dbPTM

PSD11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSD11_HUMAN
UniProt AC	O00231
Protein Name	26S proteasome non-ATPase regulatory subunit 11
Gene Name	PSMD11
Organism	Homo sapiens (Human).
Sequence Length	422
Subcellular Localization	Nucleus. Cytoplasm, cytosol.
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. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity..
Protein Sequence	MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTHLAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVERKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALETIQNMSKVVDSLYNKAKKLT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAVVEF ------CCHHHHHHH	13.05	22223895
11	Methylation	AAVVEFQRAQSLLST HHHHHHHHHHHHHCC	39.66	115489433
14	Phosphorylation	VEFQRAQSLLSTDRE HHHHHHHHHHCCCHH	30.23	25159151
17	Phosphorylation	QRAQSLLSTDREASI HHHHHHHCCCHHHHH	33.29	30266825
18	Phosphorylation	RAQSLLSTDREASID HHHHHHCCCHHHHHH	38.76	30266825
20	Methylation	QSLLSTDREASIDIL HHHHCCCHHHHHHHH	41.28	115489441
23	Phosphorylation	LSTDREASIDILHSI HCCCHHHHHHHHHHH	18.95	21044959
29	Phosphorylation	ASIDILHSIVKRDIQ HHHHHHHHHHHHHHH	26.15	20873877
32	Ubiquitination	DILHSIVKRDIQEND HHHHHHHHHHHHCCC	42.56	21890473
32	Acetylation	DILHSIVKRDIQEND HHHHHHHHHHHHCCC	42.56	25953088
32	Ubiquitination	DILHSIVKRDIQEND HHHHHHHHHHHHCCC	42.56	21906983
46	Ubiquitination	DEEAVQVKEQSILEL CHHHHHHHHHHHHHH	32.70	21906983
49	Phosphorylation	AVQVKEQSILELGSL HHHHHHHHHHHHHHH	30.17	21712546
55	Phosphorylation	QSILELGSLLAKTGQ HHHHHHHHHHHHHCC	32.60	21712546
59	Ubiquitination	ELGSLLAKTGQAAEL HHHHHHHHHCCHHHH	53.83	21906983
60	Phosphorylation	LGSLLAKTGQAAELG HHHHHHHHCCHHHHH	28.99	21712546
71	Ubiquitination	AELGGLLKYVRPFLN HHHHHHHHHHHHHHH	46.90	21906983
72	Phosphorylation	ELGGLLKYVRPFLNS HHHHHHHHHHHHHHH	11.14	28152594
79	Phosphorylation	YVRPFLNSISKAKAA HHHHHHHHHHHHHHH	30.31	20068231
81	Phosphorylation	RPFLNSISKAKAARL HHHHHHHHHHHHHHH	26.78	20068231
82	Ubiquitination	PFLNSISKAKAARLV HHHHHHHHHHHHHHH	52.84	29967540
82	Acetylation	PFLNSISKAKAARLV HHHHHHHHHHHHHHH	52.84	25953088
135	Phosphorylation	ALEARLVSLYFDTKR HHHHHHHHHHCCCHH	23.19	28152594
137	Phosphorylation	EARLVSLYFDTKRYQ HHHHHHHHCCCHHHH	7.60	28152594
140	Phosphorylation	LVSLYFDTKRYQEAL HHHHHCCCHHHHHHH	13.92	28152594
141	Acetylation	VSLYFDTKRYQEALH HHHHCCCHHHHHHHH	51.45	25953088
141	Ubiquitination	VSLYFDTKRYQEALH HHHHCCCHHHHHHHH	51.45	-
143	Phosphorylation	LYFDTKRYQEALHLG HHCCCHHHHHHHHHH	16.56	28152594
151	Phosphorylation	QEALHLGSQLLRELK HHHHHHHHHHHHHHC	24.82	30622161
175	Ubiquitination	EVQLLESKTYHALSN HHHHHHHHHHHHHCC	43.67	-
181	Phosphorylation	SKTYHALSNLPKARA HHHHHHHCCCHHHHH	36.78	28348404
185	Ubiquitination	HALSNLPKARAALTS HHHCCCHHHHHHHHC	54.38	29967540
185	Malonylation	HALSNLPKARAALTS HHHCCCHHHHHHHHC	54.38	26320211
201	Phosphorylation	RTTANAIYCPPKLQA CHHCCCCCCCHHHHH	9.11	28152594
202	S-nitrosylation	TTANAIYCPPKLQAT HHCCCCCCCHHHHHE	3.67	19483679
202	S-nitrosocysteine	TTANAIYCPPKLQAT HHCCCCCCCHHHHHE	3.67	-
205	Ubiquitination	NAIYCPPKLQATLDM CCCCCCHHHHHEEEC	38.07	29967540
209	Phosphorylation	CPPKLQATLDMQSGI CCHHHHHEEECCCCC	15.44	21044959
214	Phosphorylation	QATLDMQSGIIHAAE HHEEECCCCCCHHHH	25.89	27251275
223	Ubiquitination	IIHAAEEKDWKTAYS CCHHHHHCCHHHHHH	61.46	-
246	Ubiquitination	YDSIDSPKAITSLKY CCCCCCHHHHHHHHH	57.27	29967540
252	Ubiquitination	PKAITSLKYMLLCKI HHHHHHHHHHHHHHH	28.51	29967540
253	Phosphorylation	KAITSLKYMLLCKIM HHHHHHHHHHHHHHH	9.78	28674419
260	Sulfoxidation	YMLLCKIMLNTPEDV HHHHHHHHCCCHHHH	1.12	21406390
272	Phosphorylation	EDVQALVSGKLALRY HHHHHHHHCHHHHHH	30.94	20068231
274	Ubiquitination	VQALVSGKLALRYAG HHHHHHCHHHHHHCC	24.07	22817900
274	Acetylation	VQALVSGKLALRYAG HHHHHHCHHHHHHCC	24.07	23236377
274	Sumoylation	VQALVSGKLALRYAG HHHHHHCHHHHHHCC	24.07	28112733
284	Phosphorylation	LRYAGRQTEALKCVA HHHCCCCHHHHHHHH	23.12	-
288	Acetylation	GRQTEALKCVAQASK CCCHHHHHHHHHHHC	33.44	25953088
288	Ubiquitination	GRQTEALKCVAQASK CCCHHHHHHHHHHHC	33.44	29967540
289	S-nitrosocysteine	RQTEALKCVAQASKN CCHHHHHHHHHHHCC	2.97	-
289	S-nitrosylation	RQTEALKCVAQASKN CCHHHHHHHHHHHCC	2.97	19483679
295	Ubiquitination	KCVAQASKNRSLADF HHHHHHHCCCCHHHH	60.44	24816145
295	Acetylation	KCVAQASKNRSLADF HHHHHHHCCCCHHHH	60.44	25953088
298	Phosphorylation	AQASKNRSLADFEKA HHHHCCCCHHHHHHH	36.98	25159151
304	Acetylation	RSLADFEKALTDYRA CCHHHHHHHHHHHHH	49.00	23236377
304	Methylation	RSLADFEKALTDYRA CCHHHHHHHHHHHHH	49.00	24768953
304	Ubiquitination	RSLADFEKALTDYRA CCHHHHHHHHHHHHH	49.00	24816145
307	Phosphorylation	ADFEKALTDYRAELR HHHHHHHHHHHHHHC	35.53	29083192
309	Phosphorylation	FEKALTDYRAELRDD HHHHHHHHHHHHCCC	13.39	29083192
320	Phosphorylation	LRDDPIISTHLAKLY HCCCCCHHHHHHHHH	15.53	-
325	Ubiquitination	IISTHLAKLYDNLLE CHHHHHHHHHHHHHH	54.67	-
351	Phosphorylation	RVQIEHISSLIKLSK HHHHHHHHHHHHHCH	22.47	28348404
352	Phosphorylation	VQIEHISSLIKLSKA HHHHHHHHHHHHCHH	33.25	24719451
355	Acetylation	EHISSLIKLSKADVE HHHHHHHHHCHHHHH	52.59	25953088
355	Ubiquitination	EHISSLIKLSKADVE HHHHHHHHHCHHHHH	52.59	-
358	Ubiquitination	SSLIKLSKADVERKL HHHHHHCHHHHHHHH	60.07	29967540
364	Ubiquitination	SKADVERKLSQMILD CHHHHHHHHHHHHHH	38.70	29967540
368	Sulfoxidation	VERKLSQMILDKKFH HHHHHHHHHHHHHHC	2.70	21406390
372	Acetylation	LSQMILDKKFHGILD HHHHHHHHHHCCCEE	54.62	27452117
372	Ubiquitination	LSQMILDKKFHGILD HHHHHHHHHHCCCEE	54.62	29967540
373	Ubiquitination	SQMILDKKFHGILDQ HHHHHHHHHCCCEEC	42.11	-
396	Phosphorylation	DEPPVDKTYEAALET CCCCCCHHHHHHHHH	23.33	20068231
397	Phosphorylation	EPPVDKTYEAALETI CCCCCHHHHHHHHHH	14.87	20068231
409	Ubiquitination	ETIQNMSKVVDSLYN HHHHHHHHHHHHHHH	35.19	32015554
413	Phosphorylation	NMSKVVDSLYNKAKK HHHHHHHHHHHHHHH	22.57	28152594
415	Phosphorylation	SKVVDSLYNKAKKLT HHHHHHHHHHHHHCC	20.69	28152594
417	Ubiquitination	VVDSLYNKAKKLT-- HHHHHHHHHHHCC--	48.29	23000965
417	Acetylation	VVDSLYNKAKKLT-- HHHHHHHHHHHCC--	48.29	19608861
419	Ubiquitination	DSLYNKAKKLT---- HHHHHHHHHCC----	50.34	23000965
420	Ubiquitination	SLYNKAKKLT----- HHHHHHHHCC-----	63.32	23000965

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
14	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 PSD11_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 PSD11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GDF9_HUMAN	GDF9	physical	16169070
CCSE2_HUMAN	CCSER2	physical	16169070
CC90B_HUMAN	CCDC90B	physical	16169070
IGS21_HUMAN	IGSF21	physical	16169070
PTPRK_HUMAN	PTPRK	physical	16169070
CSN6_HUMAN	COPS6	physical	16169070
HAP1_HUMAN	HAP1	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
ZHX1_HUMAN	ZHX1	physical	16169070
MED31_HUMAN	MED31	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
G3P_HUMAN	GAPDH	physical	16169070
PTN_HUMAN	PTN	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
P53_HUMAN	TP53	physical	16169070
TBB2A_HUMAN	TUBB2A	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
ZBT16_HUMAN	ZBTB16	physical	16169070
BRD7_HUMAN	BRD7	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
RBM48_HUMAN	RBM48	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
AAPK2_HUMAN	PRKAA2	physical	19616115
AAKB2_HUMAN	PRKAB2	physical	19616115
UBP4_HUMAN	USP4	physical	23022198
A4_HUMAN	APP	physical	21832049
PSD13_HUMAN	PSMD13	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSD12_HUMAN	PSMD12	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
PSME3_HUMAN	PSME3	physical	22939629
TRUA_HUMAN	PUS1	physical	22939629
ANM6_HUMAN	PRMT6	physical	23455924
ADRM1_HUMAN	ADRM1	physical	22863883
PRS4_HUMAN	PSMC1	physical	22863883
PRS7_HUMAN	PSMC2	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSMD3_HUMAN	PSMD3	physical	22863883
PSMD6_HUMAN	PSMD6	physical	22863883
ADRM1_HUMAN	ADRM1	physical	26344197
CSN3_HUMAN	COPS3	physical	26344197
COX5A_HUMAN	COX5A	physical	26344197
DCTN1_HUMAN	DCTN1	physical	26344197
DNJA2_HUMAN	DNAJA2	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
MTCH1_HUMAN	MTCH1	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
NLRP9_HUMAN	NLRP9	physical	26344197
DPOE1_HUMAN	POLE	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
PSA5_HUMAN	PSMA5	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
PSB4_HUMAN	PSMB4	physical	26344197
PSB6_HUMAN	PSMB6	physical	26344197
PSB7_HUMAN	PSMB7	physical	26344197
PSB8_HUMAN	PSMB8	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
PSMD8_HUMAN	PSMD8	physical	26344197
PSMD9_HUMAN	PSMD9	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 PSD11_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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-79,ACETYLATION 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-417, AND MASS SPECTROMETRY.	19608861 [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-14, AND MASSSPECTROMETRY.	19690332 [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-14, AND MASSSPECTROMETRY.	18669648 [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-14 AND SER-79,ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.	17323924 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASSSPECTROMETRY.	17081983 [Abstract]