PSB8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSB8_HUMAN
• UniProt AC: P28062
• Protein Name: Proteasome subunit beta type-8
• Gene Name: PSMB8
• Organism: Homo sapiens (Human).
• Sequence Length: 276
• Subcellular Localization: Cytoplasm . Nucleus.
• Protein Description: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes..
• Protein Sequence: MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ

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
5 (in isoform 2)	Phosphorylation	-	34.21	18669648
7 (in isoform 2)	Phosphorylation	-	3.72	22985185
11	Methylation	LDVCGAPRGQRPESA CCCCCCCCCCCCCCC	54.03	115384949
28	Phosphorylation	VAGSGRRSDPGHYSF CCCCCCCCCCCCCEE	46.96	25159151
34	Phosphorylation	RSDPGHYSFSMRSPE CCCCCCCEECCCCHH	12.74	28348404
36	Phosphorylation	DPGHYSFSMRSPELA CCCCCEECCCCHHHC	13.82	25627689
39	Phosphorylation	HYSFSMRSPELALPR CCEECCCCHHHCCCC	17.68	21815630
93	Phosphorylation	AAVDSRASAGSYISA EEEECCCCCCCHHHE	31.86	28857561
96	Phosphorylation	DSRASAGSYISALRV ECCCCCCCHHHEEEC	21.00	28857561
97	Phosphorylation	SRASAGSYISALRVN CCCCCCCHHHEEECC	9.66	28152594
99	Phosphorylation	ASAGSYISALRVNKV CCCCCHHHEEECCEE	17.02	28152594
105	Ubiquitination	ISALRVNKVIEINPY HHEEECCEEEEECCH	41.55	-
112	Phosphorylation	KVIEINPYLLGTMSG EEEEECCHHHHCCCC	15.29	20090780
126	Phosphorylation	GCAADCQYWERLLAK CHHHHHHHHHHHHHH	18.63	-
133	Acetylation	YWERLLAKECRLYYL HHHHHHHHHCEEEEE	58.26	23749302
133	Ubiquitination	YWERLLAKECRLYYL HHHHHHHHHCEEEEE	58.26	-
153	Ubiquitination	ISVSAASKLLSNMMC EEHHHHHHHHHHCCH	49.04	-
156	Phosphorylation	SAASKLLSNMMCQYR HHHHHHHHHCCHHHC	32.87	28509920
162	Phosphorylation	LSNMMCQYRGMGLSM HHHCCHHHCCCCCCC	12.28	-
178	Acetylation	SMICGWDKKGPGLYY CEECCCCCCCCCEEE	53.79	25953088
179	Ubiquitination	MICGWDKKGPGLYYV EECCCCCCCCCEEEE	68.79	-
184	Phosphorylation	DKKGPGLYYVDEHGT CCCCCCEEEECCCCC	13.83	20090780
185	Phosphorylation	KKGPGLYYVDEHGTR CCCCCEEEECCCCCE	13.38	25839225
234	Phosphorylation	LGRRAIAYATHRDSY HHHHHHHHHCCCCCC	13.11	23312004
236	Phosphorylation	RRAIAYATHRDSYSG HHHHHHHCCCCCCCC	12.55	23312004
240	Phosphorylation	AYATHRDSYSGGVVN HHHCCCCCCCCCEEE	22.58	28348404
241	Phosphorylation	YATHRDSYSGGVVNM HHCCCCCCCCCEEEE	18.67	23312004
242	Phosphorylation	ATHRDSYSGGVVNMY HCCCCCCCCCEEEEE	32.78	28348404
249	Phosphorylation	SGGVVNMYHMKEDGW CCCEEEEEEECCCCC	8.11	23312004
252	Ubiquitination	VVNMYHMKEDGWVKV EEEEEEECCCCCEEE	39.06	-
258	Sumoylation	MKEDGWVKVESTDVS ECCCCCEEEEECCHH	33.50	-
258	Sumoylation	MKEDGWVKVESTDVS ECCCCCEEEEECCHH	33.50	-
258	Ubiquitination	MKEDGWVKVESTDVS ECCCCCEEEEECCHH	33.50	-
261	Phosphorylation	DGWVKVESTDVSDLL CCCEEEEECCHHHHH	32.66	23312004
262	Phosphorylation	GWVKVESTDVSDLLH CCEEEEECCHHHHHH	27.24	23312004
265	Phosphorylation	KVESTDVSDLLHQYR EEEECCHHHHHHHHH	25.92	23312004
271	Phosphorylation	VSDLLHQYREANQ-- HHHHHHHHHHHCC--	10.32	23312004

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PSB8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PSB8_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PSB8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POMP_HUMAN	POMP	physical	15944226
MDR1_HUMAN	ABCB1	physical	15488952
TAP1_HUMAN	TAP1	physical	15488952
TAP2_HUMAN	TAP2	physical	15488952
PSB3_HUMAN	PSMB3	physical	17948026
PSB1_HUMAN	PSMB1	physical	17948026
PSB6_HUMAN	PSMB6	physical	17948026
PSB7_HUMAN	PSMB7	physical	17948026
PSB8_HUMAN	PSMB8	physical	17948026
PSB9_HUMAN	PSMB9	physical	17948026
PSB10_HUMAN	PSMB10	physical	17948026
POMP_HUMAN	POMP	physical	17948026
PSMD8_HUMAN	PSMD8	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
GCN1_HUMAN	GCN1L1	physical	22863883
HNRPM_HUMAN	HNRNPM	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA3_HUMAN	PSMA3	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
PSB4_HUMAN	PSMB4	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSB6_HUMAN	PSMB6	physical	22863883
PSB7_HUMAN	PSMB7	physical	22863883
HEAT1_HUMAN	HEATR1	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
PSB6_HUMAN	PSMB6	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 256040: Nakajo syndrome (NKJO)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB08889: Carfilzomib