RD23B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RD23B_MOUSE
• UniProt AC: P54728
• Protein Name: UV excision repair protein RAD23 homolog B
• Gene Name: Rad23b
• Organism: Mus musculus (Mouse).
• Sequence Length: 416
• Subcellular Localization: Nucleus . Cytoplasm .
• 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 (By similarity).; 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:Rad23bB induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity)..
• Protein Sequence: MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILSDDTALKEYKIDEKNFVVVMVTKPKAVTTAVPATTQPSSTPSPTAVSSSPAVAAAQAPAPTPALPPTSTPASTAPASTTASSEPAPAGATQPEKPAEKPAQTPVLTSPAPADSTPGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPPQAVSTGTPQSPAVAAAAATTTATTTTTSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGSQGGGGGGGGGGGGGGGGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MQVTLKTLQQQTF --CCEEHHHHHHCEE	37.51	22790023
14	Ubiquitination	TLQQQTFKIDIDPEE HHHHCEEECCCCHHH	42.74	22790023
14	Acetylation	TLQQQTFKIDIDPEE HHHHCEEECCCCHHH	42.74	23954790
24	Acetylation	IDPEETVKALKEKIE CCHHHHHHHHHHHHH	56.26	23954790
24	Ubiquitination	IDPEETVKALKEKIE CCHHHHHHHHHHHHH	56.26	22790023
36	Malonylation	KIESEKGKDAFPVAG HHHHHCCCCCCCCCC	57.88	26320211
36	Ubiquitination	KIESEKGKDAFPVAG HHHHHCCCCCCCCCC	57.88	-
45	Malonylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	26320211
45	Acetylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	22636495
45	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	22790023
51	Acetylation	QKLIYAGKILSDDTA CEEEECCEECCCCCH	32.10	23806337
51	Malonylation	QKLIYAGKILSDDTA CEEEECCEECCCCCH	32.10	26320211
51	Ubiquitination	QKLIYAGKILSDDTA CEEEECCEECCCCCH	32.10	-
60	Acetylation	LSDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	22826441
60	Ubiquitination	LSDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	22790023
63	Ubiquitination	DTALKEYKIDEKNFV CCHHHEEECCCCCEE	44.78	-
67	Ubiquitination	KEYKIDEKNFVVVMV HEEECCCCCEEEEEE	52.52	22790023
67	Acetylation	KEYKIDEKNFVVVMV HEEECCCCCEEEEEE	52.52	22826441
76	Ubiquitination	FVVVMVTKPKAVTTA EEEEEEECCCEEEEE	32.86	22790023
76	Acetylation	FVVVMVTKPKAVTTA EEEEEEECCCEEEEE	32.86	22826441
78	Ubiquitination	VVMVTKPKAVTTAVP EEEEECCCEEEEECC	57.98	-
151	Ubiquitination	QPEKPAEKPAQTPVL CCCCCCCCCCCCCCC	48.00	22790023
155	Phosphorylation	PAEKPAQTPVLTSPA CCCCCCCCCCCCCCC	19.92	26824392
159	Phosphorylation	PAQTPVLTSPAPADS CCCCCCCCCCCCCCC	32.66	30352176
160	Phosphorylation	AQTPVLTSPAPADST CCCCCCCCCCCCCCC	18.20	26824392
166	Phosphorylation	TSPAPADSTPGDSSR CCCCCCCCCCCCCCC	38.31	29472430
167	Phosphorylation	SPAPADSTPGDSSRS CCCCCCCCCCCCCCC	31.66	26824392
171	Phosphorylation	ADSTPGDSSRSNLFE CCCCCCCCCCCCCCC	33.30	29472430
172	Phosphorylation	DSTPGDSSRSNLFED CCCCCCCCCCCCCCH	44.46	29472430
174	Phosphorylation	TPGDSSRSNLFEDAT CCCCCCCCCCCCHHH	39.57	-
186	Phosphorylation	DATSALVTGQSYENM HHHHHHHHCCCHHHH	30.29	-
199	Phosphorylation	NMVTEIMSMGYEREQ HHHHHHHHCCCCHHH	18.08	-
202	Phosphorylation	TEIMSMGYEREQVIA HHHHHCCCCHHHHHH	11.81	-
235	Phosphorylation	GIPGDRESQAVVDPP CCCCCCHHHCCCCCC	25.08	25619855
247	Phosphorylation	DPPPQAVSTGTPQSP CCCCCCCCCCCCCCH	24.92	25619855
248	Phosphorylation	PPPQAVSTGTPQSPA CCCCCCCCCCCCCHH	38.18	25619855
250	Phosphorylation	PQAVSTGTPQSPAVA CCCCCCCCCCCHHHH	20.45	25619855
253	Phosphorylation	VSTGTPQSPAVAAAA CCCCCCCCHHHHHHH	18.94	25619855
262	Phosphorylation	AVAAAAATTTATTTT HHHHHHHCCEEEEEE	21.69	25619855
263	Phosphorylation	VAAAAATTTATTTTT HHHHHHCCEEEEEEC	15.09	25619855
264	Phosphorylation	AAAAATTTATTTTTS HHHHHCCEEEEEECC	20.04	25619855
266	Phosphorylation	AAATTTATTTTTSGG HHHCCEEEEEECCCC	23.68	25619855
267	Phosphorylation	AATTTATTTTTSGGH HHCCEEEEEECCCCC	21.49	25619855
268	Phosphorylation	ATTTATTTTTSGGHP HCCEEEEEECCCCCC	24.58	25619855
269	Phosphorylation	TTTATTTTTSGGHPL CCEEEEEECCCCCCH	19.51	25619855
270	Phosphorylation	TTATTTTTSGGHPLE CEEEEEECCCCCCHH	24.23	25619855
271	Phosphorylation	TATTTTTSGGHPLEF EEEEEECCCCCCHHH	40.46	25619855
297	Phosphorylation	QIIQQNPSLLPALLQ HHHHHCCCHHHHHHH	50.52	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RD23B_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RD23B_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RD23B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAX3_HUMAN	PAX3	physical	17662948
NGLY1_MOUSE	Ngly1	physical	16249333
TERA_MOUSE	Vcp	physical	16249333
XPA_MOUSE	Xpa	physical	9734359
XPC_MOUSE	Xpc	physical	22431748
NGLY1_MOUSE	Ngly1	physical	11562482

Drug and Disease Associations

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