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Protein

Prohibitin-2

Gene

Phb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Probably involved in regulating mitochondrial respiration activity and in aging (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Prohibitin-2
Alternative name(s):
B-cell receptor-associated protein BAP37
Short name:
BAP-37
Gene namesi
Name:Phb2By similarity
Synonyms:Bcap37Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi620203. Phb2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 299298Prohibitin-2PRO_0000213886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei128 – 1281PhosphotyrosineBy similarity
Modified residuei147 – 1471N6-acetyllysineBy similarity
Modified residuei151 – 1511PhosphoserineCombined sources
Modified residuei200 – 2001N6-acetyllysineBy similarity
Modified residuei236 – 2361N6-acetyllysineBy similarity
Modified residuei250 – 2501N6-acetyllysineBy similarity
Modified residuei262 – 2621N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5XIH7.
PRIDEiQ5XIH7.

PTM databases

iPTMnetiQ5XIH7.
PhosphoSiteiQ5XIH7.

Expressioni

Gene expression databases

ExpressionAtlasiQ5XIH7. baseline.
GenevisibleiQ5XIH7. RN.

Interactioni

Subunit structurei

Interacts with PHB (PubMed:11302691). Interacts with ESR1, HDAC1 and HDAC5. Interacts with ZNF703. Interacts with STOML2. Interacts with ARFGEF3.By similarity1 Publication

Protein-protein interaction databases

BioGridi250411. 2 interactions.
IntActiQ5XIH7. 3 interactions.
MINTiMINT-4594704.
STRINGi10116.ENSRNOP00000017472.

Structurei

3D structure databases

ProteinModelPortaliQ5XIH7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 4931Necessary for transcriptional repressionBy similarityAdd
BLAST
Regioni150 – 17425Necessary for transcriptional repressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili190 – 23849Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the prohibitin family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3090. Eukaryota.
COG0330. LUCA.
GeneTreeiENSGT00550000075076.
HOGENOMiHOG000205692.
HOVERGENiHBG004457.
InParanoidiQ5XIH7.
KOiK17081.
OMAiGIQSDIY.
OrthoDBiEOG7V4B04.
PhylomeDBiQ5XIH7.
TreeFamiTF354230.

Family and domain databases

InterProiIPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view]
PANTHERiPTHR23222. PTHR23222. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00679. PROHIBITIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5XIH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQNLKDLAG RLPSGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI
60 70 80 90 100
FFNRIGGVQQ DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ
110 120 130 140 150
MVNISLRVLS RPNAQELPSM YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA
160 170 180 190 200
SQLITQRAQV SLLIRRELTE RAKDFSLILD DVAITELSFS REYTAAVEAK
210 220 230 240 250
QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE ALSKNPGYIK
260 270 280 290
LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK
Length:299
Mass (Da):33,312
Last modified:November 23, 2004 - v1
Checksum:iE7699DDD31FCCB69
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871P → T in AAB18746 (PubMed:10559001).Curated
Sequence conflicti108 – 1081V → F (PubMed:10559001).Curated
Sequence conflicti287 – 2882FT → LI in AAB18747 (PubMed:10559001).Curated
Sequence conflicti294 – 2941L → F in AAB18747 (PubMed:10559001).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083705 mRNA. Translation: AAH83705.1.
U75391 mRNA. Translation: AAB18746.1.
U75392 mRNA. Translation: AAB18747.1.
RefSeqiNP_001013053.1. NM_001013035.1.
UniGeneiRn.64535.

Genome annotation databases

EnsembliENSRNOT00000017472; ENSRNOP00000017472; ENSRNOG00000012999.
GeneIDi114766.
KEGGirno:114766.
UCSCiRGD:620203. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083705 mRNA. Translation: AAH83705.1.
U75391 mRNA. Translation: AAB18746.1.
U75392 mRNA. Translation: AAB18747.1.
RefSeqiNP_001013053.1. NM_001013035.1.
UniGeneiRn.64535.

3D structure databases

ProteinModelPortaliQ5XIH7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250411. 2 interactions.
IntActiQ5XIH7. 3 interactions.
MINTiMINT-4594704.
STRINGi10116.ENSRNOP00000017472.

PTM databases

iPTMnetiQ5XIH7.
PhosphoSiteiQ5XIH7.

Proteomic databases

PaxDbiQ5XIH7.
PRIDEiQ5XIH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017472; ENSRNOP00000017472; ENSRNOG00000012999.
GeneIDi114766.
KEGGirno:114766.
UCSCiRGD:620203. rat.

Organism-specific databases

CTDi11331.
RGDi620203. Phb2.

Phylogenomic databases

eggNOGiKOG3090. Eukaryota.
COG0330. LUCA.
GeneTreeiENSGT00550000075076.
HOGENOMiHOG000205692.
HOVERGENiHBG004457.
InParanoidiQ5XIH7.
KOiK17081.
OMAiGIQSDIY.
OrthoDBiEOG7V4B04.
PhylomeDBiQ5XIH7.
TreeFamiTF354230.

Miscellaneous databases

PROiQ5XIH7.

Gene expression databases

ExpressionAtlasiQ5XIH7. baseline.
GenevisibleiQ5XIH7. RN.

Family and domain databases

InterProiIPR001107. Band_7.
IPR000163. Prohibitin.
[Graphical view]
PANTHERiPTHR23222. PTHR23222. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00679. PROHIBITIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Heart.
  2. "A systematic analysis of 40 random genes in cultured vascular smooth muscle subtypes reveals a heterogeneity of gene expression and identifies the tight junction gene zonula occludens 2 as a marker of epithelioid 'pup' smooth muscle cells and a participant in carotid neointimal formation."
    Adams L.D., Lemire J.M., Schwartz S.M.
    Arterioscler. Thromb. Vasc. Biol. 19:2600-2608(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-110 AND 274-299.
    Strain: Wistar KyotoImported.
    Tissue: Aortic smooth muscleImported.
  3. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 148-157, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "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 PHB, SUBCELLULAR LOCATION.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPHB2_RAT
AccessioniPrimary (citable) accession number: Q5XIH7
Secondary accession number(s): P70629, P70630
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: November 23, 2004
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.