RD23A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RD23A_MOUSE
• UniProt AC: P54726
• Protein Name: UV excision repair protein RAD23 homolog A
• Gene Name: Rad23a
• Organism: Mus musculus (Mouse).
• 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 (By similarity).; 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. Reported differences to Rad23b in regard to NER activity and Xpc stabilization are probably due to differences in expression levels with Rad23a being much less expressed than Rad23b..
• Protein Sequence: MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIKEYHIDEKNFVVVMVTKAKAGQGIPAPPEASPTAVPEPSTPFPPVLASGMSHPPPTSREDKSPSEESTTTTSPESISGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQAPEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE

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
8	Ubiquitination	MAVTITLKTLQQQTF CCEEEEECHHHHCEE	38.24	22790023
16	Ubiquitination	TLQQQTFKIRMEPDE HHHHCEEEEECCCCH	32.56	22790023
26	Ubiquitination	MEPDETVKVLKEKIE CCCCHHHHHHHHHHH	49.63	22790023
36	Ubiquitination	KEKIEAEKGRDAFPV HHHHHHHCCCCCCCC	67.31	22790023
47	Acetylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	23236377
47	Malonylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	26320211
47	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	-
53	Acetylation	QKLIYAGKILSDDVP CEEEECCEECCCCCC	32.10	23236377
53	Ubiquitination	QKLIYAGKILSDDVP CEEEECCEECCCCCC	32.10	22790023
62	Ubiquitination	LSDDVPIKEYHIDEK CCCCCCCCEEEECCC	46.26	22790023
78	Acetylation	FVVVMVTKAKAGQGI EEEEEEEECCCCCCC	36.16	15614953
78	Ubiquitination	FVVVMVTKAKAGQGI EEEEEEEECCCCCCC	36.16	22790023
80	Ubiquitination	VVMVTKAKAGQGIPA EEEEEECCCCCCCCC	55.39	22790023
92	Phosphorylation	IPAPPEASPTAVPEP CCCCCCCCCCCCCCC	22.56	26824392
94	Phosphorylation	APPEASPTAVPEPST CCCCCCCCCCCCCCC	37.48	25619855
100	Phosphorylation	PTAVPEPSTPFPPVL CCCCCCCCCCCCCCC	47.23	25619855
101	Phosphorylation	TAVPEPSTPFPPVLA CCCCCCCCCCCCCCC	39.40	25619855
109	Phosphorylation	PFPPVLASGMSHPPP CCCCCCCCCCCCCCC	30.76	25619855
112	Phosphorylation	PVLASGMSHPPPTSR CCCCCCCCCCCCCCC	36.05	25619855
117	Phosphorylation	GMSHPPPTSREDKSP CCCCCCCCCCCCCCC	46.30	25619855
118	Phosphorylation	MSHPPPTSREDKSPS CCCCCCCCCCCCCCC	39.17	25619855
122	Ubiquitination	PPTSREDKSPSEEST CCCCCCCCCCCCCCC	60.56	22790023
123	Phosphorylation	PTSREDKSPSEESTT CCCCCCCCCCCCCCC	46.08	25521595
125	Phosphorylation	SREDKSPSEESTTTT CCCCCCCCCCCCCCC	62.17	27087446
128	Phosphorylation	DKSPSEESTTTTSPE CCCCCCCCCCCCCHH	27.31	25521595
129	Phosphorylation	KSPSEESTTTTSPES CCCCCCCCCCCCHHH	31.29	28973931
130	Phosphorylation	SPSEESTTTTSPESI CCCCCCCCCCCHHHH	37.04	25521595
131	Phosphorylation	PSEESTTTTSPESIS CCCCCCCCCCHHHHC	25.93	25619855
132	Phosphorylation	SEESTTTTSPESISG CCCCCCCCCHHHHCC	39.94	25619855
133	Phosphorylation	EESTTTTSPESISGS CCCCCCCCHHHHCCC	25.28	25521595
136	Phosphorylation	TTTTSPESISGSVPS CCCCCHHHHCCCCCC	25.99	21082442
138	Phosphorylation	TTSPESISGSVPSSG CCCHHHHCCCCCCCC	34.00	25619855
140	Phosphorylation	SPESISGSVPSSGSS CHHHHCCCCCCCCCC	24.86	25619855
143	Phosphorylation	SISGSVPSSGSSGRE HHCCCCCCCCCCCCH	45.21	25619855
144	Phosphorylation	ISGSVPSSGSSGREE HCCCCCCCCCCCCHH	36.30	25619855
146	Phosphorylation	GSVPSSGSSGREEDA CCCCCCCCCCCHHHH	31.41	25619855
147	Phosphorylation	SVPSSGSSGREEDAA CCCCCCCCCCHHHHH	45.45	25619855
197	Phosphorylation	NPHRAVEYLLTGIPG CHHHHHHHHHHCCCC	10.62	26239621
200	Phosphorylation	RAVEYLLTGIPGSPE HHHHHHHHCCCCCCC	30.39	26239621
205	Phosphorylation	LLTGIPGSPEPEHGS HHHCCCCCCCCCCCC	22.27	26824392
212	Phosphorylation	SPEPEHGSVQESQAP CCCCCCCCCCCCCCC	23.64	26239621
216	Phosphorylation	EHGSVQESQAPEQPA CCCCCCCCCCCCCCC	17.98	26239621
224	Phosphorylation	QAPEQPATEAAGENP CCCCCCCCHHCCCCH	32.61	26239621
295	Phosphorylation	PGELADISDVEGEVG CCCCCCHHHCCCCCC	35.83	23737553
313	Phosphorylation	EEAPQMNYIQVTPQE CCCCCCCEEEECHHH	6.33	23737553
357	Phosphorylation	LAANFLLSQNFDDE- HHHHHHHHCCCCCC-	25.81	17525332

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

Oops, there are no upstream regulatory protein records of RD23A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RD23A_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 RD23A_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RD23A_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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.
PubMed: 17525332

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASSSPECTROMETRY.
PubMed: 17242355