dbPTM

PSA7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA7_HUMAN
UniProt AC	O14818
Protein Name	Proteasome subunit alpha type-7
Gene Name	PSMA7
Organism	Homo sapiens (Human).
Sequence Length	248
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). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response..
Protein Sequence	MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYDRAITV ------CCCCEEEEE	35.42	28464451
2	Acetylation	------MSYDRAITV ------CCCCEEEEE	35.42	-
3	Phosphorylation	-----MSYDRAITVF -----CCCCEEEEEE	14.24	26074081
8	Phosphorylation	MSYDRAITVFSPDGH CCCCEEEEEECCCCC	17.95	30266825
11	Phosphorylation	DRAITVFSPDGHLFQ CEEEEEECCCCCEEE	20.11	30266825
21	Phosphorylation	GHLFQVEYAQEAVKK CCEEEHHHHHHHHHH	18.09	30266825
27	Ubiquitination	EYAQEAVKKGSTAVG HHHHHHHHHCCCEEE	59.47	21890473
27	Acetylation	EYAQEAVKKGSTAVG HHHHHHHHHCCCEEE	59.47	25953088
27	Ubiquitination	EYAQEAVKKGSTAVG HHHHHHHHHCCCEEE	59.47	-
28	Ubiquitination	YAQEAVKKGSTAVGV HHHHHHHHCCCEEEC	52.04	21906983
28 (in isoform 1)	Ubiquitination	-	52.04	21890473
30	Phosphorylation	QEAVKKGSTAVGVRG HHHHHHCCCEEECCC	23.28	20068231
31	Phosphorylation	EAVKKGSTAVGVRGR HHHHHCCCEEECCCC	33.75	20068231
45 (in isoform 2)	Ubiquitination	-	9.48	21890473
47	Ubiquitination	IVVLGVEKKSVAKLQ EEEEEECCCCHHHCC	48.19	-
48	Ubiquitination	VVLGVEKKSVAKLQD EEEEECCCCHHHCCC	36.34	-
49	Phosphorylation	VLGVEKKSVAKLQDE EEEECCCCHHHCCCH	38.07	24719451
52 (in isoform 1)	Ubiquitination	-	44.52	21890473
52	Malonylation	VEKKSVAKLQDERTV ECCCCHHHCCCHHHH	44.52	26320211
52	Acetylation	VEKKSVAKLQDERTV ECCCCHHHCCCHHHH	44.52	23749302
52	Ubiquitination	VEKKSVAKLQDERTV ECCCCHHHCCCHHHH	44.52	21906983
52	Sumoylation	VEKKSVAKLQDERTV ECCCCHHHCCCHHHH	44.52	-
52	Sumoylation	VEKKSVAKLQDERTV ECCCCHHHCCCHHHH	44.52	-
71	Sulfoxidation	ALDDNVCMAFAGLTA ECCCCEEEHHCCCCC	2.75	30846556
77	Phosphorylation	CMAFAGLTADARIVI EEHHCCCCCCEEEEE	22.90	28348404
87 (in isoform 2)	Ubiquitination	-	18.51	21890473
93	O-linked_Glycosylation	RARVECQSHRLTVED HHHHEEECCCEECCC	23.41	28510447
97	Phosphorylation	ECQSHRLTVEDPVTV EEECCCEECCCCCHH	23.08	29759185
103	Phosphorylation	LTVEDPVTVEYITRY EECCCCCHHHHHHHH	17.01	28152594
104 (in isoform 2)	Ubiquitination	-	5.53	21890473
106	Phosphorylation	EDPVTVEYITRYIAS CCCCHHHHHHHHHHH	11.85	28152594
108	Phosphorylation	PVTVEYITRYIASLK CCHHHHHHHHHHHHH	19.27	28152594
110	Phosphorylation	TVEYITRYIASLKQR HHHHHHHHHHHHHHH	7.68	23312004
113	Phosphorylation	YITRYIASLKQRYTQ HHHHHHHHHHHHHHH	26.92	20068231
115 (in isoform 1)	Ubiquitination	-	30.18	21890473
115	Ubiquitination	TRYIASLKQRYTQSN HHHHHHHHHHHHHCC	30.18	21890473
115	Acetylation	TRYIASLKQRYTQSN HHHHHHHHHHHHHCC	30.18	25953088
130	O-linked_Glycosylation	GRRPFGISALIVGFD CCCCCCEEEEEEEEC	19.87	UniProtKB CARBOHYD
134 (in isoform 2)	Ubiquitination	-	6.95	21890473
145	Phosphorylation	FDGTPRLYQTDPSGT CCCCCCEEEECCCCC	15.62	21945579
148 (in isoform 2)	Ubiquitination	-	21.60	21890473
150	Phosphorylation	RLYQTDPSGTYHAWK CEEEECCCCCCEEHH	46.72	21945579
152	Phosphorylation	YQTDPSGTYHAWKAN EEECCCCCCEEHHHC	19.23	21945579
153	Phosphorylation	QTDPSGTYHAWKANA EECCCCCCEEHHHCC	7.96	21945579
157	2-Hydroxyisobutyrylation	SGTYHAWKANAIGRG CCCCEEHHHCCCCCC	32.33	-
157 (in isoform 1)	Ubiquitination	-	32.33	21890473
157 (in isoform 2)	Ubiquitination	-	32.33	21890473
157	Methylation	SGTYHAWKANAIGRG CCCCEEHHHCCCCCC	32.33	22361341
157	Ubiquitination	SGTYHAWKANAIGRG CCCCEEHHHCCCCCC	32.33	22053931
157	Acetylation	SGTYHAWKANAIGRG CCCCEEHHHCCCCCC	32.33	22361341
163	Methylation	WKANAIGRGAKSVRE HHHCCCCCCHHHHHH	35.46	54558343
167	Phosphorylation	AIGRGAKSVREFLEK CCCCCHHHHHHHHHH	26.35	-
169	Methylation	GRGAKSVREFLEKNY CCCHHHHHHHHHHCC	35.72	115489369
174	Ubiquitination	SVREFLEKNYTDEAI HHHHHHHHCCCCCCC	58.35	22053931
174	Acetylation	SVREFLEKNYTDEAI HHHHHHHHCCCCCCC	58.35	26051181
174 (in isoform 1)	Ubiquitination	-	58.35	21890473
176	Phosphorylation	REFLEKNYTDEAIET HHHHHHCCCCCCCCC	27.00	28152594
177	Phosphorylation	EFLEKNYTDEAIETD HHHHHCCCCCCCCCC	36.44	-
183	Phosphorylation	YTDEAIETDDLTIKL CCCCCCCCCCHHHHH	28.80	-
193	Ubiquitination	LTIKLVIKALLEVVQ HHHHHHHHHHHHHHH	26.04	-
201	Phosphorylation	ALLEVVQSGGKNIEL HHHHHHHCCCCEEEE	37.59	30266825
204	Ubiquitination	EVVQSGGKNIELAVM HHHHCCCCEEEEEEE	59.27	21906983
204 (in isoform 1)	Ubiquitination	-	59.27	21890473
211	Sulfoxidation	KNIELAVMRRDQSLK CEEEEEEEECCCCCC	2.12	21406390
212	Methylation	NIELAVMRRDQSLKI EEEEEEEECCCCCCC	32.21	115489361
216	Phosphorylation	AVMRRDQSLKILNPE EEEECCCCCCCCCHH	35.60	29514088
218	Ubiquitination	MRRDQSLKILNPEEI EECCCCCCCCCHHHH	50.85	21890473
218 (in isoform 1)	Ubiquitination	-	50.85	21890473
218	Acetylation	MRRDQSLKILNPEEI EECCCCCCCCCHHHH	50.85	25953088
218	2-Hydroxyisobutyrylation	MRRDQSLKILNPEEI EECCCCCCCCCHHHH	50.85	-
227	Acetylation	LNPEEIEKYVAEIEK CCHHHHHHHHHHHHH	51.16	19608861
227	Ubiquitination	LNPEEIEKYVAEIEK CCHHHHHHHHHHHHH	51.16	22053931
227 (in isoform 1)	Ubiquitination	-	51.16	21890473
234	Succinylation	KYVAEIEKEKEENEK HHHHHHHHHHHHHHH	78.66	23954790
234	Acetylation	KYVAEIEKEKEENEK HHHHHHHHHHHHHHH	78.66	23749302
234	Ubiquitination	KYVAEIEKEKEENEK HHHHHHHHHHHHHHH	78.66	-
236	Acetylation	VAEIEKEKEENEKKK HHHHHHHHHHHHHHH	79.84	25953088

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
106	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
153	Y	Phosphorylation	Kinase	ABL	P00519	PSP
153	Y	Phosphorylation	Kinase	ARG	P42684	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:25620702

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA7_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 PSA7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HIF1A_HUMAN	HIF1A	physical	11389899
CUL1_HUMAN	CUL1	physical	16759355
RAB7A_HUMAN	RAB7A	physical	14998988
PSA3_HUMAN	PSMA3	physical	21900206
PSA2_HUMAN	PSMA2	physical	21900206
HIF1A_HUMAN	HIF1A	physical	18313384
PSMD1_HUMAN	PSMD1	physical	15221960
PSMD6_HUMAN	PSMD6	physical	15221960
PSMD7_HUMAN	PSMD7	physical	15221960
PSA6_HUMAN	PSMA6	physical	15225636
PSA1_HUMAN	PSMA1	physical	15225636
PSA3_HUMAN	PSMA3	physical	15225636
PSA4_HUMAN	PSMA4	physical	15225636
CANB1_HUMAN	PPP3R1	physical	21256111
MAVS_HUMAN	MAVS	physical	19734229
PSMD4_HUMAN	PSMD4	physical	16678104
ABL1_HUMAN	ABL1	physical	16678104
PSB9_HUMAN	PSMB9	physical	17948026
PSA6_HUMAN	PSMA6	physical	17948026
PSA7_HUMAN	PSMA7	physical	17948026
ECSCR_HUMAN	ECSCR	physical	19416853
A4_HUMAN	APP	physical	21832049
PSD13_HUMAN	PSMD13	physical	22939629
PSB1_HUMAN	PSMB1	physical	22939629
PSB2_HUMAN	PSMB2	physical	22939629
PSB3_HUMAN	PSMB3	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSB5_HUMAN	PSMB5	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
PSME1_HUMAN	PSME1	physical	22939629
SAMD1_HUMAN	SAMD1	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
SPTB2_HUMAN	SPTBN1	physical	22939629
RBM3_HUMAN	RBM3	physical	22939629
RT16_HUMAN	MRPS16	physical	22939629
PR39_PIG	PR39	physical	10930447
NOD1_HUMAN	NOD1	physical	23839082
PSMF1_HUMAN	PSMF1	physical	21988832
TERA_HUMAN	VCP	physical	21988832
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB4_HUMAN	PSMB4	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSB6_HUMAN	PSMB6	physical	22863883
PSB7_HUMAN	PSMB7	physical	22863883
P5CR3_HUMAN	PYCRL	physical	22863883
ADRM1_HUMAN	ADRM1	physical	26344197
EXOS9_HUMAN	EXOSC9	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
PSB7_HUMAN	PSMB7	physical	26344197
PSB8_HUMAN	PSMB8	physical	26344197
PSB9_HUMAN	PSMB9	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
PSD11_HUMAN	PSMD11	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
PSMD7_HUMAN	PSMD7	physical	26344197
BRCA1_HUMAN	BRCA1	physical	25620702
ABL1_HUMAN	ABL1	physical	25620702
PSA6_HUMAN	PSMA6	physical	26657688
RMD5B_HUMAN	RMND5B	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
There are no disease associations of PTM sites.

Regulatory Network of PSA7_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-227, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Interaction between c-Abl and Arg tyrosine kinases and proteasomesubunit PSMA7 regulates proteasome degradation."; Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q.,Cao C.; Mol. Cell 22:317-327(2006). Cited for: INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-153 BY ABL1 ANDABL2, AND MUTAGENESIS OF TYR-153.	16678104 [Abstract]