dbPTM

PHB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PHB_MOUSE
UniProt AC	P67778
Protein Name	Prohibitin
Gene Name	Phb
Organism	Mus musculus (Mouse).
Sequence Length	272
Subcellular Localization	Mitochondrion inner membrane .
Protein 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 (By similarity)..
Protein Sequence	MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIYTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAKVFESI ------CCHHHHHHH	18.91	-
4	Acetylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	23576753
4	Succinylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	26388266
80	Phosphorylation	PRNVPVITGSKDLQN CCCCCEEECCCCHHC	35.32	28464351
83	Succinylation	VPVITGSKDLQNVNI CCEEECCCCHHCCCE	64.90	23954790
83	Malonylation	VPVITGSKDLQNVNI CCEEECCCCHHCCCE	64.90	26320211
83	Ubiquitination	VPVITGSKDLQNVNI CCEEECCCCHHCCCE	64.90	27667366
91	Phosphorylation	DLQNVNITLRILFRP CHHCCCEEEHHHHHH	12.55	-
101	Phosphorylation	ILFRPVASQLPRIYT HHHHHHHHCCCCEEH	32.27	22817900
107	Phosphorylation	ASQLPRIYTSIGEDY HHCCCCEEHHCCCCC	8.84	23023260
109	Phosphorylation	QLPRIYTSIGEDYDE CCCCEEHHCCCCCCC	16.18	-
114	Phosphorylation	YTSIGEDYDERVLPS EHHCCCCCCCCCCCH	18.53	-
121	Phosphorylation	YDERVLPSITTEILK CCCCCCCHHHHHHHH	28.53	28066266
123	Phosphorylation	ERVLPSITTEILKSV CCCCCHHHHHHHHHH	23.78	28066266
124	Phosphorylation	RVLPSITTEILKSVV CCCCHHHHHHHHHHH	21.25	29472430
128	Succinylation	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	24315375
128	Acetylation	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	23576753
128	Ubiquitination	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	-
141	Phosphorylation	FDAGELITQRELVSR CCCCHHCCHHHHHHH	33.91	-
151	Phosphorylation	ELVSRQVSDDLTERA HHHHHHCCCHHHHHH	19.64	26824392
155	Phosphorylation	RQVSDDLTERAATFG HHCCCHHHHHHHHHC	30.35	21743459
186	Acetylation	FTEAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	23576753
186	Ubiquitination	FTEAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	-
186	Malonylation	FTEAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	26320211
202	Succinylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	-
202	Acetylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	23576753
202	Malonylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	26320211
202	Succinylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	23806337
207	Acetylation	VEKAEQQKKAAIISA HHHHHHHHHEEEEEC	44.04	2388327
208	Malonylation	EKAEQQKKAAIISAE HHHHHHHHEEEEECC	38.42	25418362
208	Acetylation	EKAEQQKKAAIISAE HHHHHHHHEEEEECC	38.42	7622489
213	Phosphorylation	QKKAAIISAEGDSKA HHHEEEEECCCCHHH	17.72	23737553
218	Phosphorylation	IISAEGDSKAAELIA EEECCCCHHHHHHHH	34.74	28066266
219	Acetylation	ISAEGDSKAAELIAN EECCCCHHHHHHHHH	57.25	23954790
249	Nitration	EAAEDIAYQLSRSRN HHHHHHHHHHHCCCC	15.43	-
249	Phosphorylation	EAAEDIAYQLSRSRN HHHHHHHHHHHCCCC	15.43	27742792
252	Phosphorylation	EDIAYQLSRSRNITY HHHHHHHHCCCCCEE	16.82	27742792
258	Phosphorylation	LSRSRNITYLPAGQS HHCCCCCEEECCCCE	23.66	22388104
259	Phosphorylation	SRSRNITYLPAGQSV HCCCCCEEECCCCEE	13.59	-
265	Phosphorylation	TYLPAGQSVLLQLPQ EEECCCCEEEECCCC	17.51	23140645

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
114	Y	Phosphorylation	Kinase	LYN	P25911	PSP
258	T	Phosphorylation	Kinase	AKT1	P31749	PSP
259	Y	Phosphorylation	Kinase	LYN	P25911	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PHB_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PHB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PHB_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PHB_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND MASSSPECTROMETRY.	18034455 [Abstract]