dbPTM

PHB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PHB2_HUMAN
UniProt AC	Q99623
Protein Name	Prohibitin-2
Gene Name	PHB2 {ECO:0000312\|EMBL:AAH14766.1, ECO:0000312\|HGNC:HGNC:30306}
Organism	Homo sapiens (Human).
Sequence Length	299
Subcellular Localization	Mitochondrion inner membrane . Cytoplasm . Nucleus .
Protein Description	Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases (By similarity). 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..
Protein Sequence	MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQNLKDLA ------CCCCHHHHC	13.63	22814378
6	Methylation	--MAQNLKDLAGRLP --CCCCHHHHCCCCC	59.24	-
6	Acetylation	--MAQNLKDLAGRLP --CCCCHHHHCCCCC	59.24	27452117
6	2-Hydroxyisobutyrylation	--MAQNLKDLAGRLP --CCCCHHHHCCCCC	59.24	-
6	Succinylation	--MAQNLKDLAGRLP --CCCCHHHHCCCCC	59.24	23954790
6	Ubiquitination	--MAQNLKDLAGRLP --CCCCHHHHCCCCC	59.24	21890473
6	Ubiquitination	--MAQNLKDLAGRLP --CCCCHHHHCCCCC	59.24	21890473
21	Phosphorylation	AGPRGMGTALKLLLG CCCCCHHHHHHHHHH	21.66	21406692
24	Acetylation	RGMGTALKLLLGAGA CCHHHHHHHHHHCCH	34.33	26051181
34	Phosphorylation	LGAGAVAYGVRESVF HHCCHHCCEEECCEE	15.00	28152594
77	Phosphorylation	FRIPWFQYPIIYDIR EECCCCCCCEEEEEC	6.21	17360941
81	Phosphorylation	WFQYPIIYDIRARPR CCCCCEEEEECCCCC	13.16	22817900
89	Succinylation	DIRARPRKISSPTGS EECCCCCCCCCCCCC	50.01	27452117
89	Ubiquitination	DIRARPRKISSPTGS EECCCCCCCCCCCCC	50.01	22817900
91	Phosphorylation	RARPRKISSPTGSKD CCCCCCCCCCCCCCC	33.04	30266825
92	Phosphorylation	ARPRKISSPTGSKDL CCCCCCCCCCCCCCC	29.92	25849741
94	Phosphorylation	PRKISSPTGSKDLQM CCCCCCCCCCCCCEE	56.91	30266825
96	O-linked_Glycosylation	KISSPTGSKDLQMVN CCCCCCCCCCCEEEE	26.02	30379171
96	Phosphorylation	KISSPTGSKDLQMVN CCCCCCCCCCCEEEE	26.02	23403867
97	Acetylation	ISSPTGSKDLQMVNI CCCCCCCCCCEEEEE	64.90	26051181
97	2-Hydroxyisobutyrylation	ISSPTGSKDLQMVNI CCCCCCCCCCEEEEE	64.90	-
97	Ubiquitination	ISSPTGSKDLQMVNI CCCCCCCCCCEEEEE	64.90	22817900
97	Ubiquitination	ISSPTGSKDLQMVNI CCCCCCCCCCEEEEE	64.90	21890473
101	Sulfoxidation	TGSKDLQMVNISLRV CCCCCCEEEEEEEEE	3.03	21406390
105	Phosphorylation	DLQMVNISLRVLSRP CCEEEEEEEEEHHCC	12.62	21712546
119	Phosphorylation	PNAQELPSMYQRLGL CCHHHCCHHHHHHCC	42.62	28152594
120	Sulfoxidation	NAQELPSMYQRLGLD CHHHCCHHHHHHCCC	2.89	28183972
121	Phosphorylation	AQELPSMYQRLGLDY HHHCCHHHHHHCCCH	8.53	28152594
123	Methylation	ELPSMYQRLGLDYEE HCCHHHHHHCCCHHH	17.15	-
128	Phosphorylation	YQRLGLDYEERVLPS HHHHCCCHHHCHHHH	25.40	22817900
135	Phosphorylation	YEERVLPSIVNEVLK HHHCHHHHHHHHHHH	34.70	20068231
142	Ubiquitination	SIVNEVLKSVVAKFN HHHHHHHHHHHHHCC	46.51	22817900
147	Ubiquitination	VLKSVVAKFNASQLI HHHHHHHHCCHHHHH	27.78	27667366
147	Ubiquitination	VLKSVVAKFNASQLI HHHHHHHHCCHHHHH	27.78	21890473
147	Acetylation	VLKSVVAKFNASQLI HHHHHHHHCCHHHHH	27.78	25825284
147	2-Hydroxyisobutyrylation	VLKSVVAKFNASQLI HHHHHHHHCCHHHHH	27.78	-
151	Phosphorylation	VVAKFNASQLITQRA HHHHCCHHHHHHHHH	26.99	21712546
155	Phosphorylation	FNASQLITQRAQVSL CCHHHHHHHHHHHHH	22.16	30108239
161	Phosphorylation	ITQRAQVSLLIRREL HHHHHHHHHHHHHHH	12.84	23312004
169	Phosphorylation	LLIRRELTERAKDFS HHHHHHHHHHHHHCE	20.76	26437602
176	Phosphorylation	TERAKDFSLILDDVA HHHHHHCEEEECCHH	25.32	-
193	Phosphorylation	ELSFSREYTAAVEAK EECCCHHHHHHHHHH	10.68	28152594
194	Phosphorylation	LSFSREYTAAVEAKQ ECCCHHHHHHHHHHH	11.91	28152594
200	Succinylation	YTAAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	27452117
200	2-Hydroxyisobutyrylation	YTAAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	-
200	Ubiquitination	YTAAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	27667366
200	Acetylation	YTAAVEAKQVAQQEA HHHHHHHHHHHHHHH	31.62	23236377
206	Ubiquitination	AKQVAQQEAQRAQFL HHHHHHHHHHHHHHH	34.39	23503661
212	Ubiquitination	QEAQRAQFLVEKAKQ HHHHHHHHHHHHHHH	8.89	22817900
215	Ubiquitination	QRAQFLVEKAKQEQR HHHHHHHHHHHHHHH	49.82	22817900
216	2-Hydroxyisobutyrylation	RAQFLVEKAKQEQRQ HHHHHHHHHHHHHHH	54.10	-
216	Acetylation	RAQFLVEKAKQEQRQ HHHHHHHHHHHHHHH	54.10	23749302
216	Malonylation	RAQFLVEKAKQEQRQ HHHHHHHHHHHHHHH	54.10	26320211
216	Ubiquitination	RAQFLVEKAKQEQRQ HHHHHHHHHHHHHHH	54.10	27667366
218	Ubiquitination	QFLVEKAKQEQRQKI HHHHHHHHHHHHHHH	66.49	22817900
224	Ubiquitination	AKQEQRQKIVQAEGE HHHHHHHHHHHHHHH	47.21	23000965
224	Acetylation	AKQEQRQKIVQAEGE HHHHHHHHHHHHHHH	47.21	26051181
224	2-Hydroxyisobutyrylation	AKQEQRQKIVQAEGE HHHHHHHHHHHHHHH	47.21	-
236	2-Hydroxyisobutyrylation	EGEAEAAKMLGEALS HHHHHHHHHHHHHHH	41.53	-
236	Acetylation	EGEAEAAKMLGEALS HHHHHHHHHHHHHHH	41.53	25953088
236	Ubiquitination	EGEAEAAKMLGEALS HHHHHHHHHHHHHHH	41.53	21906983
236	Neddylation	EGEAEAAKMLGEALS HHHHHHHHHHHHHHH	41.53	32015554
237	Sulfoxidation	GEAEAAKMLGEALSK HHHHHHHHHHHHHHH	5.08	21406390
243	Phosphorylation	KMLGEALSKNPGYIK HHHHHHHHHCCCCCH	37.12	22817900
244	Ubiquitination	MLGEALSKNPGYIKL HHHHHHHHCCCCCHH	68.93	23000965
244	Acetylation	MLGEALSKNPGYIKL HHHHHHHHCCCCCHH	68.93	25953088
244	Neddylation	MLGEALSKNPGYIKL HHHHHHHHCCCCCHH	68.93	32015554
248	Phosphorylation	ALSKNPGYIKLRKIR HHHHCCCCCHHHHHH	8.99	21082442
250	Ubiquitination	SKNPGYIKLRKIRAA HHCCCCCHHHHHHHH	33.48	23000965
250	Acetylation	SKNPGYIKLRKIRAA HHCCCCCHHHHHHHH	33.48	19608861
250	2-Hydroxyisobutyrylation	SKNPGYIKLRKIRAA HHCCCCCHHHHHHHH	33.48	-
253	Ubiquitination	PGYIKLRKIRAAQNI CCCCHHHHHHHHHHH	47.16	22817900
258	Ubiquitination	LRKIRAAQNISKTIA HHHHHHHHHHCHHHH	46.97	33845483
261	Ubiquitination	IRAAQNISKTIATSQ HHHHHHHCHHHHCCC	31.15	24816145
262	Ubiquitination	RAAQNISKTIATSQN HHHHHHCHHHHCCCC	39.90	23000965
262	Malonylation	RAAQNISKTIATSQN HHHHHHCHHHHCCCC	39.90	26320211
262	Acetylation	RAAQNISKTIATSQN HHHHHHCHHHHCCCC	39.90	25953088
262	2-Hydroxyisobutyrylation	RAAQNISKTIATSQN HHHHHHCHHHHCCCC	39.90	-
263	Phosphorylation	AAQNISKTIATSQNR HHHHHCHHHHCCCCE	14.73	26437602
266	Phosphorylation	NISKTIATSQNRIYL HHCHHHHCCCCEEEE	27.31	26437602
267	Phosphorylation	ISKTIATSQNRIYLT HCHHHHCCCCEEEEE	19.21	28985074
286	Phosphorylation	VLNLQDESFTRGSDS EEECCCCCCCCCCCC	39.96	25159151
288	Phosphorylation	NLQDESFTRGSDSLI ECCCCCCCCCCCCCC	43.32	29496963
289	Methylation	LQDESFTRGSDSLIK CCCCCCCCCCCCCCC	40.38	-
291	Phosphorylation	DESFTRGSDSLIKGK CCCCCCCCCCCCCCC	22.27	30266825
293	Phosphorylation	SFTRGSDSLIKGKK- CCCCCCCCCCCCCC-	33.42	30266825
296	Ubiquitination	RGSDSLIKGKK---- CCCCCCCCCCC----	70.71	21906983
296	Acetylation	RGSDSLIKGKK---- CCCCCCCCCCC----	70.71	25953088
299	Ubiquitination	DSLIKGKK------- CCCCCCCC-------	74.39	24816145

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
39	S	Phosphorylation	Kinase	PKCA	P17252	PSP
91	S	Phosphorylation	Kinase	AKT1	P31749	PSP
91	S	Phosphorylation	Kinase	AKT2	P31751	PSP
91	S	Phosphorylation	Kinase	CAMK4	Q16566	PSP
176	S	Phosphorylation	Kinase	AKT1	P31749	PSP
176	S	Phosphorylation	Kinase	AKT2	P31751	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PHB2_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 PHB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTNB1_HUMAN	CTNNB1	physical	17353931
PLAK_HUMAN	JUP	physical	17353931
NU205_HUMAN	NUP205	physical	17353931
UBP15_HUMAN	USP15	physical	17353931
MMS19_HUMAN	MMS19	physical	17353931
PDXD1_HUMAN	PDXDC1	physical	17353931
DDX20_HUMAN	DDX20	physical	17353931
NUP93_HUMAN	NUP93	physical	17353931
RUNX3_HUMAN	RUNX3	physical	17353931
TIM50_HUMAN	TIMM50	physical	17353931
EPIPL_HUMAN	EPPK1	physical	17353931
COPG1_HUMAN	COPG1	physical	17353931
LG3BP_HUMAN	LGALS3BP	physical	17353931
PTMA_HUMAN	PTMA	physical	12943695
HDAC1_HUMAN	HDAC1	physical	15140878
HDAC5_HUMAN	HDAC5	physical	15140878
ESR1_HUMAN	ESR1	physical	15140878
COT1_HUMAN	NR2F1	physical	15140878
COT2_HUMAN	NR2F2	physical	15140878
ESR1_HUMAN	ESR1	physical	17932104
PHB_HUMAN	PHB	physical	17932104
ESR1_HUMAN	ESR1	physical	10938099
BIG3_HUMAN	KIAA1244	physical	19496786
QCR1_HUMAN	UQCRC1	physical	22939629
MYOD1_HUMAN	MYOD1	physical	15173318
MEF2A_HUMAN	MEF2A	physical	15173318
HDAC1_HUMAN	HDAC1	physical	15173318
FHL2_HUMAN	FHL2	physical	18255255
TEAD3_HUMAN	TEAD3	physical	21988832
BIG3_HUMAN	KIAA1244	physical	24051437
ESR1_HUMAN	ESR1	physical	24051437
HDAC1_HUMAN	HDAC1	physical	24051437
NCOR1_HUMAN	NCOR1	physical	24051437
XIAP_HUMAN	XIAP	physical	26186194
NMRL1_HUMAN	NMRAL1	physical	26186194
VATC1_HUMAN	ATP6V1C1	physical	26344197
CCD47_HUMAN	CCDC47	physical	26344197
COX41_HUMAN	COX4I1	physical	26344197
GOSR1_HUMAN	GOSR1	physical	26344197
LEG1_HUMAN	LGALS1	physical	26344197
RM17_HUMAN	MRPL17	physical	26344197
NDUB8_HUMAN	NDUFB8	physical	26344197
PHB_HUMAN	PHB	physical	26344197
PTBP1_HUMAN	PTBP1	physical	26344197
SSRA_HUMAN	SSR1	physical	26344197
NMRL1_HUMAN	NMRAL1	physical	28514442
XIAP_HUMAN	XIAP	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 PHB2_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-250, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128, AND MASSSPECTROMETRY.	15592455 [Abstract]