dbPTM

PSB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSB3_HUMAN
UniProt AC	P49720
Protein Name	Proteasome subunit beta type-3
Gene Name	PSMB3
Organism	Homo sapiens (Human).
Sequence Length	205
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)..
Protein Sequence	MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSIMSYNGG ------CCCCCCCCC	27.31	20068231
2	Acetylation	------MSIMSYNGG ------CCCCCCCCC	27.31	20068231
5	Phosphorylation	---MSIMSYNGGAVM ---CCCCCCCCCEEE	17.49	21406692
6	Phosphorylation	--MSIMSYNGGAVMA --CCCCCCCCCEEEE	10.63	21406692
15	Acetylation	GGAVMAMKGKNCVAI CCEEEEECCCCEEEE	58.14	25953088
15	Ubiquitination	GGAVMAMKGKNCVAI CCEEEEECCCCEEEE	58.14	-
17	Ubiquitination	AVMAMKGKNCVAIAA EEEEECCCCEEEEEE	41.47	21906983
17	2-Hydroxyisobutyrylation	AVMAMKGKNCVAIAA EEEEECCCCEEEEEE	41.47	-
34	Sulfoxidation	RFGIQAQMVTTDFQK CCCEEEEEEECCHHH	3.03	21406390
36	Phosphorylation	GIQAQMVTTDFQKIF CEEEEEEECCHHHHC	18.46	-
37	Phosphorylation	IQAQMVTTDFQKIFP EEEEEEECCHHHHCC	24.33	-
41	Acetylation	MVTTDFQKIFPMGDR EEECCHHHHCCCCCE	46.43	26051181
41	Ubiquitination	MVTTDFQKIFPMGDR EEECCHHHHCCCCCE	46.43	21906983
48	Methylation	KIFPMGDRLYIGLAG HHCCCCCEEEEEHHH	24.54	115489409
50	Phosphorylation	FPMGDRLYIGLAGLA CCCCCEEEEEHHHHC	8.20	25332170
74	Phosphorylation	LKFRLNLYELKEGRQ HHHHHHHEEHHCCCC	20.38	28152594
77	Malonylation	RLNLYELKEGRQIKP HHHHEEHHCCCCCCH	46.30	26320211
77	Ubiquitination	RLNLYELKEGRQIKP HHHHEEHHCCCCCCH	46.30	19608861
77	Acetylation	RLNLYELKEGRQIKP HHHHEEHHCCCCCCH	46.30	19608861
83	Acetylation	LKEGRQIKPYTLMSM HHCCCCCCHHHHHHH	24.51	26051181
85	Phosphorylation	EGRQIKPYTLMSMVA CCCCCCHHHHHHHHH	13.91	28270605
86	Phosphorylation	GRQIKPYTLMSMVAN CCCCCHHHHHHHHHH	25.22	20068231
89	Phosphorylation	IKPYTLMSMVANLLY CCHHHHHHHHHHHHH	17.14	28270605
96	Phosphorylation	SMVANLLYEKRFGPY HHHHHHHHHHHHCCC	23.67	28270605
98	Ubiquitination	VANLLYEKRFGPYYT HHHHHHHHHHCCCCC	39.20	-
103	Phosphorylation	YEKRFGPYYTEPVIA HHHHHCCCCCCCEEC	24.33	20090780
104	Phosphorylation	EKRFGPYYTEPVIAG HHHHCCCCCCCEECC	14.04	28152594
105	Phosphorylation	KRFGPYYTEPVIAGL HHHCCCCCCCEECCC	28.15	28152594
168	Phosphorylation	DHLFETISQAMLNAV HHHHHHHHHHHHHCC	21.21	-
192	Ubiquitination	VIVHIIEKDKITTRT EEEEEEECCCCEEEH	54.64	2190698
192	2-Hydroxyisobutyrylation	VIVHIIEKDKITTRT EEEEEEECCCCEEEH	54.64	-

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 PSB3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSB3_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 PSB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSB2_HUMAN	PSMB2	physical	14733938
PSB2_HUMAN	PSMB2	physical	17948026
PSB3_HUMAN	PSMB3	physical	17948026
PSB5_HUMAN	PSMB5	physical	17948026
PSB7_HUMAN	PSMB7	physical	17948026
POMP_HUMAN	POMP	physical	17948026
PSB10_HUMAN	PSMB10	physical	17948026
PSB5_HUMAN	PSMB5	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSME2_HUMAN	PSME2	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSME1_HUMAN	PSME1	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
P53_HUMAN	TP53	physical	20080206
AP3M1_HUMAN	AP3M1	physical	22863883
ICAL_HUMAN	CAST	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSME4_HUMAN	PSME4	physical	22863883
P5CR3_HUMAN	PYCRL	physical	22863883
TRI27_HUMAN	TRIM27	physical	25416956
ASNA_HUMAN	ASNA1	physical	26344197
CAZA1_HUMAN	CAPZA1	physical	26344197
CPSF2_HUMAN	CPSF2	physical	26344197
ELP6_HUMAN	ELP6	physical	26344197
HEAT1_HUMAN	HEATR1	physical	26344197
KDM2A_HUMAN	KDM2A	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
PRS6A_HUMAN	PSMC3	physical	26344197
PRS6B_HUMAN	PSMC4	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD3_HUMAN	PSMD3	physical	26344197
PSMG2_HUMAN	PSMG2	physical	26344197
PSB9_HUMAN	PSMB9	physical	28514442
PSA7L_HUMAN	PSMA8	physical	28514442
PSB7_HUMAN	PSMB7	physical	28514442
PSME2_HUMAN	PSME2	physical	28514442
POMP_HUMAN	POMP	physical	28514442
PSB4_HUMAN	PSMB4	physical	28514442
AKIR2_HUMAN	AKIRIN2	physical	28514442
PSME1_HUMAN	PSME1	physical	28514442
PSA1_HUMAN	PSMA1	physical	28514442
PSME4_HUMAN	PSME4	physical	28514442
PSB1_HUMAN	PSMB1	physical	28514442
PSMG2_HUMAN	PSMG2	physical	28514442
OSER1_HUMAN	OSER1	physical	28514442
RN181_HUMAN	RNF181	physical	28514442
PSMF1_HUMAN	PSMF1	physical	28514442
PSMG4_HUMAN	PSMG4	physical	28514442
PSMG1_HUMAN	PSMG1	physical	28514442
PSMG3_HUMAN	PSMG3	physical	28514442
PSB10_HUMAN	PSMB10	physical	28514442
FBX7_HUMAN	FBXO7	physical	28514442
PSD13_HUMAN	PSMD13	physical	28514442
FANCB_HUMAN	FANCB	physical	28514442
PSMD6_HUMAN	PSMD6	physical	28514442
PRS10_HUMAN	PSMC6	physical	28514442
PSD11_HUMAN	PSMD11	physical	28514442
PSMD7_HUMAN	PSMD7	physical	28514442
PSA6_HUMAN	PSMA6	physical	28514442
PSDE_HUMAN	PSMD14	physical	28514442
PSMD1_HUMAN	PSMD1	physical	28514442
PSA7_HUMAN	PSMA7	physical	28514442
PRS7_HUMAN	PSMC2	physical	28514442
AKIR1_HUMAN	AKIRIN1	physical	28514442
PSB5_HUMAN	PSMB5	physical	28514442
PSA2_HUMAN	PSMA2	physical	28514442
PSB6_HUMAN	PSMB6	physical	28514442
PSA3_HUMAN	PSMA3	physical	28514442
PSMD8_HUMAN	PSMD8	physical	28514442
PSD12_HUMAN	PSMD12	physical	28514442
PRS8_HUMAN	PSMC5	physical	28514442
F192A_HUMAN	FAM192A	physical	28514442
PSMD3_HUMAN	PSMD3	physical	28514442
PSME3_HUMAN	PSME3	physical	28514442
PSA4_HUMAN	PSMA4	physical	28514442
PRS6A_HUMAN	PSMC3	physical	28514442
PSMD2_HUMAN	PSMD2	physical	28514442
PSMD4_HUMAN	PSMD4	physical	28514442
PRS4_HUMAN	PSMC1	physical	28514442
PRS6B_HUMAN	PSMC4	physical	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 PSB3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 SER-2, AND MASS SPECTROMETRY.	17323924 [Abstract]
"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-77, AND MASS SPECTROMETRY.	19608861 [Abstract]