dbPTM

RD23B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RD23B_HUMAN
UniProt AC	P54727
Protein Name	UV excision repair protein RAD23 homolog B
Gene Name	RAD23B
Organism	Homo sapiens (Human).
Sequence Length	409
Subcellular Localization	Nucleus. Cytoplasm. The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase upon entering mitosis, relocalizes in the cytoplasm without association wi
Protein Description	Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 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. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.; Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1..
Protein Sequence	MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGSGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MQVTLKTLQQQ ----CCEEHHHHHHC	12.97	20068231
6	Ubiquitination	--MQVTLKTLQQQTF --CCEEHHHHHHCEE	37.51	21890473
6	Ubiquitination	--MQVTLKTLQQQTF --CCEEHHHHHHCEE	37.51	21890473
6	Malonylation	--MQVTLKTLQQQTF --CCEEHHHHHHCEE	37.51	26320211
7	Phosphorylation	-MQVTLKTLQQQTFK -CCEEHHHHHHCEEE	32.67	-
14	Ubiquitination	TLQQQTFKIDIDPEE HHHHCEEECCCCHHH	42.74	21890473
14	Acetylation	TLQQQTFKIDIDPEE HHHHCEEECCCCHHH	42.74	26051181
14	Ubiquitination	TLQQQTFKIDIDPEE HHHHCEEECCCCHHH	42.74	21890473
24	Ubiquitination	IDPEETVKALKEKIE CCHHHHHHHHHHHHH	56.26	21890473
24	Ubiquitination	IDPEETVKALKEKIE CCHHHHHHHHHHHHH	56.26	21890473
27	Ubiquitination	EETVKALKEKIESEK HHHHHHHHHHHHHHC	62.92	-
32	Phosphorylation	ALKEKIESEKGKDAF HHHHHHHHHCCCCCC	48.35	25907765
34	Acetylation	KEKIESEKGKDAFPV HHHHHHHCCCCCCCC	79.23	25953088
36	Malonylation	KIESEKGKDAFPVAG HHHHHCCCCCCCCCC	57.88	26320211
36	Ubiquitination	KIESEKGKDAFPVAG HHHHHCCCCCCCCCC	57.88	-
45	Malonylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	26320211
45	2-Hydroxyisobutyrylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	-
45	Acetylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	19608861
45	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	19608861
51	Ubiquitination	QKLIYAGKILNDDTA CEEEECCEECCCCCH	35.53	21890473
51	Malonylation	QKLIYAGKILNDDTA CEEEECCEECCCCCH	35.53	26320211
51	2-Hydroxyisobutyrylation	QKLIYAGKILNDDTA CEEEECCEECCCCCH	35.53	-
51	Acetylation	QKLIYAGKILNDDTA CEEEECCEECCCCCH	35.53	23954790
51	Ubiquitination	QKLIYAGKILNDDTA CEEEECCEECCCCCH	35.53	21890473
60	Ubiquitination	LNDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	21890473
60	2-Hydroxyisobutyrylation	LNDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	-
60	Acetylation	LNDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	25953088
60	Ubiquitination	LNDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	21890473
63	Acetylation	DTALKEYKIDEKNFV CCHHHEEECCCCCEE	44.78	25953088
63	Ubiquitination	DTALKEYKIDEKNFV CCHHHEEECCCCCEE	44.78	21906983
67	Ubiquitination	KEYKIDEKNFVVVMV HEEECCCCCEEEEEE	52.52	21890473
67	Ubiquitination	KEYKIDEKNFVVVMV HEEECCCCCEEEEEE	52.52	21890473
76	Ubiquitination	FVVVMVTKPKAVSTP EEEEEEECCCEECCC	32.86	21890473
76	Acetylation	FVVVMVTKPKAVSTP EEEEEEECCCEECCC	32.86	25953088
78	Ubiquitination	VVMVTKPKAVSTPAP EEEEECCCEECCCCC	64.08	-
88	O-linked_Glycosylation	STPAPATTQQSAPAS CCCCCCCCCCCCCCC	27.07	23301498
91	O-linked_Glycosylation	APATTQQSAPASTTA CCCCCCCCCCCCCEE	26.80	23301498
95	O-linked_Glycosylation	TQQSAPASTTAVTSS CCCCCCCCCEEEEEC	25.82	23301498
96	O-linked_Glycosylation	QQSAPASTTAVTSST CCCCCCCCEEEEECC	22.38	23301498
100	O-linked_Glycosylation	PASTTAVTSSTTTTV CCCCEEEEECCCCEE	17.94	23301498
102	O-linked_Glycosylation	STTAVTSSTTTTVAQ CCEEEEECCCCEEEE	22.02	23301498
104	O-linked_Glycosylation	TAVTSSTTTTVAQAP EEEEECCCCEEEECC	23.55	23301498
105	O-linked_Glycosylation	AVTSSTTTTVAQAPT EEEECCCCEEEECCC	21.25	23301498
112	O-linked_Glycosylation	TTVAQAPTPVPALAP CEEEECCCCCCCCCC	39.68	23301498
127	O-linked_Glycosylation	TSTPASITPASATAS CCCCCCCCCCCCCCC	15.42	23301498
130	O-linked_Glycosylation	PASITPASATASSEP CCCCCCCCCCCCCCC	27.62	23301498
132	O-linked_Glycosylation	SITPASATASSEPAP CCCCCCCCCCCCCCC	25.28	OGP
134	O-linked_Glycosylation	TPASATASSEPAPAS CCCCCCCCCCCCCCC	30.77	23301498
135	O-linked_Glycosylation	PASATASSEPAPASA CCCCCCCCCCCCCCH	45.17	23301498
147	Acetylation	ASAAKQEKPAEKPAE CCHHHCCCCCCCCCC	47.21	25953088
147	Ubiquitination	ASAAKQEKPAEKPAE CCHHHCCCCCCCCCC	47.21	21906983
151	Ubiquitination	KQEKPAEKPAETPVA HCCCCCCCCCCCCCC	52.19	21906983
151	Acetylation	KQEKPAEKPAETPVA HCCCCCCCCCCCCCC	52.19	26051181
155	Phosphorylation	PAEKPAETPVATSPT CCCCCCCCCCCCCCC	25.76	29255136
159	Phosphorylation	PAETPVATSPTATDS CCCCCCCCCCCCCCC	35.16	29255136
160	Phosphorylation	AETPVATSPTATDST CCCCCCCCCCCCCCC	15.54	19664994
162	Phosphorylation	TPVATSPTATDSTSG CCCCCCCCCCCCCCC	41.79	29255136
164	Phosphorylation	VATSPTATDSTSGDS CCCCCCCCCCCCCCC	32.72	29255136
166	Phosphorylation	TSPTATDSTSGDSSR CCCCCCCCCCCCCCC	21.81	29255136
167	Phosphorylation	SPTATDSTSGDSSRS CCCCCCCCCCCCCCC	39.27	29255136
168	Phosphorylation	PTATDSTSGDSSRSN CCCCCCCCCCCCCCC	44.55	29255136
171	Phosphorylation	TDSTSGDSSRSNLFE CCCCCCCCCCCCHHC	31.04	23927012
172	Phosphorylation	DSTSGDSSRSNLFED CCCCCCCCCCCHHCH	44.46	23927012
174	Phosphorylation	TSGDSSRSNLFEDAT CCCCCCCCCHHCHHH	39.57	-
186	Phosphorylation	DATSALVTGQSYENM HHHHHHHHCCCHHHH	30.29	-
193	Sulfoxidation	TGQSYENMVTEIMSM HCCCHHHHHHHHHHC	2.36	30846556
198	Sulfoxidation	ENMVTEIMSMGYERE HHHHHHHHHCCCCHH	1.51	30846556
199	Phosphorylation	NMVTEIMSMGYEREQ HHHHHHHHCCCCHHH	18.08	-
200	Sulfoxidation	MVTEIMSMGYEREQV HHHHHHHCCCCHHHH	3.52	30846556
202	Phosphorylation	TEIMSMGYEREQVIA HHHHHCCCCHHHHHH	11.81	-
220	Methylation	ASFNNPDRAVEYLLM HHCCCHHHHHHHHHH	41.61	115490099
224	Phosphorylation	NPDRAVEYLLMGIPG CHHHHHHHHHHCCCC	9.87	25106551
227	Sulfoxidation	RAVEYLLMGIPGDRE HHHHHHHHCCCCCCH	4.17	30846556
235	O-linked_Glycosylation	GIPGDRESQAVVDPP CCCCCCHHHCCCCCC	25.08	23301498
246	O-linked_Glycosylation	VDPPQAASTGAPQSS CCCCCHHCCCCCCHH	30.32	23301498
247	O-linked_Glycosylation	DPPQAASTGAPQSSA CCCCHHCCCCCCHHH	32.41	23301498
252	O-linked_Glycosylation	ASTGAPQSSAVAAAA HCCCCCCHHHHHHHH	21.14	23301498
253	O-linked_Glycosylation	STGAPQSSAVAAAAA CCCCCCHHHHHHHHC	22.86	23301498
261	O-linked_Glycosylation	AVAAAAATTTATTTT HHHHHHCCCCEEEEE	21.69	23301498
262	O-linked_Glycosylation	VAAAAATTTATTTTT HHHHHCCCCEEEEEC	15.09	23301498
263	O-linked_Glycosylation	AAAAATTTATTTTTS HHHHCCCCEEEEECC	20.04	23301498
265	O-linked_Glycosylation	AAATTTATTTTTSSG HHCCCCEEEEECCCC	23.68	23301498
266	O-linked_Glycosylation	AATTTATTTTTSSGG HCCCCEEEEECCCCC	21.49	23301498
267	O-linked_Glycosylation	ATTTATTTTTSSGGH CCCCEEEEECCCCCC	24.58	23301498
271	O-linked_Glycosylation	ATTTTTSSGGHPLEF EEEEECCCCCCCHHH	46.86	23301498
297	Phosphorylation	QIIQQNPSLLPALLQ HHHHHCCCHHHHHHH	50.52	21712546
318	Phosphorylation	PQLLQQISQHQEHFI HHHHHHHHHHHHHHH	19.78	24275569
346	O-linked_Glycosylation	GGGGGGGSGGIAEAG CCCCCCCCCCCCCCC	36.80	OGP
359	Phosphorylation	AGSGHMNYIQVTPQE CCCCCCCEEEECHHH	5.78	-
367	Ubiquitination	IQVTPQEKEAIERLK EEECHHHHHHHHHHH	47.39	-
374	Ubiquitination	KEAIERLKALGFPEG HHHHHHHHHCCCCCC	48.03	-

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:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RD23B_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 RD23B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSMD4_HUMAN	PSMD4	physical	10488153
ATX3_HUMAN	ATXN3	physical	10915768
PAX3_HUMAN	PAX3	physical	17662948
UBE3A_HUMAN	UBE3A	physical	10373495
PRS7_YEAST	RPT1	physical	16712842
DEAF1_HUMAN	DEAF1	physical	21900206
ACBP_HUMAN	DBI	physical	21900206
PSMD4_HUMAN	PSMD4	physical	12832454
UBC_HUMAN	UBC	physical	12832454
HIF1A_HUMAN	HIF1A	physical	22537386
PSMD4_HUMAN	PSMD4	physical	20059542
ADRM1_HUMAN	ADRM1	physical	20059542
PSMD4_ARATH	RPN10	physical	20059542
RPN10_YEAST	RPN10	physical	20059542
XPC_HUMAN	XPC	physical	9372923
XPC_HUMAN	XPC	physical	9734359
PSB4_YEAST	PRE1	physical	16712842
UBA1_HUMAN	UBA1	physical	16712842
UBP5_HUMAN	USP5	physical	16712842
VIME_HUMAN	VIM	physical	16712842
EF1A1_HUMAN	EEF1A1	physical	16712842
UBC_HUMAN	UBC	physical	16712842
BRCA1_HUMAN	BRCA1	physical	16712842
PSMD1_HUMAN	PSMD1	physical	16712842
PRS7_HUMAN	PSMC2	physical	16712842
ATX3_HUMAN	ATXN3	physical	16712842
UB2V2_HUMAN	UBE2V2	physical	22939629
CHIP_HUMAN	STUB1	physical	22939629
UBQL1_HUMAN	UBQLN1	physical	22939629
SPRE_HUMAN	SPR	physical	22939629
RUXF_HUMAN	SNRPF	physical	22939629
STAT6_HUMAN	STAT6	physical	22939629
TACC3_HUMAN	TACC3	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
UBXN7_HUMAN	UBXN7	physical	22939629
SIAS_HUMAN	NANS	physical	22939629
UBC_HUMAN	UBC	physical	23314748
XPC_HUMAN	XPC	physical	21962512
PO5F1_HUMAN	POU5F1	physical	21962512
SOX2_HUMAN	SOX2	physical	21962512
CETN2_HUMAN	CETN2	physical	21962512
HDAC6_HUMAN	HDAC6	physical	23703321
PUR8_HUMAN	ADSL	physical	22863883
NUBP2_HUMAN	NUBP2	physical	22863883
PDE12_HUMAN	PDE12	physical	22863883
UBA6_HUMAN	UBA6	physical	22863883
PUF60_HUMAN	PUF60	physical	25416956
NGLY1_HUMAN	NGLY1	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
UBC_HUMAN	UBC	physical	23649778
UBC_HUMAN	UBC	physical	25752573
COMD4_HUMAN	COMMD4	physical	26344197
COR1B_HUMAN	CORO1B	physical	26344197
COR1C_HUMAN	CORO1C	physical	26344197
DAAF5_HUMAN	DNAAF5	physical	26344197
G6PD_HUMAN	G6PD	physical	26344197
ECM29_HUMAN	KIAA0368	physical	26344197
MYO6_HUMAN	MYO6	physical	26344197
PSB7_HUMAN	PSMB7	physical	26344197
SC24B_HUMAN	SEC24B	physical	26344197
SPART_HUMAN	SPG20	physical	26344197
SUMO3_HUMAN	SUMO3	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197
ZYX_HUMAN	ZYX	physical	26344197
XPC_HUMAN	XPC	physical	28514442
UBP25_HUMAN	USP25	physical	28514442
UBE4B_HUMAN	UBE4B	physical	28514442
BACD3_HUMAN	KCTD10	physical	28514442
BTBD9_HUMAN	BTBD9	physical	28514442
DDI2_HUMAN	DDI2	physical	28514442
NGLY1_HUMAN	NGLY1	physical	28514442
SPTA1_HUMAN	SPTA1	physical	16889989
PRS7_HUMAN	PSMC2	physical	28539385
PAQR3_HUMAN	PAQR3	physical	28473198
XPC_HUMAN	XPC	physical	28473198
MD2L2_HUMAN	MAD2L2	physical	28440919

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RD23B_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-45, 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-160, 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 THR-155 AND SER-160, ANDMASS SPECTROMETRY.	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-160, 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-160, 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-160, 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 THR-155 AND SER-160,INTERACTION WITH PROTEASOME, 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-160, AND MASSSPECTROMETRY.	17081983 [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 THR-155, AND MASSSPECTROMETRY.	17287340 [Abstract]