dbPTM

RD23A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RD23A_HUMAN
UniProt AC	P54725
Protein Name	UV excision repair protein RAD23 homolog A
Gene Name	RAD23A
Organism	Homo sapiens (Human).
Sequence Length	363
Subcellular Localization	Nucleus.
Protein Description	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; Involved in vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 vpr with the host proteasome..
Protein Sequence	MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MAVTITLKTLQQQTF CCEEEEECHHHHCEE	38.24	21890473
8	Ubiquitination	MAVTITLKTLQQQTF CCEEEEECHHHHCEE	38.24	21890473
8	Ubiquitination	MAVTITLKTLQQQTF CCEEEEECHHHHCEE	38.24	21890473
16	Ubiquitination	TLQQQTFKIRMEPDE HHHHCEEEEECCCCH	32.56	21890473
16	Acetylation	TLQQQTFKIRMEPDE HHHHCEEEEECCCCH	32.56	25953088
16	Ubiquitination	TLQQQTFKIRMEPDE HHHHCEEEEECCCCH	32.56	21906983
16	Ubiquitination	TLQQQTFKIRMEPDE HHHHCEEEEECCCCH	32.56	21890473
19	Sulfoxidation	QQTFKIRMEPDETVK HCEEEEECCCCHHHH	11.32	21406390
26	Ubiquitination	MEPDETVKVLKEKIE CCCCHHHHHHHHHHH	49.63	21890473
26	Ubiquitination	MEPDETVKVLKEKIE CCCCHHHHHHHHHHH	49.63	21890473
26	Ubiquitination	MEPDETVKVLKEKIE CCCCHHHHHHHHHHH	49.63	21906983
29	Ubiquitination	DETVKVLKEKIEAEK CHHHHHHHHHHHHHC	61.01	-
31	Ubiquitination	TVKVLKEKIEAEKGR HHHHHHHHHHHHCCC	44.23	-
33	Ubiquitination	KVLKEKIEAEKGRDA HHHHHHHHHHCCCCC	62.94	-
36	Ubiquitination	KEKIEAEKGRDAFPV HHHHHHHCCCCCCCC	67.31	-
47	Malonylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	26320211
47	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	21890473
47	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	21890473
47	Acetylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	23954790
47	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	21890473
53	Ubiquitination	QKLIYAGKILSDDVP CEEEECCEECCCCCC	32.10	21890473
53	Ubiquitination	QKLIYAGKILSDDVP CEEEECCEECCCCCC	32.10	21890473
53	Ubiquitination	QKLIYAGKILSDDVP CEEEECCEECCCCCC	32.10	21890473
53	Acetylation	QKLIYAGKILSDDVP CEEEECCEECCCCCC	32.10	23954790
56	Phosphorylation	IYAGKILSDDVPIRD EECCEECCCCCCCCC	34.93	-
64	Ubiquitination	DDVPIRDYRIDEKNF CCCCCCCEEECCCCE	10.30	-
69	Ubiquitination	RDYRIDEKNFVVVMV CCEEECCCCEEEEEE	52.52	21890473
69	Ubiquitination	RDYRIDEKNFVVVMV CCEEECCCCEEEEEE	52.52	21906983
69	Ubiquitination	RDYRIDEKNFVVVMV CCEEECCCCEEEEEE	52.52	21890473
70	Ubiquitination	DYRIDEKNFVVVMVT CEEECCCCEEEEEEE	32.66	-
78	Ubiquitination	FVVVMVTKTKAGQGT EEEEEEEECCCCCCC	36.30	21906983
80	Ubiquitination	VVMVTKTKAGQGTSA EEEEEECCCCCCCCC	52.67	20972266
85	Phosphorylation	KTKAGQGTSAPPEAS ECCCCCCCCCCCCCC	17.52	29496963
86	Phosphorylation	TKAGQGTSAPPEASP CCCCCCCCCCCCCCC	45.67	25850435
86	Ubiquitination	TKAGQGTSAPPEASP CCCCCCCCCCCCCCC	45.67	-
92	Phosphorylation	TSAPPEASPTAAPES CCCCCCCCCCCCCCC	22.56	25159151
94	Phosphorylation	APPEASPTAAPESST CCCCCCCCCCCCCCC	32.72	25159151
99	Phosphorylation	SPTAAPESSTSFPPA CCCCCCCCCCCCCCC	37.55	29116813
100	Phosphorylation	PTAAPESSTSFPPAP CCCCCCCCCCCCCCC	26.80	25159151
101	Phosphorylation	TAAPESSTSFPPAPT CCCCCCCCCCCCCCC	43.60	28464451
102	Phosphorylation	AAPESSTSFPPAPTS CCCCCCCCCCCCCCC	37.39	28464451
108	O-linked_Glycosylation	TSFPPAPTSGMSHPP CCCCCCCCCCCCCCC	39.76	OGP
108	Phosphorylation	TSFPPAPTSGMSHPP CCCCCCCCCCCCCCC	39.76	25850435
109	Phosphorylation	SFPPAPTSGMSHPPP CCCCCCCCCCCCCCC	31.29	28122231
112	Phosphorylation	PAPTSGMSHPPPAAR CCCCCCCCCCCCCCC	36.05	26074081
122	Ubiquitination	PPAAREDKSPSEESA CCCCCCCCCCCCCCC	60.56	18781797
122	Acetylation	PPAAREDKSPSEESA CCCCCCCCCCCCCCC	60.56	26051181
123	Phosphorylation	PAAREDKSPSEESAP CCCCCCCCCCCCCCC	46.08	29255136
125	Phosphorylation	AREDKSPSEESAPTT CCCCCCCCCCCCCCC	62.17	29255136
128	Phosphorylation	DKSPSEESAPTTSPE CCCCCCCCCCCCCCC	35.18	29255136
131	Phosphorylation	PSEESAPTTSPESVS CCCCCCCCCCCCCCC	39.35	30266825
132	Phosphorylation	SEESAPTTSPESVSG CCCCCCCCCCCCCCC	41.02	29255136
133	Phosphorylation	EESAPTTSPESVSGS CCCCCCCCCCCCCCC	29.19	23927012
136	Phosphorylation	APTTSPESVSGSVPS CCCCCCCCCCCCCCC	25.60	23927012
138	Phosphorylation	TTSPESVSGSVPSSG CCCCCCCCCCCCCCC	34.33	23927012
140	Phosphorylation	SPESVSGSVPSSGSS CCCCCCCCCCCCCCC	24.29	23927012
143	Phosphorylation	SVSGSVPSSGSSGRE CCCCCCCCCCCCCCC	45.21	23927012
144	Phosphorylation	VSGSVPSSGSSGREE CCCCCCCCCCCCCCC	36.30	23927012
146	Phosphorylation	GSVPSSGSSGREEDA CCCCCCCCCCCCCHH	31.41	23927012
147	Phosphorylation	SVPSSGSSGREEDAA CCCCCCCCCCCCHHH	45.45	23927012
155	Phosphorylation	GREEDAASTLVTGSE CCCCHHHHHCCCCHH	24.80	27251275
156	Phosphorylation	REEDAASTLVTGSEY CCCHHHHHCCCCHHH	22.11	27251275
159	Phosphorylation	DAASTLVTGSEYETM HHHHHCCCCHHHHHH	37.80	26552605
161	Phosphorylation	ASTLVTGSEYETMLT HHHCCCCHHHHHHHH	27.86	26552605
163	Phosphorylation	TLVTGSEYETMLTEI HCCCCHHHHHHHHHH	20.56	20068231
165	Phosphorylation	VTGSEYETMLTEIMS CCCHHHHHHHHHHHH	19.31	20068231
166	Sulfoxidation	TGSEYETMLTEIMSM CCHHHHHHHHHHHHC	2.66	30846556
168	O-linked_Glycosylation	SEYETMLTEIMSMGY HHHHHHHHHHHHCCC	16.79	OGP
168	Phosphorylation	SEYETMLTEIMSMGY HHHHHHHHHHHHCCC	16.79	23663014
171	Sulfoxidation	ETMLTEIMSMGYERE HHHHHHHHHCCCCHH	1.51	30846556
172	Phosphorylation	TMLTEIMSMGYERER HHHHHHHHCCCCHHH	18.08	23663014
173	Sulfoxidation	MLTEIMSMGYERERV HHHHHHHCCCCHHHH	3.52	30846556
175	Phosphorylation	TEIMSMGYERERVVA HHHHHCCCCHHHHHH	11.81	23663014
188	Phosphorylation	VAALRASYNNPHRAV HHHHHHHCCCHHHHH	20.27	28857561
197	Phosphorylation	NPHRAVEYLLTGIPG CHHHHHHHHHHCCCC	10.62	28176443
197 (in isoform 3)	Phosphorylation	-	10.62	28176443
200	Phosphorylation	RAVEYLLTGIPGSPE HHHHHHHHCCCCCCC	30.39	28176443
200 (in isoform 3)	Phosphorylation	-	30.39	30108239
205 (in isoform 3)	Phosphorylation	-	22.27	30108239
205	Phosphorylation	LLTGIPGSPEPEHGS HHHCCCCCCCCCCCC	22.27	28176443
212 (in isoform 3)	Phosphorylation	-	23.64	30108239
212	Phosphorylation	SPEPEHGSVQESQVS CCCCCCCCCCHHHCC	23.64	28176443
216 (in isoform 3)	Phosphorylation	-	20.84	30108239
216	Phosphorylation	EHGSVQESQVSEQPA CCCCCCHHHCCCCCC	20.84	28176443
219	Phosphorylation	SVQESQVSEQPATEA CCCHHHCCCCCCCHH	23.91	28176443
219 (in isoform 3)	Phosphorylation	-	23.91	30108239
224	O-linked_Glycosylation	QVSEQPATEAAGENP HCCCCCCCHHCCCCH	32.61	OGP
224 (in isoform 3)	Phosphorylation	-	32.61	30108239
224	Phosphorylation	QVSEQPATEAAGENP HCCCCCCCHHCCCCH	32.61	28176443
244	Sulfoxidation	DQPQFQNMRQVIQQN CCHHHHHHHHHHHHC	1.89	21406390
274	Phosphorylation	PQLLQQISRHQEQFI HHHHHHHHHHHHHHH	21.26	27251275
295	Phosphorylation	PGELADISDVEGEVG CCCCCCHHHCCCCCC	35.83	28348404
313	Phosphorylation	EEAPQMNYIQVTPQE CCCCCCCEEEECHHH	6.33	28464451
317	Phosphorylation	QMNYIQVTPQEKEAI CCCEEEECHHHHHHH	11.68	20068231
321	Ubiquitination	IQVTPQEKEAIERLK EEECHHHHHHHHHHH	47.39	-
357	Phosphorylation	LAANFLLSQNFDDE- HHHHHHHHCCCCCC-	25.81	17525332

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
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:10373495
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RD23A_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 RD23A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSMD4_HUMAN	PSMD4	physical	10488153
SQSTM_HUMAN	SQSTM1	physical	16189514
UBL7_HUMAN	UBL7	physical	16189514
TRAF2_HUMAN	TRAF2	physical	16189514
PSMD4_HUMAN	PSMD4	physical	12970176
UBI4P_YEAST	UBI4	physical	18054791
ATX3_HUMAN	ATXN3	physical	10915768
UBC_HUMAN	UBC	physical	16405905
P53_HUMAN	TP53	physical	15064742
MDM2_HUMAN	MDM2	physical	15064742
UBE3A_HUMAN	UBE3A	physical	10373495
FLIP1_HUMAN	FILIP1	physical	21784850
UBC_HUMAN	UBC	physical	19620964
PHYA_ARATH	PHYA	physical	19292762
VA721_ARATH	VAMP721	physical	19292762
G3PC2_ARATH	GAPC2	physical	19292762
G3PC1_ARATH	GAPC1	physical	19292762
HMGB2_ARATH	HMGB2	physical	19292762
HMGB3_ARATH	HMGB3	physical	19292762
IAR1_ARATH	IAR1	physical	19292762
KCS6_ARATH	KCS6	physical	19292762
KCS5_ARATH	KCS5	physical	19292762
UPL2_ARATH	UPL2	physical	19292762
TI11B_ARATH	JAZ6	physical	19292762
RHM1_ARATH	RHM1	physical	19292762
RHM2_ARATH	MUM4	physical	19292762
RHM3_ARATH	RHM3	physical	19292762
RL81_ARATH	EMB2296	physical	19292762
RL83_ARATH	AT4G36130	physical	19292762
PSD2A_ARATH	RPN1A	physical	19292762
PAL1_ARATH	PAL1	physical	19292762
PAL2_ARATH	PAL2	physical	19292762
PAL4_ARATH	PAL4	physical	19292762
PDX11_ARATH	PDX1.1	physical	19292762
CAPP2_ARATH	PPC2	physical	19292762
CAPP1_ARATH	PPC1	physical	19292762
CLAH2_ARATH	AT3G08530	physical	19292762
CLAH1_ARATH	AT3G11130	physical	19292762
CD48A_ARATH	CDC48	physical	19292762
CD48D_ARATH	AT3G53230	physical	19292762
CD48E_ARATH	AT5G03340	physical	19292762
METK4_ARATH	MTO3	physical	19292762
METK1_ARATH	SAM1	physical	19292762
METK3_ARATH	MAT3	physical	19292762
METK2_ARATH	SAM-2	physical	19292762
BCAT4_ARATH	BCAT4	physical	19292762
DIM_ARATH	DWF1	physical	19292762
EIN3_ARATH	EIN3	physical	19292762
AL2C4_ARATH	ALDH2C4	physical	19292762
NRL1_ARATH	NIT1	physical	19292762
PGML4_ARATH	AT3G50520	physical	19292762
SERCL_ARATH	AT5G04120	physical	19292762
RL7A2_ARATH	AT3G62870	physical	19292762
RL7A1_ARATH	AT2G47610	physical	19292762
OLEO1_ARATH	OLEO1	physical	19292762
PPI1_ARATH	PPI1	physical	19292762
CRU3_ARATH	CRU3	physical	19292762
PDX13_ARATH	RSR4	physical	19292762
MD37E_ARATH	HSC70-1	physical	19292762
HSP7E_ARATH	Hsp70b	physical	19292762
HSP7N_ARATH	ERD2	physical	19292762
HSP7C_ARATH	AT3G09440	physical	19292762
MD37C_ARATH	HSP70	physical	19292762
MD37D_ARATH	AT5G02490	physical	19292762
MD37A_ARATH	BIP1	physical	19292762
MD37F_ARATH	BIP2	physical	19292762
UBP12_ARATH	UBP12	physical	19292762
UBP13_ARATH	UBP13	physical	19292762
OLEO2_ARATH	OLEO2	physical	19292762
CRU1_ARATH	CRA1	physical	19292762
HST_ARATH	HCT	physical	19292762
CYB5E_ARATH	CB5-E	physical	19292762
CYB5B_ARATH	CB5-B	physical	19292762
HS903_ARATH	HSP81-3	physical	19292762
HS904_ARATH	Hsp81.4	physical	19292762
HS902_ARATH	HSP81-2	physical	19292762
HS901_ARATH	HSP90.1	physical	19292762
EF1A1_ARATH	AT5G60390	physical	19292762
EF1A3_ARATH	AT5G60390	physical	19292762
EF1A4_ARATH	AT5G60390	physical	19292762
EF1A2_ARATH	AT5G60390	physical	19292762
AB1F_ARATH	GCN1	physical	19292762
BAG7_ARATH	BAG7	physical	19292762
MDHC1_ARATH	AT1G04410	physical	19292762
OST1B_ARATH	AT2G01720	physical	19292762
H12_ARATH	AT2G30620	physical	19292762
RS32_ARATH	AT3G53870	physical	19292762
RS31_ARATH	AT2G31610	physical	19292762
RS33_ARATH	AT5G35530	physical	19292762
METE1_ARATH	ATMS1	physical	19292762
METE2_ARATH	MS2	physical	19292762
C71B7_ARATH	CYP71B7	physical	19292762
PATL1_ARATH	PATL1	physical	19292762
DNMT4_ARATH	DMT2	physical	19292762
PHAX_HUMAN	PHAX	physical	21900206
ACBP_HUMAN	DBI	physical	21900206
PSMD4_HUMAN	PSMD4	physical	17408689
UBC_HUMAN	UBC	physical	17408689
UBC_HUMAN	UBC	physical	14621999
PSMD4_HUMAN	PSMD4	physical	14621999
PSMD4_HUMAN	PSMD4	physical	11827521
PRKN_HUMAN	PARK2	physical	19013454
PSA1_HUMAN	PSMA1	physical	19013454
PSA2_HUMAN	PSMA2	physical	19013454
PSA3_HUMAN	PSMA3	physical	19013454
PSA4_HUMAN	PSMA4	physical	19013454
PSA5_HUMAN	PSMA5	physical	19013454
PSA6_HUMAN	PSMA6	physical	19013454
PSA7_HUMAN	PSMA7	physical	19013454
PSB1_HUMAN	PSMB1	physical	19013454
PSB2_HUMAN	PSMB2	physical	19013454
PSB3_HUMAN	PSMB3	physical	19013454
PSB4_HUMAN	PSMB4	physical	19013454
PSB5_HUMAN	PSMB5	physical	19013454
PSB6_HUMAN	PSMB6	physical	19013454
PRS4_HUMAN	PSMC1	physical	19013454
PRS7_HUMAN	PSMC2	physical	19013454
PRS6A_HUMAN	PSMC3	physical	19013454
PRS6B_HUMAN	PSMC4	physical	19013454
PRS8_HUMAN	PSMC5	physical	19013454
PSMD1_HUMAN	PSMD1	physical	19013454
PSMD2_HUMAN	PSMD2	physical	19013454
PSMD3_HUMAN	PSMD3	physical	19013454
PSMD4_HUMAN	PSMD4	physical	19013454
PSMD5_HUMAN	PSMD5	physical	19013454
PSMD6_HUMAN	PSMD6	physical	19013454
PSMD7_HUMAN	PSMD7	physical	19013454
PSMD8_HUMAN	PSMD8	physical	19013454
PSD11_HUMAN	PSMD11	physical	19013454
PSD12_HUMAN	PSMD12	physical	19013454
PSD13_HUMAN	PSMD13	physical	19013454
PSDE_HUMAN	PSMD14	physical	19013454
ATX3_HUMAN	ATXN3	physical	19013454
EF1A1_HUMAN	EEF1A1	physical	19013454
UCHL5_HUMAN	UCHL5	physical	19013454
UBP5_HUMAN	USP5	physical	19013454
UBP13_HUMAN	USP13	physical	19013454
UBP14_HUMAN	USP14	physical	19013454
UBP25_HUMAN	USP25	physical	19013454
HUWE1_HUMAN	HUWE1	physical	19013454
UBAC1_HUMAN	UBAC1	physical	19013454
UBE2N_HUMAN	UBE2N	physical	19013454
UBE3A_HUMAN	UBE3A	physical	19013454
UBR4_HUMAN	UBR4	physical	19013454
EPS15_HUMAN	EPS15	physical	19013454
FAF1_HUMAN	FAF1	physical	19013454
SQSTM_HUMAN	SQSTM1	physical	19013454
UBC_HUMAN	UBC	physical	19013454
UIMC1_HUMAN	UIMC1	physical	19013454
PSME4_HUMAN	PSME4	physical	19013454
SEM1_HUMAN	SHFM1	physical	19013454
ADRM1_HUMAN	ADRM1	physical	19013454
BASP1_HUMAN	BASP1	physical	19013454
TXNL1_HUMAN	TXNL1	physical	19013454
RB6I2_HUMAN	ERC1	physical	19013454
GCC2_HUMAN	GCC2	physical	19013454
MORC3_HUMAN	MORC3	physical	19013454
XRCC5_HUMAN	XRCC5	physical	19013454
UBQL1_HUMAN	UBQLN1	physical	17098253
PRS8_HUMAN	PSMC5	physical	14706819
TF2H1_HUMAN	GTF2H1	physical	14706819
RD23A_HUMAN	RAD23A	physical	21047872
3MG_HUMAN	MPG	physical	10854423
UBC_HUMAN	UBC	physical	12643283
RD23B_HUMAN	RAD23B	physical	8692695
CBP_HUMAN	CREBBP	physical	11196199
RD23A_HUMAN	RAD23A	physical	16105547
RD23B_HUMAN	RAD23B	physical	16105547
P53_HUMAN	TP53	physical	16105547
PSMD4_HUMAN	PSMD4	physical	16105547
CCNA2_HUMAN	CCNA2	physical	18485873
PTTG1_HUMAN	PTTG1	physical	18485873
ATX3_HUMAN	ATXN3	physical	22970133
TERA_HUMAN	VCP	physical	22970133
UBC_HUMAN	UBC	physical	16007098
ATX3_HUMAN	ATXN3	physical	17935801
UBC_HUMAN	UBC	physical	15004330
UBC_HUMAN	UBC	physical	16712842
PSMD1_HUMAN	PSMD1	physical	16712842
PRS7_HUMAN	PSMC2	physical	16712842
ATX3_HUMAN	ATXN3	physical	16712842
UBA1_HUMAN	UBA1	physical	16712842
VIME_HUMAN	VIM	physical	16712842
EF1A1_HUMAN	EEF1A1	physical	16712842
EF2_HUMAN	EEF2	physical	16712842
HSP7C_HUMAN	HSPA8	physical	16712842
SZT2_HUMAN	SZT2	physical	16712842
BRCA2_HUMAN	BRCA2	physical	16712842
SRSF2_HUMAN	SRSF2	physical	22939629
TACC3_HUMAN	TACC3	physical	22939629
DLG4_HUMAN	DLG4	physical	23260144
PRS7_HUMAN	PSMC2	physical	23260144
PCD10_HUMAN	PCDH10	physical	23260144
KCC2A_HUMAN	CAMK2A	physical	23260144
UBC_HUMAN	UBC	physical	23314748
TRAF2_HUMAN	TRAF2	physical	23357418
UBE3A_HUMAN	UBE3A	physical	23671107
TF3C4_HUMAN	GTF3C4	physical	22863883
OGFD1_HUMAN	OGFOD1	physical	22863883
PYGL_HUMAN	PYGL	physical	22863883
UBA6_HUMAN	UBA6	physical	22863883
SYWC_HUMAN	WARS	physical	22863883
UBC_HUMAN	UBC	physical	24318982
TRAF2_HUMAN	TRAF2	physical	25416956
TRAF5_HUMAN	TRAF5	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
ZBT44_HUMAN	ZBTB44	physical	25416956
UBP25_HUMAN	USP25	physical	25416956
NGLY1_HUMAN	NGLY1	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
MINY3_HUMAN	FAM188A	physical	25416956
ANR40_HUMAN	ANKRD40	physical	25416956
ZBT8A_HUMAN	ZBTB8A	physical	25416956
UBC_HUMAN	UBC	physical	18234089
UBC_HUMAN	UBC	physical	23823328
UBC_HUMAN	UBC	physical	23562397
UBC_HUMAN	UBC	physical	22542781
COR1B_HUMAN	CORO1B	physical	26344197
MYO6_HUMAN	MYO6	physical	26344197
SUMO3_HUMAN	SUMO3	physical	26344197
TMOD3_HUMAN	TMOD3	physical	26344197
TRIP6_HUMAN	TRIP6	physical	21516116
CHK1_HUMAN	CHEK1	physical	26296656
PSMD1_HUMAN	PSMD1	physical	26296656

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 RD23A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-133; SER-205; SER-295AND SER-357, AND MASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-128, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASSSPECTROMETRY.	17693683 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-122, AND MASSSPECTROMETRY.	18781797 [Abstract]