dbPTM

ATPB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATPB_HUMAN
UniProt AC	P06576
Protein Name	ATP synthase subunit beta, mitochondrial {ECO:0000305}
Gene Name	ATP5F1B {ECO:0000312\|HGNC:HGNC:830}
Organism	Homo sapiens (Human).
Sequence Length	529
Subcellular Localization	Mitochondrion inner membrane Peripheral membrane protein Matrix side .
Protein Description	Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits..
Protein Sequence	MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	SGALRRLTPSASLPP CCHHHHCCCCCCCCH	17.24	20068231
23	Phosphorylation	ALRRLTPSASLPPAQ HHHHCCCCCCCCHHH	25.84	20068231
25	Phosphorylation	RRLTPSASLPPAQLL HHCCCCCCCCHHHHH	45.83	20068231
46	Phosphorylation	AVHPVRDYAAQTSPS CCCCCHHHHCCCCCC	8.02	27642862
50	Phosphorylation	VRDYAAQTSPSPKAG CHHHHCCCCCCCCCC	37.57	26657352
51	Phosphorylation	RDYAAQTSPSPKAGA HHHHCCCCCCCCCCC	15.99	25262027
53	Phosphorylation	YAAQTSPSPKAGAAT HHCCCCCCCCCCCCC	38.51	29396449
55	Ubiquitination	AQTSPSPKAGAATGR CCCCCCCCCCCCCCC	64.88	21890473
60	Phosphorylation	SPKAGAATGRIVAVI CCCCCCCCCCEEEEE	26.85	24275569
106	O-linked_Glycosylation	VAQHLGESTVRTIAM HHHHHCCCCEEEEEE	30.33	UniProtKB CARBOHYD
106	Phosphorylation	VAQHLGESTVRTIAM HHHHHCCCCEEEEEE	30.33	28348404
107	Phosphorylation	AQHLGESTVRTIAMD HHHHCCCCEEEEEEC	15.09	28348404
109	Methylation	HLGESTVRTIAMDGT HHCCCCEEEEEECCC	22.09	-
113	Sulfoxidation	STVRTIAMDGTEGLV CCEEEEEECCCCCEE	4.28	21406390
124	Acetylation	EGLVRGQKVLDSGAP CCEECCEEEECCCCC	47.81	25825284
124	Succinylation	EGLVRGQKVLDSGAP CCEECCEEEECCCCC	47.81	-
124	Ubiquitination	EGLVRGQKVLDSGAP CCEECCEEEECCCCC	47.81	21890473
124	2-Hydroxyisobutyrylation	EGLVRGQKVLDSGAP CCEECCEEEECCCCC	47.81	-
124	Malonylation	EGLVRGQKVLDSGAP CCEECCEEEECCCCC	47.81	26320211
124	Succinylation	EGLVRGQKVLDSGAP CCEECCEEEECCCCC	47.81	-
128	Phosphorylation	RGQKVLDSGAPIKIP CCEEEECCCCCCEEC	32.47	20068231
133	Acetylation	LDSGAPIKIPVGPET ECCCCCCEECCCHHH	39.64	19608861
133	Succinylation	LDSGAPIKIPVGPET ECCCCCCEECCCHHH	39.64	-
133	Ubiquitination	LDSGAPIKIPVGPET ECCCCCCEECCCHHH	39.64	21890473
133	2-Hydroxyisobutyrylation	LDSGAPIKIPVGPET ECCCCCCEECCCHHH	39.64	-
133	Malonylation	LDSGAPIKIPVGPET ECCCCCCEECCCHHH	39.64	26320211
133	Succinylation	LDSGAPIKIPVGPET ECCCCCCEECCCHHH	39.64	-
140	Phosphorylation	KIPVGPETLGRIMNV EECCCHHHHHHHHHH	37.33	21406692
145	Sulfoxidation	PETLGRIMNVIGEPI HHHHHHHHHHHCCCC	2.93	21406390
155	Methylation	IGEPIDERGPIKTKQ HCCCCCCCCCCCCCC	53.06	-
159	Acetylation	IDERGPIKTKQFAPI CCCCCCCCCCCCCCC	53.45	25953088
159	Ubiquitination	IDERGPIKTKQFAPI CCCCCCCCCCCCCCC	53.45	-
161	Acetylation	ERGPIKTKQFAPIHA CCCCCCCCCCCCCCC	38.12	-
161	Succinylation	ERGPIKTKQFAPIHA CCCCCCCCCCCCCCC	38.12	-
161	Ubiquitination	ERGPIKTKQFAPIHA CCCCCCCCCCCCCCC	38.12	-
161	Succinylation	ERGPIKTKQFAPIHA CCCCCCCCCCCCCCC	38.12	-
185	Phosphorylation	VEQEILVTGIKVVDL CCCEEECCCCEEHHH	29.73	-
196	Phosphorylation	VVDLLAPYAKGGKIG EHHHHHCCCCCCEEE	18.48	28152594
198	Acetylation	DLLAPYAKGGKIGLF HHHHCCCCCCEEEEE	63.45	19608861
198	Ubiquitination	DLLAPYAKGGKIGLF HHHHCCCCCCEEEEE	63.45	19608861
198	2-Hydroxyisobutyrylation	DLLAPYAKGGKIGLF HHHHCCCCCCEEEEE	63.45	-
198	Succinylation	DLLAPYAKGGKIGLF HHHHCCCCCCEEEEE	63.45	27452117
201	Ubiquitination	APYAKGGKIGLFGGA HCCCCCCEEEEECCC	42.12	21890473
201	2-Hydroxyisobutyrylation	APYAKGGKIGLFGGA HCCCCCCEEEEECCC	42.12	-
201	Acetylation	APYAKGGKIGLFGGA HCCCCCCEEEEECCC	42.12	25953088
212	Acetylation	FGGAGVGKTVLIMEL ECCCCCCHHHHHHHH	32.81	21466224
213	Phosphorylation	GGAGVGKTVLIMELI CCCCCCHHHHHHHHH	18.02	28450419
217	Sulfoxidation	VGKTVLIMELINNVA CCHHHHHHHHHHHHH	2.76	28465586
230	Phosphorylation	VAKAHGGYSVFAGVG HHHHCCCEEEEECCC	13.27	28152594
230	Nitration	VAKAHGGYSVFAGVG HHHHCCCEEEEECCC	13.27	-
231	Phosphorylation	AKAHGGYSVFAGVGE HHHCCCEEEEECCCC	17.65	28152594
240	Phosphorylation	FAGVGERTREGNDLY EECCCCCCCCCCHHH	28.86	20068231
247	Phosphorylation	TREGNDLYHEMIESG CCCCCHHHHHHHHHC	9.90	-
259	Acetylation	ESGVINLKDATSKVA HHCCCCHHHCCCCEE	40.61	23954790
259	Succinylation	ESGVINLKDATSKVA HHCCCCHHHCCCCEE	40.61	-
259	Ubiquitination	ESGVINLKDATSKVA HHCCCCHHHCCCCEE	40.61	21906983
259	2-Hydroxyisobutyrylation	ESGVINLKDATSKVA HHCCCCHHHCCCCEE	40.61	-
259	Malonylation	ESGVINLKDATSKVA HHCCCCHHHCCCCEE	40.61	26320211
259	Succinylation	ESGVINLKDATSKVA HHCCCCHHHCCCCEE	40.61	-
264	Acetylation	NLKDATSKVALVYGQ CHHHCCCCEEEEEEE	27.46	25038526
264	Succinylation	NLKDATSKVALVYGQ CHHHCCCCEEEEEEE	27.46	-
264	Ubiquitination	NLKDATSKVALVYGQ CHHHCCCCEEEEEEE	27.46	21906983
264	2-Hydroxyisobutyrylation	NLKDATSKVALVYGQ CHHHCCCCEEEEEEE	27.46	-
264	Malonylation	NLKDATSKVALVYGQ CHHHCCCCEEEEEEE	27.46	26320211
264	Succinylation	NLKDATSKVALVYGQ CHHHCCCCEEEEEEE	27.46	-
269	Phosphorylation	TSKVALVYGQMNEPP CCCEEEEEEECCCCC	11.51	22817900
272	Sulfoxidation	VALVYGQMNEPPGAR EEEEEEECCCCCCHH	5.50	21406390
285	Phosphorylation	ARARVALTGLTVAEY HHHHHHHCCCCHHHH	22.02	20068231
288	Phosphorylation	RVALTGLTVAEYFRD HHHHCCCCHHHHHCC	21.00	-
292	Phosphorylation	TGLTVAEYFRDQEGQ CCCCHHHHHCCCCCC	8.32	28152594
312	Phosphorylation	IDNIFRFTQAGSEVS EECHHHHHCCCHHHH	17.16	28857561
316	Phosphorylation	FRFTQAGSEVSALLG HHHHCCCHHHHHHHC	37.53	21712546
319	Phosphorylation	TQAGSEVSALLGRIP HCCCHHHHHHHCCCC	14.78	21712546
327	Phosphorylation	ALLGRIPSAVGYQPT HHHCCCCCCCCCCCE	32.96	21406692
327	O-linked_Glycosylation	ALLGRIPSAVGYQPT HHHCCCCCCCCCCCE	32.96	26374642
331	Phosphorylation	RIPSAVGYQPTLATD CCCCCCCCCCEEECC	12.53	21406692
334	Phosphorylation	SAVGYQPTLATDMGT CCCCCCCEEECCCCC	17.31	21406692
337	Phosphorylation	GYQPTLATDMGTMQE CCCCEEECCCCCCHH	29.63	21406692
339	Sulfoxidation	QPTLATDMGTMQERI CCEEECCCCCCHHCE	4.12	28183972
341	Phosphorylation	TLATDMGTMQERITT EEECCCCCCHHCEEC	14.72	21406692
342	Sulfoxidation	LATDMGTMQERITTT EECCCCCCHHCEECC	3.01	28183972
350	Acetylation	QERITTTKKGSITSV HHCEECCCCCCEEEE	53.71	30584109
351	Ubiquitination	ERITTTKKGSITSVQ HCEECCCCCCEEEEE	56.66	-
353	Phosphorylation	ITTTKKGSITSVQAI EECCCCCCEEEEEEE	31.41	28348404
355	Phosphorylation	TTKKGSITSVQAIYV CCCCCCEEEEEEEEE	25.25	28348404
356	Phosphorylation	TKKGSITSVQAIYVP CCCCCEEEEEEEEEE	15.57	28348404
361	Phosphorylation	ITSVQAIYVPADDLT EEEEEEEEEEHHHCC	11.91	22817900
374	Phosphorylation	LTDPAPATTFAHLDA CCCCCCCCCCCCCCH	22.76	-
395	Phosphorylation	AIAELGIYPAVDPLD HHHHHCCCCCCCCCC	5.37	28152594
403	Phosphorylation	PAVDPLDSTSRIMDP CCCCCCCCCCCCCCC	35.65	24247654
404	Phosphorylation	AVDPLDSTSRIMDPN CCCCCCCCCCCCCCC	22.99	21712546
405	Phosphorylation	VDPLDSTSRIMDPNI CCCCCCCCCCCCCCC	24.62	21712546
408	Sulfoxidation	LDSTSRIMDPNIVGS CCCCCCCCCCCCCCC	7.33	28183972
415	Phosphorylation	MDPNIVGSEHYDVAR CCCCCCCCHHHHHHH	15.42	23911959
418	Phosphorylation	NIVGSEHYDVARGVQ CCCCCHHHHHHHHHH	14.20	28450419
418	Nitration	NIVGSEHYDVARGVQ CCCCCHHHHHHHHHH	14.20	-
426	Acetylation	DVARGVQKILQDYKS HHHHHHHHHHHHHHH	42.87	19608861
426	Ubiquitination	DVARGVQKILQDYKS HHHHHHHHHHHHHHH	42.87	21890473
426	2-Hydroxyisobutyrylation	DVARGVQKILQDYKS HHHHHHHHHHHHHHH	42.87	-
432	Methylation	QKILQDYKSLQDIIA HHHHHHHHHHHHHHH	53.64	-
432	Acetylation	QKILQDYKSLQDIIA HHHHHHHHHHHHHHH	53.64	25038526
433	Phosphorylation	KILQDYKSLQDIIAI HHHHHHHHHHHHHHH	25.65	27251275
443	Sulfoxidation	DIIAILGMDELSEED HHHHHHCCHHCCHHH	3.03	28183972
447	Phosphorylation	ILGMDELSEEDKLTV HHCCHHCCHHHCHHH	36.57	-
451	Acetylation	DELSEEDKLTVSRAR HHCCHHHCHHHHHHH	49.70	25038526
465	Phosphorylation	RKIQRFLSQPFQVAE HHHHHHHCCCCEEEH	32.85	28450419
475	Phosphorylation	FQVAEVFTGHMGKLV CEEEHHHHCCCCCEE	31.21	22817900
480	Acetylation	VFTGHMGKLVPLKET HHHCCCCCEEEHHHH	38.44	23954790
480	Ubiquitination	VFTGHMGKLVPLKET HHHCCCCCEEEHHHH	38.44	-
485	Acetylation	MGKLVPLKETIKGFQ CCCEEEHHHHHHHHH	46.90	23954790
485	Ubiquitination	MGKLVPLKETIKGFQ CCCEEEHHHHHHHHH	46.90	21890473
485	Malonylation	MGKLVPLKETIKGFQ CCCEEEHHHHHHHHH	46.90	26320211
489	Ubiquitination	VPLKETIKGFQQILA EEHHHHHHHHHHHHC	62.18	-
499	Phosphorylation	QQILAGEYDHLPEQA HHHHCCCCCCCCCCC	14.03	-
519	Ubiquitination	PIEEAVAKADKLAEE CHHHHHHHHHHHHHH	50.98	-
522	Acetylation	EAVAKADKLAEEHSS HHHHHHHHHHHHHCC	55.23	23954790
522	Succinylation	EAVAKADKLAEEHSS HHHHHHHHHHHHHCC	55.23	-
522	Ubiquitination	EAVAKADKLAEEHSS HHHHHHHHHHHHHCC	55.23	-
522	Succinylation	EAVAKADKLAEEHSS HHHHHHHHHHHHHCC	55.23	-
528	Phosphorylation	DKLAEEHSS------ HHHHHHHCC------	40.81	23401153
529	Phosphorylation	KLAEEHSS------- HHHHHHCC-------	46.26	28176443

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
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM63	Q969Q1	PMID:23695782

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATPG_HUMAN	ATP5C1	physical	22939629
ATPD_HUMAN	ATP5D	physical	22939629
ATPO_HUMAN	ATP5O	physical	22939629
NDUA2_HUMAN	NDUFA2	physical	22939629
NDUS1_HUMAN	NDUFS1	physical	22939629
NDUB9_HUMAN	NDUFB9	physical	22939629
QCR2_HUMAN	UQCRC2	physical	22939629
QCR1_HUMAN	UQCRC1	physical	22939629
NDUAC_HUMAN	NDUFA12	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
PDIA1_HUMAN	P4HB	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
MIA40_HUMAN	CHCHD4	physical	22939629
SDHB_HUMAN	SDHB	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
IF5A1_HUMAN	EIF5A	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
MDHM_HUMAN	MDH2	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
ROA3_HUMAN	HNRNPA3	physical	22939629
TOM22_HUMAN	TOMM22	physical	22939629
PA2G4_HUMAN	PA2G4	physical	22939629
OXA1L_HUMAN	OXA1L	physical	22939629
ODO2_HUMAN	DLST	physical	22939629
NNTM_HUMAN	NNT	physical	22939629
MYL6_HUMAN	MYL6	physical	22939629
ROA2_HUMAN	HNRNPA2B1	physical	22939629
TBA1A_HUMAN	TUBA1A	physical	22939629
ATPF2_HUMAN	ATPAF2	physical	25416956
ATPA_HUMAN	ATP5A1	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
ATPD_HUMAN	ATP5D	physical	26344197
AT5F1_HUMAN	ATP5F1	physical	26344197
ATP5H_HUMAN	ATP5H	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
ATPK_HUMAN	ATP5J2	physical	26344197
ATP5L_HUMAN	ATP5L	physical	26344197
ATPO_HUMAN	ATP5O	physical	26344197
VA0D1_HUMAN	ATP6V0D1	physical	26344197
VATB2_HUMAN	ATP6V1B2	physical	26344197
CALR_HUMAN	CALR	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
GFPT2_HUMAN	GFPT2	physical	26344197
HS90A_HUMAN	HSP90AA1	physical	26344197
HS90B_HUMAN	HSP90AB1	physical	26344197
MTCH2_HUMAN	MTCH2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
PHB_HUMAN	PHB	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
ATPF2_HUMAN	ATPAF2	physical	21516116
ATPF1_HUMAN	ATPAF1	physical	28514442
ATP5H_HUMAN	ATP5H	physical	28514442
ATPA_HUMAN	ATP5A1	physical	28514442
ATP8_HUMAN	ATP8	physical	28514442
T120A_HUMAN	TMEM120A	physical	28514442
CERS2_HUMAN	CERS2	physical	28514442
ATP5L_HUMAN	ATP5L	physical	28514442
ATPO_HUMAN	ATP5O	physical	28514442
ATP5J_HUMAN	ATP5J	physical	28514442
ATIF1_HUMAN	ATPIF1	physical	28514442

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 ATPB_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-133; LYS-198; LYS-426 ANDLYS-485, AND MASS SPECTROMETRY.	19608861 [Abstract]