dbPTM

PSD13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSD13_HUMAN
UniProt AC	Q9UNM6
Protein Name	26S proteasome non-ATPase regulatory subunit 13
Gene Name	PSMD13
Organism	Homo sapiens (Human).
Sequence Length	376
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	MKDVPGFLQQSQNSGPGQPAVWHRLEELYTKKLWHQLTLQVLDFVQDPCFAQGDGLIKLYENFISEFEHRVNPLSLVEIILHVVRQMTDPNVALTFLEKTREKVKSSDEAVILCKTAIGALKLNIGDLQVTKETIEDVEEMLNNLPGVTSVHSRFYDLSSKYYQTIGNHASYYKDALRFLGCVDIKDLPVSEQQERAFTLGLAGLLGEGVFNFGELLMHPVLESLRNTDRQWLIDTLYAFNSGNVERFQTLKTAWGQQPDLAANEAQLLRKIQLLCLMEMTFTRPANHRQLTFEEIAKSAKITVNEVELLVMKALSVGLVKGSIDEVDKRVHMTWVQPRVLDLQQIKGMKDRLEFWCTDVKSMEMLVEHQAHDILT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Ubiquitination	------MKDVPGFLQ ------CCCCCCHHH	68.39	21890473
31	Ubiquitination	RLEELYTKKLWHQLT HHHHHHHHHHHHHHH	32.10	21906983
31	Acetylation	RLEELYTKKLWHQLT HHHHHHHHHHHHHHH	32.10	27452117
32	Ubiquitination	LEELYTKKLWHQLTL HHHHHHHHHHHHHHH	49.35	22817900
65	Phosphorylation	KLYENFISEFEHRVN HHHHHHHHHCHHHCC	31.90	-
88	Phosphorylation	LHVVRQMTDPNVALT HHHHHHCCCCCHHHH	39.71	20068231
95	Phosphorylation	TDPNVALTFLEKTRE CCCCHHHHHHHHHHH	19.21	20068231
99	Ubiquitination	VALTFLEKTREKVKS HHHHHHHHHHHHHCC	55.84	23000965
100	Phosphorylation	ALTFLEKTREKVKSS HHHHHHHHHHHHCCC	34.38	29978859
101	Ubiquitination	LTFLEKTREKVKSSD HHHHHHHHHHHCCCC	53.45	23000965
101	Ubiquitination	LTFLEKTREKVKSSD HHHHHHHHHHHCCCC	53.45	21890473
103	Ubiquitination	FLEKTREKVKSSDEA HHHHHHHHHCCCCHH	52.23	23000965
105	Ubiquitination	EKTREKVKSSDEAVI HHHHHHHCCCCHHHH	56.14	23000965
106	Phosphorylation	KTREKVKSSDEAVIL HHHHHHCCCCHHHHH	46.11	22817900
107	Ubiquitination	TREKVKSSDEAVILC HHHHHCCCCHHHHHC	33.48	23000965
114	S-nitrosylation	SDEAVILCKTAIGAL CCHHHHHCHHHHHHH	2.24	2212679
115	Ubiquitination	DEAVILCKTAIGALK CHHHHHCHHHHHHHH	37.23	23000965
117	Ubiquitination	AVILCKTAIGALKLN HHHHCHHHHHHHHCC	5.45	23000965
117	Ubiquitination	AVILCKTAIGALKLN HHHHCHHHHHHHHCC	5.45	21890473
122	Ubiquitination	KTAIGALKLNIGDLQ HHHHHHHHCCCCCCC	38.67	23000965
124	Ubiquitination	AIGALKLNIGDLQVT HHHHHHCCCCCCCCC	34.31	21890473
124	Ubiquitination	AIGALKLNIGDLQVT HHHHHHCCCCCCCCC	34.31	23000965
131	Phosphorylation	NIGDLQVTKETIEDV CCCCCCCCHHHHHHH	15.37	-
132	Ubiquitination	IGDLQVTKETIEDVE CCCCCCCHHHHHHHH	54.74	21906983
134	Ubiquitination	DLQVTKETIEDVEEM CCCCCHHHHHHHHHH	31.09	22817900
141	Sulfoxidation	TIEDVEEMLNNLPGV HHHHHHHHHHCCCCC	2.84	21406390
149	Phosphorylation	LNNLPGVTSVHSRFY HHCCCCCCCHHHHHH	30.83	21044959
150	Phosphorylation	NNLPGVTSVHSRFYD HCCCCCCCHHHHHHC	18.54	21044959
156	Phosphorylation	TSVHSRFYDLSSKYY CCHHHHHHCCCCCHH	18.18	22817900
161	Ubiquitination	RFYDLSSKYYQTIGN HHHCCCCCHHHHHCC	44.60	23000965
161	Acetylation	RFYDLSSKYYQTIGN HHHCCCCCHHHHHCC	44.60	26051181
162	Phosphorylation	FYDLSSKYYQTIGNH HHCCCCCHHHHHCCC	11.62	28152594
163	Ubiquitination	YDLSSKYYQTIGNHA HCCCCCHHHHHCCCH	11.69	23000965
163	Ubiquitination	YDLSSKYYQTIGNHA HCCCCCHHHHHCCCH	11.69	21890473
163	Phosphorylation	YDLSSKYYQTIGNHA HCCCCCHHHHHCCCH	11.69	28152594
163 (in isoform 2)	Ubiquitination	-	11.69	-
171	Phosphorylation	QTIGNHASYYKDALR HHHCCCHHHHHHHHH	22.80	28152594
172	Phosphorylation	TIGNHASYYKDALRF HHCCCHHHHHHHHHH	18.47	28152594
173	Phosphorylation	IGNHASYYKDALRFL HCCCHHHHHHHHHHC	10.41	28152594
174	Ubiquitination	GNHASYYKDALRFLG CCCHHHHHHHHHHCC	28.43	23000965
176	Ubiquitination	HASYYKDALRFLGCV CHHHHHHHHHHCCCE	9.11	23000965
176 (in isoform 2)	Ubiquitination	-	9.11	-
176	Ubiquitination	HASYYKDALRFLGCV CHHHHHHHHHHCCCE	9.11	21890473
182	S-nitrosylation	DALRFLGCVDIKDLP HHHHHCCCEECCCCC	2.43	19483679
182	Glutathionylation	DALRFLGCVDIKDLP HHHHHCCCEECCCCC	2.43	22555962
182	S-nitrosocysteine	DALRFLGCVDIKDLP HHHHHCCCEECCCCC	2.43	-
186	Ubiquitination	FLGCVDIKDLPVSEQ HCCCEECCCCCCCHH	49.07	23000965
186	Acetylation	FLGCVDIKDLPVSEQ HCCCEECCCCCCCHH	49.07	26051181
188	Ubiquitination	GCVDIKDLPVSEQQE CCEECCCCCCCHHHH	3.71	23000965
191	Phosphorylation	DIKDLPVSEQQERAF ECCCCCCCHHHHHHH	27.96	21712546
218	Sulfoxidation	FNFGELLMHPVLESL CCHHHHHHHHHHHHH	5.40	28183972
252	Ubiquitination	VERFQTLKTAWGQQP HHHHHHHHHHHCCCC	39.31	21906983
254 (in isoform 2)	Ubiquitination	-	13.55	-
254	Ubiquitination	RFQTLKTAWGQQPDL HHHHHHHHHCCCCCC	13.55	22817900
295	Ubiquitination	HRQLTFEEIAKSAKI CCCCCHHHHHHHCCC	44.02	16196087
298	Ubiquitination	LTFEEIAKSAKITVN CCHHHHHHHCCCCHH	57.52	21906983
298	Acetylation	LTFEEIAKSAKITVN CCHHHHHHHCCCCHH	57.52	19608861
300	Acetylation	FEEIAKSAKITVNEV HHHHHHHCCCCHHHH	13.43	19608861
300	Ubiquitination	FEEIAKSAKITVNEV HHHHHHHCCCCHHHH	13.43	22817900
301	Ubiquitination	EEIAKSAKITVNEVE HHHHHHCCCCHHHHH	46.10	22817900
303	Ubiquitination	IAKSAKITVNEVELL HHHHCCCCHHHHHHH	19.30	22817900
312	Sulfoxidation	NEVELLVMKALSVGL HHHHHHHHHHHHHCC	1.80	21406390
313	Ubiquitination	EVELLVMKALSVGLV HHHHHHHHHHHHCCC	38.40	33845483
313	Acetylation	EVELLVMKALSVGLV HHHHHHHHHHHHCCC	38.40	7978785
315	Ubiquitination	ELLVMKALSVGLVKG HHHHHHHHHHCCCCC	3.39	33845483
321	Ubiquitination	ALSVGLVKGSIDEVD HHHHCCCCCCHHHHH	52.57	22817900
323	Ubiquitination	SVGLVKGSIDEVDKR HHCCCCCCHHHHHHH	22.58	22817900
323	Phosphorylation	SVGLVKGSIDEVDKR HHCCCCCCHHHHHHH	22.58	-
323 (in isoform 2)	Ubiquitination	-	22.58	-
323	Ubiquitination	SVGLVKGSIDEVDKR HHCCCCCCHHHHHHH	22.58	21890473
329	Acetylation	GSIDEVDKRVHMTWV CCHHHHHHHHHEEEE	62.59	27452117
329	Ubiquitination	GSIDEVDKRVHMTWV CCHHHHHHHHHEEEE	62.59	-
347	Malonylation	VLDLQQIKGMKDRLE CCCHHHHCCCHHHHH	48.92	26320211
347	Acetylation	VLDLQQIKGMKDRLE CCCHHHHCCCHHHHH	48.92	25953088
347	Ubiquitination	VLDLQQIKGMKDRLE CCCHHHHCCCHHHHH	48.92	22817900
349 (in isoform 2)	Ubiquitination	-	3.29	-
349	Ubiquitination	DLQQIKGMKDRLEFW CHHHHCCCHHHHHHE	3.29	22817900
349	Ubiquitination	DLQQIKGMKDRLEFW CHHHHCCCHHHHHHE	3.29	21890473
350	Ubiquitination	LQQIKGMKDRLEFWC HHHHCCCHHHHHHEE	48.65	22817900
352	Ubiquitination	QIKGMKDRLEFWCTD HHCCCHHHHHHEECC	30.51	22817900
361	Ubiquitination	EFWCTDVKSMEMLVE HHEECCHHHHHHHHH	47.06	16196087
362	Phosphorylation	FWCTDVKSMEMLVEH HEECCHHHHHHHHHH	21.59	28348404
363	Ubiquitination	WCTDVKSMEMLVEHQ EECCHHHHHHHHHHH	2.66	16196087
363	Sulfoxidation	WCTDVKSMEMLVEHQ EECCHHHHHHHHHHH	2.66	30846556
365	Sulfoxidation	TDVKSMEMLVEHQAH CCHHHHHHHHHHHHH	3.68	30846556

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 PSD13_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSD13_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 PSD13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSMD2_HUMAN	PSMD2	physical	17353931
PSD12_HUMAN	PSMD12	physical	17353931
PSMD1_HUMAN	PSMD1	physical	17353931
PSD11_HUMAN	PSMD11	physical	17353931
PRS6A_HUMAN	PSMC3	physical	17353931
PSMD3_HUMAN	PSMD3	physical	17353931
PRS4_HUMAN	PSMC1	physical	17353931
PRS6B_HUMAN	PSMC4	physical	17353931
PRS7_HUMAN	PSMC2	physical	17353931
PRS8_HUMAN	PSMC5	physical	17353931
PSDE_HUMAN	PSMD14	physical	17353931
PSMD7_HUMAN	PSMD7	physical	17353931
PSMD8_HUMAN	PSMD8	physical	17353931
PSMD4_HUMAN	PSMD4	physical	17353931
PSA3_HUMAN	PSMA3	physical	17353931
MTDC_HUMAN	MTHFD2	physical	17353931
PRS10_HUMAN	PSMC6	physical	17353931
PSMD6_HUMAN	PSMD6	physical	17353931
PSA1_HUMAN	PSMA1	physical	17353931
PSA6_HUMAN	PSMA6	physical	17353931
GHC1_HUMAN	SLC25A22	physical	17353931
PSA7_HUMAN	PSMA7	physical	17353931
CRUM1_HUMAN	CRB1	physical	17353931
FES_HUMAN	FES	physical	17353931
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
UBP14_HUMAN	USP14	physical	22939629
RD23B_HUMAN	RAD23B	physical	22939629
UN45A_HUMAN	UNC45A	physical	22939629
ZCHC8_HUMAN	ZCCHC8	physical	22939629
RBBP4_HUMAN	RBBP4	physical	22939629
ADRM1_HUMAN	ADRM1	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
LIPA1_HUMAN	PPFIA1	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
PSD11_HUMAN	PSMD11	physical	22863883
PSDE_HUMAN	PSMD14	physical	22863883
PSMD1_HUMAN	PSMD1	physical	22863883
PSMD2_HUMAN	PSMD2	physical	22863883
PSMD3_HUMAN	PSMD3	physical	22863883
PSMD4_HUMAN	PSMD4	physical	22863883
PSMD6_HUMAN	PSMD6	physical	22863883
RANB9_HUMAN	RANBP9	physical	22863883
RS21_HUMAN	RPS21	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
STRN4_HUMAN	STRN4	physical	22863883
TXNL1_HUMAN	TXNL1	physical	22863883
UBR4_HUMAN	UBR4	physical	22863883
UCHL5_HUMAN	UCHL5	physical	22863883
RPE65_HUMAN	RPE65	physical	24849605
PSB8_HUMAN	PSMB8	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD8_HUMAN	PSMD8	physical	26344197
ANCHR_HUMAN	ZFYVE19	physical	26344197
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 PSD13_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-298, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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-106, AND MASSSPECTROMETRY.	17323924 [Abstract]