P06576

PTMD Annotation Information

※ Protein Information

Tag	Content
UniProt Accession	ATPB_HUMAN; P06576;
Entrez ID	506
GenBank Protein ID
GenBank Nucleotide ID
Protein Name	ATP synthase subunit beta, mitochondrial (EC 3.6.3.14)
Gene Name	ATP5B; ATPMB; ATPSB
Organism	Homo sapiens
NCBI Taxa ID	9606
Functional 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. Functional 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.
Sequence (Fasta)	MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT 60 GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV 120 RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ 180 EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT 240 REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 300 VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI 360 YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV 420 ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK 480 LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHSS Fasta Sequence >P06576\|ATP5B; ATPMB; ATPSB\|Homo sapiens (Human) MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS

※ PTM-Disease Association

Num	PTM	Disease	Cell Type	Type	PTM Site	PMID
1	Threonine Phosphorylation	Diabetes mellitus		U	T213	20012595
1	[Reference]: Obese individuals with and without type 2 diabetes were characterised by impaired insulin-stimulated glucose disposal rates, and showed a approximately 30% higher phosphorylation of ATPsyn-beta at Tyr361 and Thr213 (within the nucleotide-binding region of ATP synthase) as well as a coordinated downregulation of ATPsyn-beta protein and other OxPhos components.?
2	Tyrosine Phosphorylation	Diabetes mellitus		U	Y361	20012595
2	[Reference]: 32% increase in obese non-diabetic patients and patients with type II diabetes

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 4)	MESH:D058186 ; Acute Kidney Injury MESH:D000860 ; Hypoxia MESH:D011230 ; Precancerous Conditions MESH:C564616 ; Spinocerebellar Ataxia 17

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 29) (view all)	128 RGQKVLDSGAPIKIP dbPAF 140 KIPVGPETLGRIMNV dbPAF 196 VVDLLAPYAKGGKIG dbPAF 21 SGALRRLTPSASLPP dbPAF 213 GGAGVGKTVLIMELI dbPAF 23 ALRRLTPSASLPPAQ dbPAF 230 VAKAHGGYSVFAGVG dbPAF 231 AKAHGGYSVFAGVGE dbPAF 240 FAGVGERTREGNDLY dbPAF 25 RRLTPSASLPPAQLL dbPAF 269 TSKVALVYGQMNEPP dbPAF 285 ARARVALTGLTVAEY dbPAF 292 TGLTVAEYFRDQEGQ dbPAF 312 IDNIFRFTQAGSEVS dbPAF 316 FRFTQAGSEVSALLG dbPAF 319 TQAGSEVSALLGRIP dbPAF 361 ITSVQAIYVPADDLT dbPAF 395 AIAELGIYPAVDPLD dbPAF 415 MDPNIVGSEHYDVAR dbPAF 418 NIVGSEHYDVARGVQ dbPAF 433 KILQDYKSLQDIIAI dbPAF 447 ILGMDELSEEDKLTV dbPAF 465 RKIQRFLSQPFQVAE dbPAF 475 FQVAEVFTGHMGKLV dbPAF 499 QQILAGEYDHLPEQA dbPAF 50 VRDYAAQTSPSPKAG dbPAF 51 RDYAAQTSPSPKAGA dbPAF 528 DKLAEEHSS**** dbPAF 529 KLAEEHSS***** dbPAF
Acetylation (count: 14) (view all)	124 EGLVRGQKVLDSGAP PLMD 133 LDSGAPIKIPVGPET PLMD 159 IDERGPIKTKQFAPI PLMD 198 DLLAPYAKGGKIGLF PLMD 201 APYAKGGKIGLFGGA PLMD 212 FGGAGVGKTVLIMEL PLMD 259 ESGVINLKDATSKVA PLMD 264 NLKDATSKVALVYGQ PLMD 426 DVARGVQKILQDYKS PLMD 432 QKILQDYKSLQDIIA PLMD 451 DELSEEDKLTVSRAR PLMD 480 VFTGHMGKLVPLKET PLMD 485 MGKLVPLKETIKGFQ PLMD 522 EAVAKADKLAEEHSS PLMD
Ubiquitination (count: 13) (view all)	124 EGLVRGQKVLDSGAP PLMD 133 LDSGAPIKIPVGPET PLMD 159 IDERGPIKTKQFAPI PLMD 161 ERGPIKTKQFAPIHA PLMD 198 DLLAPYAKGGKIGLF PLMD 201 APYAKGGKIGLFGGA PLMD 259 ESGVINLKDATSKVA PLMD 264 NLKDATSKVALVYGQ PLMD 351 ERITTTKKGSITSVQ PLMD 426 DVARGVQKILQDYKS PLMD 480 VFTGHMGKLVPLKET PLMD 485 MGKLVPLKETIKGFQ PLMD 55 AQTSPSPKAGAATGR PLMD
Malonylation (count: 5)	124 EGLVRGQKVLDSGAP PLMD 133 LDSGAPIKIPVGPET PLMD 259 ESGVINLKDATSKVA PLMD 264 NLKDATSKVALVYGQ PLMD 485 MGKLVPLKETIKGFQ PLMD
Succinylation (count: 3)	124 EGLVRGQKVLDSGAP PLMD 198 DLLAPYAKGGKIGLF PLMD 426 DVARGVQKILQDYKS PLMD

※ Protein-Protein Interaction

Network

Interaction

A

B

Source

P00533	P06576	IntAct
P03372	P06576	IntAct
P05496	P06576	BioGRID
P06576	P38936	MINT
P06576	Q06187	IntAct
P06576	Q13526	MINT