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P35232 (PHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prohibitin
Gene names
Name:PHB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

Interacts with PHB2. Interacts with STOML2. Ref.7 Ref.10

Subcellular location

Mitochondrion inner membrane By similarity.

Tissue specificity

Widely expressed in different tissues.

Developmental stage

Levels of expression in fibroblasts decrease heterogeneously during cellular aging. Ref.7

Induction

Expression increases approximately 3-fold upon entry into G1 phase compared with other phases of the cell cycle. Also induced following inhibition of mitochondrial protein synthesis by thiamphenicol. Ref.7

Sequence similarities

Belongs to the prohibitin family.

Ontologies

Keywords
   Biological processDNA synthesis
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to interleukin-6

Inferred from direct assay PubMed 17324931. Source: BHF-UCL

histone deacetylation

Inferred from direct assay PubMed 12466959. Source: UniProtKB

negative regulation of androgen receptor signaling pathway

Inferred from direct assay PubMed 16964284. Source: BHF-UCL

negative regulation of cell growth

Inferred from mutant phenotype PubMed 12065415. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 18487222. Source: BHF-UCL

negative regulation of glucocorticoid receptor signaling pathway

Inferred from direct assay PubMed 16964284. Source: BHF-UCL

negative regulation of transcription by competitive promoter binding

Inferred from direct assay PubMed 18487222. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16964284. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12566959. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14500729. Source: UniProtKB

progesterone receptor signaling pathway

Inferred from direct assay PubMed 16964284. Source: BHF-UCL

regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14500729. Source: UniProtKB

signal transduction

Traceable author statement PubMed 16130169. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16964284. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Inferred from direct assay PubMed 15274632. Source: HGNC

mitochondrial inner membrane

Traceable author statement PubMed 14500729. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: LIFEdb

nucleoplasm

Inferred from direct assay PubMed 12466959. Source: UniProtKB

nucleus

Traceable author statement PubMed 16130169. Source: UniProtKB

   Molecular_functionhistone deacetylase binding

Inferred from physical interaction PubMed 16964284. Source: BHF-UCL

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18487222. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Prohibitin
PRO_0000213878

Regions

Coiled coil177 – 21135 Potential

Amino acid modifications

Modified residue1281N6-acetyllysine By similarity
Modified residue1861N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine; alternate Ref.8
Modified residue2021N6-succinyllysine; alternate By similarity
Modified residue2491Phosphotyrosine By similarity

Natural variations

Natural variant881V → A in a breast cancer sample; somatic mutation. Ref.1
VAR_006479
Natural variant1051R → H in a breast cancer sample; somatic mutation. Ref.1
VAR_006480

Secondary structure

....................................... 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35232 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 915494273E342C76

FASTA27229,804
        10         20         30         40         50         60 
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW 

        70         80         90        100        110        120 
VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP 

       130        140        150        160        170        180 
SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT 

       190        200        210        220        230        240 
EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK 

       250        260        270 
LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ 

« Hide

References

« Hide 'large scale' references
[1]"The human prohibitin gene located on chromosome 17q21 is mutated in sporadic breast cancer."
Sato T., Saito H., Swensen J., Olifant A., Wood C., Danner D., Sakamoto T., Takita K., Kasumi F., Miki Y., Skolnick M., Nakamura Y.
Cancer Res. 52:1643-1646(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-88 AND HIS-105.
Tissue: Mammary gland.
[2]"The human prohibitin (PHB) gene family and its somatic mutations in human tumors."
Sato T., Sakamoto T., Takita K., Saito H., Okui K., Nakamura Y.
Genomics 17:762-764(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Muscle.
[5]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-11; 84-93; 106-128; 134-143; 178-186 AND 209-219, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 75-83; 94-117; 134-143; 158-177; 220-253 AND 256-272, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence."
Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H., Hall P.A., Wright E.G.
Exp. Cell Res. 265:262-273(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PHB2, DEVELOPMENTAL STAGE, INDUCTION.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.
Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STOML2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S85655 mRNA. Translation: AAB21614.1.
L14272 Genomic DNA. Translation: AAO18340.1.
BT007411 mRNA. Translation: AAP36079.1.
BC013401 mRNA. Translation: AAH13401.1.
BC095460 mRNA. Translation: AAH95460.1.
PIRI52690.
RefSeqNP_001268425.1. NM_001281496.1.
NP_001268644.1. NM_001281715.1.
NP_002625.1. NM_002634.3.
UniGeneHs.514303.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LU7model-A1-272[»]
ProteinModelPortalP35232.
SMRP35232. Positions 61-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111264. 72 interactions.
DIPDIP-24248N.
IntActP35232. 56 interactions.
MINTMINT-1158239.
STRING9606.ENSP00000300408.

PTM databases

PhosphoSiteP35232.

Polymorphism databases

DMDM464371.

2D gel databases

DOSAC-COBS-2DPAGEP35232.
OGPP35232.
REPRODUCTION-2DPAGEIPI00017334.
P35232.
SWISS-2DPAGEP35232.
UCD-2DPAGEP35232.

Proteomic databases

PaxDbP35232.
PeptideAtlasP35232.
PRIDEP35232.

Protocols and materials databases

DNASU5245.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300408; ENSP00000300408; ENSG00000167085.
GeneID5245.
KEGGhsa:5245.
UCSCuc002iox.1. human.

Organism-specific databases

CTD5245.
GeneCardsGC17M047481.
HGNCHGNC:8912. PHB.
HPAHPA003280.
MIM176705. gene.
neXtProtNX_P35232.
PharmGKBPA33251.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0330.
HOGENOMHOG000205692.
HOVERGENHBG004457.
InParanoidP35232.
KOK17080.
OMAIIFDVRS.
OrthoDBEOG7V4B04.
PhylomeDBP35232.
TreeFamTF300095.

Gene expression databases

ArrayExpressP35232.
BgeeP35232.
CleanExHS_PHB.
GenevestigatorP35232.

Family and domain databases

InterProIPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view]
PANTHERPTHR23222. PTHR23222. 1 hit.
PfamPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSPR00679. PROHIBITIN.
SMARTSM00244. PHB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiProhibitin.
GenomeRNAi5245.
NextBio20266.
PROP35232.
SOURCESearch...

Entry information

Entry namePHB_HUMAN
AccessionPrimary (citable) accession number: P35232
Secondary accession number(s): Q4VBQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM