dbPTM

PSB7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSB7_HUMAN
UniProt AC	Q99436
Protein Name	Proteasome subunit beta type-7
Gene Name	PSMB7
Organism	Homo sapiens (Human).
Sequence Length	277
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). Within the 20S core complex, PSMB7 displays a trypsin-like activity..
Protein Sequence	MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAAVSVYAPPVG ---CCEEEEECCCCC	12.51	-
7	Phosphorylation	-MAAVSVYAPPVGGF -CCEEEEECCCCCCC	13.09	-
31	Ubiquitination	VLEADFAKRGYKLPK HHHHHHHHCCCCCCC	46.48	21890473
31	Acetylation	VLEADFAKRGYKLPK HHHHHHHHCCCCCCC	46.48	25953088
31	Ubiquitination	VLEADFAKRGYKLPK HHHHHHHHCCCCCCC	46.48	21890473
41	Ubiquitination	YKLPKVRKTGTTIAG CCCCCEECCCCEEEE	55.05	-
41	Ubiquitination	YKLPKVRKTGTTIAG CCCCCEECCCCEEEE	55.05	-
42	Phosphorylation	KLPKVRKTGTTIAGV CCCCEECCCCEEEEE	29.24	22199227
44	Phosphorylation	PKVRKTGTTIAGVVY CCEECCCCEEEEEEE	21.91	22199227
45	Phosphorylation	KVRKTGTTIAGVVYK CEECCCCEEEEEEEC	15.35	22199227
51	Phosphorylation	TTIAGVVYKDGIVLG CEEEEEEECCCEEEE	10.85	-
52	Ubiquitination	TIAGVVYKDGIVLGA EEEEEEECCCEEEEC	37.56	21890473
52	Ubiquitination	TIAGVVYKDGIVLGA EEEEEEECCCEEEEC	37.56	21890473
67	Sulfoxidation	DTRATEGMVVADKNC CCCCCCCCEEECCCC	1.46	21406390
72	Acetylation	EGMVVADKNCSKIHF CCCEEECCCCCEEEE	50.55	25953088
72	Ubiquitination	EGMVVADKNCSKIHF CCCEEECCCCCEEEE	50.55	21890473
72	2-Hydroxyisobutyrylation	EGMVVADKNCSKIHF CCCEEECCCCCEEEE	50.55	-
72	Ubiquitination	EGMVVADKNCSKIHF CCCEEECCCCCEEEE	50.55	21890473
76	Ubiquitination	VADKNCSKIHFISPN EECCCCCEEEEECCC	42.26	-
76	Ubiquitination	VADKNCSKIHFISPN EECCCCCEEEEECCC	42.26	-
110	Phosphorylation	SSNLELHSLSTGRLP HCCCEEEECCCCCCC	36.32	24275569
127	Ubiquitination	VTANRMLKQMLFRYQ HCHHHHHHHHHHHHC	25.07	21890473
127	Acetylation	VTANRMLKQMLFRYQ HCHHHHHHHHHHHHC	25.07	25953088
127	Ubiquitination	VTANRMLKQMLFRYQ HCHHHHHHHHHHHHC	25.07	21890473
138 (in isoform 2)	Phosphorylation	-	9.05	26270265
154	Phosphorylation	DVTGPHLYSIYPHGS CCCCCCEEEECCCCC	7.03	22817900
189	Sulfoxidation	EDKFRPDMEEEEAKN HCCCCCCCCHHHHHH	8.49	21406390
225	Acetylation	LCVISKNKLDFLRPY EEEEECCCCCEECCC	53.85	25953088
225	Ubiquitination	LCVISKNKLDFLRPY EEEEECCCCCEECCC	53.85	21890473
232	Phosphorylation	KLDFLRPYTVPNKKG CCCEECCCCCCCCCC	17.59	28152594
233	Phosphorylation	LDFLRPYTVPNKKGT CCEECCCCCCCCCCC	31.97	28152594
237	Acetylation	RPYTVPNKKGTRLGR CCCCCCCCCCCEEEE	46.65	25953088
237	Malonylation	RPYTVPNKKGTRLGR CCCCCCCCCCCEEEE	46.65	26320211
237	Ubiquitination	RPYTVPNKKGTRLGR CCCCCCCCCCCEEEE	46.65	-
238	Ubiquitination	PYTVPNKKGTRLGRY CCCCCCCCCCEEEEE	72.63	-
249	Ubiquitination	LGRYRCEKGTTAVLT EEEEECCCCCEEEEE	66.25	21890473
249	Acetylation	LGRYRCEKGTTAVLT EEEEECCCCCEEEEE	66.25	25953088
251	Phosphorylation	RYRCEKGTTAVLTEK EEECCCCCEEEEECC	23.73	26074081
252	Phosphorylation	YRCEKGTTAVLTEKI EECCCCCEEEEECCC	24.36	26074081
256	Phosphorylation	KGTTAVLTEKITPLE CCCEEEEECCCCCHH	28.74	26074081
270	Phosphorylation	EIEVLEETVQTMDTS HHHHHHHHHHHCCCC	14.45	29514088
273	Phosphorylation	VLEETVQTMDTS--- HHHHHHHHCCCC---	16.81	20068231
274	Sulfoxidation	LEETVQTMDTS---- HHHHHHHCCCC----	2.71	21406390
276	Phosphorylation	ETVQTMDTS------ HHHHHCCCC------	26.05	30278072
277	Phosphorylation	TVQTMDTS------- HHHHCCCC-------	33.68	30278072

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 PSB7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSB7_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 PSB7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSB3_HUMAN	PSMB3	physical	14733938
POMP_HUMAN	POMP	physical	14733938
PSB5_HUMAN	PSMB5	physical	14733938
PSB1_HUMAN	PSMB1	physical	17948026
PSB3_HUMAN	PSMB3	physical	17948026
PSB6_HUMAN	PSMB6	physical	17948026
PSB7_HUMAN	PSMB7	physical	17948026
PSA7L_HUMAN	PSMA8	physical	17948026
POMP_HUMAN	POMP	physical	17948026
PSB9_HUMAN	PSMB9	physical	17948026
PSB8_HUMAN	PSMB8	physical	16423992
PSB9_HUMAN	PSMB9	physical	16423992
PSA4_HUMAN	PSMA4	physical	16423992
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
UB2D1_HUMAN	UBE2D1	physical	22939629
RD23B_HUMAN	RAD23B	physical	22939629
SYAP1_HUMAN	SYAP1	physical	22939629
SMAP_HUMAN	C11orf58	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
TMOD3_HUMAN	TMOD3	physical	22939629
PSMD1_HUMAN	PSMD1	physical	20723761
PSA4_HUMAN	PSMA4	physical	20723761
ICAL_HUMAN	CAST	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
PSB2_HUMAN	PSMB2	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSB6_HUMAN	PSMB6	physical	22863883
PSA2_HUMAN	PSMA2	physical	26186194
PSA3_HUMAN	PSMA3	physical	26186194
PSB1_HUMAN	PSMB1	physical	26186194
PSA6_HUMAN	PSMA6	physical	26186194
PSME4_HUMAN	PSME4	physical	26186194
PSA7L_HUMAN	PSMA8	physical	26186194
PSA7_HUMAN	PSMA7	physical	26186194
PSD11_HUMAN	PSMD11	physical	26186194
PRS10_HUMAN	PSMC6	physical	26186194
PSB2_HUMAN	PSMB2	physical	26186194
PSME1_HUMAN	PSME1	physical	26186194
PSA4_HUMAN	PSMA4	physical	26186194
NAA25_HUMAN	NAA25	physical	26186194
PSD12_HUMAN	PSMD12	physical	26186194
FBX7_HUMAN	FBXO7	physical	26186194
POMP_HUMAN	POMP	physical	26186194
PSA5_HUMAN	PSMA5	physical	26186194
PSB5_HUMAN	PSMB5	physical	26186194
PSB6_HUMAN	PSMB6	physical	26186194
PSB3_HUMAN	PSMB3	physical	26186194
PSME2_HUMAN	PSME2	physical	26186194
PSMG1_HUMAN	PSMG1	physical	26186194
PSMG3_HUMAN	PSMG3	physical	26186194
PSMF1_HUMAN	PSMF1	physical	26186194
PSB9_HUMAN	PSMB9	physical	26186194
ADRM1_HUMAN	ADRM1	physical	26344197
CLIC4_HUMAN	CLIC4	physical	26344197
HUWE1_HUMAN	HUWE1	physical	26344197
RPAC1_HUMAN	POLR1C	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
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
PSB8_HUMAN	PSMB8	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
PRS6A_HUMAN	PSMC3	physical	26344197
PRS6B_HUMAN	PSMC4	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
PYGL_HUMAN	PYGL	physical	26344197
RD23A_HUMAN	RAD23A	physical	26344197
PSA7L_HUMAN	PSMA8	physical	28514442
NAA25_HUMAN	NAA25	physical	28514442
PSB9_HUMAN	PSMB9	physical	28514442
PSME4_HUMAN	PSME4	physical	28514442
POMP_HUMAN	POMP	physical	28514442
PSME2_HUMAN	PSME2	physical	28514442
PSMF1_HUMAN	PSMF1	physical	28514442
PSME1_HUMAN	PSME1	physical	28514442
FBX7_HUMAN	FBXO7	physical	28514442
PSA2_HUMAN	PSMA2	physical	28514442
PSMG1_HUMAN	PSMG1	physical	28514442
PSB5_HUMAN	PSMB5	physical	28514442
PSA3_HUMAN	PSMA3	physical	28514442
PSA6_HUMAN	PSMA6	physical	28514442
PSA7_HUMAN	PSMA7	physical	28514442
PSA4_HUMAN	PSMA4	physical	28514442
PSA5_HUMAN	PSMA5	physical	28514442
PSB6_HUMAN	PSMB6	physical	28514442
PSMG3_HUMAN	PSMG3	physical	28514442
PSD11_HUMAN	PSMD11	physical	28514442
PSMD3_HUMAN	PSMD3	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 PSB7_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASSSPECTROMETRY.	15592455 [Abstract]