSTTSSTRATPAPS
CCCCCCCCCCCCCCC		24.8830059200
319PhosphorylationPYLPSGESLPQTADE
HCCCCCCCCCCCHHH		49.2024275569
371UbiquitinationEAVEAANKGDVEAFA
HHHHHHHHCCHHHHH		52.33-
379UbiquitinationGDVEAFAKAMQNNAK
CCHHHHHHHHHHCCC		37.6321906983
386UbiquitinationKAMQNNAKPEQKEGD
HHHHHCCCHHHCCCC		51.7321906983
390UbiquitinationNNAKPEQKEGDTKDK
HCCCHHHCCCCCCCC		63.1021906983
395UbiquitinationEQKEGDTKDKKDEEE
HHCCCCCCCCHHHHH		72.7521906983
397UbiquitinationKEGDTKDKKDEEEDM
CCCCCCCCHHHHHHC		64.7821906983
398UbiquitinationEGDTKDKKDEEEDMS
CCCCCCCHHHHHHCC		79.2121906983
405PhosphorylationKDEEEDMSLD-----
HHHHHHCCCC-----		41.5330278072
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 ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADRM1_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 ADRM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
18497827
PSMD2_HUMANPSMD2physical
16990800
PRS8_HUMANPSMC5physical
16990800
PSMD4_HUMANPSMD4physical
16990800
UCHL5_HUMANUCHL5physical
16990800
UCHL5_HUMANUCHL5physical
16906146
UCHL5_HUMANUCHL5physical
20471946
UCHL5_HUMANUCHL5physical
17139257
PSMD1_HUMANPSMD1physical
19781552
PSMD4_HUMANPSMD4physical
16815440
VA0D2_HUMANATP6V0D2physical
19818731
A4_HUMANAPPphysical
21832049
UBC_HUMANUBCphysical
18497817
UCHL5_HUMANUCHL5physical
25416956
PSMD1_HUMANPSMD1physical
26186194
PSD13_HUMANPSMD13physical
26186194
PSMD3_HUMANPSMD3physical
26186194
PSD11_HUMANPSMD11physical
26186194
PRS10_HUMANPSMC6physical
26186194
PRS6A_HUMANPSMC3physical
26186194
PRS6B_HUMANPSMC4physical
26186194
PRS4_HUMANPSMC1physical
26186194
PRS8_HUMANPSMC5physical
26186194
PSMD2_HUMANPSMD2physical
26186194
PSD10_HUMANPSMD10physical
26186194
PSDE_HUMANPSMD14physical
26186194
PRS7_HUMANPSMC2physical
26186194
PSMD8_HUMANPSMD8physical
26186194
PSD12_HUMANPSMD12physical
26186194
PSMD6_HUMANPSMD6physical
26186194
PSMD4_HUMANPSMD4physical
26186194
PAAF1_HUMANPAAF1physical
26186194
BAG1_HUMANBAG1physical
26186194
UBC_HUMANUBCphysical
25702870
PSA1_HUMANPSMA1physical
26344197
PSA2_HUMANPSMA2physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSA5_HUMANPSMA5physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB4_HUMANPSMB4physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB6_HUMANPSMB6physical
26344197
PSB8_HUMANPSMB8physical
26344197
PRS4_HUMANPSMC1physical
26344197
PRS10_HUMANPSMC6physical
26344197
PSD12_HUMANPSMD12physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD6_HUMANPSMD6physical
26344197
UCHL5_HUMANUCHL5physical
21516116
PSMD1_HUMANPSMD1physical
26466095
UBC_HUMANUBCphysical
27396824
UBQL2_HUMANUBQLN2physical
27396824
PSD12_HUMANPSMD12physical
28514442
PSD10_HUMANPSMD10physical
28514442
PSMD4_HUMANPSMD4physical
28514442
PRS6B_HUMANPSMC4physical
28514442
PSD13_HUMANPSMD13physical
28514442
PSDE_HUMANPSMD14physical
28514442
PSMD1_HUMANPSMD1physical
28514442
PSD11_HUMANPSMD11physical
28514442
PRS4_HUMANPSMC1physical
28514442
PRS10_HUMANPSMC6physical
28514442
PSMD6_HUMANPSMD6physical
28514442
PRS6A_HUMANPSMC3physical
28514442
PRS7_HUMANPSMC2physical
28514442
PSMD3_HUMANPSMD3physical
28514442
PSMD8_HUMANPSMD8physical
28514442
PSMD2_HUMANPSMD2physical
28514442
BAG1_HUMANBAG1physical
28514442
UBE2N_HUMANUBE2Nphysical
27173435
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 ADRM1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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-21, AND MASS SPECTROMETRY.
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND THR-217, ANDMASS SPECTROMETRY.
"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-211; THR-217; SER-220AND SER-405, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-34, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory