dbPTM

PSD12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSD12_HUMAN
UniProt AC	O00232
Protein Name	26S proteasome non-ATPase regulatory subunit 12
Gene Name	PSMD12
Organism	Homo sapiens (Human).
Sequence Length	456
Subcellular Localization
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..
Protein Sequence	MADGGSERADGRIVKMEVDYSATVDQRLPECAKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAVVKMCYEAKEWDLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPIKLRLIDTLRMVTEGKIYVEIERARLTKTLATIKEQNGDVKEAASILQELQVETYGSMEKKERVEFILEQMRLCLAVKDYIRTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSYLSICKHYRAIYDTPCIQAESEKWQQALKSVVLYVILAPFDNEQSDLVHRISGDKKLEEIPKYKDLLKLFTTMELMRWSTLVEDYGMELRKGSLESPATDVFGSTEEGEKRWKDLKNRVVEHNIRIMAKYYTRITMKRMAQLLDLSVDESEAFLSNLVVNKTIFAKVDRLAGIINFQRPKDPNNLLNDWSQKLNSLMSLVNKTTHLIAKEEMIHNLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGGSERA ------CCCCCCCCC	24.93	19413330
6	Phosphorylation	--MADGGSERADGRI --CCCCCCCCCCCCE	29.46	29514088
16	Sulfoxidation	ADGRIVKMEVDYSAT CCCCEEEEEEECCCC	4.15	21406390
20	Phosphorylation	IVKMEVDYSATVDQR EEEEEEECCCCCCCC	12.84	28796482
21	Phosphorylation	VKMEVDYSATVDQRL EEEEEECCCCCCCCC	17.01	28796482
23	Phosphorylation	MEVDYSATVDQRLPE EEEECCCCCCCCCHH	20.76	28796482
33	Acetylation	QRLPECAKLAKEGRL CCCHHHHHHHHHCCH	61.71	25953088
33	Malonylation	QRLPECAKLAKEGRL CCCHHHHHHHHHCCH	61.71	32601280
33	Ubiquitination	QRLPECAKLAKEGRL CCCHHHHHHHHHCCH	61.71	-
36	Ubiquitination	PECAKLAKEGRLQEV HHHHHHHHHCCHHHH	71.75	-
52	Ubiquitination	ETLLSLEKQTRTASD HHHHHHHHHCCCHHH	63.36	21890473
56	Phosphorylation	SLEKQTRTASDMVST HHHHHCCCHHHHHCH	33.62	20068231
58	Phosphorylation	EKQTRTASDMVSTSR HHHCCCHHHHHCHHH	26.15	20068231
60	Sulfoxidation	QTRTASDMVSTSRIL HCCCHHHHHCHHHHH	2.07	30846556
62	Phosphorylation	RTASDMVSTSRILVA CCHHHHHCHHHHHHH	17.64	24114839
64	Phosphorylation	ASDMVSTSRILVAVV HHHHHCHHHHHHHHH	15.15	24114839
88	Sulfoxidation	DLLNENIMLLSKRRS HHHCHHHHHHHHHHH	4.67	30846556
92	Sumoylation	ENIMLLSKRRSQLKQ HHHHHHHHHHHHHHH	52.37	-
92	Sumoylation	ENIMLLSKRRSQLKQ HHHHHHHHHHHHHHH	52.37	25114211
92	Ubiquitination	ENIMLLSKRRSQLKQ HHHHHHHHHHHHHHH	52.37	-
98	2-Hydroxyisobutyrylation	SKRRSQLKQAVAKMV HHHHHHHHHHHHHHH	28.68	-
98	Acetylation	SKRRSQLKQAVAKMV HHHHHHHHHHHHHHH	28.68	25953088
98	Succinylation	SKRRSQLKQAVAKMV HHHHHHHHHHHHHHH	28.68	23954790
98	Ubiquitination	SKRRSQLKQAVAKMV HHHHHHHHHHHHHHH	28.68	-
103	Ubiquitination	QLKQAVAKMVQQCCT HHHHHHHHHHHHHHH	32.76	-
104	Sulfoxidation	LKQAVAKMVQQCCTY HHHHHHHHHHHHHHH	2.07	30846556
109	Glutathionylation	AKMVQQCCTYVEEIT HHHHHHHHHHHHHHH	2.40	22555962
111	Phosphorylation	MVQQCCTYVEEITDL HHHHHHHHHHHHHCC	7.61	-
121	Ubiquitination	EITDLPIKLRLIDTL HHHCCCHHHHHHHHH	26.14	21890473
127	Phosphorylation	IKLRLIDTLRMVTEG HHHHHHHHHHHHHCC	14.85	23898821
132	Phosphorylation	IDTLRMVTEGKIYVE HHHHHHHHCCCEEEE	29.67	23898821
137	Phosphorylation	MVTEGKIYVEIERAR HHHCCCEEEEEEHHH	8.77	20393185
147	Malonylation	IERARLTKTLATIKE EEHHHHHHHHHHHHH	46.24	32601280
147	Ubiquitination	IERARLTKTLATIKE EEHHHHHHHHHHHHH	46.24	21890473
148	Phosphorylation	ERARLTKTLATIKEQ EHHHHHHHHHHHHHH	19.18	21406692
151	Phosphorylation	RLTKTLATIKEQNGD HHHHHHHHHHHHCCC	35.38	21406692
153	Ubiquitination	TKTLATIKEQNGDVK HHHHHHHHHHCCCHH	49.22	21890473
160	Ubiquitination	KEQNGDVKEAASILQ HHHCCCHHHHHHHHH	46.50	21890473
162	Acetylation	QNGDVKEAASILQEL HCCCHHHHHHHHHHH	10.78	19608861
162	Ubiquitination	QNGDVKEAASILQEL HCCCHHHHHHHHHHH	10.78	19608861
164	Phosphorylation	GDVKEAASILQELQV CCHHHHHHHHHHHHC	30.77	27080861
173	Phosphorylation	LQELQVETYGSMEKK HHHHHCCCCCCCCHH	34.03	30108239
174	Nitration	QELQVETYGSMEKKE HHHHCCCCCCCCHHH	8.16	-
174	Phosphorylation	QELQVETYGSMEKKE HHHHCCCCCCCCHHH	8.16	27080861
176	Phosphorylation	LQVETYGSMEKKERV HHCCCCCCCCHHHHH	17.23	30576142
177	Sulfoxidation	QVETYGSMEKKERVE HCCCCCCCCHHHHHH	8.32	30846556
179	Ubiquitination	ETYGSMEKKERVEFI CCCCCCCHHHHHHHH	51.82	21890473
192	Ubiquitination	FILEQMRLCLAVKDY HHHHHHHHHHHHHHH	2.05	21890473
197	2-Hydroxyisobutyrylation	MRLCLAVKDYIRTQI HHHHHHHHHHHHHHH	38.93	-
197	Acetylation	MRLCLAVKDYIRTQI HHHHHHHHHHHHHHH	38.93	27452117
197	Ubiquitination	MRLCLAVKDYIRTQI HHHHHHHHHHHHHHH	38.93	-
201	Acetylation	LAVKDYIRTQIISKK HHHHHHHHHHHHHHH	17.85	19608861
201	Ubiquitination	LAVKDYIRTQIISKK HHHHHHHHHHHHHHH	17.85	19608861
206	Phosphorylation	YIRTQIISKKINTKF HHHHHHHHHHHCCHH	29.53	24719451
207	2-Hydroxyisobutyrylation	IRTQIISKKINTKFF HHHHHHHHHHCCHHH	47.46	-
212	2-Hydroxyisobutyrylation	ISKKINTKFFQEENT HHHHHCCHHHCCCCC	39.43	-
212	Acetylation	ISKKINTKFFQEENT HHHHHCCHHHCCCCC	39.43	26051181
212	Malonylation	ISKKINTKFFQEENT HHHHHCCHHHCCCCC	39.43	26320211
212	Ubiquitination	ISKKINTKFFQEENT HHHHHCCHHHCCCCC	39.43	21890473
219	Phosphorylation	KFFQEENTEKLKLKY HHHCCCCCHHHHHEE	37.46	-
221	Acetylation	FQEENTEKLKLKYYN HCCCCCHHHHHEEEE	49.21	19608861
221	Ubiquitination	FQEENTEKLKLKYYN HCCCCCHHHHHEEEE	49.21	21906983
227	Phosphorylation	EKLKLKYYNLMIQLD HHHHHEEEEEEEEEC	10.55	18452278
251	Phosphorylation	CKHYRAIYDTPCIQA HHHHHHHHCCCCHHH	16.87	20068231
253	Phosphorylation	HYRAIYDTPCIQAES HHHHHHCCCCHHHCC	11.77	20068231
255	S-nitrosocysteine	RAIYDTPCIQAESEK HHHHCCCCHHHCCHH	3.80	-
255	S-nitrosylation	RAIYDTPCIQAESEK HHHHCCCCHHHCCHH	3.80	19483679
262	Acetylation	CIQAESEKWQQALKS CHHHCCHHHHHHHHH	60.63	25038526
262	Ubiquitination	CIQAESEKWQQALKS CHHHCCHHHHHHHHH	60.63	-
295	Ubiquitination	HRISGDKKLEEIPKY HHHCCCCCHHHCCCH	66.91	-
301	Ubiquitination	KKLEEIPKYKDLLKL CCHHHCCCHHHHHHH	71.27	-
309	Acetylation	YKDLLKLFTTMELMR HHHHHHHHHHHHHHH	5.23	19608861
312	Sulfoxidation	LLKLFTTMELMRWST HHHHHHHHHHHHHHH	3.19	21406390
326	Sulfoxidation	TLVEDYGMELRKGSL HHHHHHCCCCCCCCC	3.40	30846556
330	Ubiquitination	DYGMELRKGSLESPA HHCCCCCCCCCCCCC	66.53	21890473
332	Phosphorylation	GMELRKGSLESPATD CCCCCCCCCCCCCCC	31.81	29255136
335	Phosphorylation	LRKGSLESPATDVFG CCCCCCCCCCCCCCC	25.73	29255136
338	Phosphorylation	GSLESPATDVFGSTE CCCCCCCCCCCCCCH	35.76	25850435
343	Phosphorylation	PATDVFGSTEEGEKR CCCCCCCCCHHHHHH	22.60	30622161
344	Phosphorylation	ATDVFGSTEEGEKRW CCCCCCCCHHHHHHH	38.13	30622161
348	Acetylation	FGSTEEGEKRWKDLK CCCCHHHHHHHHHHH	42.60	19608861
349	2-Hydroxyisobutyrylation	GSTEEGEKRWKDLKN CCCHHHHHHHHHHHH	74.54	-
349	Ubiquitination	GSTEEGEKRWKDLKN CCCHHHHHHHHHHHH	74.54	-
368	Acetylation	HNIRIMAKYYTRITM HHHHHHHHHHHHHHH	22.78	19608861
368	Malonylation	HNIRIMAKYYTRITM HHHHHHHHHHHHHHH	22.78	26320211
368	Ubiquitination	HNIRIMAKYYTRITM HHHHHHHHHHHHHHH	22.78	19608861
369	Phosphorylation	NIRIMAKYYTRITMK HHHHHHHHHHHHHHH	10.67	25884760
370	Phosphorylation	IRIMAKYYTRITMKR HHHHHHHHHHHHHHH	6.71	25884760
389	Acetylation	LDLSVDESEAFLSNL HCCCCCCCHHHHHHH	29.75	19608861
389	Ubiquitination	LDLSVDESEAFLSNL HCCCCCCCHHHHHHH	29.75	19608861
401	Phosphorylation	SNLVVNKTIFAKVDR HHHCCCCCHHHHHHH	19.00	23403867
405	Succinylation	VNKTIFAKVDRLAGI CCCCHHHHHHHHHCC	33.64	23954790
419	Acetylation	IINFQRPKDPNNLLN CCCCCCCCCCCCHHH	84.06	26822725
419	Ubiquitination	IINFQRPKDPNNLLN CCCCCCCCCCCCHHH	84.06	-
428	Ubiquitination	PNNLLNDWSQKLNSL CCCHHHHHHHHHHHH	11.11	21890473
428	Acetylation	PNNLLNDWSQKLNSL CCCHHHHHHHHHHHH	11.11	19608861
428	Ubiquitination	PNNLLNDWSQKLNSL CCCHHHHHHHHHHHH	11.11	19608861
431	Ubiquitination	LLNDWSQKLNSLMSL HHHHHHHHHHHHHHH	44.09	-
434	Phosphorylation	DWSQKLNSLMSLVNK HHHHHHHHHHHHHHH	35.57	21712546
436	Sulfoxidation	SQKLNSLMSLVNKTT HHHHHHHHHHHHHHH	2.67	21406390
437	Phosphorylation	QKLNSLMSLVNKTTH HHHHHHHHHHHHHHH	34.16	21712546
441	Acetylation	SLMSLVNKTTHLIAK HHHHHHHHHHHHHHH	47.52	25953088
441	Ubiquitination	SLMSLVNKTTHLIAK HHHHHHHHHHHHHHH	47.52	-
448	2-Hydroxyisobutyrylation	KTTHLIAKEEMIHNL HHHHHHHHHHHHHHC	47.41	-
448	Acetylation	KTTHLIAKEEMIHNL HHHHHHHHHHHHHHC	47.41	23749302
448	Malonylation	KTTHLIAKEEMIHNL HHHHHHHHHHHHHHC	47.41	26320211
448	Ubiquitination	KTTHLIAKEEMIHNL HHHHHHHHHHHHHHC	47.41	21890473

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 PSD12_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSD12_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 PSD12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSD12_HUMAN	PSMD12	physical	20890303
EIF3D_HUMAN	EIF3D	physical	20890303
PRS10_HUMAN	PSMC6	physical	20890303
EIF3E_HUMAN	EIF3E	physical	20890303
PSD13_HUMAN	PSMD13	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSME1_HUMAN	PSME1	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
UBP14_HUMAN	USP14	physical	22939629
VIGLN_HUMAN	HDLBP	physical	22939629
UGGG1_HUMAN	UGGT1	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22863883
PRS4_HUMAN	PSMC1	physical	22863883
PRS7_HUMAN	PSMC2	physical	22863883
PRS6B_HUMAN	PSMC4	physical	22863883
PRS8_HUMAN	PSMC5	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSD11_HUMAN	PSMD11	physical	22863883
PSD13_HUMAN	PSMD13	physical	22863883
PSDE_HUMAN	PSMD14	physical	22863883
PSMD1_HUMAN	PSMD1	physical	22863883
PSMD3_HUMAN	PSMD3	physical	22863883
PSMD7_HUMAN	PSMD7	physical	22863883
FUS_HUMAN	FUS	physical	25192599
EIF3E_HUMAN	EIF3E	physical	26344197
MCM7_HUMAN	MCM7	physical	26344197
NAA15_HUMAN	NAA15	physical	26344197
NAA16_HUMAN	NAA16	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
PSB8_HUMAN	PSMB8	physical	26344197
PRS4_HUMAN	PSMC1	physical	26344197
PRS6B_HUMAN	PSMC4	physical	26344197
PRS10_HUMAN	PSMC6	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
PSMD8_HUMAN	PSMD8	physical	26344197
SGTA_HUMAN	SGTA	physical	26344197
PSD11_HUMAN	PSMD11	physical	28514442
PSMD6_HUMAN	PSMD6	physical	28514442
PSD13_HUMAN	PSMD13	physical	28514442
PSD10_HUMAN	PSMD10	physical	28514442
PSDE_HUMAN	PSMD14	physical	28514442
PSMD1_HUMAN	PSMD1	physical	28514442
PRS6B_HUMAN	PSMC4	physical	28514442
PRS10_HUMAN	PSMC6	physical	28514442
PSMD3_HUMAN	PSMD3	physical	28514442
PSMD4_HUMAN	PSMD4	physical	28514442
STKL1_HUMAN	STKLD1	physical	28514442
PSMD2_HUMAN	PSMD2	physical	28514442
EIF3E_HUMAN	EIF3E	physical	28514442
EIF3L_HUMAN	EIF3L	physical	28514442
EIF3C_HUMAN	EIF3C	physical	28514442
TRI11_HUMAN	TRIM11	physical	28514442
INTU_HUMAN	INTU	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 PSD12_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]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.	12665801 [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-221; LYS-368 AND LYS-448,AND MASS SPECTROMETRY.	19608861 [Abstract]