PAAF1_HUMAN - dbPTM
PAAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAAF1_HUMAN
UniProt AC Q9BRP4
Protein Name Proteasomal ATPase-associated factor 1
Gene Name PAAF1
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization
Protein Description Inhibits proteasome 26S assembly and proteolytic activity by impairing the association of the 19S regulatory complex with the 20S core. In case of HIV-1 infection, recruited by viral Tat to the HIV-1 promoter, where it promotes the recruitment of 19S regulatory complex through dissociation of the proteasome 26S. This presumably promotes provirus transcription efficiency. Protects SUPT6H from proteasomal degradation..
Protein Sequence MAAPLRIQSDWAQALRKDEGEAWLSCHPPGKPSLYGSLTCQGIGLDGIPEVTASEGFTVNEINKKSIHISCPKENASSKFLAPYTTFSRIHTKSITCLDISSRGGLGVSSSTDGTMKIWQASNGELRRVLEGHVFDVNCCRFFPSGLVVLSGGMDAQLKIWSAEDASCVVTFKGHKGGILDTAIVDRGRNVVSASRDGTARLWDCGRSACLGVLADCGSSINGVAVGAADNSINLGSPEQMPSEREVGTEAKMLLLAREDKKLQCLGLQSRQLVFLFIGSDAFNCCTFLSGFLLLAGTQDGNIYQLDVRSPRAPVQVIHRSGAPVLSLLSVRDGFIASQGDGSCFIVQQDLDYVTELTGADCDPVYKVATWEKQIYTCCRDGLVRRYQLSDL
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------MAAPLRIQS
------CCCCEEECC		20.1419413330
7 (in isoform 3)Phosphorylation-6.3928842319
65UbiquitinationTVNEINKKSIHISCP
EEEECCCCEEEEECC		50.59-
73UbiquitinationSIHISCPKENASSKF
EEEEECCCCCCCCCC		68.85-
77PhosphorylationSCPKENASSKFLAPY
ECCCCCCCCCCCCCC		45.7229978859
78PhosphorylationCPKENASSKFLAPYT
CCCCCCCCCCCCCCC		25.6429978859
84PhosphorylationSSKFLAPYTTFSRIH
CCCCCCCCCCCEECC		16.8928152594
85PhosphorylationSKFLAPYTTFSRIHT
CCCCCCCCCCEECCC		21.9528152594
86PhosphorylationKFLAPYTTFSRIHTK
CCCCCCCCCEECCCC		17.4828152594
88PhosphorylationLAPYTTFSRIHTKSI
CCCCCCCEECCCCCE		28.3828152594
94PhosphorylationFSRIHTKSITCLDIS
CEECCCCCEEEEEEC		25.0428450419
96PhosphorylationRIHTKSITCLDISSR
ECCCCCEEEEEECCC		17.6928450419
103MethylationTCLDISSRGGLGVSS
EEEEECCCCCCCCCC		36.0930760577
116SulfoxidationSSSTDGTMKIWQASN
CCCCCCCEEEEECCC		3.4721406390
173UbiquitinationASCVVTFKGHKGGIL
CCEEEEECCCCCEEE		51.22-
176UbiquitinationVVTFKGHKGGILDTA
EEEECCCCCEEEEEE		68.45-
182PhosphorylationHKGGILDTAIVDRGR
CCCEEEEEEEEECCC		18.1621406692
187MethylationLDTAIVDRGRNVVSA
EEEEEEECCCCEEEC		34.77115486229
193PhosphorylationDRGRNVVSASRDGTA
ECCCCEEECCCCCCC		19.08-
195PhosphorylationGRNVVSASRDGTARL
CCCEEECCCCCCCCH		24.33-
199PhosphorylationVSASRDGTARLWDCG
EECCCCCCCCHHHCC		16.94-
208PhosphorylationRLWDCGRSACLGVLA
CHHHCCHHHHHHHHH		14.49-
243PhosphorylationGSPEQMPSEREVGTE
CCCCCCCCHHHHCHH		43.9026356563
249PhosphorylationPSEREVGTEAKMLLL
CCHHHHCHHHHHHHH		37.6426356563
252UbiquitinationREVGTEAKMLLLARE
HHHCHHHHHHHHHCC		24.69-
373UbiquitinationYKVATWEKQIYTCCR
EEEEECHHHHHHHHH		33.29-
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 PAAF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAAF1_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 PAAF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSMD2_HUMANPSMD2physical
17353931
PSMD3_HUMANPSMD3physical
17353931
PRS8_HUMANPSMC5physical
17353931
PRS4_HUMANPSMC1physical
17353931
A16A1_HUMANALDH16A1physical
17353931
PSMD1_HUMANPSMD1physical
17353931
DEOC_HUMANDERAphysical
17353931
PRS6B_HUMANPSMC4physical
17353931
PRS6A_HUMANPSMC3physical
17353931
PSDE_HUMANPSMD14physical
17353931
PSMD7_HUMANPSMD7physical
17353931
PSD10_HUMANPSMD10physical
17353931
PSD12_HUMANPSMD12physical
17353931
PSD11_HUMANPSMD11physical
17353931
PSMD8_HUMANPSMD8physical
17353931
PSMD6_HUMANPSMD6physical
17353931
PRS7_HUMANPSMC2physical
17353931
PRS10_HUMANPSMC6physical
17353931
PRS8_HUMANPSMC5physical
19490896
PRS8_HUMANPSMC5physical
15831487
PSMD8_HUMANPSMD8physical
15831487
PSA1_HUMANPSMA1physical
15831487
SPT6H_HUMANSUPT6Hphysical
22316138
UBCP1_HUMANUBLCP1physical
28539385
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 PAAF1_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.

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