PSMF1_HUMAN - dbPTM
PSMF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSMF1_HUMAN
UniProt AC Q92530
Protein Name Proteasome inhibitor PI31 subunit
Gene Name PSMF1
Organism Homo sapiens (Human).
Sequence Length 271
Subcellular Localization Cytoplasm . Endoplasmic reticulum .
Protein Description Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28..
Protein Sequence MAGLEVLFASAAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSELLPAGWNNNKDLYVLRYEYKDGSRKLLVKAITVESSMILNVLEYGSQQVADLTLNLDDYIDAEHLGDFHRTYKNSEELRSRIVSGIITPIHEQWEKANVSSPHREFPPATAREVDPLRIPPHHPHTSRQPPWCDPLGPFVVGGEDLDPFGPRRGGMIVDPLRSGFPRALIDPSSGLPNRLPPGAVPPGARFDPFGPIGTSPPGPNPDHLPPPGYDDMYL
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------MAGLEVLFA
------CCCHHHEEC		31.1422223895
50UbiquitinationQPGPNDKKSELLPAG
CCCCCCCCCCCCCCC		52.61-
72AcetylationYVLRYEYKDGSRKLL
EEEEEEECCCCEEEE		43.6125953088
84PhosphorylationKLLVKAITVESSMIL
EEEEEEEEECHHHHH		24.0729759185
88PhosphorylationKAITVESSMILNVLE
EEEEECHHHHHHHHH		9.0629759185
123PhosphorylationHLGDFHRTYKNSEEL
HHHHHHHHHCCHHHH		30.2226437602
125AcetylationGDFHRTYKNSEELRS
HHHHHHHCCHHHHHH		54.0827452117
125UbiquitinationGDFHRTYKNSEELRS
HHHHHHHCCHHHHHH		54.0821890473
127PhosphorylationFHRTYKNSEELRSRI
HHHHHCCHHHHHHHH		28.4426437602
136PhosphorylationELRSRIVSGIITPIH
HHHHHHHHCCCCCHH		23.1528122231
140PhosphorylationRIVSGIITPIHEQWE
HHHHCCCCCHHHHHH		17.8030622161
148UbiquitinationPIHEQWEKANVSSPH
CHHHHHHHCCCCCCC		42.1521890473
152PhosphorylationQWEKANVSSPHREFP
HHHHCCCCCCCCCCC		37.6523927012
153PhosphorylationWEKANVSSPHREFPP
HHHCCCCCCCCCCCC		22.0525159151
162PhosphorylationHREFPPATAREVDPL
CCCCCCCCCCCCCCC		31.8323927012
205MethylationLDPFGPRRGGMIVDP
CCCCCCCCCCEEECC		49.5012019811
214MethylationGMIVDPLRSGFPRAL
CEEECCHHHCCCCHH		39.87115489491
219MethylationPLRSGFPRALIDPSS
CHHHCCCCHHCCCCC		39.5054549453
219Asymmetric dimethylargininePLRSGFPRALIDPSS
CHHHCCCCHHCCCCC		39.50-
231MethylationPSSGLPNRLPPGAVP
CCCCCCCCCCCCCCC		46.7824129315
251PhosphorylationDPFGPIGTSPPGPNP
CCCCCCCCCCCCCCC		38.4928176443
252PhosphorylationPFGPIGTSPPGPNPD
CCCCCCCCCCCCCCC		24.7228176443
266PhosphorylationDHLPPPGYDDMYL--
CCCCCCCCCCCCC--		17.9728796482
270PhosphorylationPPGYDDMYL------
CCCCCCCCC------		19.0928796482
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 PSMF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSMF1_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 PSMF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KHDR3_HUMANKHDRBS3physical
16189514
MID49_HUMANMIEF2physical
16189514
HOOK2_HUMANHOOK2physical
16189514
RN126_HUMANRNF126physical
16189514
CPSF5_HUMANNUDT21physical
16189514
BEND7_HUMANBEND7physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
RBMX_HUMANRBMXphysical
16189514
RHXF2_HUMANRHOXF2physical
16189514
FBX7_HUMANFBXO7physical
18495667
KHDR3_HUMANKHDRBS3physical
19447967
RHXF2_HUMANRHOXF2physical
19447967
RALYL_HUMANRALYLphysical
19447967
DVL3_HUMANDVL3physical
19447967
BEND7_HUMANBEND7physical
19060904
PAK5_HUMANPAK7physical
19060904
LDOC1_HUMANLDOC1physical
19060904
RFOX2_HUMANRBFOX2physical
19060904
FBX7_HUMANFBXO7physical
25416956
PSA2_BOVINPSMA2physical
24770418
PSMD8_BOVINPSMD8physical
24770418
PSMD4_BOVINPSMD4physical
24770418
H11_HUMANHIST1H1Aphysical
26186194
PSA1_HUMANPSMA1physical
26186194
PSMF1_HUMANPSMF1physical
25266262
PSB1_HUMANPSMB1physical
28514442
H11_HUMANHIST1H1Aphysical
28514442
PSA1_HUMANPSMA1physical
28514442
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 PSMF1_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.
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-251 AND SER-252, 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-252, AND MASSSPECTROMETRY.

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