Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00261
Entry Name
UniProt Accession
Theoretical PI
5.57
Molecular Weight
29804.1
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Prohibitin
Protein Synonyms/Alias
Gene Name
PHB
Gene Synonyms/Alias
Created Date
01-FEB-1994
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
69
Canonical
QKPIIFDCRSRPRNV
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Ande SR, Mishra S. Palmitoylation of prohibitin at cysteine 69 facilitates itsmembrane translocation and interaction with Eps 15 homology domain protein 2(EHD2). Biochem Cell Biol. 2010 Jun;88(3):553-8. doi: 10.1139/o09-177. PubMedPMID: 20555396.[PMID:20555396]
Functional Description
Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging.
Sequence Annotation
Modified residue: 128 128 N6-acetyllysine.
Modified residue: 186 186 N6-acetyllysine.
Modified residue: 202 202 N6-acetyllysine; alternate.
Modified residue: 202 202 N6-succinyllysine; alternate.
Modified residue: 249 249 Phosphotyrosine.
Protein Length
272 AA.
Protein Sequence
(Canonical)
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW  60
VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP  120
SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT  180
EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK  240
LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ                                272
FASTA
(Canonical)
>LipidDB-9606-00261|P35232
MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPW
VQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLP
SITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFT
EAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRK
LEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
Gene Ontology
GO:0005737; C:cytoplasm; IDA:BHF-UCL
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005887; C:integral component of plasma membrane; IDA:HGNC
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB
GO:0005739; C:mitochondrion; IDA:LIFEdb
GO:0005654; C:nucleoplasm; IDA:UniProtKB
GO:0005634; C:nucleus; TAS:UniProtKB
GO:0019899; F:enzyme binding; IPI:BHF-UCL
GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL
GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL
GO:0071354; P:cellular response to interleukin-6; IDA:BHF-UCL
GO:0006260; P:DNA replication; IEA:UniProtKB-KW
GO:0016575; P:histone deacetylation; IDA:UniProtKB
GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:BHF-UCL
GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL
GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL
GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; IDA:BHF-UCL
GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL
GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB
GO:0001649; P:osteoblast differentiation; IDA:UniProt
GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB
GO:0050847; P:progesterone receptor signaling pathway; IDA:BHF-UCL
GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB
GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB
GO:0007165; P:signal transduction; TAS:UniProtKB
Interpro
InterPro; IPR001107; Band_7
InterPro; IPR000163; Prohibitin
Pfam
Pfam; PF01145; Band_7;
SMART
SMART; SM00244; PHB;
PROSITE
PRINTS
PRINTS; PR00679; PROHIBITIN;