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Protein Page:
JunB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
JunB Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[CG]TCA-3'. Binds DNA as an homodimer or as an heterodimer with another member of the Jun/Fos family. Interacts with ITCH (via its WW domains). By growth factors. Belongs to the bZIP family. Jun subfamily. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Oncoprotein; Transcription factor
Chromosomal Location of Human Ortholog: 19p13.2
Cellular Component: chromatin; nuclear chromatin; nucleoplasm; transcription factor complex
Molecular Function: DNA binding; protein binding; transcription coactivator activity; transcription corepressor activity; transcription factor binding
Biological Process: cellular response to hormone stimulus; decidualization; embryonic process involved in female pregnancy; negative regulation of transcription from RNA polymerase II promoter; osteoblast differentiation; osteoblast proliferation; osteoclast differentiation; positive regulation of cell differentiation; positive regulation of transcription from RNA polymerase II promoter; regulation of cell cycle; regulation of cell proliferation; regulation of transcription from RNA polymerase II promoter; response to cAMP; response to corticosterone stimulus; response to cytokine stimulus; response to drug; response to light stimulus; response to lipopolysaccharide; response to mechanical stimulus; response to peptide hormone stimulus; response to progesterone stimulus; response to radiation; transcription from RNA polymerase II promoter; trophectodermal cell differentiation; vasculogenesis
Reference #:  P17275 (UniProtKB)
Gene Symbols: JUNB
Molecular weight: 35,879 Da
Basal Isoelectric point: 9.27  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

JunB

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: S79‑p, T102‑p, T104‑p
transcription, induced: Y173‑p, Y182‑p, Y188‑p
activity, induced: S79‑p, T102‑p, T104‑p
molecular association, regulation: T102‑p, T104‑p
protein degradation: S251‑p, T255‑p, S259‑p

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


 LTP 

LTP: 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.


 HTP 

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


       human

 
1 5 A23 TATGYGRAPGGLSLH
0 1 K36‑ac LHDYKLLkPSLAVNL
0 1 K36‑ub LHDYKLLkPSLAVNL
1 5 Y47‑p AVNLADPyRsLKAPG
0 1 S49‑p NLADPyRsLKAPGAR
0 2 Y68‑p EGGGGGSyFSGQGSD
2 1 S79‑p QGSDTGAsLKLASSE
0 1 T100 PNSNGVITTtPtPPG
0 1 T101 NSNGVITTtPtPPGQ
1 4 T102‑p SNGVITTtPtPPGQy
1 9 T104‑p GVITTtPtPPGQyFy
1 4 Y109‑p tPtPPGQyFyPRGGG
0 2 Y111‑p tPPGQyFyPRGGGsG
0 6 S117‑p FyPRGGGsGGGAGGA
0 1 T129‑p GGAGGGVtEEQEGFA
1 0 T153 LHKMNHVTPPNVSLG
1 1 Y173‑p PAGPGGVyAGPEPPP
1 1 Y182‑p GPEPPPVyTNLSSyS
1 1 Y188‑p VyTNLSSySPASASS
1 0 S189 yTNLSSySPASASSG
0 1 S237 LGLGRGAStFkEEPQ
0 1 T238‑p GLGRGAStFkEEPQT
1 0 K240 GRGAStFKEEPQTVP
0 3 K240‑ac GRGAStFkEEPQTVP
0 1 K240‑ub GRGAStFkEEPQTVP
1 36 S251‑p QTVPEARsRDAtPPV
1 53 T255‑p EARsRDAtPPVsPIN
2 60 S259‑p RDAtPPVsPINMEDQ
1 0 K270 MEDQERIKVERKRLR
0 1 T302 RLEDKVKTLKAENAG
1 0 K304 EDKVKTLKAENAGLS
0 1 S312‑p AENAGLSsTAGLLRE
0 1 K325‑ub REQVAQLkQKVMtHV
0 1 T330‑p QLkQKVMtHVSNGCQ
8053 : Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb
8053 : Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb
  mouse

 
S23‑p AAAGYGRsPGSLSLH
K36 LHDYKLLKPTLALNL
K36 LHDYKLLKPTLALNL
Y47 ALNLADPYRGLKGPG
G49 NLADPYRGLKGPGAR
Y68 EGSGAGSYFSGQGSD
S79 QGSDTGASLKLASTE
T100‑p PNSNGVItttPtPPG
T101‑p NSNGVItttPtPPGQ
T102‑p SNGVItttPtPPGQY
T104‑p GVItttPtPPGQYFY
Y109 tPtPPGQYFYPRGGG
Y111 tPPGQYFYPRGGGSG
S117 FYPRGGGSGGGTGGG
T126 GGTGGGVTEEQEGFA
T150 LHKMNHVTPPNVSLG
Y170 QAGPGGVYAGPEPPP
Y179 GPEPPPVYTNLSSYS
Y185 VYTNLSSYSPASAPS
S186 YTNLSSYSPASAPSG
S234‑p LGLSRGAsAFkEEPQ
A235 GLSRGAsAFkEEPQT
K237‑sm SRGAsAFkEEPQTVP
K237 SRGAsAFKEEPQTVP
K237 SRGAsAFKEEPQTVP
S248‑p QTVPEARsRDAtPPV
T252‑p EARsRDAtPPVsPIN
S256‑p RDAtPPVsPINMEDQ
K267‑sm MEDQERIkVERKRLR
T299‑p RLEDKVKtLkAENAG
K301‑sm EDKVKtLkAENAGLS
S309 AENAGLSSAAGLLRE
K322 REQVAQLKQKVMTHV
T327 QLKQKVMTHVSNGCQ
8053 : Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb
8053 : Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb
  rat

 
S23‑p AAAGYGRsPGSLSLH
K36 LHDYKLLKPTLALNL
K36 LHDYKLLKPTLALNL
Y47 ALNLADPYRGLKGPG
G49 NLADPYRGLKGPGAR
Y68 EGSGAGSYFSGQGSD
S79 QGSDTGASLKLASTE
T100 PNSNGVITTTPTPPG
T101 NSNGVITTTPTPPGQ
T102 SNGVITTTPTPPGQY
T104 GVITTTPTPPGQYFY
Y109 TPTPPGQYFYPRGGG
Y111 TPPGQYFYPRGGGSG
S117 FYPRGGGSGGGTGGG
T126 GGTGGGVTEEQEGFA
T150‑p LHKMNHVtPPNVSLG
Y170 QAGPGGVYAGPEPPP
Y179 GPEPPPVYTNLSSYs
Y185 VYTNLSSYsPASAPS
S186‑p YTNLSSYsPASAPSG
S234 LGLSRGASAFkEEPQ
A235 GLSRGASAFkEEPQT
K237 SRGASAFKEEPQTVP
K237‑ac SRGASAFkEEPQTVP
K237 SRGASAFKEEPQTVP
S248 QTVPEARSRDAtPPV
T252‑p EARSRDAtPPVsPIN
S256‑p RDAtPPVsPINMEDQ
K267 MEDQERIKVERKRLR
T299 RLEDKVKTLKAENAG
K301 EDKVKTLKAENAGLS
S309 AENAGLSSAAGLLRE
K322 REQVAQLKQKVMTHV
T327 QLKQKVMTHVSNGCQ
8053 : Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb
8053 : Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb
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