dbPTM

PRS8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRS8_HUMAN
UniProt AC	P62195
Protein Name	26S proteasome regulatory subunit 8
Gene Name	PSMC5
Organism	Homo sapiens (Human).
Sequence Length	406
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides..
Protein Sequence	MALDGPEQMELEEGKAGSGLRQYYLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1 (in isoform 2)	Acetylation	-	8.24	22814378
2	Acetylation	------MALDGPEQM ------CCCCCHHHC	17.85	19413330
9	Sulfoxidation	ALDGPEQMELEEGKA CCCCHHHCCCCCCCC	6.39	28465586
15	Ubiquitination	QMELEEGKAGSGLRQ HCCCCCCCCCCCHHH	53.51	21906983
15	Acetylation	QMELEEGKAGSGLRQ HCCCCCCCCCCCHHH	53.51	25953088
21	Methylation	GKAGSGLRQYYLSKI CCCCCCHHHHHHHHH	26.44	115492879
24	Phosphorylation	GSGLRQYYLSKIEEL CCCHHHHHHHHHHHH	9.00	-
26	Phosphorylation	GLRQYYLSKIEELQL CHHHHHHHHHHHHHH	18.57	-
27	Ubiquitination	LRQYYLSKIEELQLI HHHHHHHHHHHHHHH	52.09	-
38	Ubiquitination	LQLIVNDKSQNLRRL HHHHHCCCCHHHHHH	49.06	21906983
55	Ubiquitination	QRNELNAKVRLLREE HHHHHHHHHHHHHHH	27.15	21906983
55	Acetylation	QRNELNAKVRLLREE HHHHHHHHHHHHHHH	27.15	25953088
72	Phosphorylation	LLQEQGSYVGEVVRA HHHHCCCCHHHHHHH	21.21	-
80	Ubiquitination	VGEVVRAMDKKKVLV HHHHHHHCCCCCEEE	5.63	21890473
86	Ubiquitination	AMDKKKVLVKVHPEG HCCCCCEEEEEECCC	4.19	21890473
88	Ubiquitination	DKKKVLVKVHPEGKF CCCCEEEEEECCCCE	30.57	21906983
88	Acetylation	DKKKVLVKVHPEGKF CCCCEEEEEECCCCE	30.57	23236377
94	Acetylation	VKVHPEGKFVVDVDK EEEECCCCEEEEECC	33.07	25953088
94	Ubiquitination	VKVHPEGKFVVDVDK EEEECCCCEEEEECC	33.07	21906983
101	Ubiquitination	KFVVDVDKNIDINDV CEEEEECCCCCCCCC	56.50	-
101	Acetylation	KFVVDVDKNIDINDV CEEEEECCCCCCCCC	56.50	26051181
109	Phosphorylation	NIDINDVTPNCRVAL CCCCCCCCCCCEEEE	16.20	20068231
112	Glutathionylation	INDVTPNCRVALRND CCCCCCCCEEEECCC	3.79	22555962
117	Ubiquitination	PNCRVALRNDSYTLH CCCEEEECCCCEEHH	34.86	21890473
120	Phosphorylation	RVALRNDSYTLHKIL EEEECCCCEEHHHHC	24.46	23401153
121	Phosphorylation	VALRNDSYTLHKILP EEECCCCEEHHHHCC	19.04	28796482
121	Nitration	VALRNDSYTLHKILP EEECCCCEEHHHHCC	19.04	-
122	Phosphorylation	ALRNDSYTLHKILPN EECCCCEEHHHHCCC	26.74	28796482
122	Ubiquitination	ALRNDSYTLHKILPN EECCCCEEHHHHCCC	26.74	21890473
125	Ubiquitination	NDSYTLHKILPNKVD CCCEEHHHHCCCCCC	49.39	21906983
130	Ubiquitination	LHKILPNKVDPLVSL HHHHCCCCCCCHHHH	46.18	21906983
136	Phosphorylation	NKVDPLVSLMMVEKV CCCCCHHHHEEEEEC	20.45	20068231
142	Ubiquitination	VSLMMVEKVPDSTYE HHHEEEEECCCCHHH	47.89	-
146	Phosphorylation	MVEKVPDSTYEMIGG EEEECCCCHHHHCCC	27.15	30622161
147	Phosphorylation	VEKVPDSTYEMIGGL EEECCCCHHHHCCCH	30.77	30622161
148	Phosphorylation	EKVPDSTYEMIGGLD EECCCCHHHHCCCHH	13.88	25147952
150	Sulfoxidation	VPDSTYEMIGGLDKQ CCCCHHHHCCCHHHH	2.13	21406390
156	Ubiquitination	EMIGGLDKQIKEIKE HHCCCHHHHHHHHHH	59.99	21906983
162	Ubiquitination	DKQIKEIKEVIELPV HHHHHHHHHHHCCCC	47.20	21906983
170	Acetylation	EVIELPVKHPELFEA HHHCCCCCCHHHHHH	52.05	21466224
170	Ubiquitination	EVIELPVKHPELFEA HHHCCCCCCHHHHHH	52.05	21906983
184	Ubiquitination	ALGIAQPKGVLLYGP HHCCCCCCEEEEECC	49.96	21906983
188	Ubiquitination	AQPKGVLLYGPPGTG CCCCEEEEECCCCCC	4.28	21890473
189	Phosphorylation	QPKGVLLYGPPGTGK CCCEEEEECCCCCCH	24.35	28152594
194	Phosphorylation	LLYGPPGTGKTLLAR EEECCCCCCHHHHHH	41.08	28152594
196	Ubiquitination	YGPPGTGKTLLARAV ECCCCCCHHHHHHHH	35.52	21906983
196	Acetylation	YGPPGTGKTLLARAV ECCCCCCHHHHHHHH	35.52	25953088
197	Phosphorylation	GPPGTGKTLLARAVA CCCCCCHHHHHHHHH	28.48	23186163
214	Acetylation	TDCTFIRVSGSELVQ CCCEEEECCHHHHHH	6.94	19608861
214	Ubiquitination	TDCTFIRVSGSELVQ CCCEEEECCHHHHHH	6.94	19608861
214	Ubiquitination	TDCTFIRVSGSELVQ CCCEEEECCHHHHHH	6.94	21890473
217	Phosphorylation	TFIRVSGSELVQKFI EEEECCHHHHHHHHH	21.91	-
222	Ubiquitination	SGSELVQKFIGEGAR CHHHHHHHHHHHHHH	31.31	21906983
222	Acetylation	SGSELVQKFIGEGAR CHHHHHHHHHHHHHH	31.31	19608861
244	Phosphorylation	MAREHAPSIIFMDEI HHHHHCCEEEEEECC	29.15	20071362
248	Sulfoxidation	HAPSIIFMDEIDSIG HCCEEEEEECCCCCC	2.96	30846556
256	Phosphorylation	DEIDSIGSSRLEGGS ECCCCCCCCCCCCCC	15.60	20071362
257	Phosphorylation	EIDSIGSSRLEGGSG CCCCCCCCCCCCCCC	35.35	20071362
263	Phosphorylation	SSRLEGGSGGDSEVQ CCCCCCCCCCCHHHH	50.92	21712546
267	Phosphorylation	EGGSGGDSEVQRTML CCCCCCCHHHHHHHH	42.83	25262027
273	Sulfoxidation	DSEVQRTMLELLNQL CHHHHHHHHHHHHHC	2.74	28183972
287	Ubiquitination	LDGFEATKNIKVIMA CCCHHHCCCCEEEEE	64.82	21906983
290	Ubiquitination	FEATKNIKVIMATNR HHHCCCCEEEEECCC	34.79	-
303	Phosphorylation	NRIDILDSALLRPGR CCCCCCCHHHCCCCC	19.85	20068231
314	Ubiquitination	RPGRIDRKIEFPPPN CCCCCCCCCCCCCCC	42.72	21906983
330	Ubiquitination	EARLDILKIHSRKMN HHHHHHHHHHHHCCC	38.41	21906983
330	Acetylation	EARLDILKIHSRKMN HHHHHHHHHHHHCCC	38.41	25953088
346	Ubiquitination	TRGINLRKIAELMPG CCCCCHHHHHHHCCC	49.81	-
351	Sulfoxidation	LRKIAELMPGASGAE HHHHHHHCCCCCCCE	1.85	21406390
360	Ubiquitination	GASGAEVKGVCTEAG CCCCCEEEEEECHHH	36.81	-
363	Glutathionylation	GAEVKGVCTEAGMYA CCEEEEEECHHHHHH	3.76	22555962
364	Phosphorylation	AEVKGVCTEAGMYAL CEEEEEECHHHHHHH	26.85	-
368	Sulfoxidation	GVCTEAGMYALRERR EEECHHHHHHHHHCC	1.97	21406390
369	Phosphorylation	VCTEAGMYALRERRV EECHHHHHHHHHCCC	11.10	23917254
379	Phosphorylation	RERRVHVTQEDFEMA HHCCCCCCHHHHHHH	16.03	20068231
385	Sulfoxidation	VTQEDFEMAVAKVMQ CCHHHHHHHHHHHHH	3.52	21406390
389	Ubiquitination	DFEMAVAKVMQKDSE HHHHHHHHHHHHHHH	31.47	21906983
397	Ubiquitination	VMQKDSEKNMSIKKL HHHHHHHHCCCCHHH	63.00	21906983
397	Acetylation	VMQKDSEKNMSIKKL HHHHHHHHCCCCHHH	63.00	25953088
402	Ubiquitination	SEKNMSIKKLWK--- HHHCCCCHHHCC---	34.21	-
403	Ubiquitination	EKNMSIKKLWK---- HHCCCCHHHCC----	58.89	-

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
120	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRS8_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 PRS8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RORA_HUMAN	RORA	physical	16189514
TNNT1_HUMAN	TNNT1	physical	16189514
UBE3C_HUMAN	UBE3C	physical	12692129
SP1_HUMAN	SP1	physical	10816420
PRS6A_HUMAN	PSMC3	physical	11463857
PRS4_HUMAN	PSMC1	physical	11361004
PRS10_HUMAN	PSMC6	physical	11361004
NLRC4_HUMAN	NLRC4	physical	20085538
P53_HUMAN	TP53	physical	17224908
MDM2_HUMAN	MDM2	physical	20479273
P53_HUMAN	TP53	physical	20479273
C2TA_HUMAN	CIITA	physical	20351748
PSME1_HUMAN	PSME1	physical	10799514
PSA1_HUMAN	PSMA1	physical	10799514
PRS6B_HUMAN	PSMC4	physical	19781552
PRS8_HUMAN	PSMC5	physical	17646385
PSMD2_HUMAN	PSMD2	physical	17646385
UBP14_HUMAN	USP14	physical	17646385
PSMD4_HUMAN	PSMD4	physical	17646385
PRS6B_HUMAN	PSMC4	physical	19490896
PSME1_HUMAN	PSME1	physical	9620878
PSMD1_HUMAN	PSMD1	physical	15831487
PSA1_HUMAN	PSMA1	physical	15831487
PAAF1_HUMAN	PAAF1	physical	15831487
PRS4_HUMAN	PSMC1	physical	21628461
PSMD8_HUMAN	PSMD8	physical	21628461
PSB5_HUMAN	PSMB5	physical	21628461
PSMD2_HUMAN	PSMD2	physical	22275368
PSMD1_HUMAN	PSMD1	physical	22275368
PRS7_HUMAN	PSMC2	physical	22275368
PRS4_HUMAN	PSMC1	physical	22275368
PRS10_HUMAN	PSMC6	physical	22275368
PRS6B_HUMAN	PSMC4	physical	22275368
PRS6A_HUMAN	PSMC3	physical	22275368
PRS6A_HUMAN	PSMC3	physical	20431057
C2TA_HUMAN	CIITA	physical	18215421
MY18B_HUMAN	MYO18B	physical	16499872
HOME3_HUMAN	HOMER3	physical	22486777
MYC_HUMAN	MYC	physical	12963825
PKHO1_HUMAN	PLEKHO1	physical	23032291
UBP4_HUMAN	USP4	physical	23022198
HD_HUMAN	HTT	physical	18986984
PSD13_HUMAN	PSMD13	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSD10_HUMAN	PSMD10	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSA3_HUMAN	PSMA3	physical	22939629
PSA5_HUMAN	PSMA5	physical	22939629
PSA7_HUMAN	PSMA7	physical	22939629
PSA6_HUMAN	PSMA6	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSB1_HUMAN	PSMB1	physical	22939629
PSA1_HUMAN	PSMA1	physical	22939629
PSA4_HUMAN	PSMA4	physical	22939629
PSB2_HUMAN	PSMB2	physical	22939629
PSB3_HUMAN	PSMB3	physical	22939629
PSME2_HUMAN	PSME2	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
PSB5_HUMAN	PSMB5	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSA7L_HUMAN	PSMA8	physical	22939629
ECD_HUMAN	ECD	physical	22939629
ZCHC8_HUMAN	ZCCHC8	physical	22939629
TBB5_HUMAN	TUBB	physical	22939629
ADRM1_HUMAN	ADRM1	physical	22863883
DC1I2_HUMAN	DYNC1I2	physical	22863883
PRS6B_HUMAN	PSMC4	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSD11_HUMAN	PSMD11	physical	22863883
PSD13_HUMAN	PSMD13	physical	22863883
PSMD7_HUMAN	PSMD7	physical	22863883
KRT38_HUMAN	KRT38	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
ADRM1_HUMAN	ADRM1	physical	26344197
ELP6_HUMAN	ELP6	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
LONM_HUMAN	LONP1	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSD10_HUMAN	PSMD10	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
PSMD3_HUMAN	PSMD3	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
PSMD8_HUMAN	PSMD8	physical	26344197
PSMG2_HUMAN	PSMG2	physical	26344197
RD23B_HUMAN	RAD23B	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
SYHC_HUMAN	HARS	physical	15604093
LAMB1_HUMAN	LAMB1	physical	15604093
LAMC1_HUMAN	LAMC1	physical	15604093
VIME_HUMAN	VIM	physical	15604093
ERR1_HUMAN	ESRRA	physical	15604093
RORG_HUMAN	RORC	physical	15604093
PHOS_HUMAN	PDC	physical	15604093
PRS6B_HUMAN	PSMC4	physical	15604093
RORA_HUMAN	RORA	physical	15604093
TNNI3_HUMAN	TNNI3	physical	15604093
TNNT1_HUMAN	TNNT1	physical	21516116
VCAM1_HUMAN	VCAM1	physical	26337389
PSDE_HUMAN	PSMD14	physical	26337389
TERA_HUMAN	VCP	physical	26337389
SHOC2_HUMAN	SHOC2	physical	26519477
RASM_HUMAN	MRAS	physical	26519477
CEP83_HUMAN	CEP83	physical	28514442
PRS6B_HUMAN	PSMC4	physical	28514442
RGPD8_HUMAN	RGPD8	physical	28514442
PSD10_HUMAN	PSMD10	physical	28514442
PSD12_HUMAN	PSMD12	physical	28514442
MTG8_HUMAN	RUNX1T1	physical	28514442
SSNA1_HUMAN	SSNA1	physical	28514442
RBP1_HUMAN	RALBP1	physical	28514442
ATF7_HUMAN	ATF7	physical	28514442
THA11_HUMAN	THAP11	physical	28514442
FGOP2_HUMAN	FGFR1OP2	physical	28514442
SKA1_HUMAN	SKA1	physical	28514442
RGPD5_HUMAN	RGPD5	physical	28514442
ADRM1_HUMAN	ADRM1	physical	28514442
PRS6A_HUMAN	PSMC3	physical	28514442
PAAF1_HUMAN	PAAF1	physical	28514442
COG4_HUMAN	COG4	physical	28514442
RECQ1_HUMAN	RECQL	physical	28514442
SIKE1_HUMAN	SIKE1	physical	28514442
PSMD4_HUMAN	PSMD4	physical	28514442
PRS4_HUMAN	PSMC1	physical	28514442
PSD11_HUMAN	PSMD11	physical	28514442
PRS10_HUMAN	PSMC6	physical	28514442
EDEM2_HUMAN	EDEM2	physical	28514442
PSMD1_HUMAN	PSMD1	physical	28514442
TRAF6_HUMAN	TRAF6	physical	28514442
PSDE_HUMAN	PSMD14	physical	28514442
PSMD6_HUMAN	PSMD6	physical	28514442
STRN_HUMAN	STRN	physical	28514442
UBP4_HUMAN	USP4	physical	28514442
PRS7_HUMAN	PSMC2	physical	28514442
PHOCN_HUMAN	MOB4	physical	28514442
IKIP_HUMAN	IKBIP	physical	28514442
PSD13_HUMAN	PSMD13	physical	28514442
HBB_HUMAN	HBB	physical	28514442
PSMD3_HUMAN	PSMD3	physical	28514442
GCC2_HUMAN	GCC2	physical	28514442
MED4_HUMAN	MED4	physical	28514442
GIT1_HUMAN	GIT1	physical	28514442
BIRC6_HUMAN	BIRC6	physical	28514442
PSMD2_HUMAN	PSMD2	physical	28514442
VPS52_HUMAN	VPS52	physical	28514442
STRP1_HUMAN	STRIP1	physical	28514442
TXD11_HUMAN	TXNDC11	physical	28514442
IPRI_HUMAN	ITPRIP	physical	28514442
KGP1_HUMAN	PRKG1	physical	28514442
PHLP_HUMAN	PDCL	physical	28514442
KIF3B_HUMAN	KIF3B	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 PRS8_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 ALA-2, 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 ALA-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-222, AND MASS SPECTROMETRY.	19608861 [Abstract]