AIM21_YEAST - dbPTM
AIM21_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIM21_YEAST
UniProt AC P40563
Protein Name Altered inheritance of mitochondria protein 21
Gene Name AIM21
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 679
Subcellular Localization Cytoplasm, cytoskeleton, actin patch . Cortical actin patches. Localizes at the shmoo tip.
Protein Description Involved in mitochondrial migration along actin filaments..
Protein Sequence MPSEVTPKVPERPSRRKTSELFPLSGSESGDIKANSEPPTPAGTPNVPTRRPILKAKTMTSFESGMDQESLPKVPLQRPVRRSTTEELNNVMNNTSKELEEIESLISKHNIHNVSRKKSPTSVEEGKVAAIHQNGQRSASDNKTSTNPSPLEKNEHEGAEGNESAISPSNLVNKSNNEVTEHSDSEDLTEKQKVHAALDNEAGDRSHFEEKLIPGDMKVQVDVSKDVEEGSLNALPPSGITESDDKAEKFTKHPESSLEELQKHQEQQEEKIFQNPTDEESTTSLNEKQEGKDNMEVNSQPQGPSDTETVIAATSSNVPSQIASEEENDVPVIPRSRPKKDFEAHVQKEELPNTQEKRVSEECDSTLISTEEESKIPKIPSERPKRRAPPPVPKKPSSRIAAFQEMLQKQQQQDLHNNGNSSATTASADIAKKHTDSSITSDTTKADFTSKLNGLFALPGMVNPGQLPPSLEKKLSSPDTESKLGPQDQSQAKTGPLGGTRRGRGPRGRKLPSKVASVEKIEEDDNTNKIEIFNNWNVSSSFSKEKVLIDTTPGEQAERALDEKSKSIPEEQREQSPNKMEAALCPFELDEKEKLPANAESDPLSQLPQTNAVGNRKAISEESLSPSEAIANRDQNDTTEIQEQQMEDQMEVDMERELSGGYEDVDSALHSEEASFHSL
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
14PhosphorylationPKVPERPSRRKTSEL
CCCCCCCCCCCCCCC		51.4419823750
18PhosphorylationERPSRRKTSELFPLS
CCCCCCCCCCCCCCC		26.1425521595
19PhosphorylationRPSRRKTSELFPLSG
CCCCCCCCCCCCCCC		35.0222369663
25PhosphorylationTSELFPLSGSESGDI
CCCCCCCCCCCCCCC		40.2822369663
27PhosphorylationELFPLSGSESGDIKA
CCCCCCCCCCCCCCC		25.8022369663
29PhosphorylationFPLSGSESGDIKANS
CCCCCCCCCCCCCCC		43.3820377248
36PhosphorylationSGDIKANSEPPTPAG
CCCCCCCCCCCCCCC		57.2322369663
40PhosphorylationKANSEPPTPAGTPNV
CCCCCCCCCCCCCCC		36.1622369663
44PhosphorylationEPPTPAGTPNVPTRR
CCCCCCCCCCCCCCC		17.5022369663
49PhosphorylationAGTPNVPTRRPILKA
CCCCCCCCCCCCCCC		34.7222369663
58PhosphorylationRPILKAKTMTSFESG
CCCCCCCCCCCCCCC		30.4622369663
60PhosphorylationILKAKTMTSFESGMD
CCCCCCCCCCCCCCC		35.1822369663
61PhosphorylationLKAKTMTSFESGMDQ
CCCCCCCCCCCCCCH		19.0522369663
64PhosphorylationKTMTSFESGMDQESL
CCCCCCCCCCCHHHC		37.0922890988
70PhosphorylationESGMDQESLPKVPLQ
CCCCCHHHCCCCCCC		44.3222890988
83PhosphorylationLQRPVRRSTTEELNN
CCCCCCCCCHHHHHH		29.1722369663
84PhosphorylationQRPVRRSTTEELNNV
CCCCCCCCHHHHHHH		36.0922369663
85PhosphorylationRPVRRSTTEELNNVM
CCCCCCCHHHHHHHH		28.8022369663
95PhosphorylationLNNVMNNTSKELEEI
HHHHHHCCHHHHHHH		35.8522369663
96PhosphorylationNNVMNNTSKELEEIE
HHHHHCCHHHHHHHH		26.6822369663
104PhosphorylationKELEEIESLISKHNI
HHHHHHHHHHHHHCC		36.3422369663
107PhosphorylationEEIESLISKHNIHNV
HHHHHHHHHHCCCCC		32.9128152593
108AcetylationEIESLISKHNIHNVS
HHHHHHHHHCCCCCC		33.4124489116
115PhosphorylationKHNIHNVSRKKSPTS
HHCCCCCCCCCCCCC		43.6419823750
119PhosphorylationHNVSRKKSPTSVEEG
CCCCCCCCCCCHHHC		36.1225521595
121PhosphorylationVSRKKSPTSVEEGKV
CCCCCCCCCHHHCCE		53.1222369663
122PhosphorylationSRKKSPTSVEEGKVA
CCCCCCCCHHHCCEE		30.8022369663
138PhosphorylationIHQNGQRSASDNKTS
EEECCCCCCCCCCCC		25.0022369663
140PhosphorylationQNGQRSASDNKTSTN
ECCCCCCCCCCCCCC		42.8522369663
144PhosphorylationRSASDNKTSTNPSPL
CCCCCCCCCCCCCCC		47.2222369663
145PhosphorylationSASDNKTSTNPSPLE
CCCCCCCCCCCCCCC		28.0022369663
146PhosphorylationASDNKTSTNPSPLEK
CCCCCCCCCCCCCCC		57.2822369663
149PhosphorylationNKTSTNPSPLEKNEH
CCCCCCCCCCCCCCC		44.1622369663
153AcetylationTNPSPLEKNEHEGAE
CCCCCCCCCCCCCCC		75.2724489116
164PhosphorylationEGAEGNESAISPSNL
CCCCCCCCCCCHHHH		34.6029136822
167PhosphorylationEGNESAISPSNLVNK
CCCCCCCCHHHHCCC		23.2222369663
169PhosphorylationNESAISPSNLVNKSN
CCCCCCHHHHCCCCC		35.6929136822
175PhosphorylationPSNLVNKSNNEVTEH
HHHHCCCCCCCCCCC		39.4222890988
180PhosphorylationNKSNNEVTEHSDSED
CCCCCCCCCCCCCCC		23.0822369663
183PhosphorylationNNEVTEHSDSEDLTE
CCCCCCCCCCCCCCH		36.2822369663
185PhosphorylationEVTEHSDSEDLTEKQ
CCCCCCCCCCCCHHH		35.7022369663
189PhosphorylationHSDSEDLTEKQKVHA
CCCCCCCCHHHHHHH		54.1622890988
191UbiquitinationDSEDLTEKQKVHAAL
CCCCCCHHHHHHHHH		50.6223749301
206PhosphorylationDNEAGDRSHFEEKLI
CCCCCCCHHHHHHCC		36.9522369663
211AcetylationDRSHFEEKLIPGDMK
CCHHHHHHCCCCCEE		44.5124489116
231PhosphorylationSKDVEEGSLNALPPS
CCCCCCCCCCCCCCC		23.0228889911
251PhosphorylationDDKAEKFTKHPESSL
HHHHHHHHHCCCHHH		39.2422369663
256PhosphorylationKFTKHPESSLEELQK
HHHHCCCHHHHHHHH		44.6822369663
257PhosphorylationFTKHPESSLEELQKH
HHHCCCHHHHHHHHH		37.8322369663
277PhosphorylationEKIFQNPTDEESTTS
HHHHCCCCCHHHCCC		64.6922369663
281PhosphorylationQNPTDEESTTSLNEK
CCCCCHHHCCCCCHH		34.6322369663
282PhosphorylationNPTDEESTTSLNEKQ
CCCCHHHCCCCCHHH		24.5525521595
283PhosphorylationPTDEESTTSLNEKQE
CCCHHHCCCCCHHHC		40.2625521595
284PhosphorylationTDEESTTSLNEKQEG
CCHHHCCCCCHHHCC		29.3222369663
320PhosphorylationATSSNVPSQIASEEE
EECCCCCCCCCCCCC		29.9025521595
324PhosphorylationNVPSQIASEEENDVP
CCCCCCCCCCCCCCC		47.3627214570
360PhosphorylationNTQEKRVSEECDSTL
CHHHHHHHHHHHCCE		31.5428889911
365PhosphorylationRVSEECDSTLISTEE
HHHHHHHCCEECCHH		36.4519779198
374PhosphorylationLISTEEESKIPKIPS
EECCHHHHCCCCCCC		38.8821551504
381PhosphorylationSKIPKIPSERPKRRA
HCCCCCCCCCCCCCC		50.1130377154
435PhosphorylationADIAKKHTDSSITSD
HHHHHHHCCCCCCCC		46.5930377154
437PhosphorylationIAKKHTDSSITSDTT
HHHHHCCCCCCCCCC		25.4630377154
438PhosphorylationAKKHTDSSITSDTTK
HHHHCCCCCCCCCCH		32.4728132839
440PhosphorylationKHTDSSITSDTTKAD
HHCCCCCCCCCCHHH		23.6230377154
476PhosphorylationPSLEKKLSSPDTESK
HHHHHHHCCCCCCHH		49.0219823750
477PhosphorylationSLEKKLSSPDTESKL
HHHHHHCCCCCCHHC		36.9125521595
480PhosphorylationKKLSSPDTESKLGPQ
HHHCCCCCCHHCCCC		45.6122890988
482PhosphorylationLSSPDTESKLGPQDQ
HCCCCCCHHCCCCCH		34.9622890988
517PhosphorylationKLPSKVASVEKIEED
CCCCCEECCEEEECC		33.5222369663
551PhosphorylationKEKVLIDTTPGEQAE
CCEEEEECCCHHHHH		28.0922369663
552PhosphorylationEKVLIDTTPGEQAER
CEEEEECCCHHHHHH		26.0822369663
565PhosphorylationERALDEKSKSIPEEQ
HHHHHHHHHCCCHHH		29.5922369663
567PhosphorylationALDEKSKSIPEEQRE
HHHHHHHCCCHHHHH		50.9320377248
576PhosphorylationPEEQREQSPNKMEAA
CHHHHHHCCCHHHHH		26.2022369663
601PhosphorylationKLPANAESDPLSQLP
CCCCCCCCCCHHHCC		41.9619779198
620PhosphorylationVGNRKAISEESLSPS
CCCCCCCCCCCCCHH		39.9222369663
623PhosphorylationRKAISEESLSPSEAI
CCCCCCCCCCHHHHH		30.0522369663
625PhosphorylationAISEESLSPSEAIAN
CCCCCCCCHHHHHHC		35.3422369663
627PhosphorylationSEESLSPSEAIANRD
CCCCCCHHHHHHCCC		35.9622369663
659PhosphorylationVDMERELSGGYEDVD
HHHHHHHHCCCCCHH		25.9722369663
662PhosphorylationERELSGGYEDVDSAL
HHHHHCCCCCHHHHH		16.6922369663
667PhosphorylationGGYEDVDSALHSEEA
CCCCCHHHHHHCCCC		32.3622369663
671PhosphorylationDVDSALHSEEASFHS
CHHHHHHCCCCCCCC		37.6722369663
675PhosphorylationALHSEEASFHSL---
HHHCCCCCCCCC---		27.1122369663
678PhosphorylationSEEASFHSL------
CCCCCCCCC------		33.4922369663
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 AIM21_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIM21_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 AIM21_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABP1_YEASTABP1physical
14737190
CAPZA_YEASTCAP1physical
16429126
CAPZB_YEASTCAP2physical
16429126
TDA2_YEASTTDA2physical
16429126
BBC1_YEASTBBC1physical
18467557
TDA2_YEASTTDA2physical
18719252
CP51_YEASTERG11genetic
27708008
VRP1_YEASTVRP1genetic
27708008
APC11_YEASTAPC11genetic
27708008
PRP9_YEASTPRP9genetic
27708008
PDC2_YEASTPDC2genetic
27708008
ACT_YEASTACT1genetic
27708008
NBP35_YEASTNBP35genetic
27708008
DNA2_YEASTDNA2genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
MAK11_YEASTMAK11genetic
27708008
COFI_YEASTCOF1genetic
27708008
MED14_YEASTRGR1genetic
27708008
UTP13_YEASTUTP13genetic
27708008
TAD3_YEASTTAD3genetic
27708008
CAP_YEASTSRV2genetic
27708008
TIM23_YEASTTIM23genetic
27708008
PROF_YEASTPFY1genetic
27708008
SLA1_YEASTSLA1genetic
27708008
FIG1_YEASTFIG1genetic
27708008
QDR3_YEASTQDR3genetic
27708008
MGR1_YEASTMGR1genetic
27708008
RV161_YEASTRVS161genetic
27708008
PEX19_YEASTPEX19genetic
27708008
SWF1_YEASTSWF1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
PMP3_YEASTPMP3genetic
27708008
RV167_YEASTRVS167genetic
27708008
SNA2_YEASTSNA2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
YE14_YEASTTOG1genetic
27708008
KA122_YEASTKAP122genetic
27708008
ASK10_YEASTASK10genetic
27708008
CHO2_YEASTCHO2genetic
27708008
MED20_YEASTSRB2genetic
27708008
YIQ5_YEASTYIL165Cgenetic
27708008
YJ09_YEASTYJR039Wgenetic
27708008
AIM24_YEASTAIM24genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
IME1_YEASTIME1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
KNS1_YEASTKNS1genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
STE23_YEASTSTE23genetic
27708008
ATP10_YEASTATP10genetic
27708008
PRM6_YEASTPRM6genetic
27708008
SIN3_YEASTSIN3genetic
27708008
INO4_YEASTINO4genetic
27708008
HOS1_YEASTHOS1genetic
27708008
TDA2_YEASTTDA2physical
28706108
BBC1_YEASTBBC1physical
28706108
CAPZA_YEASTCAP1physical
28706108
CAPZB_YEASTCAP2physical
28706108
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AIM21_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 THR-18; SER-19; SER-25;SER-36; THR-58; THR-60; SER-61; SER-83; THR-84; THR-85; SER-104;SER-119; THR-121; SER-167; THR-180; SER-183; SER-185; SER-231;SER-257; THR-277; SER-281; THR-282; SER-284; SER-324; SER-476;SER-477; SER-517; THR-552; SER-567; SER-576; SER-620; SER-623;SER-625; SER-659; SER-667; SER-671 AND SER-675, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; THR-58; THR-84;SER-119; SER-183; SER-257; THR-277 AND SER-625, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-36; THR-58;THR-85; SER-183; THR-277; SER-625 AND SER-678, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, AND MASSSPECTROMETRY.

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