ATM1_YEAST - dbPTM
ATM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATM1_YEAST
UniProt AC P40416
Protein Name Iron-sulfur clusters transporter ATM1, mitochondrial
Gene Name ATM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 690
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins. Hydrolyzes ATP. Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound..
Protein Sequence MLLLPRCPVIGRIVRSKFRSGLIRNHSPVIFTVSKLSTQRPLLFNSAVNLWNQAQKDITHKKSVEQFSSAPKVKTQVKKTSKAPTLSELKILKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLFGELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILTYQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDSQIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFKLRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESGRILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGLMISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVREEGKHLELLAMPGSLYRELWTIQEDLDHLENELKDQQEL
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
63PhosphorylationKDITHKKSVEQFSSA
HHCCCHHHHHHHHCC		35.3728889911
68PhosphorylationKKSVEQFSSAPKVKT
HHHHHHHHCCCCCCC		25.8630377154
90AcetylationAPTLSELKILKDLFR
CCCHHHHHHHHHHHH		41.7724489116
181AcetylationLRNAVFAKVAQNAIR
HHHHHHHHHHHHHHH		27.0024489116
315AcetylationVKYFNNEKYLADKYN
HHHHCCCHHHHHHCC		47.9224489116
321PhosphorylationEKYLADKYNGSLMNY
CHHHHHHCCCCCCCH		25.8827017623
328PhosphorylationYNGSLMNYRDSQIKV
CCCCCCCHHHHHEEH		11.2227017623
475AcetylationVGSSGSGKSTILKLV
EECCCCCHHHHHEEE		46.2324489116
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 ATM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATM1_YEAST !!
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 ATM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATM1_YEASTATM1physical
15225610
MDL1_YEASTMDL1genetic
12875842
MRS3_YEASTMRS3genetic
18625724
MRS4_YEASTMRS4genetic
18625724
ATM1_YEASTATM1physical
24604199
SNU56_YEASTSNU56genetic
27708008
ERS1_YEASTERS1genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
SEI1_YEASTFLD1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
PMT3_YEASTPMT3genetic
27708008
CKS1_YEASTCKS1genetic
27708008
KRR1_YEASTKRR1genetic
27708008
TECR_YEASTTSC13genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
SAD1_YEASTSAD1genetic
27708008
ERG26_YEASTERG26genetic
27708008
SDA1_YEASTSDA1genetic
27708008
ARP4_YEASTARP4genetic
27708008
HSP77_YEASTSSC1genetic
27708008
FIP1_YEASTFIP1genetic
27708008
TIM14_YEASTPAM18genetic
27708008
SEC22_YEASTSEC22genetic
27708008
ERB1_YEASTERB1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
NOP2_YEASTNOP2genetic
27708008
CH10_YEASTHSP10genetic
27708008
TYSY_YEASTCDC21genetic
27708008
APC5_YEASTAPC5genetic
27708008
CLP1_YEASTCLP1genetic
27708008
SEC62_YEASTSEC62genetic
27708008
TBF1_YEASTTBF1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
HSP71_YEASTSSA1genetic
27708008
HIR1_YEASTHIR1genetic
27708008
YBF9_YEASTYBL059Wgenetic
27708008
NU170_YEASTNUP170genetic
27708008
RTG3_YEASTRTG3genetic
27708008
SHG1_YEASTSHG1genetic
27708008
CHK1_YEASTCHK1genetic
27708008
HXKG_YEASTGLK1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
ATG15_YEASTATG15genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
RPN4_YEASTRPN4genetic
27708008
RS16A_YEASTRPS16Bgenetic
27708008
RS16B_YEASTRPS16Bgenetic
27708008
VPS41_YEASTVPS41genetic
27708008
ARX1_YEASTARX1genetic
27708008
H2A1_YEASTHTA1genetic
27708008
MNN10_YEASTMNN10genetic
27708008
PUF6_YEASTPUF6genetic
27708008
AIM11_YEASTAIM11genetic
27708008
GEP7_YEASTGEP7genetic
27708008
MTC3_YEASTMTC3genetic
27708008
PEF1_YEASTPEF1genetic
27708008
PFD3_YEASTPAC10genetic
27708008
CGS6_YEASTCLB6genetic
27708008
PHB1_YEASTPHB1genetic
27708008
PHB2_YEASTPHB2genetic
27708008
TBP7_YEASTYTA7genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
DSE2_YEASTDSE2genetic
27708008
AIM18_YEASTAIM18genetic
27708008
FLX1_YEASTFLX1genetic
27708008
MDM35_YEASTMDM35genetic
27708008
SAC1_YEASTSAC1genetic
27708008
POM33_YEASTPOM33genetic
27708008
ALAM_YEASTALT1genetic
27708008
MDL1_YEASTMDL1genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
VID22_YEASTVID22genetic
27708008
PUN1_YEASTPUN1genetic
27708008
CDC73_YEASTCDC73genetic
27708008
RS3A1_YEASTRPS1Agenetic
27708008
GMC2_YEASTGMC2genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
MGR3_YEASTMGR3genetic
27708008
RAD14_YEASTRAD14genetic
27708008
PET8_YEASTPET8genetic
27708008
MDM38_YEASTMDM38genetic
27708008
NOP12_YEASTNOP12genetic
27708008
RRP6_YEASTRRP6genetic
27708008
WHI5_YEASTWHI5genetic
27708008
DGK1_YEASTDGK1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
VTS1_YEASTVTS1genetic
27708008
PDE2_YEASTPDE2genetic
27708008
RAD1_YEASTRAD1genetic
27708008
MGR2_YEASTMGR2genetic
27708008
ISU1_YEASTISU1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATM1_YEAST

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Related Literatures of Post-Translational Modification

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