dbPTM

PSB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSB1_HUMAN
UniProt AC	P20618
Protein Name	Proteasome subunit beta type-1
Gene Name	PSMB1
Organism	Homo sapiens (Human).
Sequence Length	241
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	MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MLSSTAMY -------CCCCCCCC	8.06	22814378
3	Phosphorylation	-----MLSSTAMYSA -----CCCCCCCCCC	25.09	29978859
4	Phosphorylation	----MLSSTAMYSAP ----CCCCCCCCCCC	19.07	29978859
5	Phosphorylation	---MLSSTAMYSAPG ---CCCCCCCCCCCC	16.45	29978859
8	Phosphorylation	MLSSTAMYSAPGRDL CCCCCCCCCCCCCCC	10.14	25106551
9	Phosphorylation	LSSTAMYSAPGRDLG CCCCCCCCCCCCCCC	18.20	29978859
58	Phosphorylation	VASDTRLSEGFSIHT EEECCCCCCCEEEEE	32.17	23186163
58	O-linked_Glycosylation	VASDTRLSEGFSIHT EEECCCCCCCEEEEE	32.17	UniProtKB CARBOHYD
62	Phosphorylation	TRLSEGFSIHTRDSP CCCCCCEEEEECCCC	25.07	22617229
65	Phosphorylation	SEGFSIHTRDSPKCY CCCEEEEECCCCCCE	34.21	23403867
68	Phosphorylation	FSIHTRDSPKCYKLT EEEEECCCCCCEECC	23.98	25159151
72	Phosphorylation	TRDSPKCYKLTDKTV ECCCCCCEECCCCEE	18.37	29496907
73	Acetylation	RDSPKCYKLTDKTVI CCCCCCEECCCCEEE	55.15	25953088
73	Ubiquitination	RDSPKCYKLTDKTVI CCCCCCEECCCCEEE	55.15	-
75	Phosphorylation	SPKCYKLTDKTVIGC CCCCEECCCCEEEEC	31.16	-
77	Acetylation	KCYKLTDKTVIGCSG CCEECCCCEEEECCC	39.18	25953088
77	Ubiquitination	KCYKLTDKTVIGCSG CCEECCCCEEEECCC	39.18	21906983
78	Phosphorylation	CYKLTDKTVIGCSGF CEECCCCEEEECCCC	21.84	21406692
82	S-nitrosocysteine	TDKTVIGCSGFHGDC CCCEEEECCCCCCHH	2.18	-
82	S-nitrosylation	TDKTVIGCSGFHGDC CCCEEEECCCCCCHH	2.18	19483679
83	Phosphorylation	DKTVIGCSGFHGDCL CCEEEECCCCCCHHH	39.00	21406692
89	S-nitrosocysteine	CSGFHGDCLTLTKII CCCCCCHHHHHHHHH	3.56	-
89	S-nitrosylation	CSGFHGDCLTLTKII CCCCCCHHHHHHHHH	3.56	19483679
91	Phosphorylation	GFHGDCLTLTKIIEA CCCCHHHHHHHHHHH	38.42	21406692
93	Phosphorylation	HGDCLTLTKIIEARL CCHHHHHHHHHHHHH	18.24	20068231
94	Ubiquitination	GDCLTLTKIIEARLK CHHHHHHHHHHHHHH	44.81	21906983
104	Ubiquitination	EARLKMYKHSNNKAM HHHHHHHHHCCCHHH	36.74	21906983
125	Phosphorylation	AMLSTILYSRRFFPY HHHHHHHHHHCCCCH	9.04	-
126	Phosphorylation	MLSTILYSRRFFPYY HHHHHHHHHCCCCHH	17.34	24719451
132	Phosphorylation	YSRRFFPYYVYNIIG HHHCCCCHHHHEEEC	10.62	20090780
133	Phosphorylation	SRRFFPYYVYNIIGG HHCCCCHHHHEEECC	9.19	29496907
135	Phosphorylation	RFFPYYVYNIIGGLD CCCCHHHHEEECCCC	5.64	29496907
146	Ubiquitination	GGLDEEGKGAVYSFD CCCCCCCCCCEEEEC	47.15	-
150	Phosphorylation	EEGKGAVYSFDPVGS CCCCCCEEEECCCCC	11.77	28152594
151	Phosphorylation	EGKGAVYSFDPVGSY CCCCCEEEECCCCCC	19.30	28152594
157	Phosphorylation	YSFDPVGSYQRDSFK EEECCCCCCCCCCCC	20.51	23186163
158	Phosphorylation	SFDPVGSYQRDSFKA EECCCCCCCCCCCCC	11.13	28152594
158	Nitration	SFDPVGSYQRDSFKA EECCCCCCCCCCCCC	11.13	-
162	Phosphorylation	VGSYQRDSFKAGGSA CCCCCCCCCCCCCCH	30.73	25159151
164	Ubiquitination	SYQRDSFKAGGSASA CCCCCCCCCCCCHHH	50.50	21906983
172	Sulfoxidation	AGGSASAMLQPLLDN CCCCHHHHHHHHHCC	3.11	30846556
184	Ubiquitination	LDNQVGFKNMQNVEH HCCCCCCCCCCCCEE	45.65	21906983
184	Acetylation	LDNQVGFKNMQNVEH HCCCCCCCCCCCCEE	45.65	25953088
186	Sulfoxidation	NQVGFKNMQNVEHVP CCCCCCCCCCCEECC	2.94	21406390
195	Phosphorylation	NVEHVPLSLDRAMRL CCEECCCCHHHHHHH	23.35	26437602
204	Acetylation	DRAMRLVKDVFISAA HHHHHHHHHHHHHHH	53.41	19608861
204	Malonylation	DRAMRLVKDVFISAA HHHHHHHHHHHHHHH	53.41	26320211
204	Ubiquitination	DRAMRLVKDVFISAA HHHHHHHHHHHHHHH	53.41	21906983
209	O-linked_Glycosylation	LVKDVFISAAERDVY HHHHHHHHHHHCCCC	15.23	UniProtKB CARBOHYD
209	Phosphorylation	LVKDVFISAAERDVY HHHHHHHHHHHCCCC	15.23	21712546
216	Phosphorylation	SAAERDVYTGDALRI HHHHCCCCCCCCEEE	14.86	22817900
224	S-nitrosylation	TGDALRICIVTKEGI CCCCEEEEEEECCCC	1.33	19483679
224	S-nitrosocysteine	TGDALRICIVTKEGI CCCCEEEEEEECCCC	1.33	-
224	S-palmitoylation	TGDALRICIVTKEGI CCCCEEEEEEECCCC	1.33	29575903
228	2-Hydroxyisobutyrylation	LRICIVTKEGIREET EEEEEEECCCCCCCC	42.95	-
228	Acetylation	LRICIVTKEGIREET EEEEEEECCCCCCCC	42.95	26822725
228	Ubiquitination	LRICIVTKEGIREET EEEEEEECCCCCCCC	42.95	21906983
239	Methylation	REETVSLRKD----- CCCCCCCCCC-----	33.32	115489377
240	Ubiquitination	EETVSLRKD------ CCCCCCCCC------	73.42	-

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 PSB1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSB1_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 PSB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCL3_HUMAN	BCL3	physical	20558726
PSB3_HUMAN	PSMB3	physical	14733938
PSB7_HUMAN	PSMB7	physical	14733938
PSB5_HUMAN	PSMB5	physical	14733938
POMP_HUMAN	POMP	physical	14733938
PAI2_HUMAN	SERPINB2	physical	14732874
PSN1_HUMAN	PSEN1	physical	10527805
PSB5_HUMAN	PSMB5	physical	17506986
PSB8_HUMAN	PSMB8	physical	17506986
PSA7_HUMAN	PSMA7	physical	17506986
PSB3_HUMAN	PSMB3	physical	17506986
POMP_HUMAN	POMP	physical	17506986
PSB2_HUMAN	PSMB2	physical	17948026
PSB3_HUMAN	PSMB3	physical	17948026
PSB5_HUMAN	PSMB5	physical	17948026
PSB7_HUMAN	PSMB7	physical	17948026
PSB8_HUMAN	PSMB8	physical	17948026
POMP_HUMAN	POMP	physical	17948026
PSB3_HUMAN	PSMB3	physical	22939629
PSB5_HUMAN	PSMB5	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSB2_HUMAN	PSMB2	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSME1_HUMAN	PSME1	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSME2_HUMAN	PSME2	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
RBM8A_HUMAN	RBM8A	physical	22939629
TCPE_HUMAN	CCT5	physical	22939629
UBE2A_HUMAN	UBE2A	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
UB2V1_HUMAN	UBE2V1	physical	22939629
SNX3_HUMAN	SNX3	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
SRSF2_HUMAN	SRSF2	physical	22939629
SGT1_HUMAN	SUGT1	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
BAG3_HUMAN	BAG3	physical	23824909
AP3M1_HUMAN	AP3M1	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSME4_HUMAN	PSME4	physical	22863883
P5CR3_HUMAN	PYCRL	physical	22863883
CDN1B_HUMAN	CDKN1B	physical	23725357
PSA7_HUMAN	PSMA7	physical	23725357
TRI27_HUMAN	TRIM27	physical	25416956
TRAF1_HUMAN	TRAF1	physical	25416956
MARE3_HUMAN	MAPRE3	physical	25416956
ADRM1_HUMAN	ADRM1	physical	26344197
ASNA_HUMAN	ASNA1	physical	26344197
CLIC4_HUMAN	CLIC4	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
RT09_HUMAN	MRPS9	physical	26344197
PEX19_HUMAN	PEX19	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
POMP_HUMAN	POMP	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
PSA2_HUMAN	PSMA2	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSA5_HUMAN	PSMA5	physical	26344197
PSA6_HUMAN	PSMA6	physical	26344197
PSA7_HUMAN	PSMA7	physical	26344197
PSA7L_HUMAN	PSMA8	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
PSB4_HUMAN	PSMB4	physical	26344197
PSB5_HUMAN	PSMB5	physical	26344197
PSB6_HUMAN	PSMB6	physical	26344197
PSB7_HUMAN	PSMB7	physical	26344197
PSB8_HUMAN	PSMB8	physical	26344197
PRS4_HUMAN	PSMC1	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
PRS6A_HUMAN	PSMC3	physical	26344197
PRS6B_HUMAN	PSMC4	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PRS10_HUMAN	PSMC6	physical	26344197
PSMD1_HUMAN	PSMD1	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD4_HUMAN	PSMD4	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
UCHL5_HUMAN	UCHL5	physical	26344197
PSA7L_HUMAN	PSMA8	physical	28514442
PSME4_HUMAN	PSME4	physical	28514442
PSB4_HUMAN	PSMB4	physical	28514442
PSB7_HUMAN	PSMB7	physical	28514442
POMP_HUMAN	POMP	physical	28514442
PSME2_HUMAN	PSME2	physical	28514442
PSMG2_HUMAN	PSMG2	physical	28514442
PSA1_HUMAN	PSMA1	physical	28514442
PSME1_HUMAN	PSME1	physical	28514442
PSB9_HUMAN	PSMB9	physical	28514442
PSA7_HUMAN	PSMA7	physical	28514442
PSA2_HUMAN	PSMA2	physical	28514442
PSA6_HUMAN	PSMA6	physical	28514442
PSA4_HUMAN	PSMA4	physical	28514442
PSMG1_HUMAN	PSMG1	physical	28514442
PSB5_HUMAN	PSMB5	physical	28514442
PSA5_HUMAN	PSMA5	physical	28514442
PSA3_HUMAN	PSMA3	physical	28514442
PSB6_HUMAN	PSMB6	physical	28514442
FBX7_HUMAN	FBXO7	physical	28514442
PSMD7_HUMAN	PSMD7	physical	28514442
PSD11_HUMAN	PSMD11	physical	28514442
PRS6B_HUMAN	PSMC4	physical	28514442
PSMD1_HUMAN	PSMD1	physical	28514442
MARE2_HUMAN	MAPRE2	physical	27173435
MARE1_HUMAN	MAPRE1	physical	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
DB00188	Bortezomib
DB08889	Carfilzomib

Regulatory Network of PSB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-204, AND MASS SPECTROMETRY.	19608861 [Abstract]