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P67778 (PHB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prohibitin
Alternative name(s):
B-cell receptor-associated protein 32
Short name=BAP 32
Gene names
Name:Phb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Subunit structure

Interacts with PHB2. Interacts with STOML2 By similarity. Ref.6

Subcellular location

Mitochondrion inner membrane Ref.6.

Tissue specificity

Widely expressed in different tissues. Ref.1

Developmental stage

Throughout gestation, highly expressed in brown fat, heart, liver, developing renal tubules and neurons, and detected at lower levels in tissues such as lung and exocrine pancreas. Ref.6

Sequence similarities

Belongs to the prohibitin family.

Ontologies

Keywords
   Biological processDNA synthesis
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA biosynthetic process

Inferred from mutant phenotype PubMed 18480465. Source: MGI

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to interleukin-6

Inferred from electronic annotation. Source: Ensembl

histone deacetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of glucocorticoid receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription by competitive promoter binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18480465. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

progesterone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18480465. Source: GOC

   Cellular_componentintegral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrion

Inferred from direct assay PubMed 11884367PubMed 14651853PubMed 17597094PubMed 18614015. Source: MGI

nucleoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 18480465. Source: MGI

   Molecular_functionsequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 18480465. Source: MGI

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Prohibitin
PRO_0000213879

Regions

Coiled coil177 – 21135 Potential

Amino acid modifications

Modified residue1281N6-acetyllysine Ref.9
Modified residue1861N6-acetyllysine Ref.9
Modified residue2021N6-acetyllysine; alternate Ref.9
Modified residue2021N6-succinyllysine; alternate Ref.8
Modified residue2491Phosphotyrosine Ref.7

Experimental info

Sequence conflict2551R → W in BAE29988. Ref.2
Sequence conflict2551R → W in BAE30089. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P67778 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 6B26073E169C2FFC

FASTA27229,820
        10         20         30         40         50         60 
MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW 

        70         80         90        100        110        120 
VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIYTSI 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 IgM antigen receptor of B lymphocytes is associated with prohibitin and a prohibitin-related protein."
Terashima M., Kim K.-M., Adachi T., Nielsen P.J., Reth M., Koehler G., Lamers M.C.
EMBO J. 13:3782-3792(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Lymphoid tissue.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Bone marrow, Heart and Kidney.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Strain: C57BL/6.
Tissue: Eye.
[5]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-34; 94-105; 158-177; 220-239 AND 241-253, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[6]"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: INTERACTION WITH PHB2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[9]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128; LYS-186 AND LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78682 mRNA. Translation: CAA55349.1.
AK002714 mRNA. Translation: BAB22305.1.
AK010619 mRNA. Translation: BAB27067.1.
AK150956 mRNA. Translation: BAE29988.1.
AK151073 mRNA. Translation: BAE30089.1.
AK168248 mRNA. Translation: BAE40198.1.
AK168656 mRNA. Translation: BAE40512.1.
AL732490 Genomic DNA. Translation: CAI24279.1.
BC083354 mRNA. Translation: AAH83354.1.
BC089034 mRNA. Translation: AAH89034.1.
RefSeqNP_032857.1. NM_008831.4.
UniGeneMm.263862.

3D structure databases

ProteinModelPortalP67778.
SMRP67778. Positions 60-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202141. 1 interaction.
IntActP67778. 9 interactions.
MINTMINT-1841697.

PTM databases

PhosphoSiteP67778.

2D gel databases

REPRODUCTION-2DPAGEIPI00133440.
P67778.
SWISS-2DPAGEP67778.

Proteomic databases

PaxDbP67778.
PRIDEP67778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000125172; ENSMUSP00000119603; ENSMUSG00000038845.
GeneID18673.
KEGGmmu:18673.
UCSCuc007lan.2. mouse.

Organism-specific databases

CTD5245.
MGIMGI:97572. Phb.

Phylogenomic databases

eggNOGCOG0330.
GeneTreeENSGT00550000074770.
HOGENOMHOG000205692.
HOVERGENHBG004457.
InParanoidP67778.
KOK17080.
OMAIIFDVRS.
OrthoDBEOG7V4B04.
TreeFamTF300095.

Gene expression databases

BgeeP67778.
CleanExMM_PHB.
GenevestigatorP67778.

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

NextBio294690.
PROP67778.
SOURCESearch...

Entry information

Entry namePHB_MOUSE
AccessionPrimary (citable) accession number: P67778
Secondary accession number(s): P24142, Q3UB75, Q5SQG4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot