Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PHB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PHB a pleiotropic membrane protein that suppresses cell proliferation, apoptosis and senescence. It plays a role both in maintaining mitochondrial integrity and in cell cycle regulation. Expression increases approximately 3-fold upon entry into G1 phase compared with other phases of the cell cycle. It helps prevent ROS-induced senescence and its expression decreases heterogeneously during cellular aging. Helps maintain the angiogenic capacity of endothelial cells. Up-regulated during activation of primary human T cells via CD3/CD28 pathways. Present in multiple cellular compartments. Large assemblies of PHB and PHB2 localize in the inner membrane of mitochondria. Acts as a mitochondrial chaperone protein, regulates mitochondrial morphogenesis, and helps regulate the organization of mitochondrial DNA. Reported to target lipid rafts. In the nucleus, it has been reported to interact with various transcription factors, modulating their activity. A potential tumor suppressor that functions as a potent transcriptional corepressor for estrogen receptor alpha. It is downregulated by androgens, and represses androgen receptor activity. Co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression. In vivo promoter occupancy studies have suggested that the PHB gene is a direct target of c-Myc. May bind to and enhance the transcriptional activity of p53. Both Phb and Phb2 are present in the circulation and can be internalized by cultured cells. Overexpressed in endometrioid ovarian adenocarcinoma and papillary serous ovarian carcinoma. Mutated in sporadic breast cancer. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor; Motility/polarity/chemotaxis; Cell cycle regulation; Apoptosis; Mitochondrial; Chaperone
Cellular Component: nucleoplasm; membrane; mitochondrion; integral to plasma membrane; cytoplasm; mitochondrial inner membrane; nucleus
Molecular Function: protein binding; enzyme binding; histone deacetylase binding
Biological Process: osteoblast differentiation; transcription from RNA polymerase II promoter; regulation of apoptosis; negative regulation of cell proliferation; progesterone receptor signaling pathway; regulation of transcription, DNA-dependent; positive regulation of transcription, DNA-dependent; histone deacetylation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of cell growth; DNA replication; negative regulation of transcription, DNA-dependent; signal transduction
Reference #:  P35232 (UniProtKB)
Alt. Names/Synonyms: PHB; PHB1; Prohibitin
Gene Symbols: PHB
Molecular weight: 29,804 Da
Basal Isoelectric point: 5.57  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PHB

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
molecular association, regulation: Y114‑p
O-GlcNAc glycosylation: Y114‑p, Y259‑p
phosphorylation: Y114‑p, S121‑gl, T258‑gl

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 1 K4-m1 ____MAAkVFESIGk
0 1 K11-m1 kVFESIGkFGLALAV
0 1 S82-p NVPVITGskDLQNVN
0 1 K83-ub VPVITGskDLQNVNI
0 1 K83 VPVITGsKDLQNVNI
0 1 T91-p DLQNVNItLRILFRP
0 4 S101-p ILFRPVAsQLPRIFt
0 1 F107 AsQLPRIFtsIGEDy
0 1 T108-p sQLPRIFtsIGEDyD
0 3 S109-p QLPRIFtsIGEDyDE
5 0 Y114-p FtsIGEDyDERVLPs
1 0 S121-gl yDERVLPsItTEILk
0 1 T123-p ERVLPsItTEILkSV
0 6 K128-ub sItTEILkSVVARFD
0 1 K128 sItTEILKSVVARFD
0 2 K128-ac sItTEILkSVVARFD
0 3 S151-p ELVSRQVsDDLTERA
0 1 K177-ub LTHLTFGkEFTEAVE
0 4 K186-ub FTEAVEAkQVAQQEA
0 1 K186 FTEAVEAKQVAQQEA
0 2 K186 FTEAVEAKQVAQQEA
0 4 K202-ac RARFVVEkAEQQkKA
0 1 K202-ub RARFVVEkAEQQkKA
0 22 K207-ac VEkAEQQkKAAIIsA
0 1 K208 EkAEQQkKAAIIsAE
0 1 S213-p QkKAAIIsAEGDskA
0 1 S218-p IIsAEGDskAAELIA
0 1 K219 IsAEGDsKAAELIAN
0 5 K219-ub IsAEGDskAAELIAN
0 1 K240-ub DGLIELRkLEAAEDI
0 444 Y249-p EAAEDIAyQLSRSRN
2 1 T258-p LSRSRNItyLPAGQs
1 0 T258-gl LSRSRNItyLPAGQs
3 0 Y259-p SRSRNItyLPAGQsV
0 1 S265-p tyLPAGQsVLLQLPQ
  mouse

 
K4 ____MAAKVFESIGK
K11 KVFESIGKFGLALAV
S82 NVPVITGSkDLQNVN
K83 VPVITGSKDLQNVNI
K83-sc VPVITGSkDLQNVNI
T91 DLQNVNITLRILFRP
S101-p ILFRPVAsQLPRIYT
Y107 AsQLPRIYTsIGEDy
T108 sQLPRIYTsIGEDyD
S109-p QLPRIYTsIGEDyDE
Y114-p YTsIGEDyDERVLPS
S121 yDERVLPSITTEILk
T123 ERVLPSITTEILkSV
K128-ub SITTEILkSVVARFD
K128-sc SITTEILkSVVARFD
K128-ac SITTEILkSVVARFD
S151-p ELVSRQVsDDLTERA
K177 LTHLTFGKEFTEAVE
K186-ub FTEAVEAkQVAQQEA
K186-sc FTEAVEAkQVAQQEA
K186-ac FTEAVEAkQVAQQEA
K202-ac RARFVVEkAEQQkkA
K202 RARFVVEKAEQQkkA
K207-ac VEkAEQQkkAAIISA
K208-ac EkAEQQkkAAIISAE
S213 QkkAAIISAEGDSkA
S218 IISAEGDSkAAELIA
K219-ac ISAEGDSkAAELIAN
K219 ISAEGDSKAAELIAN
K240 DGLIELRKLEAAEDI
Y249-p EAAEDIAyQLSRSRN
T258-p LSRSRNItyLPAGQs
T258 LSRSRNITyLPAGQs
Y259-p SRSRNItyLPAGQsV
S265-p tyLPAGQsVLLQLPQ
  rat

 
K4 ____MAAKVFESIGK
K11 KVFESIGKFGLALAV
S82 NVPVITGSKDLQNVN
K83 VPVITGSKDLQNVNI
K83 VPVITGSKDLQNVNI
T91 DLQNVNITLRILFRP
S101 ILFRPVASQLPRIyT
Y107-p ASQLPRIyTSIGEDY
T108 SQLPRIyTSIGEDYD
S109 QLPRIyTSIGEDYDE
Y114 yTSIGEDYDERVLPS
S121 YDERVLPSITTEILK
T123 ERVLPSITTEILKSV
K128 SITTEILKSVVARFD
K128 SITTEILKSVVARFD
K128 SITTEILKSVVARFD
S151 ELVSRQVSDDLTERA
K177 LTHLTFGKEFTEAVE
K186 FTEAVEAKQVAQQEA
K186 FTEAVEAKQVAQQEA
K186 FTEAVEAKQVAQQEA
K202 RARFVVEKAEQQKKA
K202 RARFVVEKAEQQKKA
K207 VEKAEQQKKAAIISA
K208 EKAEQQKKAAIISAE
S213 QKKAAIISAEGDSKA
S218 IISAEGDSKAAELIA
K219 ISAEGDSKAAELIAN
K219 ISAEGDSKAAELIAN
K240 DGLIELRKLEAAEDI
Y249-p EAAEDIAyQLSRSRN
T258 LSRSRNITYLPAGQS
T258 LSRSRNITYLPAGQS
Y259 SRSRNITYLPAGQSV
S265 TYLPAGQSVLLQLPQ
  pig

 
R4 ____MAARVFESIAS
S11 RVFESIASLAWPLAV
S82 NVPVITGSKDLQNVN
K83 VPVITGSKDLQNVNI
K83 VPVITGSKDLQNVNI
T91 DLQNVNITLRILFRP
S101 ILFRPVASQLPRIFT
F107 ASQLPRIFTSIGEDY
T108 SQLPRIFTSIGEDYD
S109 QLPRIFTSIGEDYDE
Y114 FTSIGEDYDERVLPS
S121 YDERVLPSITTEILK
T123 ERVLPSITTEILKSV
K128 SITTEILKSVVARFD
K128 SITTEILKSVVARFD
K128 SITTEILKSVVARFD
S151 ELVSRQVSDDLTERA
K177 LTHLTFGKEFTEAVE
K186 FTEAVEAKQVAQQEA
K186 FTEAVEAKQVAQQEA
K186 FTEAVEAKQVAQQEA
K202 RARFVVEKAEQQKKA
K202 RARFVVEKAEQQKKA
K207 VEKAEQQKKAAIISA
K208 EKAEQQKKAAIISAE
S213 QKKAAIISAEGDSKA
S218 IISAEGDSKAAELIA
K219 ISAEGDSKAAELIAN
K219 ISAEGDSKAAELIAN
K240 DGLIELRKLEAAEDI
Y249-p EAAEDIAyQLSRSRN
T258 LSRSRNITYLPAGQS
T258 LSRSRNITYLPAGQS
Y259 SRSRNITYLPAGQSV
S265 TYLPAGQSVLLQLPQ
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.