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Protein Page:
RAD23B (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RAD23B 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. Belongs to the RAD23 family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis
Cellular Component: proteasome complex; nucleoplasm; cytoplasm; nucleolus; nucleus
Molecular Function: protein binding; damaged DNA binding; polyubiquitin binding; single-stranded DNA binding
Biological Process: nucleotide-excision repair, DNA damage recognition; proteasomal ubiquitin-dependent protein catabolic process; nucleotide-excision repair; regulation of proteasomal ubiquitin-dependent protein catabolic process; nucleotide-excision repair, DNA damage removal; spermatogenesis; DNA repair
Reference #:  P54727 (UniProtKB)
Alt. Names/Synonyms: hHR23B; HR23B; p58; RAD23 homolog B (S. cerevisiae); RAD23, yeast homolog of, B; RAD23B; RD23B; UV excision repair protein RAD23 homolog B; XP-C repair complementing complex 58 kDa; XP-C repair complementing protein; XP-C repair-complementing complex 58 kDa protein
Gene Symbols: RAD23B
Molecular weight: 43,171 Da
Basal Isoelectric point: 4.79  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RAD23B

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 K6-u __MQVTLkTLQQQTF
0 16 K14-u TLQQQTFkIDIDPEE
0 11 K24-u IDPEETVkALkEKIE
0 2 K27-u EETVkALkEKIESEK
0 24 K36-u KIESEKGkDAFPVAG
0 55 K45-u AFPVAGQkLIYAGkI
0 86 K51-u QkLIYAGkILNDDTA
0 38 K60-u LNDDTALkEYkIDEk
0 7 K63-u DTALkEYkIDEkNFV
0 49 K67-u kEYkIDEkNFVVVMV
0 80 K76-u FVVVMVTkPkAVSTP
0 9 K78-u VVMVTkPkAVSTPAP
0 40 K147-u ASAAKQEkPAEkPAE
0 68 K151-u KQEkPAEkPAEtPVA
0 14 T155-p PAEkPAEtPVAtsPT
0 3 T159-p PAEtPVAtsPTAtdS
0 24 S160-p AEtPVAtsPTAtdST
0 1 T164-p VAtsPTAtdSTSGDS
0 2 D165-ca AtsPTAtdSTSGDSS
0 1 S174 TSGDSSRSNLFEDAT
0 1 T186 DATSALVTGQSYENM
0 1 S189 SALVTGQSYENMVTE
0 1 S199 NMVTEIMSMGYEREQ
0 1 Y202 TEIMSMGYEREQVIA
0 1 S252 ASTGAPQSSAVAAAA
  mouse

 
K6-u __MQVTLkTLQQQTF
K14-u TLQQQTFkIDIDPEE
K24-u IDPEETVkALKEKIE
K27 EETVkALKEKIESEK
K36-u KIESEKGkDAFPVAG
K45-u AFPVAGQkLIYAGkI
K51-u QkLIYAGkILSDDTA
K60-u LSDDTALkEYkIDEk
K63-u DTALkEYkIDEkNFV
K67-u kEYkIDEkNFVVVMV
K76-u FVVVMVTkPkAVTTA
K78-u VVMVTkPkAVTTAVP
K147 AGATQPEKPAEkPAQ
K151-u QPEKPAEkPAQTPVL
T155 PAEkPAQTPVLTSPA
T159 PAQTPVLTSPAPADS
S160 AQTPVLTSPAPADST
A164 VLTSPAPADSTPGDS
D165 LTSPAPADSTPGDSS
S174 TPGDSSRSNLFEDAT
T186 DATSALVTGQSYENM
S189 SALVTGQSYENMVTE
S199 NMVTEIMSMGYEREQ
Y202 TEIMSMGYEREQVIA
S253-p VSTGTPQsPAVAAAA
  rat

 
K6 __MQVTLKTLQQQTF
K14 TLQQQTFKIDIDPEE
K24 IDPEETVKALKEKIE
K27 EETVKALKEKIESEK
K36 KIESEKGKDAFPVAG
K45 AFPVAGQKLIYAGkI
K51-u QKLIYAGkILSDDTA
K60 LSDDTALKEYKIDEK
K63 DTALKEYKIDEKNFV
K67 KEYKIDEKNFVVVMV
K76-u FVVVMVTkPKAVTSA
K78 VVMVTkPKAVTSAVP
K147 TGATQPEKPAEKPAQ
K151 QPEKPAEKPAQTPVL
T155 PAEKPAQTPVLTSPA
T159 PAQTPVLTSPAPADS
S160 AQTPVLTSPAPADST
A164 VLTSPAPADSTPGDS
D165 LTSPAPADSTPGDSS
S174-p TPGDSSRsNLFEDAT
T186-p DATSALVtGQsYENM
S189-p SALVtGQsYENMVTE
S199-p NMVTEIMsMGyEREQ
Y202-p TEIMsMGyEREQVIA
S253 VSTGTPQSPAVAAAA
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