dbPTM

PSA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA5_HUMAN
UniProt AC	P28066
Protein Name	Proteasome subunit alpha type-5
Gene Name	PSMA5
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	MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MFLTRSEY -------CCCCHHHC	5.84	-
6	Phosphorylation	--MFLTRSEYDRGVN --CCCCHHHCCCCCC	34.96	21945579
8	Phosphorylation	MFLTRSEYDRGVNTF CCCCHHHCCCCCCCC	16.52	21945579
10	Methylation	LTRSEYDRGVNTFSP CCHHHCCCCCCCCCC	50.48	115489329
14	Phosphorylation	EYDRGVNTFSPEGRL HCCCCCCCCCCCCCE	24.08	21945579
16	Phosphorylation	DRGVNTFSPEGRLFQ CCCCCCCCCCCCEEE	21.72	29255136
20	Methylation	NTFSPEGRLFQVEYA CCCCCCCCEEEHHHH	30.57	115489321
26	Phosphorylation	GRLFQVEYAIEAIKL CCEEEHHHHHHHHHC	17.64	28796482
36	Phosphorylation	EAIKLGSTAIGIQTS HHHHCCCEEEEEECC	22.09	-
43	Phosphorylation	TAIGIQTSEGVCLAV EEEEEECCCCEEEEE	18.91	-
52	Ubiquitination	GVCLAVEKRITSPLM CEEEEEEECCCCCCC	42.37	-
55	Phosphorylation	LAVEKRITSPLMEPS EEEEECCCCCCCCCC	28.46	23927012
56	Phosphorylation	AVEKRITSPLMEPSS EEEECCCCCCCCCCH	17.42	19664994
59	Sulfoxidation	KRITSPLMEPSSIEK ECCCCCCCCCCHHHH	8.92	21406390
62	Phosphorylation	TSPLMEPSSIEKIVE CCCCCCCCHHHHHHE	30.55	30266825
63	Phosphorylation	SPLMEPSSIEKIVEI CCCCCCCHHHHHHEE	45.54	30266825
66	Ubiquitination	MEPSSIEKIVEIDAH CCCCHHHHHHEECHH	50.83	-
79	Phosphorylation	AHIGCAMSGLIADAK HHHHHHHHHHHHCHH	16.36	-
86	Ubiquitination	SGLIADAKTLIDKAR HHHHHCHHHHHHHHH	44.40	21890473
91	Acetylation	DAKTLIDKARVETQN CHHHHHHHHHHEEEC	30.97	23749302
91	Ubiquitination	DAKTLIDKARVETQN CHHHHHHHHHHEEEC	30.97	-
91	Malonylation	DAKTLIDKARVETQN CHHHHHHHHHHEEEC	30.97	26320211
149	Ubiquitination	LFGGVDEKGPQLFHM EECCCCCCCCCCEEE	72.00	-
149	Sumoylation	LFGGVDEKGPQLFHM EECCCCCCCCCCEEE	72.00	-
156	Sulfoxidation	KGPQLFHMDPSGTFV CCCCCEEECCCCCEE	6.76	30846556
159	Phosphorylation	QLFHMDPSGTFVQCD CCEEECCCCCEEEEC	46.32	30622161
161	Phosphorylation	FHMDPSGTFVQCDAR EEECCCCCEEEECCE	25.60	30622161
172	Phosphorylation	CDARAIGSASEGAQS ECCEEECCCCCHHHH	23.62	28258704
174	Phosphorylation	ARAIGSASEGAQSSL CEEECCCCCHHHHHH	37.96	-
179	Phosphorylation	SASEGAQSSLQEVYH CCCCHHHHHHHHHHH	32.27	23186163
180	Phosphorylation	ASEGAQSSLQEVYHK CCCHHHHHHHHHHHH	23.22	23186163
185	Phosphorylation	QSSLQEVYHKSMTLK HHHHHHHHHHCCCHH	11.63	28152594
187	Acetylation	SLQEVYHKSMTLKEA HHHHHHHHCCCHHHH	25.00	25953088
187	Ubiquitination	SLQEVYHKSMTLKEA HHHHHHHHCCCHHHH	25.00	21890473
187	Ubiquitination	SLQEVYHKSMTLKEA HHHHHHHHCCCHHHH	25.00	21890473
192	Succinylation	YHKSMTLKEAIKSSL HHHCCCHHHHHHHHH	35.61	23954790
192	Ubiquitination	YHKSMTLKEAIKSSL HHHCCCHHHHHHHHH	35.61	21890473
192	2-Hydroxyisobutyrylation	YHKSMTLKEAIKSSL HHHCCCHHHHHHHHH	35.61	-
192	Sumoylation	YHKSMTLKEAIKSSL HHHCCCHHHHHHHHH	35.61	-
192	Ubiquitination	YHKSMTLKEAIKSSL HHHCCCHHHHHHHHH	35.61	21890473
192	Sumoylation	YHKSMTLKEAIKSSL HHHCCCHHHHHHHHH	35.61	-
196	Ubiquitination	MTLKEAIKSSLIILK CCHHHHHHHHHHHHH	40.83	21890473
196	2-Hydroxyisobutyrylation	MTLKEAIKSSLIILK CCHHHHHHHHHHHHH	40.83	-
196	Sumoylation	MTLKEAIKSSLIILK CCHHHHHHHHHHHHH	40.83	-
196	Acetylation	MTLKEAIKSSLIILK CCHHHHHHHHHHHHH	40.83	25953088
196	Ubiquitination	MTLKEAIKSSLIILK CCHHHHHHHHHHHHH	40.83	21890473
196	Sumoylation	MTLKEAIKSSLIILK CCHHHHHHHHHHHHH	40.83	-
198	O-linked_Glycosylation	LKEAIKSSLIILKQV HHHHHHHHHHHHHHH	20.70	23301498
203	Sumoylation	KSSLIILKQVMEEKL HHHHHHHHHHHHHHH	30.36	-
203	Acetylation	KSSLIILKQVMEEKL HHHHHHHHHHHHHHH	30.36	25038526
203	Ubiquitination	KSSLIILKQVMEEKL HHHHHHHHHHHHHHH	30.36	21890473
203	Sumoylation	KSSLIILKQVMEEKL HHHHHHHHHHHHHHH	30.36	-
203	2-Hydroxyisobutyrylation	KSSLIILKQVMEEKL HHHHHHHHHHHHHHH	30.36	-
209	Ubiquitination	LKQVMEEKLNATNIE HHHHHHHHHCCCCEE	33.46	21890473
209	Acetylation	LKQVMEEKLNATNIE HHHHHHHHHCCCCEE	33.46	23954790
213	Phosphorylation	MEEKLNATNIELATV HHHHHCCCCEEEEEE	35.34	30622161
219	Phosphorylation	ATNIELATVQPGQNF CCCEEEEEECCCCCE	32.09	30622161
228	Sulfoxidation	QPGQNFHMFTKEELE CCCCCEECEEHHHHH	3.90	21406390
230	Phosphorylation	GQNFHMFTKEELEEV CCCEECEEHHHHHHH	29.94	30622161
231	Sumoylation	QNFHMFTKEELEEVI CCEECEEHHHHHHHH	37.62	-
231	Ubiquitination	QNFHMFTKEELEEVI CCEECEEHHHHHHHH	37.62	21890473
239	Ubiquitination	EELEEVIKDI----- HHHHHHHHCC-----	55.32	-
239	Acetylation	EELEEVIKDI----- HHHHHHHHCC-----	55.32	26822725
239	Succinylation	EELEEVIKDI----- HHHHHHHHCC-----	55.32	23954790

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 PSA5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA5_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 PSA5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLK1_HUMAN	PLK1	physical	11205743
PSA4_HUMAN	PSMA4	physical	15225636
PSA7_HUMAN	PSMA7	physical	15225636
PSN1_HUMAN	PSEN1	physical	10527805
A4_HUMAN	APP	physical	21832049
PSA7_HUMAN	PSMA7	physical	22939629
PSA6_HUMAN	PSMA6	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
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSME2_HUMAN	PSME2	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSA7L_HUMAN	PSMA8	physical	22939629
UBE2C_HUMAN	UBE2C	physical	22939629
UBQL1_HUMAN	UBQLN1	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
SH3L1_HUMAN	SH3BGRL	physical	22939629
TYSY_HUMAN	TYMS	physical	22939629
SRXN1_HUMAN	SRXN1	physical	22939629
SC24C_HUMAN	SEC24C	physical	22939629
RT16_HUMAN	MRPS16	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
SYAP1_HUMAN	SYAP1	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
TCPG_HUMAN	CCT3	physical	22939629
UB2L3_HUMAN	UBE2L3	physical	22939629
RT07_HUMAN	MRPS7	physical	22939629
PSME4_HUMAN	PSME4	physical	22863883
CLIC1_HUMAN	CLIC1	physical	26344197
CLIC4_HUMAN	CLIC4	physical	26344197
DCTN2_HUMAN	DCTN2	physical	26344197
DDX23_HUMAN	DDX23	physical	26344197
EXOS4_HUMAN	EXOSC4	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
HEAT1_HUMAN	HEATR1	physical	26344197
ECM29_HUMAN	KIAA0368	physical	26344197
NELFE_HUMAN	NELFE	physical	26344197
PEX19_HUMAN	PEX19	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
PEPL_HUMAN	PPL	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	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
PSD13_HUMAN	PSMD13	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
PSMG2_HUMAN	PSMG2	physical	26344197
SRSF2_HUMAN	SRSF2	physical	26344197
U2AF2_HUMAN	U2AF2	physical	26344197
SAE2_HUMAN	UBA2	physical	26344197

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 PSA5_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 MET-1, AND MASS SPECTROMETRY.	17323924 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-55 AND SER-56,AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-16 AND THR-55, 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-16 AND SER-56, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.	17924679 [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-16, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY.	15302935 [Abstract]