dbPTM

PSB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSB2_HUMAN
UniProt AC	P49721
Protein Name	Proteasome subunit beta type-2
Gene Name	PSMB2
Organism	Homo sapiens (Human).
Sequence Length	201
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	MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEYLIGIQ -------CCEECCCC	7.43	22814378
3	Phosphorylation	-----MEYLIGIQGP -----CCEECCCCCC	11.43	20230923
12	Phosphorylation	IGIQGPDYVLVASDR CCCCCCCEEEEECCC	9.98	27642862
23	Phosphorylation	ASDRVAASNIVQMKD ECCCEEHHHCEECCC	19.83	21712546
28	Sulfoxidation	AASNIVQMKDDHDKM EHHHCEECCCCHHHH	3.39	21406390
29	2-Hydroxyisobutyrylation	ASNIVQMKDDHDKMF HHHCEECCCCHHHHH	42.80	-
29	Acetylation	ASNIVQMKDDHDKMF HHHCEECCCCHHHHH	42.80	26822725
29	Ubiquitination	ASNIVQMKDDHDKMF HHHCEECCCCHHHHH	42.80	21890473
34	2-Hydroxyisobutyrylation	QMKDDHDKMFKMSEK ECCCCHHHHHHHCHH	42.70	-
34	Ubiquitination	QMKDDHDKMFKMSEK ECCCCHHHHHHHCHH	42.70	21890473
34	Acetylation	QMKDDHDKMFKMSEK ECCCCHHHHHHHCHH	42.70	27178108
37	Ubiquitination	DDHDKMFKMSEKILL CCHHHHHHHCHHHHH	37.71	21890473
37	2-Hydroxyisobutyrylation	DDHDKMFKMSEKILL CCHHHHHHHCHHHHH	37.71	-
37	Acetylation	DDHDKMFKMSEKILL CCHHHHHHHCHHHHH	37.71	25953088
59	Phosphorylation	DTVQFAEYIQKNVQL CHHHHHHHHHHHCCC	12.77	28258704
62	Ubiquitination	QFAEYIQKNVQLYKM HHHHHHHHHCCCEEC	49.91	21890473
67	Phosphorylation	IQKNVQLYKMRNGYE HHHHCCCEECCCCCC	5.90	-
68	Succinylation	QKNVQLYKMRNGYEL HHHCCCEECCCCCCC	39.72	23954790
68	2-Hydroxyisobutyrylation	QKNVQLYKMRNGYEL HHHCCCEECCCCCCC	39.72	-
68	Acetylation	QKNVQLYKMRNGYEL HHHCCCEECCCCCCC	39.72	19608861
68	Ubiquitination	QKNVQLYKMRNGYEL HHHCCCEECCCCCCC	39.72	21890473
70	Methylation	NVQLYKMRNGYELSP HCCCEECCCCCCCCH	29.30	115489393
73	Phosphorylation	LYKMRNGYELSPTAA CEECCCCCCCCHHHH	19.76	28152594
76	Phosphorylation	MRNGYELSPTAAANF CCCCCCCCHHHHHHC	14.31	26055452
78	Phosphorylation	NGYELSPTAAANFTR CCCCCCHHHHHHCCH	26.08	28122231
84	Phosphorylation	PTAAANFTRRNLADC HHHHHHCCHHCHHHH	28.64	25599653
86	Methylation	AAANFTRRNLADCLR HHHHCCHHCHHHHHH	39.18	115489401
91	S-nitrosocysteine	TRRNLADCLRSRTPY CHHCHHHHHHHCCCC	2.57	-
91	S-nitrosylation	TRRNLADCLRSRTPY CHHCHHHHHHHCCCC	2.57	19483679
93	Methylation	RNLADCLRSRTPYHV HCHHHHHHHCCCCEE	30.35	81452711
134	Phosphorylation	APFAAHGYGAFLTLS CCHHHCCCCEEHHHH	8.73	-
141	Phosphorylation	YGAFLTLSILDRYYT CCEEHHHHHHHHHCC	18.83	24719451
146	Phosphorylation	TLSILDRYYTPTISR HHHHHHHHCCCCCCH	16.03	20068231
147	Phosphorylation	LSILDRYYTPTISRE HHHHHHHCCCCCCHH	13.72	20090780
148	Phosphorylation	SILDRYYTPTISRER HHHHHHCCCCCCHHH	12.67	20068231
152	Phosphorylation	RYYTPTISRERAVEL HHCCCCCCHHHHHHH	30.48	20068231
161	Methylation	ERAVELLRKCLEELQ HHHHHHHHHHHHHHH	40.02	115489385
162	Malonylation	RAVELLRKCLEELQK HHHHHHHHHHHHHHH	43.04	26320211
162	Ubiquitination	RAVELLRKCLEELQK HHHHHHHHHHHHHHH	43.04	21890473
169	Acetylation	KCLEELQKRFILNLP HHHHHHHHHHHHCCC	63.00	25953088
169	Ubiquitination	KCLEELQKRFILNLP HHHHHHHHHHHHCCC	63.00	21890473
179	Phosphorylation	ILNLPTFSVRIIDKN HHCCCEEEEEEECCC	16.99	21712546
185	2-Hydroxyisobutyrylation	FSVRIIDKNGIHDLD EEEEEECCCCCCCCC	46.82	-
185	Ubiquitination	FSVRIIDKNGIHDLD EEEEEECCCCCCCCC	46.82	21906983
185	Acetylation	FSVRIIDKNGIHDLD EEEEEECCCCCCCCC	46.82	23749302
198	Sumoylation	LDNISFPKQGS---- CCCCCCCCCCC----	66.34	-
198	Ubiquitination	LDNISFPKQGS---- CCCCCCCCCCC----	66.34	21890473
198	Sumoylation	LDNISFPKQGS---- CCCCCCCCCCC----	66.34	-
201	Phosphorylation	ISFPKQGS------- CCCCCCCC-------	34.26	30624053

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 PSB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSB2_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 PSB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSB3_HUMAN	PSMB3	physical	14733938
PSB3_HUMAN	PSMB3	physical	17506986
PSB1_HUMAN	PSMB1	physical	17948026
PSB3_HUMAN	PSMB3	physical	17948026
PSB5_HUMAN	PSMB5	physical	17948026
PSB3_HUMAN	PSMB3	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSB5_HUMAN	PSMB5	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSME1_HUMAN	PSME1	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
RL40_HUMAN	UBA52	physical	22939629
RD23B_HUMAN	RAD23B	physical	22939629
THTR_HUMAN	TST	physical	22939629
UBE2A_HUMAN	UBE2A	physical	22939629
PYGB_HUMAN	PYGB	physical	22939629
YBOX1_HUMAN	YBX1	physical	22939629
RASH_HUMAN	HRAS	physical	22939629
SMCA2_HUMAN	SMARCA2	physical	22939629
TBB5_HUMAN	TUBB	physical	22939629
SMAP_HUMAN	C11orf58	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
SC23A_HUMAN	SEC23A	physical	22939629
VIME_HUMAN	VIM	physical	22939629
HXA2_HUMAN	HOXA2	physical	24244684
PSA1_HUMAN	PSMA1	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSA6_HUMAN	PSMA6	physical	22863883
PSA7_HUMAN	PSMA7	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB8_HUMAN	PSMB8	physical	22863883
P5CR3_HUMAN	PYCRL	physical	22863883
KCTD9_HUMAN	KCTD9	physical	25416956
ACACA_HUMAN	ACACA	physical	26344197
ASNA_HUMAN	ASNA1	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSMD4_HUMAN	PSMD4	physical	26344197
XPOT_HUMAN	XPOT	physical	26344197
PSB4_HUMAN	PSMB4	physical	28514442
PSME4_HUMAN	PSME4	physical	28514442
AKIR2_HUMAN	AKIRIN2	physical	28514442
PSB1_HUMAN	PSMB1	physical	28514442
PSB3_HUMAN	PSMB3	physical	28514442
PSB7_HUMAN	PSMB7	physical	28514442
PSMG2_HUMAN	PSMG2	physical	28514442
PSME2_HUMAN	PSME2	physical	28514442
POMP_HUMAN	POMP	physical	28514442
PSA1_HUMAN	PSMA1	physical	28514442
PSME1_HUMAN	PSME1	physical	28514442
PSMF1_HUMAN	PSMF1	physical	28514442
PSA3_HUMAN	PSMA3	physical	28514442
PSA7_HUMAN	PSMA7	physical	28514442
PSB5_HUMAN	PSMB5	physical	28514442
PSA2_HUMAN	PSMA2	physical	28514442
FBX7_HUMAN	FBXO7	physical	28514442
PSB6_HUMAN	PSMB6	physical	28514442
PSMG1_HUMAN	PSMG1	physical	28514442
PSA4_HUMAN	PSMA4	physical	28514442
PSA5_HUMAN	PSMA5	physical	28514442
PSA6_HUMAN	PSMA6	physical	28514442
PSD11_HUMAN	PSMD11	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
DB00188	Bortezomib
DB08889	Carfilzomib

Regulatory Network of PSB2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 MET-1, 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-68 AND LYS-185, AND MASSSPECTROMETRY.	19608861 [Abstract]