RD23B_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RD23B_RAT
• UniProt AC: Q4KMA2
• Protein Name: UV excision repair protein RAD23 homolog B
• Gene Name: Rad23b
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 415
• 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 (By similarity).; 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:Rad22b induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity)..
• Protein Sequence: MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILSDDTALKEYKIDEKNFVVVMVTKPKAVTSAVPATTQQSSSPSTTTVSSSPAAAVAQAPAPTPALAPTSTPASTTPASTTASSEPAPTGATQPEKPAEKPAQTPVLTSPAPADSTPGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPPQAVSTGTPQSPAVAAAAATTTATTTTTSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGGGGGGGGGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED

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
14	Acetylation	TLQQQTFKIDIDPEE HHHHCEEECCCCHHH	42.74	22902405
24	Acetylation	IDPEETVKALKEKIE CCHHHHHHHHHHHHH	56.26	22902405
24	Ubiquitination	IDPEETVKALKEKIE CCHHHHHHHHHHHHH	56.26	-
36	Ubiquitination	KIESEKGKDAFPVAG HHHHHCCCCCCCCCC	57.88	-
45	Acetylation	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	22902405
45	Ubiquitination	AFPVAGQKLIYAGKI CCCCCCCEEEECCEE	35.61	-
51	Acetylation	QKLIYAGKILSDDTA CEEEECCEECCCCCH	32.10	22902405
51	Ubiquitination	QKLIYAGKILSDDTA CEEEECCEECCCCCH	32.10	-
54	Phosphorylation	IYAGKILSDDTALKE EECCEECCCCCHHHE	36.59	30181290
57	Phosphorylation	GKILSDDTALKEYKI CEECCCCCHHHEEEC	38.59	30181290
60	Ubiquitination	LSDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	-
60	Acetylation	LSDDTALKEYKIDEK CCCCCHHHEEECCCC	57.44	22902405
63	Acetylation	DTALKEYKIDEKNFV CCHHHEEECCCCCEE	44.78	22902405
67	Ubiquitination	KEYKIDEKNFVVVMV HEEECCCCCEEEEEE	52.52	-
76	Acetylation	FVVVMVTKPKAVTSA EEEEEECCCCEECCC	32.86	22902405
76	Ubiquitination	FVVVMVTKPKAVTSA EEEEEECCCCEECCC	32.86	-
155	Phosphorylation	PAEKPAQTPVLTSPA CCCCCCCCCCCCCCC	19.92	22673903
159	Phosphorylation	PAQTPVLTSPAPADS CCCCCCCCCCCCCCC	32.66	23984901
160	Phosphorylation	AQTPVLTSPAPADST CCCCCCCCCCCCCCC	18.20	27097102
166	Phosphorylation	TSPAPADSTPGDSSR CCCCCCCCCCCCCCC	38.31	23984901
167	Phosphorylation	SPAPADSTPGDSSRS CCCCCCCCCCCCCCC	31.66	23984901
171	Phosphorylation	ADSTPGDSSRSNLFE CCCCCCCCCCCCCCC	33.30	22673903
172	Phosphorylation	DSTPGDSSRSNLFED CCCCCCCCCCCCCCH	44.46	22673903
174	Phosphorylation	TPGDSSRSNLFEDAT CCCCCCCCCCCCHHH	39.57	16641100
186	Phosphorylation	DATSALVTGQSYENM HHHHHHHHCCCHHHH	30.29	16641100
189	Phosphorylation	SALVTGQSYENMVTE HHHHHCCCHHHHHHH	35.44	16641100
199	Phosphorylation	NMVTEIMSMGYEREQ HHHHHHHHCCCCHHH	18.08	16641100
202	Phosphorylation	TEIMSMGYEREQVIA HHHHHCCCCHHHHHH	11.81	16641100
250	Phosphorylation	PQAVSTGTPQSPAVA CCCCCCCCCCCHHHH	20.45	22668510
253	Phosphorylation	VSTGTPQSPAVAAAA CCCCCCCCHHHHHHH	18.94	30240740
267	Phosphorylation	AATTTATTTTTSGGH HHCCEEEEEECCCCC	21.49	28689409

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

Oops, there are no upstream regulatory protein records of RD23B_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RD23B_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYH4_RAT	Myh4	physical	19182904
RPN2_RAT	Rpn2	physical	19182904
RPN1_RAT	Rpn1	physical	19182904
HSP74_RAT	Hspa4	physical	19182904
TERA_RAT	Vcp	physical	19182904
PRS6A_RAT	Psmc3	physical	19182904
UBC_RAT	Ubc	physical	19182904
EF1A1_RAT	Eef1a1	physical	19182904
EF2_RAT	Eef2	physical	19182904
NPL4_RAT	Nploc4	physical	19182904
UFD1_RAT	Ufd1l	physical	19182904
NSF1C_RAT	Nsfl1c	physical	19182904
PSMF1_RAT	Psmf1	physical	19182904
ADRM1_RAT	Adrm1	physical	19182904
SQSTM_RAT	Sqstm1	physical	19182904
UBR4_RAT	Ubr4	physical	19182904
UBP7_RAT	Usp7	physical	19182904
ACTC_RAT	Actc1	physical	19182904
ACTB_RAT	Actb	physical	19182904
DCTN2_RAT	Dctn2	physical	19182904
MYL1_RAT	Myl1	physical	19182904
TPM1_RAT	Tpm1	physical	19182904
TPM2_RAT	Tpm2	physical	19182904
TNNT3_RAT	Tnnt3	physical	19182904
VIME_RAT	Vim	physical	19182904
G3P_RAT	Gapdh	physical	19182904
ALDOC_RAT	Aldoc	physical	19182904
KPYM_RAT	Pkm	physical	19182904
TPIS_RAT	Tpi1	physical	19182904
KCRM_RAT	Ckm	physical	19182904
CATA_RAT	Cat	physical	19182904
ARGI1_RAT	Arg1	physical	19182904
TGM1_RAT	Tgm1	physical	19182904
TGM3_RAT	Tgm3	physical	19182904
FAS_RAT	Fasn	physical	19182904
ANXA1_RAT	Anxa1	physical	19182904
ANXA2_RAT	Anxa2	physical	19182904
GFAP_RAT	Gfap	physical	19182904
PRDX1_RAT	Prdx1	physical	19182904
PRDX2_RAT	Prdx2	physical	19182904
TTLL1_RAT	Ttll1	physical	19182904
CYC_RAT	Cycs	physical	19182904

Drug and Disease Associations

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