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JunB (human)

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; Transcription factor Cellular Component: nucleoplasm; nucleolus; nucleus; chromatin Molecular Function: protein binding; DNA binding; sequence-specific DNA binding; double-stranded DNA binding; transcription coactivator activity; transcription corepressor activity; transcription factor activity Biological Process: response to peptide hormone stimulus; response to cAMP; regulation of cell cycle; osteoclast differentiation; decidualization; osteoblast proliferation; transforming growth factor beta receptor signaling pathway; vasculogenesis; positive regulation of transcription from RNA polymerase II promoter, mitotic; response to corticosterone stimulus; response to drug; transcription initiation from RNA polymerase II promoter; response to light stimulus; transcription, DNA-dependent; embryonic process involved in female pregnancy; cellular response to hormone stimulus; trophectodermal cell differentiation; regulation of transcription from RNA polymerase II promoter; osteoblast differentiation; response to mechanical stimulus; response to cytokine stimulus; gene expression; positive regulation of transcription from RNA polymerase II promoter; positive regulation of cell differentiation; response to progesterone stimulus Reference #:  P17275 (UniProtKB) Alt. Names/Synonyms: activator protein 1; AP-1; jun B proto-oncogene; JUNB; Transcription factor jun-B 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®

Select Structure to View Below JunB

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	Sites Implicated In
transcription, altered: S79‑p, T102‑p, T104‑p activation: S79‑p, T102‑p, T104‑p molecular association, regulation: T102‑p, T104‑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

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
1	3		A23	TATGYGRAPGGLSLH
0	1		K36-u	LHDYKLLkPSLAVNL
0	3		Y47-p	AVNLADPyRSLKAPG
0	2		Y68-p	EGGGGGSyFSGQGSD
2	1		S79-p	QGSDTGAsLKLASSE
1	2		T102-p	SNGVITTtPtPPGQy
1	3		T104-p	GVITTtPtPPGQyFy
0	3		Y109-p	tPtPPGQyFyPRGGG
0	2		Y111-p	tPPGQyFyPRGGGsG
0	2		S117-p	FyPRGGGsGGGAGGA
1	0		T153	LHKMNHVTPPNVSLG
1	0		S189	YTNLSSYSPASASSG
1	0		K240	GRGASTFKEEPQTVP
0	2		K240-a	GRGASTFkEEPQTVP
0	1		K240-u	GRGASTFkEEPQTVP
1	19		S251-p	QTVPEARsRDAtPPV
1	32		T255-p	EARsRDAtPPVsPIN
1	37		S259-p	RDAtPPVsPINMEDQ
1	0		K270	MEDQERIKVERKRLR
0	1		T302	RLEDKVKTLKAENAG
1	0		K304	EDKVKTLKAENAGLS
0	1		S312-p	AENAGLSsTAGLLRE
0	1		K325-u	REQVAQLkQKVMtHV
0	1		T330-p	QLkQKVMtHVSNGCQ

	mouse
S23-p	AAAGYGRsPGSLSLH
K36	LHDYKLLKPTLALNL
Y47	ALNLADPYRGLKGPG
Y68	EGSGAGSYFSGQGSD
S79	QGSDTGASLKLASTE
T102	SNGVITTTPTPPGQY
T104	GVITTTPTPPGQYFY
Y109	TPTPPGQYFYPRGGG
Y111	TPPGQYFYPRGGGSG
S117	FYPRGGGSGGGTGGG
T150	LHKMNHVTPPNVSLG
S186	YTNLSSYSPASAPSG
K237-s	SRGASAFkEEPQTVP
K237	SRGASAFKEEPQTVP
K237	SRGASAFKEEPQTVP
S248-p	QTVPEARsRDAtPPV
T252-p	EARsRDAtPPVsPIN
S256-p	RDAtPPVsPINMEDQ
K267-s	MEDQERIkVERKRLR
T299-p	RLEDKVKtLkAENAG
K301-s	EDKVKtLkAENAGLS
S309	AENAGLSSAAGLLRE
K322	REQVAQLKQKVMTHV
T327	QLKQKVMTHVSNGCQ

	rat
S23-p	AAAGYGRsPGSLSLH
K36	LHDYKLLKPTLALNL
Y47	ALNLADPYRGLKGPG
Y68	EGSGAGSYFSGQGSD
S79	QGSDTGASLKLASTE
T102	SNGVITTTPTPPGQY
T104	GVITTTPTPPGQYFY
Y109	TPTPPGQYFYPRGGG
Y111	TPPGQYFYPRGGGSG
S117	FYPRGGGSGGGTGGG
T150-p	LHKMNHVtPPNVSLG
S186-p	YTNLSSYsPASAPSG
K237	SRGASAFKEEPQTVP
K237	SRGASAFKEEPQTVP
K237	SRGASAFKEEPQTVP
S248	QTVPEARSRDATPPV
T252	EARSRDATPPVSPIN
S256	RDATPPVSPINMEDQ
K267	MEDQERIKVERKRLR
T299	RLEDKVKTLKAENAG
K301	EDKVKTLKAENAGLS
S309	AENAGLSSAAGLLRE
K322	REQVAQLKQKVMTHV
T327	QLKQKVMTHVSNGCQ

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