ARB1_YEAST - dbPTM
ARB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARB1_YEAST
UniProt AC P40024
Protein Name ABC transporter ATP-binding protein ARB1
Gene Name ARB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 610
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the cytoplasm and the nucleus.
Protein Description Stimulates 40S and 60S ribosome biogenesis..
Protein Sequence MPPVSASKAKRDAKKAEREAKKAAAGKTIRKLGRKKEAAAEESEVDAAAREIKMMKLQQDKDGLSDRVVTGVLSSLETSRDIKLSSVSLLFHGKVLIQDSGLELNYGRRYGLLGENGCGKSTFLKALATREYPIPEHIDIYLLDEPAEPSELSALDYVVTEAQHELKRIEDLVEKTILEDGPESELLEPLYERMDSLDPDTFESRAAIILIGLGFNKKTILKKTKDMSGGWKMRVALAKALFVKPTLLLLDDPTAHLDLEACVWLEEYLKRFDRTLVLVSHSQDFLNGVCTNMIDMRAQKLTAYGGNYDSYHKTRSELETNQMKQYNKQQEEIQHIKKFIASAGTYANLVKQAKSRQKILDKMEADGLVQPVVPDKVFSFRFPQVERLPPPVLAFDDISFHYESNPSENLYEHLNFGVDMDSRIALVGPNGVGKSTLLKIMTGELTPQSGRVSRHTHVKLGVYSQHSQDQLDLTKSALEFVRDKYSNISQDFQFWRGQLGRYGLTGEGQTVQMATLSEGQRSRVVFALLALEQPNVLLLDEPTNGLDIPTIDSLADAINEFNGGVVVVSHDFRLLDKIAQDIFVVENKTATRWDGSILQYKNKLAKNVVL
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
27AcetylationAKKAAAGKTIRKLGR
HHHHHHCHHHHHHCH
35.7325381059
43PhosphorylationKEAAAEESEVDAAAR
HHHHHHHHHHHHHHH
34.1325533186
56AcetylationAREIKMMKLQQDKDG
HHHHHHHHHHCCCCC
39.3825381059
61UbiquitinationMMKLQQDKDGLSDRV
HHHHHCCCCCCCHHH
49.7323749301
61AcetylationMMKLQQDKDGLSDRV
HHHHHCCCCCCCHHH
49.7324489116
65PhosphorylationQQDKDGLSDRVVTGV
HCCCCCCCHHHHHHH
28.9721440633
74PhosphorylationRVVTGVLSSLETSRD
HHHHHHHHHCCCCCC
30.3930377154
75PhosphorylationVVTGVLSSLETSRDI
HHHHHHHHCCCCCCC
26.5127214570
86PhosphorylationSRDIKLSSVSLLFHG
CCCCCHHHHHEEECC
26.6028889911
125AcetylationCGKSTFLKALATREY
CCHHHHHHHHHCCCC
36.8424489116
125UbiquitinationCGKSTFLKALATREY
CCHHHHHHHHHCCCC
36.8423749301
196PhosphorylationPLYERMDSLDPDTFE
HHHHHHHCCCCCCHH
25.9025752575
239AcetylationKMRVALAKALFVKPT
HHHHHHHHHHCCCCE
46.6122865919
300AcetylationMIDMRAQKLTAYGGN
HHHHHHHHHHHCCCC
46.9824489116
313AcetylationGNYDSYHKTRSELET
CCHHHCCCCHHHHHH
37.0824489116
342PhosphorylationHIKKFIASAGTYANL
HHHHHHHHHHHHHHH
23.5530377154
345PhosphorylationKFIASAGTYANLVKQ
HHHHHHHHHHHHHHH
21.1224961812
346PhosphorylationFIASAGTYANLVKQA
HHHHHHHHHHHHHHH
7.8025752575
362AcetylationSRQKILDKMEADGLV
HHHHHHHHHHHCCCC
34.8824489116
376AcetylationVQPVVPDKVFSFRFP
CCCCCCCCEEEEECC
38.8324489116
434AcetylationVGPNGVGKSTLLKIM
ECCCCCCHHHHHHHH
37.5524489116
439AcetylationVGKSTLLKIMTGELT
CCHHHHHHHHCCCCC
33.2824489116
439UbiquitinationVGKSTLLKIMTGELT
CCHHHHHHHHCCCCC
33.2823749301
442PhosphorylationSTLLKIMTGELTPQS
HHHHHHHCCCCCCCC
30.8621126336
446PhosphorylationKIMTGELTPQSGRVS
HHHCCCCCCCCCCCC
18.2525752575
467PhosphorylationLGVYSQHSQDQLDLT
EEEECCCCHHHHHHH
28.0227214570
475AcetylationQDQLDLTKSALEFVR
HHHHHHHHHHHHHHH
40.8224489116
476PhosphorylationDQLDLTKSALEFVRD
HHHHHHHHHHHHHHH
32.6227214570
484AcetylationALEFVRDKYSNISQD
HHHHHHHHCCCCCHH
39.7624489116
577AcetylationHDFRLLDKIAQDIFV
CCHHHHHHHHCCEEE
39.6524489116
588AcetylationDIFVVENKTATRWDG
CEEEECCCCCCCCCC
26.4824489116
588UbiquitinationDIFVVENKTATRWDG
CEEEECCCCCCCCCC
26.4823749301
601AcetylationDGSILQYKNKLAKNV
CCHHHHHHHHHHHCC
34.3524489116

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 ARB1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARB1_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 ARB1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATH_YEASTVMA13physical
11805826
ARX1_YEASTARX1physical
11805826
IF2P_YEASTFUN12physical
11805826
RL8A_YEASTRPL8Aphysical
16260602
RL6A_YEASTRPL6Aphysical
16260602
RS19B_YEASTRPS19Bphysical
16260602
RL16A_YEASTRPL16Aphysical
16260602
EIF2A_YEASTYGR054Wphysical
16260602
RL33B_YEASTRPL33Bphysical
16260602
RL14A_YEASTRPL14Aphysical
16260602
RS21A_YEASTRPS21Aphysical
16260602
RLA2_YEASTRPP2Aphysical
16260602
RS21B_YEASTRPS21Bphysical
16260602
DED1_YEASTDED1physical
16260602
ZUO1_YEASTZUO1physical
16260602
IF6_YEASTTIF6physical
16260602
CBF5_YEASTCBF5physical
16260602
NOP56_YEASTNOP56physical
16260602
DCA13_YEASTSOF1physical
16260602
LSG1_YEASTLSG1physical
16260602
ARX1_YEASTARX1physical
16260602
NOP58_YEASTNOP58physical
16260602
UTP7_YEASTUTP7physical
16260602
SC160_YEASTSCP160physical
16260602
C1TM_YEASTMIS1physical
16260602
C1TC_YEASTADE3physical
16260602
MAS5_YEASTYDJ1physical
16260602
LSM12_YEASTLSM12physical
16260602
IF2P_YEASTFUN12physical
16260602
CLU_YEASTCLU1physical
16260602
EIF3A_YEASTRPG1physical
16260602
EF3A_YEASTYEF3physical
16260602
MNP1_YEASTMNP1physical
16260602
RM19_YEASTMRPL19physical
16260602
IDHP_YEASTIDP1physical
16260602
ATPG_YEASTATP3physical
16260602
ILVB_YEASTILV2physical
16260602
SEC1_YEASTSEC1physical
16260602
VATB_YEASTVMA2physical
16260602
HSP72_YEASTSSA2physical
16260602
FAS1_YEASTFAS1physical
16260602
VMS1_YEASTVMS1physical
16260602
TMA46_YEASTTMA46physical
16260602
RL3_YEASTRPL3physical
16429126
RL6A_YEASTRPL6Aphysical
16429126
RL8A_YEASTRPL8Aphysical
16429126
VATH_YEASTVMA13physical
16429126
RL17A_YEASTRPL17Aphysical
16429126
RL28_YEASTRPL28physical
16429126
IF2P_YEASTFUN12physical
16429126
RL8B_YEASTRPL8Bphysical
16429126
RS3_YEASTRPS3physical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
PMP1_YEASTPMP1physical
26404137

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARB1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-65; SER-196 ANDTHR-446, AND MASS SPECTROMETRY.

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