dbPTM

PSA4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA4_HUMAN
UniProt AC	P25789
Protein Name	Proteasome subunit alpha type-4
Gene Name	PSMA4
Organism	Homo sapiens (Human).
Sequence Length	261
Subcellular Localization	Cytoplasm . Nucleus . Colocalizes with TRIM5 in the cytoplasmic bodies.
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	MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRRYDSRT ------CCCCCCCCC	26.01	26074081
5	Phosphorylation	---MSRRYDSRTTIF ---CCCCCCCCCEEE	19.70	28555341
7	Phosphorylation	-MSRRYDSRTTIFSP -CCCCCCCCCEEECC	23.69	30622161
9	Phosphorylation	SRRYDSRTTIFSPEG CCCCCCCCEEECCCC	28.35	23927012
10	Phosphorylation	RRYDSRTTIFSPEGR CCCCCCCEEECCCCC	20.93	23927012
13	Phosphorylation	DSRTTIFSPEGRLYQ CCCCEEECCCCCEEE	20.42	19664994
54	Acetylation	AERRNIHKLLDEVFF HHHCCHHHHHHHHHH	47.12	25953088
54	Ubiquitination	AERRNIHKLLDEVFF HHHCCHHHHHHHHHH	47.12	21890473
54	2-Hydroxyisobutyrylation	AERRNIHKLLDEVFF HHHCCHHHHHHHHHH	47.12	-
56	Acetylation	RRNIHKLLDEVFFSE HCCHHHHHHHHHHCH	6.69	19608861
56	Ubiquitination	RRNIHKLLDEVFFSE HCCHHHHHHHHHHCH	6.69	19608861
62	Phosphorylation	LLDEVFFSEKIYKLN HHHHHHHCHHHHHCC	26.90	21712546
64	Ubiquitination	DEVFFSEKIYKLNED HHHHHCHHHHHCCCC	50.57	21890473
64	2-Hydroxyisobutyrylation	DEVFFSEKIYKLNED HHHHHCHHHHHCCCC	50.57	-
67	Ubiquitination	FFSEKIYKLNEDMAC HHCHHHHHCCCCCCC	48.59	21906983
72	Sulfoxidation	IYKLNEDMACSVAGI HHHCCCCCCCHHHCC	3.10	30846556
74	Glutathionylation	KLNEDMACSVAGITS HCCCCCCCHHHCCCC	2.42	22555962
75	Phosphorylation	LNEDMACSVAGITSD CCCCCCCHHHCCCCC	12.88	20068231
80	Phosphorylation	ACSVAGITSDANVLT CCHHHCCCCCHHHHH	21.45	20068231
81	Phosphorylation	CSVAGITSDANVLTN CHHHCCCCCHHHHHH	32.57	20068231
87	Phosphorylation	TSDANVLTNELRLIA CCCHHHHHHHHHHHH	23.51	20068231
105	Ubiquitination	LLQYQEPIPCEQLVT HHHCCCCCCHHHHHH	6.32	19608861
105	Acetylation	LLQYQEPIPCEQLVT HHHCCCCCCHHHHHH	6.32	19608861
105	Ubiquitination	LLQYQEPIPCEQLVT HHHCCCCCCHHHHHH	6.32	21890473
121	Phosphorylation	LCDIKQAYTQFGGKR HHHHHHHHHHHCCCC	9.89	28152594
122	Phosphorylation	CDIKQAYTQFGGKRP HHHHHHHHHHCCCCC	22.04	28152594
127	Ubiquitination	AYTQFGGKRPFGVSL HHHHHCCCCCCCEEE	58.22	19608861
127	Sumoylation	AYTQFGGKRPFGVSL HHHHHCCCCCCCEEE	58.22	19608861
127	Acetylation	AYTQFGGKRPFGVSL HHHHHCCCCCCCEEE	58.22	19608861
128	Ubiquitination	YTQFGGKRPFGVSLL HHHHCCCCCCCEEEE	34.75	21890473
134	Ubiquitination	KRPFGVSLLYIGWDK CCCCCEEEEEEEECC	3.80	21890473
139	Ubiquitination	VSLLYIGWDKHYGFQ EEEEEEEECCCCCEE	11.26	21890473
143	Phosphorylation	YIGWDKHYGFQLYQS EEEECCCCCEEEEEC	25.94	-
148	Phosphorylation	KHYGFQLYQSDPSGN CCCCEEEEECCCCCC	8.66	29496907
156	Phosphorylation	QSDPSGNYGGWKATC ECCCCCCCCCEEEEE	22.12	29496907
160	Sumoylation	SGNYGGWKATCIGNN CCCCCCEEEEEECCC	36.77	-
160	Ubiquitination	SGNYGGWKATCIGNN CCCCCCEEEEEECCC	36.77	-
160	Acetylation	SGNYGGWKATCIGNN CCCCCCEEEEEECCC	36.77	68717
160	Ubiquitination	SGNYGGWKATCIGNN CCCCCCEEEEEECCC	36.77	21890473
162	Phosphorylation	NYGGWKATCIGNNSA CCCCEEEEEECCCHH	10.83	21406692
167	Ubiquitination	KATCIGNNSAAAVSM EEEEECCCHHHHHHH	28.01	19608861
167	Ubiquitination	KATCIGNNSAAAVSM EEEEECCCHHHHHHH	28.01	21890473
167	Acetylation	KATCIGNNSAAAVSM EEEEECCCHHHHHHH	28.01	19608861
168	Phosphorylation	ATCIGNNSAAAVSML EEEECCCHHHHHHHH	24.24	21406692
173	Phosphorylation	NNSAAAVSMLKQDYK CCHHHHHHHHHCCHH	17.42	25159151
174	Sulfoxidation	NSAAAVSMLKQDYKE CHHHHHHHHHCCHHH	4.33	21406390
176	Acetylation	AAAVSMLKQDYKEGE HHHHHHHHCCHHHCC	32.26	19608861
176	Ubiquitination	AAAVSMLKQDYKEGE HHHHHHHHCCHHHCC	32.26	21890473
180	Succinylation	SMLKQDYKEGEMTLK HHHHCCHHHCCCCHH	68.48	23954790
180	Acetylation	SMLKQDYKEGEMTLK HHHHCCHHHCCCCHH	68.48	25953088
180	Ubiquitination	SMLKQDYKEGEMTLK HHHHCCHHHCCCCHH	68.48	-
187	Ubiquitination	KEGEMTLKSALALAI HHCCCCHHHHHHHHH	25.23	21906983
188	Phosphorylation	EGEMTLKSALALAIK HCCCCHHHHHHHHHH	31.46	23312004
195	2-Hydroxyisobutyrylation	SALALAIKVLNKTMD HHHHHHHHHHHCCCC	34.75	-
195	Acetylation	SALALAIKVLNKTMD HHHHHHHHHHHCCCC	34.75	25953088
195	Ubiquitination	SALALAIKVLNKTMD HHHHHHHHHHHCCCC	34.75	-
199	Acetylation	LAIKVLNKTMDVSKL HHHHHHHCCCCHHHH	40.85	26822725
199	Ubiquitination	LAIKVLNKTMDVSKL HHHHHHHCCCCHHHH	40.85	21890473
205	2-Hydroxyisobutyrylation	NKTMDVSKLSAEKVE HCCCCHHHHCHHHEE	46.43	-
205	Ubiquitination	NKTMDVSKLSAEKVE HCCCCHHHHCHHHEE	46.43	21906983
205	Acetylation	NKTMDVSKLSAEKVE HCCCCHHHHCHHHEE	46.43	25953088
207	Phosphorylation	TMDVSKLSAEKVEIA CCCHHHHCHHHEEEE	37.81	26091039
210	Ubiquitination	VSKLSAEKVEIATLT HHHHCHHHEEEEEEE	44.90	21890473
210	Acetylation	VSKLSAEKVEIATLT HHHHCHHHEEEEEEE	44.90	23749302
215	Phosphorylation	AEKVEIATLTRENGK HHHEEEEEEEECCCE	34.03	21406692
217	Phosphorylation	KVEIATLTRENGKTV HEEEEEEEECCCEEE	31.42	21406692
222	Ubiquitination	TLTRENGKTVIRVLK EEEECCCEEEEEEEC	51.72	-
222	Acetylation	TLTRENGKTVIRVLK EEEECCCEEEEEEEC	51.72	25953088
223	Phosphorylation	LTRENGKTVIRVLKQ EEECCCEEEEEEECH	23.67	-
229	Ubiquitination	KTVIRVLKQKEVEQL EEEEEEECHHHHHHH	57.37	-
231	Ubiquitination	VIRVLKQKEVEQLIK EEEEECHHHHHHHHH	63.24	21890473
231	Malonylation	VIRVLKQKEVEQLIK EEEEECHHHHHHHHH	63.24	26320211
231	Acetylation	VIRVLKQKEVEQLIK EEEEECHHHHHHHHH	63.24	23749302
238	Ubiquitination	KEVEQLIKKHEEEEA HHHHHHHHHHHHHHH	57.58	21906983
238	Acetylation	KEVEQLIKKHEEEEA HHHHHHHHHHHHHHH	57.58	19608861
246	Ubiquitination	KHEEEEAKAEREKKE HHHHHHHHHHHHHHH	54.80	2190698

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 PSA4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA4_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 PSA4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLK1_HUMAN	PLK1	physical	11205743
CUL1_HUMAN	CUL1	physical	16759355
PSA6_HUMAN	PSMA6	physical	16759355
PRKN_RAT	Park2	physical	15987638
PRKN_HUMAN	PARK2	physical	15987638
PSA7_HUMAN	PSMA7	physical	15225636
PSA3_HUMAN	PSMA3	physical	15225636
PSA5_HUMAN	PSMA5	physical	15225636
PSA6_HUMAN	PSMA6	physical	15225636
PSA2_HUMAN	PSMA2	physical	14733938
PSA3_HUMAN	PSMA3	physical	14733938
PSA7_HUMAN	PSMA7	physical	14733938
PSA1_HUMAN	PSMA1	physical	9311996
PSA2_HUMAN	PSMA2	physical	9311996
PSA3_HUMAN	PSMA3	physical	9311996
PSA5_HUMAN	PSMA5	physical	9311996
PSA6_HUMAN	PSMA6	physical	9311996
PSA7_HUMAN	PSMA7	physical	9311996
PSB1_HUMAN	PSMB1	physical	9311996
PSB4_HUMAN	PSMB4	physical	9311996
PSB5_HUMAN	PSMB5	physical	9311996
PSB6_HUMAN	PSMB6	physical	9311996
PSB7_HUMAN	PSMB7	physical	9311996
PSB8_HUMAN	PSMB8	physical	9311996
PSB9_HUMAN	PSMB9	physical	9311996
IKBA_HUMAN	NFKBIA	physical	9875328
NFKB1_HUMAN	NFKB1	physical	8692272
PSA7_HUMAN	PSMA7	physical	17948026
PSB8_HUMAN	PSMB8	physical	15303969
PSA6_HUMAN	PSMA6	physical	22939629
PSA5_HUMAN	PSMA5	physical	22939629
PSA7_HUMAN	PSMA7	physical	22939629
PSB7_HUMAN	PSMB7	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
PSB8_HUMAN	PSMB8	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
PSA7L_HUMAN	PSMA8	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
YBOX1_HUMAN	YBX1	physical	22939629
TERA_HUMAN	VCP	physical	22939629
AP3M1_HUMAN	AP3M1	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB2_HUMAN	PSMB2	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSME4_HUMAN	PSME4	physical	22863883
P5CR3_HUMAN	PYCRL	physical	22863883
IKZF1_HUMAN	IKZF1	physical	25416956
CCAR2_HUMAN	CCAR2	physical	26344197
ELP6_HUMAN	ELP6	physical	26344197
EXOS4_HUMAN	EXOSC4	physical	26344197
EXOS5_HUMAN	EXOSC5	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PRS10_HUMAN	PSMC6	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD3_HUMAN	PSMD3	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
PSMD8_HUMAN	PSMD8	physical	26344197
RAN_HUMAN	RAN	physical	26344197
U2AF2_HUMAN	U2AF2	physical	26344197
TERA_HUMAN	VCP	physical	26344197
WDR11_HUMAN	WDR11	physical	26344197
HIF1A_HUMAN	HIF1A	physical	27918549

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 PSA4_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-127; LYS-176 AND LYS-238,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	18691976 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.	17323924 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	16964243 [Abstract]