AT5F1_HUMAN - dbPTM
AT5F1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT5F1_HUMAN
UniProt AC P24539
Protein Name ATP synthase F(0) complex subunit B1, mitochondrial
Gene Name ATP5F1
Organism Homo sapiens (Human).
Sequence Length 256
Subcellular Localization Mitochondrion. Mitochondrion inner membrane.
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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements..
Protein Sequence MLSRVVLSAAATAAPSLKNAAFLGPGVLQATRTFHTGQPHLVPVPPLPEYGGKVRYGLIPEEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETFTALSVLGVMVYGIKKYGPFVADFADKLNEQKLAQLEEAKQASIQHIQNAIDTEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYHISVQNMMRRKEQEHMINWVEKHVVQSISTQQEKETIAKCIADLKLLAKKAQAQPVM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
18UbiquitinationATAAPSLKNAAFLGP
HHHCHHCCCHHHCCC
49.21-
31PhosphorylationGPGVLQATRTFHTGQ
CCCCHHHHEEEECCC
19.79-
53AcetylationPLPEYGGKVRYGLIP
CCCCCCCEEECEECC
21.1230584097
53UbiquitinationPLPEYGGKVRYGLIP
CCCCCCCEEECEECC
21.12-
71PhosphorylationFQFLYPKTGVTGPYV
HHHHCCCCCCCCCCH
32.1725219547
74PhosphorylationLYPKTGVTGPYVLGT
HCCCCCCCCCCHHHH
33.5125219547
77PhosphorylationKTGVTGPYVLGTGLI
CCCCCCCCHHHHHHH
15.0625219547
81PhosphorylationTGPYVLGTGLILYAL
CCCCHHHHHHHHHHH
25.3425219547
86PhosphorylationLGTGLILYALSKEIY
HHHHHHHHHHCCCEE
9.8625219547
89PhosphorylationGLILYALSKEIYVIS
HHHHHHHCCCEEEEE
21.7725219547
115AcetylationVMVYGIKKYGPFVAD
HHHHHHHHHCCHHHH
54.2225038526
116PhosphorylationMVYGIKKYGPFVADF
HHHHHHHHCCHHHHH
25.6521406692
126AcetylationFVADFADKLNEQKLA
HHHHHHHHHCHHHHH
50.1925038526
126UbiquitinationFVADFADKLNEQKLA
HHHHHHHHHCHHHHH
50.1921906983
131UbiquitinationADKLNEQKLAQLEEA
HHHHCHHHHHHHHHH
39.34-
131SuccinylationADKLNEQKLAQLEEA
HHHHCHHHHHHHHHH
39.3423954790
1312-HydroxyisobutyrylationADKLNEQKLAQLEEA
HHHHCHHHHHHHHHH
39.34-
131AcetylationADKLNEQKLAQLEEA
HHHHCHHHHHHHHHH
39.3423236377
131SuccinylationADKLNEQKLAQLEEA
HHHHCHHHHHHHHHH
39.34-
139AcetylationLAQLEEAKQASIQHI
HHHHHHHHHHHHHHH
50.0727452117
139UbiquitinationLAQLEEAKQASIQHI
HHHHHHHHHHHHHHH
50.0721906983
142PhosphorylationLEEAKQASIQHIQNA
HHHHHHHHHHHHHHH
21.9320860994
152PhosphorylationHIQNAIDTEKSQQAL
HHHHHHCCHHHHHHH
38.9221406692
154AcetylationQNAIDTEKSQQALVQ
HHHHCCHHHHHHHHH
56.5123954790
1542-HydroxyisobutyrylationQNAIDTEKSQQALVQ
HHHHCCHHHHHHHHH
56.51-
154UbiquitinationQNAIDTEKSQQALVQ
HHHHCCHHHHHHHHH
56.5121906983
154MalonylationQNAIDTEKSQQALVQ
HHHHCCHHHHHHHHH
56.5126320211
155PhosphorylationNAIDTEKSQQALVQK
HHHCCHHHHHHHHHH
22.6926437602
1622-HydroxyisobutyrylationSQQALVQKRHYLFDV
HHHHHHHHHHHHHHH
33.39-
162AcetylationSQQALVQKRHYLFDV
HHHHHHHHHHHHHHH
33.3923236377
162UbiquitinationSQQALVQKRHYLFDV
HHHHHHHHHHHHHHH
33.3921906983
165PhosphorylationALVQKRHYLFDVQRN
HHHHHHHHHHHHHHC
17.0728152594
187PhosphorylationVTYRERLYRVYKEVK
HHHHHHHHHHHHHHH
12.3129496907
190PhosphorylationRERLYRVYKEVKNRL
HHHHHHHHHHHHHHH
7.7629496907
199PhosphorylationEVKNRLDYHISVQNM
HHHHHHHHHHHHHHH
12.9723403867
206SulfoxidationYHISVQNMMRRKEQE
HHHHHHHHHHHHHHH
0.9328183972
207SulfoxidationHISVQNMMRRKEQEH
HHHHHHHHHHHHHHH
5.0028183972
2102-HydroxyisobutyrylationVQNMMRRKEQEHMIN
HHHHHHHHHHHHHHH
54.08-
210UbiquitinationVQNMMRRKEQEHMIN
HHHHHHHHHHHHHHH
54.08-
221UbiquitinationHMINWVEKHVVQSIS
HHHHHHHHHHHHHCC
31.8919608861
221AcetylationHMINWVEKHVVQSIS
HHHHHHHHHHHHHCC
31.8919608861
226PhosphorylationVEKHVVQSISTQQEK
HHHHHHHHCCCHHHH
13.5925159151
228PhosphorylationKHVVQSISTQQEKET
HHHHHHCCCHHHHHH
25.9725159151
229PhosphorylationHVVQSISTQQEKETI
HHHHHCCCHHHHHHH
32.3825159151
233UbiquitinationSISTQQEKETIAKCI
HCCCHHHHHHHHHHH
56.6819608861
233MalonylationSISTQQEKETIAKCI
HCCCHHHHHHHHHHH
56.6826320211
233AcetylationSISTQQEKETIAKCI
HCCCHHHHHHHHHHH
56.6819608861
235PhosphorylationSTQQEKETIAKCIAD
CCHHHHHHHHHHHHH
36.9824641631
238UbiquitinationQEKETIAKCIADLKL
HHHHHHHHHHHHHHH
23.4819608861
238AcetylationQEKETIAKCIADLKL
HHHHHHHHHHHHHHH
23.4825825284
244UbiquitinationAKCIADLKLLAKKAQ
HHHHHHHHHHHHHHH
41.84-
244AcetylationAKCIADLKLLAKKAQ
HHHHHHHHHHHHHHH
41.8425953088
244SuccinylationAKCIADLKLLAKKAQ
HHHHHHHHHHHHHHH
41.8423954790
248AcetylationADLKLLAKKAQAQPV
HHHHHHHHHHHCCCC
48.926567955

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

Oops, there are no upstream regulatory protein records of AT5F1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT5F1_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 AT5F1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATPD_HUMANATP5Dphysical
22939629
ATPG_HUMANATP5C1physical
22939629
QCR7_HUMANUQCRBphysical
22939629
NDUB5_HUMANNDUFB5physical
22939629
NDUB9_HUMANNDUFB9physical
22939629
NDUS7_HUMANNDUFS7physical
22939629
VATH_HUMANATP6V1Hphysical
22939629
RM42_HUMANMRPL42physical
22939629
TOM20_HUMANTOMM20physical
22939629
RS2_HUMANRPS2physical
22939629
SDHA_HUMANSDHAphysical
22939629
CLIC1_HUMANCLIC1physical
21988832
ATP8_HUMANATP8physical
26186194
CERS6_HUMANCERS6physical
26186194
RETR3_HUMANFAM134Cphysical
26186194
CERS2_HUMANCERS2physical
26186194
KDM1A_HUMANKDM1Aphysical
26186194
ATPG_HUMANATP5C1physical
26186194
ATP5H_HUMANATP5Hphysical
26186194
ATPB_HUMANATP5Bphysical
26186194
CH60_HUMANHSPD1physical
26186194
ATPA_HUMANATP5A1physical
26186194
RCOR3_HUMANRCOR3physical
26186194
ZMYM3_HUMANZMYM3physical
26186194
PDPR_HUMANPDPRphysical
26186194
DJC28_HUMANDNAJC28physical
26186194
S19A2_HUMANSLC19A2physical
26186194
AFG32_HUMANAFG3L2physical
26344197
ATPG_HUMANATP5C1physical
26344197
ATPD_HUMANATP5Dphysical
26344197
ATP5I_HUMANATP5Iphysical
26344197
VA0D1_HUMANATP6V0D1physical
26344197
ROA1_HUMANHNRNPA1physical
26344197
LDB3_HUMANLDB3physical
26344197
LMAN1_HUMANLMAN1physical
26344197
RM40_HUMANMRPL40physical
26344197
MTCH1_HUMANMTCH1physical
26344197
MTCH2_HUMANMTCH2physical
26344197
COX2_HUMANCOX2physical
26344197
NDUA9_HUMANNDUFA9physical
26344197
NDUS1_HUMANNDUFS1physical
26344197
NDUS2_HUMANNDUFS2physical
26344197
NDUS4_HUMANNDUFS4physical
26344197
NDUV1_HUMANNDUFV1physical
26344197
SGPL1_HUMANSGPL1physical
26344197
STML2_HUMANSTOML2physical
26344197
TOM22_HUMANTOMM22physical
26344197
TPM1_HUMANTPM1physical
26344197
TPM2_HUMANTPM2physical
26344197
TPM3_HUMANTPM3physical
26344197
TPM4_HUMANTPM4physical
26344197
QCR8_HUMANUQCRQphysical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
VDAC3_HUMANVDAC3physical
26344197
YMEL1_HUMANYME1L1physical
26344197
DJC28_HUMANDNAJC28physical
28514442
ATPB_HUMANATP5Bphysical
28514442
S19A2_HUMANSLC19A2physical
28514442
ATPA_HUMANATP5A1physical
28514442
ATP8_HUMANATP8physical
28514442
ATPG_HUMANATP5C1physical
28514442
ATP5H_HUMANATP5Hphysical
28514442
ZMYM3_HUMANZMYM3physical
28514442
RCOR3_HUMANRCOR3physical
28514442
ATIF1_HUMANATPIF1physical
28514442
CERS2_HUMANCERS2physical
28514442
RETR3_HUMANFAM134Cphysical
28514442
CH60_HUMANHSPD1physical
28514442
PDPR_HUMANPDPRphysical
28514442
ATPO_HUMANATP5Ophysical
28514442
ATP5J_HUMANATP5Jphysical
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 AT5F1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-221 AND LYS-233, AND MASSSPECTROMETRY.

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