dbPTM

PHB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PHB_HUMAN
UniProt AC	P35232
Protein Name	Prohibitin
Gene Name	PHB
Organism	Homo sapiens (Human).
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..
Protein Sequence	MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAKVFESI ------CCHHHHHHH	18.91	25944712
4	Methylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	23644510
4	Acetylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	25825284
4	Ubiquitination	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	-
4	Succinylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	23954790
4	Ubiquitination	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	-
4	Methylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	-
4	Acetylation	----MAAKVFESIGK ----CCHHHHHHHHH	37.61	-
11	Methylation	KVFESIGKFGLALAV HHHHHHHHHHHHHHH	34.29	23644510
11	Methylation	KVFESIGKFGLALAV HHHHHHHHHHHHHHH	34.29	-
41	Methylation	HRAVIFDRFRGVQDI CCEEEEECCCCCEEE	16.65	115487351
63	Acetylation	FLIPWVQKPIIFDCR CEECCCCCCEEEECC	28.68	26051181
80	Phosphorylation	PRNVPVITGSKDLQN CCCCCEEECCCCHHC	35.32	20068231
82	Phosphorylation	NVPVITGSKDLQNVN CCCEEECCCCHHCCC	17.85	20068231
83	Acetylation	VPVITGSKDLQNVNI CCEEECCCCHHCCCE	64.90	26051181
83	Ubiquitination	VPVITGSKDLQNVNI CCEEECCCCHHCCCE	64.90	21890473
83	Ubiquitination	VPVITGSKDLQNVNI CCEEECCCCHHCCCE	64.90	21890473
91	Phosphorylation	DLQNVNITLRILFRP CHHCCCEEEHHHHHH	12.55	30108239
93	Methylation	QNVNITLRILFRPVA HCCCEEEHHHHHHHH	18.21	115487361
101	Phosphorylation	ILFRPVASQLPRIFT HHHHHHHHCCCHHHH	32.27	30108239
108	Phosphorylation	SQLPRIFTSIGEDYD HCCCHHHHHCCCCCC	19.64	20833797
109	Phosphorylation	QLPRIFTSIGEDYDE CCCHHHHHCCCCCCC	20.18	28985074
114	Phosphorylation	FTSIGEDYDERVLPS HHHCCCCCCCCCCCH	18.53	28152594
121	O-linked_Glycosylation	YDERVLPSITTEILK CCCCCCCHHHHHHHH	28.53	19238206
121	Phosphorylation	YDERVLPSITTEILK CCCCCCCHHHHHHHH	28.53	27050516
123	Phosphorylation	ERVLPSITTEILKSV CCCCCHHHHHHHHHH	23.78	20833797
124	Phosphorylation	RVLPSITTEILKSVV CCCCHHHHHHHHHHH	21.25	24641631
128	Ubiquitination	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	21890473
128	Acetylation	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	-
128	Succinylation	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	27452117
128	Ubiquitination	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	21890473
128	Acetylation	SITTEILKSVVARFD HHHHHHHHHHHHHCC	47.03	23954790
141	O-linked_Glycosylation	FDAGELITQRELVSR CCCCHHCCHHHHHHH	33.91	29351928
151	Phosphorylation	ELVSRQVSDDLTERA HHHHHHCCCHHHHHH	19.64	30108239
155	Phosphorylation	RQVSDDLTERAATFG HHCCCHHHHHHHHHC	30.35	30108239
177	Ubiquitination	LTHLTFGKEFTEAVE CCEEECCHHHHHHHH	45.52	-
186	Ubiquitination	FTEAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	21890473
186	Acetylation	FTEAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	25953088
202	Ubiquitination	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	21906983
202	Succinylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	-
202	Malonylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	26320211
202	Succinylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	-
202	Acetylation	RARFVVEKAEQQKKA HHHHHHHHHHHHHHE	45.68	19608861
207	Acetylation	VEKAEQQKKAAIISA HHHHHHHHHEEEEEC	44.04	2402135
208	Succinylation	EKAEQQKKAAIISAE HHHHHHHHEEEEECC	38.42	27452117
208	Ubiquitination	EKAEQQKKAAIISAE HHHHHHHHEEEEECC	38.42	-
213	Phosphorylation	QKKAAIISAEGDSKA HHHEEEEECCCCHHH	17.72	29255136
218	Phosphorylation	IISAEGDSKAAELIA EEECCCCHHHHHHHH	34.74	21712546
219	Ubiquitination	ISAEGDSKAAELIAN EECCCCHHHHHHHHH	57.25	21890473
240	Ubiquitination	DGLIELRKLEAAEDI CCHHHHHHHHHHHHH	64.40	21890473
249	Phosphorylation	EAAEDIAYQLSRSRN HHHHHHHHHHHCCCC	15.43	27273156
252	Phosphorylation	EDIAYQLSRSRNITY HHHHHHHHCCCCCEE	16.82	21082442
254	Phosphorylation	IAYQLSRSRNITYLP HHHHHHCCCCCEEEC	26.71	22817900
258	Phosphorylation	LSRSRNITYLPAGQS HHCCCCCEEECCCCE	23.66	22410782
258	O-linked_Glycosylation	LSRSRNITYLPAGQS HHCCCCCEEECCCCE	23.66	19238206
259	Phosphorylation	SRSRNITYLPAGQSV HCCCCCEEECCCCEE	13.59	19238206
265	Phosphorylation	TYLPAGQSVLLQLPQ EEECCCCEEEECCCC	17.51	19060867

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	INSR	P06213	PSP
258	T	Phosphorylation	Kinase	AKT1	P31749	PSP
258	T	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
259	Y	Phosphorylation	Kinase	KIT	P10721	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:24658274

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E2F1_HUMAN	E2F1	physical	14637159
HDAC1_HUMAN	HDAC1	physical	14637159
E2F1_HUMAN	E2F1	physical	14500729
P53_HUMAN	TP53	physical	14500729
ANXA2_HUMAN	ANXA2	physical	12628297
ACTN1_HUMAN	ACTN1	physical	12628297
E2F1_HUMAN	E2F1	physical	12065415
SMCA4_HUMAN	SMARCA4	physical	12065415
SMCA2_HUMAN	SMARCA2	physical	12065415
E2F1_HUMAN	E2F1	physical	10523633
RAF1_HUMAN	RAF1	physical	10523633
RB_HUMAN	RB1	physical	10523633
RBL2_HUMAN	RBL2	physical	10376528
ANDR_HUMAN	AR	physical	16964284
E2F1_HUMAN	E2F1	physical	15141164
SMCA4_HUMAN	SMARCA4	physical	15141164
SMCA2_HUMAN	SMARCA2	physical	15141164
ESR1_HUMAN	ESR1	physical	17932104
PHB2_HUMAN	PHB2	physical	17932104
HDAC1_HUMAN	HDAC1	physical	17932104
RING2_HUMAN	RNF2	physical	17873902
QCR2_HUMAN	UQCRC2	physical	22939629
XPO1_HUMAN	XPO1	physical	16319068
ADT2_HUMAN	SLC25A5	physical	19725029
RL7_HUMAN	RPL7	physical	19725029
1433B_HUMAN	YWHAB	physical	19725029
IPO11_HUMAN	IPO11	physical	19725029
VDAC2_HUMAN	VDAC2	physical	19725029
RS4X_HUMAN	RPS4X	physical	19725029
CO9A2_HUMAN	COL9A2	physical	19725029
CAZA1_HUMAN	CAPZA1	physical	19725029
NPM_HUMAN	NPM1	physical	19725029
ACTB_HUMAN	ACTB	physical	19725029
LMNA_HUMAN	LMNA	physical	19725029
SMG5_HUMAN	SMG5	physical	19725029
PLEC_HUMAN	PLEC	physical	19725029
TF3C1_HUMAN	GTF3C1	physical	19725029
RAPH1_HUMAN	RAPH1	physical	19725029
HS90B_HUMAN	HSP90AB1	physical	19725029
DREB_HUMAN	DBN1	physical	19725029
KPCD_HUMAN	PRKCD	physical	19725029
1433Z_HUMAN	YWHAZ	physical	19725029
RAF1_HUMAN	RAF1	physical	16041367
LONF3_HUMAN	LONRF3	physical	20195357
COX6C_HUMAN	COX6C	physical	20195357
NP1L1_HUMAN	NAP1L1	physical	20195357
ATLA3_HUMAN	ATL3	physical	26344197
BAP29_HUMAN	BCAP29	physical	26344197
BAP31_HUMAN	BCAP31	physical	26344197
SSRG_HUMAN	SSR3	physical	26344197
BCAS3_HUMAN	BCAS3	physical	25640309
CASC3_HUMAN	CASC3	physical	25640309
CCL5_HUMAN	CCL5	physical	25640309
ST14_HUMAN	ST14	physical	25640309
HIKES_HUMAN	C11orf73	physical	28514442
STOM_HUMAN	STOM	physical	27173435

Drug and Disease Associations

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

Regulatory Network of PHB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-254, ANDMASS SPECTROMETRY.	17081983 [Abstract]