dbPTM

PSMD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSMD2_HUMAN
UniProt AC	Q13200
Protein Name	26S proteasome non-ATPase regulatory subunit 2
Gene Name	PSMD2
Organism	Homo sapiens (Human).
Sequence Length	908
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.; Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1..
Protein Sequence	MEEGGRDKAPVQPQQSPAAAPGGTDEKPSGKERRDAGDKDKEQELSEEDKQLQDELEMLVERLGEKDTSLYRPALEELRRQIRSSTTSMTSVPKPLKFLRPHYGKLKEIYENMAPGENKRFAADIISVLAMTMSGERECLKYRLVGSQEELASWGHEYVRHLAGEVAKEWQELDDAEKVQREPLLTLVKEIVPYNMAHNAEHEACDLLMEIEQVDMLEKDIDENAYAKVCLYLTSCVNYVPEPENSALLRCALGVFRKFSRFPEALRLALMLNDMELVEDIFTSCKDVVVQKQMAFMLGRHGVFLELSEDVEEYEDLTEIMSNVQLNSNFLALARELDIMEPKVPDDIYKTHLENNRFGGSGSQVDSARMNLASSFVNGFVNAAFGQDKLLTDDGNKWLYKNKDHGMLSAAASLGMILLWDVDGGLTQIDKYLYSSEDYIKSGALLACGIVNSGVRNECDPALALLSDYVLHNSNTMRLGSIFGLGLAYAGSNREDVLTLLLPVMGDSKSSMEVAGVTALACGMIAVGSCNGDVTSTILQTIMEKSETELKDTYARWLPLGLGLNHLGKGEAIEAILAALEVVSEPFRSFANTLVDVCAYAGSGNVLKVQQLLHICSEHFDSKEKEEDKDKKEKKDKDKKEAPADMGAHQGVAVLGIALIAMGEEIGAEMALRTFGHLLRYGEPTLRRAVPLALALISVSNPRLNILDTLSKFSHDADPEVSYNSIFAMGMVGSGTNNARLAAMLRQLAQYHAKDPNNLFMVRLAQGLTHLGKGTLTLCPYHSDRQLMSQVAVAGLLTVLVSFLDVRNIILGKSHYVLYGLVAAMQPRMLVTFDEELRPLPVSVRVGQAVDVVGQAGKPKTITGFQTHTTPVLLAHGERAELATEEFLPVTPILEGFVILRKNPNYDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEEGGRDK -------CCCCCCCC	10.77	-
4 (in isoform 3)	Phosphorylation	-	24.11	25159151
8	Acetylation	MEEGGRDKAPVQPQQ CCCCCCCCCCCCCCC	53.91	26051181
8	Ubiquitination	MEEGGRDKAPVQPQQ CCCCCCCCCCCCCCC	53.91	21906983
11	Ubiquitination	GGRDKAPVQPQQSPA CCCCCCCCCCCCCCC	18.12	27667366
12 (in isoform 3)	Phosphorylation	-	29.08	22210691
16	Phosphorylation	APVQPQQSPAAAPGG CCCCCCCCCCCCCCC	15.97	19664994
17	Phosphorylation	PVQPQQSPAAAPGGT CCCCCCCCCCCCCCC	22.91	32645325
19	Ubiquitination	QPQQSPAAAPGGTDE CCCCCCCCCCCCCCC	19.99	21890473
19	Neddylation	QPQQSPAAAPGGTDE CCCCCCCCCCCCCCC	19.99	32015554
19	Ubiquitination	QPQQSPAAAPGGTDE CCCCCCCCCCCCCCC	19.99	27667366
23 (in isoform 3)	Phosphorylation	-	29.00	22210691
24	Phosphorylation	PAAAPGGTDEKPSGK CCCCCCCCCCCCCCH	47.07	23927012
27	Acetylation	APGGTDEKPSGKERR CCCCCCCCCCCHHCC	47.49	26051181
27	Ubiquitination	APGGTDEKPSGKERR CCCCCCCCCCCHHCC	47.49	23000965
28 (in isoform 3)	Phosphorylation	-	46.39	22210691
29	Phosphorylation	GGTDEKPSGKERRDA CCCCCCCCCHHCCCC	73.83	23927012
30	Ubiquitination	GTDEKPSGKERRDAG CCCCCCCCHHCCCCC	44.35	16196087
31	Acetylation	TDEKPSGKERRDAGD CCCCCCCHHCCCCCC	53.00	26051181
31	Ubiquitination	TDEKPSGKERRDAGD CCCCCCCHHCCCCCC	53.00	23000965
38	Ubiquitination	KERRDAGDKDKEQEL HHCCCCCCHHHHHHH	58.67	-
38	Ubiquitination	KERRDAGDKDKEQEL HHCCCCCCHHHHHHH	58.67	21963094
39	Ubiquitination	ERRDAGDKDKEQELS HCCCCCCHHHHHHHC	70.54	21906983
41	Ubiquitination	RDAGDKDKEQELSEE CCCCCHHHHHHHCHH	68.02	21906983
46	Phosphorylation	KDKEQELSEEDKQLQ HHHHHHHCHHHHHHH	37.88	30576142
48	Ubiquitination	KEQELSEEDKQLQDE HHHHHCHHHHHHHHH	68.11	-
48	Neddylation	KEQELSEEDKQLQDE HHHHHCHHHHHHHHH	68.11	32015554
48	Ubiquitination	KEQELSEEDKQLQDE HHHHHCHHHHHHHHH	68.11	27667366
50	Ubiquitination	QELSEEDKQLQDELE HHHCHHHHHHHHHHH	57.07	22817900
58	Sulfoxidation	QLQDELEMLVERLGE HHHHHHHHHHHHHCC	8.75	30846556
59	Ubiquitination	LQDELEMLVERLGEK HHHHHHHHHHHHCCC	2.36	16196087
66	2-Hydroxyisobutyrylation	LVERLGEKDTSLYRP HHHHHCCCCCHHHHH	65.59	-
66	Ubiquitination	LVERLGEKDTSLYRP HHHHHCCCCCHHHHH	65.59	23000965
66	Ubiquitination	LVERLGEKDTSLYRP HHHHHCCCCCHHHHH	65.59	21890473
68	Phosphorylation	ERLGEKDTSLYRPAL HHHCCCCCHHHHHHH	31.53	20873877
69	Ubiquitination	RLGEKDTSLYRPALE HHCCCCCHHHHHHHH	33.27	21890473
69	Phosphorylation	RLGEKDTSLYRPALE HHCCCCCHHHHHHHH	33.27	28555341
69	Ubiquitination	RLGEKDTSLYRPALE HHCCCCCHHHHHHHH	33.27	22817900
71	Phosphorylation	GEKDTSLYRPALEEL CCCCCHHHHHHHHHH	17.83	28152594
79	Methylation	RPALEELRRQIRSST HHHHHHHHHHHHHCC	31.56	115489449
84	Phosphorylation	ELRRQIRSSTTSMTS HHHHHHHHCCCCCCC	33.40	20068231
85	Phosphorylation	LRRQIRSSTTSMTSV HHHHHHHCCCCCCCC	26.34	28985074
86	Phosphorylation	RRQIRSSTTSMTSVP HHHHHHCCCCCCCCC	24.92	20068231
87	Phosphorylation	RQIRSSTTSMTSVPK HHHHHCCCCCCCCCC	20.60	20068231
88	Phosphorylation	QIRSSTTSMTSVPKP HHHHCCCCCCCCCCC	21.83	20068231
89	Sulfoxidation	IRSSTTSMTSVPKPL HHHCCCCCCCCCCCC	2.80	21406390
90	Phosphorylation	RSSTTSMTSVPKPLK HHCCCCCCCCCCCCH	26.75	20068231
91	Phosphorylation	SSTTSMTSVPKPLKF HCCCCCCCCCCCCHH	27.99	20068231
94	Acetylation	TSMTSVPKPLKFLRP CCCCCCCCCCHHHHC	61.91	26051181
94	Ubiquitination	TSMTSVPKPLKFLRP CCCCCCCCCCHHHHC	61.91	23000965
97	Ubiquitination	TSVPKPLKFLRPHYG CCCCCCCHHHHCCCH	51.37	23000965
98	Ubiquitination	SVPKPLKFLRPHYGK CCCCCCHHHHCCCHH	10.35	-
98	Ubiquitination	SVPKPLKFLRPHYGK CCCCCCHHHHCCCHH	10.35	22817900
105	Acetylation	FLRPHYGKLKEIYEN HHHCCCHHHHHHHHH	49.58	25953088
105	Ubiquitination	FLRPHYGKLKEIYEN HHHCCCHHHHHHHHH	49.58	21906983
107	Acetylation	RPHYGKLKEIYENMA HCCCHHHHHHHHHCC	45.62	26051181
107	Ubiquitination	RPHYGKLKEIYENMA HCCCHHHHHHHHHCC	45.62	21906983
110	Phosphorylation	YGKLKEIYENMAPGE CHHHHHHHHHCCCCC	11.44	21945579
113	Sulfoxidation	LKEIYENMAPGENKR HHHHHHHCCCCCCHH	2.96	30846556
119	2-Hydroxyisobutyrylation	NMAPGENKRFAADII HCCCCCCHHHHHHHH	44.59	-
119	Ubiquitination	NMAPGENKRFAADII HCCCCCCHHHHHHHH	44.59	21906983
127	Ubiquitination	RFAADIISVLAMTMS HHHHHHHHHHHHHHC	16.06	21890473
127	Phosphorylation	RFAADIISVLAMTMS HHHHHHHHHHHHHHC	16.06	20068231
127	Ubiquitination	RFAADIISVLAMTMS HHHHHHHHHHHHHHC	16.06	23000965
131	Sulfoxidation	DIISVLAMTMSGERE HHHHHHHHHHCCCHH	2.56	28465586
132	Phosphorylation	IISVLAMTMSGEREC HHHHHHHHHCCCHHH	11.54	24719451
133	Ubiquitination	ISVLAMTMSGERECL HHHHHHHHCCCHHHH	2.88	21890473
133	Ubiquitination	ISVLAMTMSGERECL HHHHHHHHCCCHHHH	2.88	23000965
134	Phosphorylation	SVLAMTMSGERECLK HHHHHHHCCCHHHHH	28.47	27422710
137	Methylation	AMTMSGERECLKYRL HHHHCCCHHHHHHEE	43.38	115386331
141	Ubiquitination	SGERECLKYRLVGSQ CCCHHHHHHEECCCH	39.73	27667366
147	Phosphorylation	LKYRLVGSQEELASW HHHEECCCHHHHHHH	27.26	22617229
153	Phosphorylation	GSQEELASWGHEYVR CCHHHHHHHHHHHHH	46.33	25850435
156	Ubiquitination	EELASWGHEYVRHLA HHHHHHHHHHHHHHH	19.56	-
156	Ubiquitination	EELASWGHEYVRHLA HHHHHHHHHHHHHHH	19.56	23000965
158	Phosphorylation	LASWGHEYVRHLAGE HHHHHHHHHHHHHHH	9.34	23312004
162	Ubiquitination	GHEYVRHLAGEVAKE HHHHHHHHHHHHHHH	4.60	-
162	Ubiquitination	GHEYVRHLAGEVAKE HHHHHHHHHHHHHHH	4.60	23000965
168	Ubiquitination	HLAGEVAKEWQELDD HHHHHHHHHHHHCCC	65.74	21906983
178	Neddylation	QELDDAEKVQREPLL HHCCCHHHHCCCHHH	45.44	32015554
178	Ubiquitination	QELDDAEKVQREPLL HHCCCHHHHCCCHHH	45.44	21906983
184	Ubiquitination	EKVQREPLLTLVKEI HHHCCCHHHHHHHHH	4.97	21890473
184	Ubiquitination	EKVQREPLLTLVKEI HHHCCCHHHHHHHHH	4.97	21906983
184	Ubiquitination	EKVQREPLLTLVKEI HHHCCCHHHHHHHHH	4.97	22817900
186	Phosphorylation	VQREPLLTLVKEIVP HCCCHHHHHHHHHCC	36.87	-
189	Ubiquitination	EPLLTLVKEIVPYNM CHHHHHHHHHCCCCC	44.85	16196087
191	Ubiquitination	LLTLVKEIVPYNMAH HHHHHHHHCCCCCCC	2.91	21890473
191	Ubiquitination	LLTLVKEIVPYNMAH HHHHHHHHCCCCCCC	2.91	21906983
191	Ubiquitination	LLTLVKEIVPYNMAH HHHHHHHHCCCCCCC	2.91	23000965
194	Phosphorylation	LVKEIVPYNMAHNAE HHHHHCCCCCCCCCH	13.48	17323924
213	Ubiquitination	DLLMEIEQVDMLEKD HHHHHHHHHCCCCCC	42.02	-
213	Ubiquitination	DLLMEIEQVDMLEKD HHHHHHHHHCCCCCC	42.02	22817900
220	Acetylation	QVDMLEKDIDENAYA HHCCCCCCCCCCHHH	44.17	-
220	Ubiquitination	QVDMLEKDIDENAYA HHCCCCCCCCCCHHH	44.17	-
220	Ubiquitination	QVDMLEKDIDENAYA HHCCCCCCCCCCHHH	44.17	23000965
226	Phosphorylation	KDIDENAYAKVCLYL CCCCCCHHHHHHHHH	20.66	25159151
228	Ubiquitination	IDENAYAKVCLYLTS CCCCHHHHHHHHHHH	22.32	21906983
230	Ubiquitination	ENAYAKVCLYLTSCV CCHHHHHHHHHHHHH	1.72	16196087
238	Ubiquitination	LYLTSCVNYVPEPEN HHHHHHHHCCCCCCC	36.09	21890473
238	Ubiquitination	LYLTSCVNYVPEPEN HHHHHHHHCCCCCCC	36.09	21906983
238	Ubiquitination	LYLTSCVNYVPEPEN HHHHHHHHCCCCCCC	36.09	23000965
242	Ubiquitination	SCVNYVPEPENSALL HHHHCCCCCCCHHHH	56.02	23000965
244	Ubiquitination	VNYVPEPENSALLRC HHCCCCCCCHHHHHH	63.25	23000965
259	Ubiquitination	ALGVFRKFSRFPEAL HHHHHHHHCCCHHHH	5.74	16196087
267	Ubiquitination	SRFPEALRLALMLND CCCHHHHHHHHHHCC	25.59	21890473
267	Acetylation	SRFPEALRLALMLND CCCHHHHHHHHHHCC	25.59	-
267	Ubiquitination	SRFPEALRLALMLND CCCHHHHHHHHHHCC	25.59	-
267	Ubiquitination	SRFPEALRLALMLND CCCHHHHHHHHHHCC	25.59	23000965
271	Ubiquitination	EALRLALMLNDMELV HHHHHHHHHCCHHHH	2.46	23000965
273	Ubiquitination	LRLALMLNDMELVED HHHHHHHCCHHHHHH	32.39	23000965
282	Ubiquitination	MELVEDIFTSCKDVV HHHHHHHHHHCHHHH	6.77	21890473
282	Ubiquitination	MELVEDIFTSCKDVV HHHHHHHHHHCHHHH	6.77	23000965
286	Ubiquitination	EDIFTSCKDVVVQKQ HHHHHHCHHHHHHHH	54.01	23000965
292	Ubiquitination	CKDVVVQKQMAFMLG CHHHHHHHHHHHHHH	30.36	23000965
292	Ubiquitination	CKDVVVQKQMAFMLG CHHHHHHHHHHHHHH	30.36	21890473
311	Ubiquitination	FLELSEDVEEYEDLT EEEECCCHHHHHHHH	5.45	-
311	Ubiquitination	FLELSEDVEEYEDLT EEEECCCHHHHHHHH	5.45	23000965
340	Sulfoxidation	LARELDIMEPKVPDD HHHHHCCCCCCCCCC	7.82	30846556
343	Ubiquitination	ELDIMEPKVPDDIYK HHCCCCCCCCCCHHH	53.76	21906983
349	Phosphorylation	PKVPDDIYKTHLENN CCCCCCHHHHHCCCC	19.48	-
350	2-Hydroxyisobutyrylation	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	-
350	Acetylation	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	23954790
350	Malonylation	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	26320211
350	Ubiquitination	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	23000965
357	Methylation	KTHLENNRFGGSGSQ HHHCCCCCCCCCCHH	43.07	115489457
361	Phosphorylation	ENNRFGGSGSQVDSA CCCCCCCCCHHHHHH	35.33	29255136
363	Phosphorylation	NRFGGSGSQVDSARM CCCCCCCHHHHHHHH	28.82	30266825
367	Phosphorylation	GSGSQVDSARMNLAS CCCHHHHHHHHHHHH	20.93	30266825
379	Ubiquitination	LASSFVNGFVNAAFG HHHHHHHHHHHHHHC	23.68	16196087
386	Ubiquitination	GFVNAAFGQDKLLTD HHHHHHHCCCCEECC	30.01	23503661
389	Ubiquitination	NAAFGQDKLLTDDGN HHHHCCCCEECCCCC	37.19	16196087
392	Ubiquitination	FGQDKLLTDDGNKWL HCCCCEECCCCCEEE	42.34	21890473
392	Ubiquitination	FGQDKLLTDDGNKWL HCCCCEECCCCCEEE	42.34	27667366
397	2-Hydroxyisobutyrylation	LLTDDGNKWLYKNKD EECCCCCEEEEECCC	44.07	-
397	Acetylation	LLTDDGNKWLYKNKD EECCCCCEEEEECCC	44.07	23236377
397	Ubiquitination	LLTDDGNKWLYKNKD EECCCCCEEEEECCC	44.07	23000965
397	Ubiquitination	LLTDDGNKWLYKNKD EECCCCCEEEEECCC	44.07	21890473
401	Acetylation	DGNKWLYKNKDHGML CCCEEEEECCCCCHH	56.18	25953088
401	Ubiquitination	DGNKWLYKNKDHGML CCCEEEEECCCCCHH	56.18	23000965
403	Ubiquitination	NKWLYKNKDHGMLSA CEEEEECCCCCHHHH	47.12	23000965
410	Ubiquitination	KDHGMLSAAASLGMI CCCCHHHHHHHHCCE	11.77	16196087
415	Ubiquitination	LSAAASLGMILLWDV HHHHHHHCCEEEEEC	9.89	23503661
421	Ubiquitination	LGMILLWDVDGGLTQ HCCEEEEECCCCCHH	28.71	21906983
421	Ubiquitination	LGMILLWDVDGGLTQ HCCEEEEECCCCCHH	28.71	27667366
432	Phosphorylation	GLTQIDKYLYSSEDY CCHHHHHHHHCCCHH	13.71	20860994
434	Phosphorylation	TQIDKYLYSSEDYIK HHHHHHHHCCCHHHH	13.68	20860994
435	Phosphorylation	QIDKYLYSSEDYIKS HHHHHHHCCCHHHHC	25.34	20860994
436	Phosphorylation	IDKYLYSSEDYIKSG HHHHHHCCCHHHHCC	22.41	20860994
439	Phosphorylation	YLYSSEDYIKSGALL HHHCCCHHHHCCHHH	13.24	20860994
439	Ubiquitination	YLYSSEDYIKSGALL HHHCCCHHHHCCHHH	13.24	16196087
441	Ubiquitination	YSSEDYIKSGALLAC HCCCHHHHCCHHHHH	36.29	23000965
441	Ubiquitination	YSSEDYIKSGALLAC HCCCHHHHCCHHHHH	36.29	21890473
442	Phosphorylation	SSEDYIKSGALLACG CCCHHHHCCHHHHHC	21.53	21712546
459	Glutathionylation	NSGVRNECDPALALL CCCCCCCCCHHHHHH	9.67	22555962
464	Ubiquitination	NECDPALALLSDYVL CCCCHHHHHHHHHHH	14.46	16196087
493	Ubiquitination	GLAYAGSNREDVLTL CCCCCCCCHHHHHHH	50.90	16196087
499	Phosphorylation	SNREDVLTLLLPVMG CCHHHHHHHHHHHHC	18.40	-
508	Phosphorylation	LLPVMGDSKSSMEVA HHHHHCCCCCHHHHH	28.80	-
509	Ubiquitination	LPVMGDSKSSMEVAG HHHHCCCCCHHHHHH	51.82	16196087
545	Ubiquitination	ILQTIMEKSETELKD HHHHHHHHCCCHHHH	35.89	23503661
548	Phosphorylation	TIMEKSETELKDTYA HHHHHCCCHHHHHHH	54.42	28152594
551	2-Hydroxyisobutyrylation	EKSETELKDTYARWL HHCCCHHHHHHHHHH	41.62	-
551	Acetylation	EKSETELKDTYARWL HHCCCHHHHHHHHHH	41.62	25953088
551	Ubiquitination	EKSETELKDTYARWL HHCCCHHHHHHHHHH	41.62	21906983
553	Phosphorylation	SETELKDTYARWLPL CCCHHHHHHHHHHHC	19.93	28152594
553	Ubiquitination	SETELKDTYARWLPL CCCHHHHHHHHHHHC	19.93	16196087
554	Phosphorylation	ETELKDTYARWLPLG CCHHHHHHHHHHHCC	12.33	28152594
569	Ubiquitination	LGLNHLGKGEAIEAI CCCCCCCCHHHHHHH	61.00	16196087
582	Ubiquitination	AILAALEVVSEPFRS HHHHHHHHHCHHHHH	6.29	16196087
595	Ubiquitination	RSFANTLVDVCAYAG HHHHHHHHHHHHHCC	4.95	21890473
595	Ubiquitination	RSFANTLVDVCAYAG HHHHHHHHHHHHHCC	4.95	23000965
614	Ubiquitination	LKVQQLLHICSEHFD CCHHHHHHHHHHHCC	27.83	16196087
623	2-Hydroxyisobutyrylation	CSEHFDSKEKEEDKD HHHHCCHHHHHHHHH	74.73	-
623	Ubiquitination	CSEHFDSKEKEEDKD HHHHCCHHHHHHHHH	74.73	16196087
624	Ubiquitination	SEHFDSKEKEEDKDK HHHCCHHHHHHHHHH	70.43	21906983
624	Ubiquitination	SEHFDSKEKEEDKDK HHHCCHHHHHHHHHH	70.43	23000965
643	Ubiquitination	DKDKKEAPADMGAHQ HHCCCCCCCCCCHHH	29.86	-
643	Ubiquitination	DKDKKEAPADMGAHQ HHCCCCCCCCCCHHH	29.86	16196087
654	Ubiquitination	GAHQGVAVLGIALIA CHHHHHHHHHHHHHH	4.71	16196087
681	Phosphorylation	TFGHLLRYGEPTLRR HHHHHHHHCCCHHHH	26.30	25367160
683	Ubiquitination	GHLLRYGEPTLRRAV HHHHHHCCCHHHHHH	26.61	16196087
698	Phosphorylation	PLALALISVSNPRLN HHHHHHHHCCCCCCC	21.97	22210691
699	Ubiquitination	LALALISVSNPRLNI HHHHHHHCCCCCCCH	5.20	21890473
699	Ubiquitination	LALALISVSNPRLNI HHHHHHHCCCCCCCH	5.20	27667366
700	Phosphorylation	ALALISVSNPRLNIL HHHHHHCCCCCCCHH	34.03	22210691
701	Ubiquitination	LALISVSNPRLNILD HHHHHCCCCCCCHHH	24.45	21890473
701	Ubiquitination	LALISVSNPRLNILD HHHHHCCCCCCCHHH	24.45	21963094
709	Phosphorylation	PRLNILDTLSKFSHD CCCCHHHHHHHCCCC	29.50	22210691
711	Phosphorylation	LNILDTLSKFSHDAD CCHHHHHHHCCCCCC	33.47	21712546
712	Ubiquitination	NILDTLSKFSHDADP CHHHHHHHCCCCCCC	54.74	16196087
728	Ubiquitination	VSYNSIFAMGMVGSG CCHHHHCCEECCCCC	7.61	-
728	Ubiquitination	VSYNSIFAMGMVGSG CCHHHHCCEECCCCC	7.61	27667366
730	Ubiquitination	YNSIFAMGMVGSGTN HHHHCCEECCCCCCH	12.28	-
730	Ubiquitination	YNSIFAMGMVGSGTN HHHHCCEECCCCCCH	12.28	21963094
743	Ubiquitination	TNNARLAAMLRQLAQ CHHHHHHHHHHHHHH	11.35	33845483
751	Phosphorylation	MLRQLAQYHAKDPNN HHHHHHHHHCCCCCC	9.72	28102081
754	Ubiquitination	QLAQYHAKDPNNLFM HHHHHHCCCCCCEEE	61.48	23000965
754	Ubiquitination	QLAQYHAKDPNNLFM HHHHHHCCCCCCEEE	61.48	21890473
761	Sulfoxidation	KDPNNLFMVRLAQGL CCCCCEEEHHHCCCC	1.61	21406390
772	Ubiquitination	AQGLTHLGKGTLTLC CCCCCCCCCCEEEEC	20.81	-
772	Ubiquitination	AQGLTHLGKGTLTLC CCCCCCCCCCEEEEC	20.81	33845483
773	Ubiquitination	QGLTHLGKGTLTLCP CCCCCCCCCEEEECC	55.90	16196087
777	Phosphorylation	HLGKGTLTLCPYHSD CCCCCEEEECCCCCC	26.59	28152594
781	Phosphorylation	GTLTLCPYHSDRQLM CEEEECCCCCCHHHH	16.98	28152594
783	Phosphorylation	LTLCPYHSDRQLMSQ EEECCCCCCHHHHHH	28.75	28152594
813	Ubiquitination	VRNIILGKSHYVLYG HHHHHCCCCHHHHHH	30.52	16196087
832	Phosphorylation	MQPRMLVTFDEELRP HCCCEEEEECCCCCC	22.77	27762562
858	Acetylation	DVVGQAGKPKTITGF EEECCCCCCCEECEE	46.48	26051181
858	Malonylation	DVVGQAGKPKTITGF EEECCCCCCCEECEE	46.48	26320211
858	Ubiquitination	DVVGQAGKPKTITGF EEECCCCCCCEECEE	46.48	27667366
860	Ubiquitination	VGQAGKPKTITGFQT ECCCCCCCEECEEEC	56.92	21906983
860	Ubiquitination	VGQAGKPKTITGFQT ECCCCCCCEECEEEC	56.92	21890473
884	Phosphorylation	GERAELATEEFLPVT CCHHHHHCCCCCCCC	48.98	25338102
902	Ubiquitination	EGFVILRKNPNYDL- ECEEEEECCCCCCC-	73.62	33845483
906	Phosphorylation	ILRKNPNYDL----- EEECCCCCCC-----	21.63	29449344

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
361	S	Phosphorylation	Kinase	HPK1	Q92918	PSP
361	S	Phosphorylation	Kinase	GCK	Q12851	PSP
361	S	Phosphorylation	Kinase	NEK6	Q9HC98	PSP
361	S	Phosphorylation	Kinase	PIM1	P11309	PSP
361	S	Phosphorylation	Kinase	PIM2	Q9P1W9	PSP
361	S	Phosphorylation	Kinase	PIM3	Q86V86	PSP
361	S	Phosphorylation	Kinase	PKACA	-	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSMD2_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 PSMD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBCP1_HUMAN	UBLCP1	physical	16189514
UBE3C_HUMAN	UBE3C	physical	12692129
LRIF1_HUMAN	LRIF1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
ZBT16_HUMAN	ZBTB16	physical	16169070
PTN_HUMAN	PTN	physical	16169070
PSMD5_HUMAN	PSMD5	physical	10625621
PRS4_HUMAN	PSMC1	physical	10625621
PRS7_HUMAN	PSMC2	physical	10625621
TNR1A_HUMAN	TNFRSF1A	physical	9126987
ADRM1_HUMAN	ADRM1	physical	16990800
MDM4_HUMAN	MDM4	physical	18086887
MDM2_HUMAN	MDM2	physical	18086887
CDN1A_HUMAN	CDKN1A	physical	18086887
HERP1_HUMAN	HERPUD1	physical	21149444
UBQL4_HUMAN	UBQLN4	physical	18079109
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSME2_HUMAN	PSME2	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
UCHL5_HUMAN	UCHL5	physical	22939629
RD23B_HUMAN	RAD23B	physical	22939629
UBQL1_HUMAN	UBQLN1	physical	22939629
TPM4_HUMAN	TPM4	physical	22939629
SRXN1_HUMAN	SRXN1	physical	22939629
ECD_HUMAN	ECD	physical	22939629
UB2L3_HUMAN	UBE2L3	physical	22939629
SC24A_HUMAN	SEC24A	physical	22939629
PRS4_HUMAN	PSMC1	physical	19060904
UBCP1_HUMAN	UBLCP1	physical	23667555
UBE3C_HUMAN	UBE3C	physical	24158444
CXA1_HUMAN	GJA1	physical	24256120
ADRM1_HUMAN	ADRM1	physical	22863883
PRS4_HUMAN	PSMC1	physical	22863883
PRS7_HUMAN	PSMC2	physical	22863883
PRS6A_HUMAN	PSMC3	physical	22863883
PRS6B_HUMAN	PSMC4	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSDE_HUMAN	PSMD14	physical	22863883
PSMD1_HUMAN	PSMD1	physical	22863883
PSMD4_HUMAN	PSMD4	physical	22863883
PSMD6_HUMAN	PSMD6	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS21_HUMAN	RPS21	physical	22863883
TXNL1_HUMAN	TXNL1	physical	22863883
UBE3C_HUMAN	UBE3C	physical	11278995
UBCP1_HUMAN	UBLCP1	physical	25416956
COPB_HUMAN	COPB1	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
PFKAL_HUMAN	PFKL	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
RD23A_HUMAN	RAD23A	physical	26344197
RD23B_HUMAN	RAD23B	physical	26344197
UBCP1_HUMAN	UBLCP1	physical	28539385
RD23B_HUMAN	RAD23B	physical	28539385
UBP14_HUMAN	USP14	physical	28539385

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
DB00188	Bortezomib

Regulatory Network of PSMD2_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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361,ACETYLATION 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 SER-361, 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 AND SER-361, AND MASSSPECTROMETRY.	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 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 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]
"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-16 AND SER-361,ACETYLATION AT MET-1, 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-16 AND THR-90, AND MASSSPECTROMETRY.	17081983 [Abstract]