ABF2_YEAST - dbPTM
ABF2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABF2_YEAST
UniProt AC Q02486
Protein Name ARS-binding factor 2, mitochondrial
Gene Name ABF2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 183
Subcellular Localization Mitochondrion. Nucleus .
Protein Description Specific binding to the autonomously replicating sequence 1 (ARS1). Interaction with regulatory regions: probably involved in compacting the mitochondrial genome. It might play a positive role in gene expression and replication..
Protein Sequence MNSYSLLTRSFHESSKPLFNLASTLLKASKRTQLRNELIKQGPKRPTSAYFLYLQDHRSQFVKENPTLRPAEISKIAGEKWQNLEADIKEKYISERKKLYSEYQKAKKEFDEKLPPKKPAGPFIKYANEVRSQVFAQHPDKSQLDLMKIIGDKWQSLDQSIKDKYIQEYKKAIQEYNARYPLN
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
47PhosphorylationKQGPKRPTSAYFLYL
HHCCCCCCCHHEEEH
29.9830377154
48PhosphorylationQGPKRPTSAYFLYLQ
HCCCCCCCHHEEEHH
24.5330377154
59PhosphorylationLYLQDHRSQFVKENP
EEHHHHHHHHHHHCC
25.2624961812
63AcetylationDHRSQFVKENPTLRP
HHHHHHHHHCCCCCH
53.7324489116
74PhosphorylationTLRPAEISKIAGEKW
CCCHHHHHHHHCHHH
14.9828889911
75AcetylationLRPAEISKIAGEKWQ
CCHHHHHHHHCHHHH
42.0924489116
80AcetylationISKIAGEKWQNLEAD
HHHHHCHHHHCCCHH
53.8424489116
89AcetylationQNLEADIKEKYISER
HCCCHHHHHHHHHHH
49.0224489116
91AcetylationLEADIKEKYISERKK
CCHHHHHHHHHHHHH
42.7724489116
100PhosphorylationISERKKLYSEYQKAK
HHHHHHHHHHHHHHH
14.3422369663
101PhosphorylationSERKKLYSEYQKAKK
HHHHHHHHHHHHHHH
40.0222369663
103PhosphorylationRKKLYSEYQKAKKEF
HHHHHHHHHHHHHHH
14.9022369663
105AcetylationKLYSEYQKAKKEFDE
HHHHHHHHHHHHHHH
62.3625381059
125AcetylationKPAGPFIKYANEVRS
CCCCHHHHHHHHHHH
38.3924489116
132PhosphorylationKYANEVRSQVFAQHP
HHHHHHHHHHHHHCC
35.5521440633
141AcetylationVFAQHPDKSQLDLMK
HHHHCCCHHHHHHHH
44.5524489116
142PhosphorylationFAQHPDKSQLDLMKI
HHHCCCHHHHHHHHH
43.2730377154
148AcetylationKSQLDLMKIIGDKWQ
HHHHHHHHHHHHHHH
38.1724489116
153AcetylationLMKIIGDKWQSLDQS
HHHHHHHHHHHHCHH
41.7524489116
1622-HydroxyisobutyrylationQSLDQSIKDKYIQEY
HHHCHHHHHHHHHHH
54.11-
162SuccinylationQSLDQSIKDKYIQEY
HHHCHHHHHHHHHHH
54.1123954790
164AcetylationLDQSIKDKYIQEYKK
HCHHHHHHHHHHHHH
38.9724489116
170AcetylationDKYIQEYKKAIQEYN
HHHHHHHHHHHHHHH
34.6725381059

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 ABF2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABF2_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 ABF2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ILV5_YEASTILV5genetic
7621838
YHM2_YEASTYHM2genetic
9742088
CHD1_YEASTCHD1physical
16554755
H4_YEASTHHF1physical
16429126
ISW1_YEASTISW1physical
16429126
MOT1_YEASTMOT1physical
16429126
PDR1_YEASTPDR1physical
16429126
RSC3_YEASTRSC3physical
16429126
RUVB1_YEASTRVB1physical
16429126
TOP1_YEASTTOP1physical
16429126
VPS1_YEASTVPS1physical
16429126
ACT_YEASTACT1physical
16429126
RSC8_YEASTRSC8physical
16429126
RSSA2_YEASTRPS0Bphysical
16429126
RSC6_YEASTRSC6physical
16429126
SNF5_YEASTSNF5physical
16429126
SWI3_YEASTSWI3physical
16429126
RIR1_YEASTRNR1genetic
17721079
ILV5_YEASTILV5physical
18023287
ILV5_YEASTILV5genetic
18023287
MLH1_YEASTMLH1physical
18467557
ACON_YEASTACO1physical
18477605
ALDH4_YEASTALD4physical
18477605
IDH1_YEASTIDH1physical
18477605
IDH2_YEASTIDH2physical
18477605
ODO1_YEASTKGD1physical
18477605
UBP3_YEASTUBP3genetic
19547744
ACON_YEASTACO1genetic
15692048
ODO2_YEASTKGD2genetic
10869431
IES4_YEASTIES4genetic
20959818
EAF7_YEASTEAF7genetic
20959818
UBP3_YEASTUBP3genetic
20959818
RRG1_YEASTRRG1genetic
21987634
SEC1_YEASTSEC1genetic
21987634
HAP2_YEASTHAP2genetic
21987634
MIC60_YEASTMIC60genetic
21987634
GEP5_YEASTGEP5genetic
21987634
ARPC3_YEASTARC18genetic
21987634
AIM34_YEASTAIM34genetic
21987634
SYKM_YEASTMSK1genetic
21987634
TOM22_YEASTTOM22genetic
21987634
MDM38_YEASTMDM38genetic
21987634
TIM18_YEASTTIM18genetic
21987634
MGR2_YEASTMGR2genetic
21987634
FUMH_YEASTFUM1genetic
21987634
SYFM_YEASTMSF1genetic
21987634
YLH47_YEASTYLH47genetic
21987634
GGC1_YEASTGGC1genetic
8905928
UAP1_YEASTQRI1genetic
27708008
NSE4_YEASTNSE4genetic
27708008
TIM22_YEASTTIM22genetic
27708008
FAL1_YEASTFAL1genetic
27708008
SLU7_YEASTSLU7genetic
27708008
CDC1_YEASTCDC1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
COG3_YEASTCOG3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
BRR6_YEASTBRR6genetic
27708008
SLN1_YEASTSLN1genetic
27708008
ARP3_YEASTARP3genetic
27708008
CDC11_YEASTCDC11genetic
27708008
KCY_YEASTURA6genetic
27708008
BOS1_YEASTBOS1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
GSP1_YEASTGSP1genetic
27708008
LIP1_YEASTLIP1genetic
27708008
GPI15_YEASTGPI15genetic
27708008
NOP2_YEASTNOP2genetic
27708008
PRS10_YEASTRPT4genetic
27708008
TF2B_YEASTSUA7genetic
27708008
NAA38_YEASTMAK31genetic
27708008
SNT1_YEASTSNT1genetic
27708008
MBP1_YEASTMBP1genetic
27708008
CWC15_YEASTCWC15genetic
27708008
PEX10_YEASTPEX10genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
YG1O_YEASTYGR035Cgenetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
SAC1_YEASTSAC1genetic
27708008
SET3_YEASTSET3genetic
27708008
UPS2_YEASTUPS2genetic
27708008
MMR1_YEASTMMR1genetic
27708008
CCE1_YEASTCCE1physical
27908236

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABF2_YEAST

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Related Literatures of Post-Translational Modification

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