dbPTM

PSME3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSME3_HUMAN
UniProt AC	P61289
Protein Name	Proteasome activator complex subunit 3
Gene Name	PSME3
Organism	Homo sapiens (Human).
Sequence Length	254
Subcellular Localization	Nucleus . Cytoplasm. Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase..
Protein Description	Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition. [PubMed: 25361978]
Protein Sequence	MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASLLKVDQ ------CCCCCCCCH	14.64	22814378
3	Phosphorylation	-----MASLLKVDQE -----CCCCCCCCHH	32.70	25003641
6	Acetylation	--MASLLKVDQEVKL --CCCCCCCCHHHHH	49.40	23749302
6	Sumoylation	--MASLLKVDQEVKL --CCCCCCCCHHHHH	49.40	-
6	Ubiquitination	--MASLLKVDQEVKL --CCCCCCCCHHHHH	49.40	-
6 (in isoform 2)	Ubiquitination	-	49.40	-
6	2-Hydroxyisobutyrylation	--MASLLKVDQEVKL --CCCCCCCCHHHHH	49.40	-
6	Sumoylation	--MASLLKVDQEVKL --CCCCCCCCHHHHH	49.40	-
6	Succinylation	--MASLLKVDQEVKL --CCCCCCCCHHHHH	49.40	23954790
12	2-Hydroxyisobutyrylation	LKVDQEVKLKVDSFR CCCCHHHHHHHHHHH	41.67	-
12	Ubiquitination	LKVDQEVKLKVDSFR CCCCHHHHHHHHHHH	41.67	-
12	Sumoylation	LKVDQEVKLKVDSFR CCCCHHHHHHHHHHH	41.67	-
12	Acetylation	LKVDQEVKLKVDSFR CCCCHHHHHHHHHHH	41.67	25953088
12	Sumoylation	LKVDQEVKLKVDSFR CCCCHHHHHHHHHHH	41.67	-
14	Sumoylation	VDQEVKLKVDSFRER CCHHHHHHHHHHHHH	37.97	-
14 (in isoform 1)	Ubiquitination	-	37.97	21890473
14	Ubiquitination	VDQEVKLKVDSFRER CCHHHHHHHHHHHHH	37.97	21906983
14	Sumoylation	VDQEVKLKVDSFRER CCHHHHHHHHHHHHH	37.97	-
14	Acetylation	VDQEVKLKVDSFRER CCHHHHHHHHHHHHH	37.97	62154813
14 (in isoform 2)	Ubiquitination	-	37.97	21890473
14	2-Hydroxyisobutyrylation	VDQEVKLKVDSFRER CCHHHHHHHHHHHHH	37.97	-
17	Phosphorylation	EVKLKVDSFRERITS HHHHHHHHHHHHHHH	29.23	23186163
23	Phosphorylation	DSFRERITSEAEDLV HHHHHHHHHHHHHHH	27.08	26503892
23 (in isoform 2)	Phosphorylation	-	27.08	21406692
24 (in isoform 2)	Phosphorylation	-	32.22	24719451
24	Phosphorylation	SFRERITSEAEDLVA HHHHHHHHHHHHHHH	32.22	29255136
36 (in isoform 2)	Ubiquitination	-	51.39	21890473
36	2-Hydroxyisobutyrylation	LVANFFPKKLLELDS HHHHHCCHHHHCHHH	51.39	-
36	Ubiquitination	LVANFFPKKLLELDS HHHHHCCHHHHCHHH	51.39	21906983
36	Acetylation	LVANFFPKKLLELDS HHHHHCCHHHHCHHH	51.39	23236377
36 (in isoform 1)	Ubiquitination	-	51.39	21890473
37	Acetylation	VANFFPKKLLELDSF HHHHCCHHHHCHHHH	59.55	27452117
37 (in isoform 2)	Ubiquitination	-	59.55	21890473
37 (in isoform 1)	Ubiquitination	-	59.55	21890473
37	Ubiquitination	VANFFPKKLLELDSF HHHHCCHHHHCHHHH	59.55	21890473
43	Phosphorylation	KKLLELDSFLKEPIL HHHHCHHHHHCCCCC	45.14	21815630
73	Phosphorylation	VPDPILLTNSHDGLD CCCCEEECCCCCCCC	31.09	27251275
73 (in isoform 2)	Phosphorylation	-	31.09	27251275
75	Phosphorylation	DPILLTNSHDGLDGP CCEEECCCCCCCCCC	20.09	25159151
84	Phosphorylation	DGLDGPTYKKRRLDE CCCCCCCCCCCCHHH	20.04	-
85	Ubiquitination	GLDGPTYKKRRLDEC CCCCCCCCCCCHHHH	42.13	-
86	Ubiquitination	LDGPTYKKRRLDECE CCCCCCCCCCHHHHH	32.13	-
92	Glutathionylation	KKRRLDECEEAFQGT CCCCHHHHHHHHCCC	5.98	22555962
99	Phosphorylation	CEEAFQGTKVFVMPN HHHHHCCCEEEECCC	17.16	28555341
100	Ubiquitination	EEAFQGTKVFVMPNG HHHHCCCEEEECCCC	40.26	-
110 (in isoform 1)	Ubiquitination	-	38.17	21890473
110	Methylation	VMPNGMLKSNQQLVD ECCCCCCCCCHHHHH	38.17	44500383
110	Ubiquitination	VMPNGMLKSNQQLVD ECCCCCCCCCHHHHH	38.17	21890473
110 (in isoform 2)	Ubiquitination	-	38.17	21890473
111	Phosphorylation	MPNGMLKSNQQLVDI CCCCCCCCCHHHHHH	35.59	21712546
121 (in isoform 2)	Ubiquitination	-	45.19	21890473
121	Methylation	QLVDIIEKVKPEIRL HHHHHHHHHCHHHHH	45.19	-
121	2-Hydroxyisobutyrylation	QLVDIIEKVKPEIRL HHHHHHHHHCHHHHH	45.19	-
121	Ubiquitination	QLVDIIEKVKPEIRL HHHHHHHHHCHHHHH	45.19	22053931
121 (in isoform 1)	Ubiquitination	-	45.19	21890473
132	Acetylation	EIRLLIEKCNTVKMW HHHHHHHHCCHHHHH	26.28	25953088
132	Ubiquitination	EIRLLIEKCNTVKMW HHHHHHHHCCHHHHH	26.28	-
167	Phosphorylation	ETVAELRTVESEAAS HHHHHHHCHHHHHHH	41.05	28152594
170	Phosphorylation	AELRTVESEAASYLD HHHHCHHHHHHHHHH	28.35	28152594
174	Phosphorylation	TVESEAASYLDQISR CHHHHHHHHHHHHHH	33.02	28152594
175	Phosphorylation	VESEAASYLDQISRY HHHHHHHHHHHHHHH	15.01	20860994
180	Phosphorylation	ASYLDQISRYYITRA HHHHHHHHHHHHHHH	14.48	28152594
195	2-Hydroxyisobutyrylation	KLVSKIAKYPHVEDY HHHHHHHCCCCHHHH	63.89	-
195 (in isoform 1)	Ubiquitination	-	63.89	21890473
195	Acetylation	KLVSKIAKYPHVEDY HHHHHHHCCCCHHHH	63.89	19608861
195	Ubiquitination	KLVSKIAKYPHVEDY HHHHHHHCCCCHHHH	63.89	19608861
196	Phosphorylation	LVSKIAKYPHVEDYR HHHHHHCCCCHHHHC	6.91	28152594
205	Phosphorylation	HVEDYRRTVTEIDEK CHHHHCCCEEECCHH	23.84	21082442
207	Phosphorylation	EDYRRTVTEIDEKEY HHHCCCEEECCHHHH	26.98	21082442
208	Acetylation	DYRRTVTEIDEKEYI HHCCCEEECCHHHHH	44.07	19608861
208	Ubiquitination	DYRRTVTEIDEKEYI HHCCCEEECCHHHHH	44.07	19608861
208 (in isoform 2)	Acetylation	-	44.07	-
208 (in isoform 2)	Ubiquitination	-	44.07	21890473
212	2-Hydroxyisobutyrylation	TVTEIDEKEYISLRL CEEECCHHHHHHHHH	52.66	-
212	Acetylation	TVTEIDEKEYISLRL CEEECCHHHHHHHHH	52.66	23236377
212	Methylation	TVTEIDEKEYISLRL CEEECCHHHHHHHHH	52.66	-
214	Phosphorylation	TEIDEKEYISLRLII EECCHHHHHHHHHHH	13.59	-
222	Phosphorylation	ISLRLIISELRNQYV HHHHHHHHHHHHCCC	24.47	24719451
237	Acetylation	TLHDMILKNIEKIKR CHHHHHHHHHHHHCC	44.98	27452117
247	Phosphorylation	EKIKRPRSSNAETLY HHHCCCCCCCCCCCC	30.54	25159151
248	Phosphorylation	KIKRPRSSNAETLY- HHCCCCCCCCCCCC-	41.14	25159151
252	Phosphorylation	PRSSNAETLY----- CCCCCCCCCC-----	29.01	23403867
254	Phosphorylation	SSNAETLY------- CCCCCCCC-------	24.75	23403867
260 (in isoform 2)	Phosphorylation	-		24719451

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
247	S	Phosphorylation	Kinase	CHK2	O96017	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
195	K	Acetylation	23612972
Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates.
247	S	Phosphorylation	25361978
Phosphorylation at Ser-247 promotes its association with CCAR2.

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 PSME3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR25_HUMAN	WDR25	physical	16189514
ZCH10_HUMAN	ZCCHC10	physical	16189514
KANL1_HUMAN	KANSL1	physical	16189514
NUD18_HUMAN	NUDT18	physical	16189514
PSME3_HUMAN	PSME3	physical	16189514
ATPB_HUMAN	ATP5B	physical	16169070
ADAP1_HUMAN	ADAP1	physical	16169070
PSME3_HUMAN	PSME3	physical	16169070
GRP78_HUMAN	HSPA5	physical	16169070
MDM2_HUMAN	MDM2	physical	18309296
P53_HUMAN	TP53	physical	18309296
CDN1A_HUMAN	CDKN1A	physical	17588519
CDN2A_HUMAN	CDKN2A	physical	17588519
ARF_HUMAN	CDKN2A	physical	17588519
SMUF1_HUMAN	SMURF1	physical	20580715
P53_HUMAN	TP53	physical	21084564
UL27_HCMVM	UL27	physical	21320693
NCOA3_HUMAN	NCOA3	physical	16439211
CHK2_HUMAN	CHEK2	physical	19556897
AICDA_HUMAN	AICDA	physical	22042974
PSME3_HUMAN	PSME3	physical	9325261
SIR1_HUMAN	SIRT1	physical	23612972
PSME3_HUMAN	PSME3	physical	23612972
PSME3_HUMAN	PSME3	physical	25416956
DIP2A_HUMAN	DIP2A	physical	25416956
FBX7_HUMAN	FBXO7	physical	25416956
THIOM_HUMAN	TXN2	physical	25416956
PRR13_HUMAN	PRR13	physical	25416956
ZCH10_HUMAN	ZCCHC10	physical	25416956
EAF1_HUMAN	EAF1	physical	25416956
TP8L1_HUMAN	TNFAIP8L1	physical	25416956
F192A_HUMAN	FAM192A	physical	26186194
TSH3_HUMAN	TSHZ3	physical	26186194
CSR2B_HUMAN	CSRP2BP	physical	26186194
YETS2_HUMAN	YEATS2	physical	26186194
PR14L_HUMAN	PRR14L	physical	26186194
SALL2_HUMAN	SALL2	physical	26186194
SNPC4_HUMAN	SNAPC4	physical	26186194
ZKSC1_HUMAN	ZKSCAN1	physical	26186194
Z324A_HUMAN	ZNF324	physical	26186194
THA11_HUMAN	THAP11	physical	26186194
FWCH2_HUMAN	FLYWCH2	physical	26186194
P66A_HUMAN	GATAD2A	physical	26186194
SNPC1_HUMAN	SNAPC1	physical	26186194
MGAP_HUMAN	MGA	physical	26186194
CHD8_HUMAN	CHD8	physical	26186194
CBX2_HUMAN	CBX2	physical	26186194
PSA1_HUMAN	PSMA1	physical	26186194
ZBTB9_HUMAN	ZBTB9	physical	26186194
STRBP_HUMAN	STRBP	physical	26186194
ZZZ3_HUMAN	ZZZ3	physical	26186194
TSR1_HUMAN	TSR1	physical	26186194
BAP1_HUMAN	BAP1	physical	26186194
TRM6_HUMAN	TRMT6	physical	26186194
COIL_HUMAN	COIL	physical	26186194
T2FA_HUMAN	GTF2F1	physical	26186194
DIEXF_HUMAN	DIEXF	physical	26186194
LMBL2_HUMAN	L3MBTL2	physical	26186194
MBTD1_HUMAN	MBTD1	physical	26186194
TAD2A_HUMAN	TADA2A	physical	26186194
FXL19_HUMAN	FBXL19	physical	26186194
PML_HUMAN	PML	physical	26186194
RALY_HUMAN	RALY	physical	26186194
ELF2_HUMAN	ELF2	physical	26186194
ZN891_HUMAN	ZNF891	physical	26186194
TRI33_HUMAN	TRIM33	physical	26186194
MBIP1_HUMAN	MBIP	physical	26186194
PCGF6_HUMAN	PCGF6	physical	26186194
RAD18_HUMAN	RAD18	physical	26186194
RTEL1_HUMAN	RTEL1	physical	26186194
SNPC3_HUMAN	SNAPC3	physical	26186194
CCAR2_HUMAN	CCAR2	physical	25361978
SAHH2_HUMAN	AHCYL1	physical	26344197
F192A_HUMAN	FAM192A	physical	26344197
HDGF_HUMAN	HDGF	physical	26344197
HIBCH_HUMAN	HIBCH	physical	26344197
PSA5_HUMAN	PSMA5	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
SF3B5_HUMAN	SF3B5	physical	26344197
1433S_HUMAN	SFN	physical	26344197
EAF2_HUMAN	EAF2	physical	21516116
DPTOR_HUMAN	DEPTOR	physical	21516116
EAF1_HUMAN	EAF1	physical	21516116
KLF2_HUMAN	KLF2	physical	26776519
PIAS1_HUMAN	PIAS1	physical	21445096
CDN1A_HUMAN	CDKN1A	physical	21445096
FXL19_HUMAN	FBXL19	physical	28514442
SNPC1_HUMAN	SNAPC1	physical	28514442
BAP1_HUMAN	BAP1	physical	28514442
SNPC4_HUMAN	SNAPC4	physical	28514442
SNPC3_HUMAN	SNAPC3	physical	28514442
ELF2_HUMAN	ELF2	physical	28514442
ZBTB9_HUMAN	ZBTB9	physical	28514442
MBTD1_HUMAN	MBTD1	physical	28514442
CHD8_HUMAN	CHD8	physical	28514442
CBX2_HUMAN	CBX2	physical	28514442
CSR2B_HUMAN	CSRP2BP	physical	28514442
ZZZ3_HUMAN	ZZZ3	physical	28514442
YETS2_HUMAN	YEATS2	physical	28514442
DIEXF_HUMAN	DIEXF	physical	28514442
F192A_HUMAN	FAM192A	physical	28514442
TRM6_HUMAN	TRMT6	physical	28514442
ZKSC1_HUMAN	ZKSCAN1	physical	28514442
TSH3_HUMAN	TSHZ3	physical	28514442
TAD2A_HUMAN	TADA2A	physical	28514442
LMBL2_HUMAN	L3MBTL2	physical	28514442
RL15_HUMAN	RPL15	physical	28514442
RALY_HUMAN	RALY	physical	28514442
MGAP_HUMAN	MGA	physical	28514442
MBIP1_HUMAN	MBIP	physical	28514442
THA11_HUMAN	THAP11	physical	28514442
T2FA_HUMAN	GTF2F1	physical	28514442
ZN891_HUMAN	ZNF891	physical	28514442
PCGF6_HUMAN	PCGF6	physical	28514442
RTEL1_HUMAN	RTEL1	physical	28514442
SALL2_HUMAN	SALL2	physical	28514442
RAD18_HUMAN	RAD18	physical	28514442
Z324A_HUMAN	ZNF324	physical	28514442
FWCH2_HUMAN	FLYWCH2	physical	28514442
P66A_HUMAN	GATAD2A	physical	28514442
COIL_HUMAN	COIL	physical	28514442
P66B_HUMAN	GATAD2B	physical	28514442
TSYL1_HUMAN	TSPYL1	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PSME3_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-195, AND MASS SPECTROMETRY.	19608861 [Abstract]

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