PHB2
entrez
11331
canonical
uniprot
Q99623
canonical
ensembl
ENSG00000215021
resolver
ensp
ENSP00000412856
resolver
ensp
ENSP00000441875
resolver
ensp
ENSP00000504481
resolver
enst
ENST00000676496
resolver
genesymbol
PHB2
resolver
genesymbol_syn
BAP
resolver
genesymbol_syn
REA
resolver
hgnc
HGNC:30306
resolver
uniprot
A0A7I2V5F0
resolver
uniprot
B4DP75
resolver
uniprot
Q2YDA4
resolver
uniprot
Q7KYU3
resolver
uniprot
Q92978
resolver
uniprot_entry
A0A7I2V5F0_HUMAN
resolver
uniprot_entry
PHB2_HUMAN
resolver
uniprot_sec
B4DP75
resolver
uniprot_sec
Q2YDA4
resolver
uniprot_sec
Q7KYU3
resolver
uniprot_sec
Q92978
resolver
amino_acid_sequence
MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK
uniprot
proteins
function
FUNCTION: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus. {ECO:0000269|PubMed:10359819, ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:24003225, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117}.; FUNCTION: In the mitochondria, together with PHB1, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as a chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner (By similarity). Also regulates cytochrome-c oxidase assembly (COX) and mitochondrial respiration (PubMed:11302691, PubMed:20959514). Binding to sphingoid 1-phosphate (SPP) modulates its regulator activity (PubMed:11302691, PubMed:20959514). Has a key role of mitophagy receptor involved in targeting mitochondria for autophagic degradation (PubMed:28017329). Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6 (PubMed:31522117). {ECO:0000250|UniProtKB:O35129, ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117, ECO:0000305|PubMed:25904163}.; FUNCTION: In the nucleus, serves as transcriptional co-regulator (Probable). Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases. Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity (By similarity). {ECO:0000250|UniProtKB:O35129, ECO:0000305|PubMed:25904163}.; FUNCTION: In the plasma membrane, is involved in IGFBP6-induced cell migration (PubMed:24003225). Cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation (By similarity). {ECO:0000250|UniProtKB:O35129, ECO:0000269|PubMed:24003225}.; FUNCTION: (Microbial infection) Involved in human enterovirus 71/EV-71 infection by enhancing the autophagy mechanism during the infection. {ECO:0000269|PubMed:32276428}.
uniprot
proteins
mass_dalton
33296
uniprot
proteins
mutagenesis
MUTAGEN 77; /note="Y->K: No effect on interaction with MAP1LC3B."; /evidence="ECO:0000269|PubMed:28017329"; MUTAGEN 121..124; /note="YQRL->AQRA: Abolishes interaction with MAP1LC3B. No effect on interaction with PHB. No effect on mitochondrial location. Abolishes rescue of Parkin-mediated mitophagy."; /evidence="ECO:0000269|PubMed:28017329"; MUTAGEN 175..178; /note="FSLI->ASLA: Decreases interaction with MAP1LC3B."; /evidence="ECO:0000269|PubMed:28017329"; MUTAGEN 225; /note="I->P: Reduces helicity. Decreases homodimerization and interaction with PHB. Disrupts mitochondrial dynamics. Disrupts mitochondrial-mediated antiviral innate immune response."; /evidence="ECO:0000269|PubMed:31522117"; MUTAGEN 229..233; /note="EGEAE->KGKAK: No effect on homodimerization or interaction with PHB. Decreases mitochondrial dynamics. Disrupts mitochondrial-mediated antiviral innate immune response."; /evidence="ECO:0000269|PubMed:31522117
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Tyrosine phosphorylation is indirectly stimulated by IGFBP6. {ECO:0000269|PubMed:24003225}.
uniprot
proteins
protein_family
Prohibitin family
uniprot
proteins
pubmed
10359819
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
11302691
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17565718
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19496786
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19640993
uniprot
proteins
pubmed
19906925
uniprot
proteins
pubmed
20959514
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21328542
uniprot
proteins
pubmed
21746876
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22997079
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24003225
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25904163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28017329
uniprot
proteins
pubmed
31522117
uniprot
proteins
pubmed
32276428
uniprot
proteins
pubmed
41398051
uniprot
proteins
pubmed
9074930
uniprot
proteins
sequence_length
299
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:28017329}. Cytoplasm {ECO:0000269|PubMed:17565718, ECO:0000269|PubMed:19496786, ECO:0000269|PubMed:32276428}. Nucleus {ECO:0000269|PubMed:17565718, ECO:0000269|PubMed:19496786, ECO:0000269|PubMed:20959514}. Cell membrane {ECO:0000269|PubMed:22997079, ECO:0000269|PubMed:24003225}. Note=Localizes within both nucleus and cytoplasm in proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. {ECO:0000269|PubMed:17565718}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane {ECO:0000305|PubMed:31522117}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane {ECO:0000305|PubMed:31522117}.
uniprot
proteins