CPLM-006446

Genbank Nucleotide ID

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
4	****MAAKVFESIGK	ubiquitination	[1]
83	VPVITGSKDLQNVNI	ubiquitination	[1, 2, 3]
128	SITTEILKSVVARFD	ubiquitination	[1, 2, 3, 4]
177	LTHLTFGKEFTEAVE	ubiquitination	[3]
186	FTEAVEAKQVAQQEA	ubiquitination	[1, 2, 3]
202	RARFVVEKAEQQKKA	acetylation	[5]
202	RARFVVEKAEQQKKA	ubiquitination	[1, 2, 3]
208	EKAEQQKKAAIISAE	ubiquitination	[1, 3]
219	ISAEGDSKAAELIAN	ubiquitination	[2, 3]
240	DGLIELRKLEAAEDI	ubiquitination	[1, 2]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

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.

MOD_RES 202 202 N6-acetyllysine.
MOD_RES 249 249 Phosphotyrosine (By similarity).

3D-structure; Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; DNA synthesis; Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005887; C:integral to plasma membrane; IDA:HGNC.
GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB.
GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IEA:Compara.
GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO:0071354; P:cellular response to interleukin-6; IDA:BHF-UCL.
GO:0071897; P:DNA biosynthetic process; IEA:Compara.
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:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
GO:0050847; P:progesterone receptor signaling pathway; IDA:BHF-UCL.
GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.

IPR001107; Band_7.
IPR000163; Prohibitin.

PR00679; PROHIBITIN.