RAX2_YEAST - dbPTM
RAX2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAX2_YEAST
UniProt AC Q12465
Protein Name Bud site selection protein RAX2
Gene Name RAX2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1220
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Bud neck. Bud tip. Before cytokinesis, RAX2 concentrates as a ring at the mother-bud neck and to the tip of the bud. The RAX2 ring splits at cytokinesis, endowing each progeny cell with a RAX2 ring
Protein Description Required for the maintenance of the bipolar budding pattern. Involved in selecting bud sites at both the distal and proximal poles of daughter cells as well as near previously used division sites on mother cells..
Protein Sequence MFVHRLWTLAFPFLVEISKASQLENIKSLLDIEDNVLPNLNISQNNSNAVQILGGVDALSFYEYTGQQNFTKEIGPETSSHGLVYYSNNTYIQLEDASDDTRIDKITPFGVDSFILSGSGTINNISVGNQILYNLSTLSMTPIFNQSLGAVQAVLADNSSIYFGGNFSYNNGSMTGYSALIWDSISNTTQLLPFGGFGENSSVNSIVKLNNDNILFAGQFYTLDDPSALISSSNNGTNSTSSLNATTLELGQRIPLRYASWDSQGSTTFASDSLVCPNTNEDAWLYPDTSGSLVCNLPYEVSPTKIRLYNSQRSDSEISVFQILTDPSSSIMNLTYLDPLSGELKNCGEFCPLYSRATLLSASQNVSSSMDMITFIDNNKTDVKWTSDFQDFAFVNELPVSSLKFVALNSYGGSVGLSGLELYQDTFSTYANDSLNEYGCSALTNDSSSSTLSSNDWYNGLTGESYIAAKYVPDQNEPIPRVKFYPNIIHPGHYTINMYTPGCLQDNTCSARGIVNVTMWNQQNNTIMKTYLIYQNNDNLKYDQIYSGYLDFSPEIVLEYVSGIYTTNTATVVVADQVNVITVSLDAFNTLSDSSNAKKETLLNGILQYQKSNFTSTRLNETKVGNTTLNLFPVKNYPKNSSLYADIYDNKLVIGGVSNRISIVDLNDDFEVTSSKNQTIQGDVHGITKTNQGLLIFGDILSSNNQSAVFLFNGSFENVFNQSRTVNSALNISLANNDFIVLDNDYVVNASSNALIRNSSSFSLSLWAAGNNGDGDVLFSGAVSHMQYGNLNGSVRFLNENEIEPLNLEGGIVPYLGAYLNESATAYAYEVDSLNKIYFSNEVYPSWNWSSGITQMLYADNQTLLAVSAGSSTTAELSIFDLRNLTMIANETLGSNARINALVNFEKNCSMLVGGDFQMTEPNCTGLCLYNYESKTWSTFLNNTIFGEITQLSFTNSSELIISGLFETKEYQSIRLGSFNLTNSTMIPLLSGSEGKLNSFTVTEDSIVAWNDTSLFIYRNQEWNITSLPGNASSISSVSAIYTDIESNTLNKRGINNVNNGSILLLNGNFNISQYGYLQSLLFDFQKWTPYFISETTNTSNYNPIIFINRDVSTEFNSQSPLANVNITVTSPQSTSSQPPSSSASSESKSKSKKKKIGRGFVVLIGLALALGTVSVLGIAGVILAYVFKDPEGDYKPIKPRIDENEMLDTVPPEKLMKFV
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
41N-linked_GlycosylationDNVLPNLNISQNNSN
CCCCCCCCCCCCCCC		38.21-
45N-linked_GlycosylationPNLNISQNNSNAVQI
CCCCCCCCCCCCEEE		47.29-
69N-linked_GlycosylationYEYTGQQNFTKEIGP
EEECCCCCCEECCCC		38.37-
88N-linked_GlycosylationHGLVYYSNNTYIQLE
CEEEEEECCEEEEEE		28.83-
124N-linked_GlycosylationSGSGTINNISVGNQI
CCCCCCCCEEECCEE		24.86-
134N-linked_GlycosylationVGNQILYNLSTLSMT
ECCEEEEECCCCCCC		24.87-
145N-linked_GlycosylationLSMTPIFNQSLGAVQ
CCCCHHCCCCCCCCE		31.11-
158N-linked_GlycosylationVQAVLADNSSIYFGG
CEEEECCCCCEEECC		31.86-
166N-linked_GlycosylationSSIYFGGNFSYNNGS
CCEEECCEEEECCCC		24.07-
171N-linked_GlycosylationGGNFSYNNGSMTGYS
CCEEEECCCCCCCCE		35.37-
187N-linked_GlycosylationLIWDSISNTTQLLPF
EEEECCCCEEEEECC		45.54-
200N-linked_GlycosylationPFGGFGENSSVNSIV
CCCCCCCCCCCCEEE		39.71-
208UbiquitinationSSVNSIVKLNNDNIL
CCCCEEEEECCCCEE		43.7715699485
235N-linked_GlycosylationALISSSNNGTNSTSS
HEEECCCCCCCCCCC		61.69-
238N-linked_GlycosylationSSSNNGTNSTSSLNA
ECCCCCCCCCCCCCC		44.69-
244N-linked_GlycosylationTNSTSSLNATTLELG
CCCCCCCCCEEECCC		36.87-
333N-linked_GlycosylationDPSSSIMNLTYLDPL
CCCCCCCCCEEEECC		27.79-
365N-linked_GlycosylationTLLSASQNVSSSMDM
HHHHHHCCCCCCCCE		32.89-
379N-linked_GlycosylationMITFIDNNKTDVKWT
EEEEEECCCCCEEEC		44.87-
432N-linked_GlycosylationDTFSTYANDSLNEYG
CCHHHHCCCCCHHCC		29.05-
445N-linked_GlycosylationYGCSALTNDSSSSTL
CCCCCCCCCCCCCCC		48.28-
516N-linked_GlycosylationCSARGIVNVTMWNQQ
CCCCCEEEEEEEECC		22.94-
524N-linked_GlycosylationVTMWNQQNNTIMKTY
EEEEECCCCEEEEEE		37.54-
613N-linked_GlycosylationILQYQKSNFTSTRLN
HHHHHHCCCCCCCCC		51.77-
620N-linked_GlycosylationNFTSTRLNETKVGNT
CCCCCCCCCCCCCCE		52.15-
626N-linked_GlycosylationLNETKVGNTTLNLFP
CCCCCCCCEEEEEEE		32.64-
640N-linked_GlycosylationPVKNYPKNSSLYADI
ECCCCCCCCCCEEEE		32.12-
658PhosphorylationKLVIGGVSNRISIVD
CEEEECCCCCEEEEE		24.5428889911
677N-linked_GlycosylationFEVTSSKNQTIQGDV
CEEECCCCCEEECCC		46.29-
705N-linked_GlycosylationGDILSSNNQSAVFLF
EEECCCCCCEEEEEE		38.85-
713N-linked_GlycosylationQSAVFLFNGSFENVF
CEEEEEECCCHHHHH		47.55-
721N-linked_GlycosylationGSFENVFNQSRTVNS
CCHHHHHCCCCCHHH		34.34-
731N-linked_GlycosylationRTVNSALNISLANND
CCHHHHHEEEECCCC		22.86-
749N-linked_GlycosylationLDNDYVVNASSNALI
ECCCEEEECCCCCEE		24.86-
758N-linked_GlycosylationSSNALIRNSSSFSLS
CCCCEECCCCCEEEE		38.97-
792N-linked_GlycosylationHMQYGNLNGSVRFLN
CEEECCCCCCEEECC		44.70-
821N-linked_GlycosylationPYLGAYLNESATAYA
HHHHHHCCCCCCEEE		28.62-
848N-linked_GlycosylationNEVYPSWNWSSGITQ
CCCCCCCCCCCCCEE		32.84-
861N-linked_GlycosylationTQMLYADNQTLLAVS
EEEEEECCCEEEEEE		28.68-
884N-linked_GlycosylationLSIFDLRNLTMIANE
EEEEEHHHCEEEEEC		47.35-
890N-linked_GlycosylationRNLTMIANETLGSNA
HHCEEEEECCCCCCH		31.68-
908N-linked_GlycosylationALVNFEKNCSMLVGG
EEEECHHCCCEEECC		18.85-
923N-linked_GlycosylationDFQMTEPNCTGLCLY
CCCCCCCCCCEEEEE		29.74-
942N-linked_GlycosylationKTWSTFLNNTIFGEI
CCHHHHHCCCCCCEE		39.13-
956N-linked_GlycosylationITQLSFTNSSELIIS
EEEEEECCCCCEEEE		41.34-
980N-linked_GlycosylationSIRLGSFNLTNSTMI
EEEEECEECCCCCEE		47.88-
983N-linked_GlycosylationLGSFNLTNSTMIPLL
EECEECCCCCEEEEE		38.35-
1011N-linked_GlycosylationEDSIVAWNDTSLFIY
CCEEEEECCCEEEEE		32.70-
1024N-linked_GlycosylationIYRNQEWNITSLPGN
EECCCCEECEECCCC		27.23-
1031N-linked_GlycosylationNITSLPGNASSISSV
ECEECCCCHHHHHEE		34.41-
1060N-linked_GlycosylationRGINNVNNGSILLLN
CCCCCCCCCCEEEEC		41.11-
1071N-linked_GlycosylationLLLNGNFNISQYGYL
EEECCCCCHHHCCHH		36.68-
1098N-linked_GlycosylationYFISETTNTSNYNPI
EEEECCCCCCCCCCE		49.26-
1126N-linked_GlycosylationQSPLANVNITVTSPQ
CCCCCEEEEEEECCC		24.83-
1153UbiquitinationSESKSKSKKKKIGRG
CCCCCHHHHCCHHHH		72.8015699485
1154UbiquitinationESKSKSKKKKIGRGF
CCCCHHHHCCHHHHH		67.4015699485
1155UbiquitinationSKSKSKKKKIGRGFV
CCCHHHHCCHHHHHH		54.0515699485
1156UbiquitinationKSKSKKKKIGRGFVV
CCHHHHCCHHHHHHH		60.3115699485
1215UbiquitinationLDTVPPEKLMKFV--
CCCCCHHHHHHCC--		60.7023749301
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 RAX2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAX2_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 RAX2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL19A_YEASTRPL19Bgenetic
20093466
RL19B_YEASTRPL19Bgenetic
20093466
MTO1_YEASTMTO1genetic
20093466
ATC1_YEASTPMR1genetic
20093466
FLX1_YEASTFLX1genetic
20093466
ICE2_YEASTICE2genetic
20093466
CBT1_YEASTCBT1genetic
20093466
HAP4_YEASTHAP4genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
ATP10_YEASTATP10genetic
20093466
IOC4_YEASTIOC4genetic
20093466
GTO3_YEASTGTO3genetic
20093466
YNM2_YEASTYNL122Cgenetic
20093466
ATP23_YEASTATP23genetic
20093466
RTG1_YEASTRTG1genetic
20093466
KES1_YEASTKES1genetic
20093466
RL21B_YEASTRPL21Bgenetic
20093466
YP078_YEASTYPR078Cgenetic
20093466
QCR2_YEASTQCR2genetic
20093466
RS8A_YEASTRPS8Agenetic
21987634
RS8B_YEASTRPS8Agenetic
21987634
ATC1_YEASTPMR1genetic
21987634
AIM36_YEASTAIM36genetic
21987634
YME1_YEASTYME1genetic
21987634
RAX2_YEASTRAX2physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
SSB1_YEASTSSB1physical
22940862
NIS1_YEASTNIS1physical
25416945
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAX2_YEAST

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Related Literatures of Post-Translational Modification

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