PLXA1_MOUSE - dbPTM
PLXA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXA1_MOUSE
UniProt AC P70206
Protein Name Plexin-A1
Gene Name Plxna1
Organism Mus musculus (Mouse).
Sequence Length 1894
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm..
Protein Sequence MPLPPLSSRTLLLLLLLLLRGVWIAISSPPAGLGPQPAFRTFVASDWGLTHLVVHEQTGEVYVGAVNRIYKLSGNLTLLRAHVTGPVEDNEKCYPPPSVQSCPHGLGSTDNVNKLLLLDYAANRLLACGSASQGICQFLRLDDLFKLGEPHHRKEHYLSSVREAGSMAGVLIAGPPGQGQAKLFVGTPIDGKSEYFPTLSSRRLMANEEDADMFGFVYQDEFVSSQLKIPSDTLSKFPAFDIYYVYSFRSEQFVYYLTLQLDTQLTSPDAAGEHFFTSKIVRLCVNDPKFYSYVEFPIGCEQAGVEYRLVQDAYLSRPGQALAKQLGLAEDEEVLFTVFAQGQKNRVKPPKESALCLFTLRAIKEKIKERIQSCYRGEGKLSLPWLLNKELGCINSPLQIDDDFCGQDFNQPLGGTVTIEGTPLFVDKEDGLTAVAAYDYQGRTVVFAGTRSGRIRKILVDLANPSGRPALAYESVVAQEGNPILRDLVLSPNRQYLYAMTEKQVTQVPVESCVQYTSCELCLGSRDPHCGWCVLHSICSRQDACERAEEPQRFASDLLQCVQLTVQPRNVSVTMSQVPLVLQAWNVPDLSAGVNCSFEDFTETESILEDGRIHCHSPSAREVAPITQGQGDQRVVKLYLKSKETGKKFASVDFVFYNCSVHQSCLACVNGSFPCHWCKYRHVCTNNAADCAFLEGRVNMSEDCPQILPSTHIYVPVGVVKPITLAARNLPQPQSGQRGYECLFHIPGSPARVTALRFNSSSLQCQNSSYSYEGNDVSDLPVNLSVVWNGNFVIDNPQNIQAHLYKCPALRQSCGLCLKADPRFECGWCVAERRCSLRHHCPADSPASWMHAHHGSSRCTDPKILKLSPETGPRQGGTRLTITGENLGLRFEDVRLGVHVGKVLCSPVESEYISAEQIVCEIGDASTLRAHDALVEVCVRDCSLHYRALSPKRFTFVTPTFYRVSPSRGPLSGGTWIGIEGSHLNAGSDVAVSIGGRPCSFSWRNSREIRCLTPPGHTPGSAPIVININRAQLSNPEVKYNYTEDPTILRIDPEWSINSGGTLLTVTGTNLATVREPRIRAKYGGIERENSCMVYNDTTMVCRAPSIDNPKRSPPELGERPDEIGFIMDNVRTLLVLNSSSFLYYPDPVLEPLSPTGLLELKPSSPLILKGRNLLPPAPGNSRLNYTVLIGSTPCILTVSETQLLCEAPNLTGQHKVTVRAGGFEFSPGMLQVYSDSLLTLPAIVGIGGGGGLLLLVIVAVLIAYKRKSRDADRTLKRLQLQMDNLESRVALECKEAFAELQTDIHELTSDLDGAGIPFLDYRTYAMRVLFPGIEDHPVLKEMEVQANVEKSLTLFGQLLTKKHFLLTFIRTLEAQRSFSMRDRGNVASLIMTALQGEMEYATGVLKQLLSDLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLNCVNPEHENAPEVPVKGLNCDTVTQVKEKLLDAVYKGVPYSQRPKAGDMDLEWRQGRMARIILQDEDVTTKIDNDWKRLNTLAHYQVTDGSSVALVPKQTSAYNISNSSTFTKSLSRYESMLRTASSPDSLRSRTPMITPDLESGTKLWHLVKNHDHLDQREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHQIHDSDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHKLGKDSPSNKLLYAKDIPNYKSWVERYYADIAKMPAISDQDMSAYLAEQSRLHLSQFNSMSALHEIYSYIAKYKDEILVALEKDEQARRQRLRSKLEQVVDTMALSS
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
75N-linked_GlycosylationRIYKLSGNLTLLRAH
HEEEECCCEEEEEEE		26.86-
120PhosphorylationNKLLLLDYAANRLLA
CHHHHHHHHHHHHHH		13.9517203969
132PhosphorylationLLACGSASQGICQFL
HHHCCCCCCCHHHHH		30.5428059163
444PhosphorylationAYDYQGRTVVFAGTR
EEECCCCEEEEEECC		28.0420139300
452PhosphorylationVVFAGTRSGRIRKIL
EEEEECCCCHHEEEE		32.0620139300
491PhosphorylationILRDLVLSPNRQYLY
HHHHHCCCCCHHHEE		16.7926824392
658N-linked_GlycosylationSVDFVFYNCSVHQSC
ECEEEEEECCCCHHH		10.50-
670N-linked_GlycosylationQSCLACVNGSFPCHW
HHHHHHHCCCCCCCC		40.03-
699N-linked_GlycosylationAFLEGRVNMSEDCPQ
HHHCCCCCCCCCCCC		27.23-
878PhosphorylationTGPRQGGTRLTITGE
CCCCCCCEEEEEECC		29.3628285833
881PhosphorylationRQGGTRLTITGENLG
CCCCEEEEEECCCCC		17.1328285833
950PhosphorylationSLHYRALSPKRFTFV
CCEEHHCCCCCEEEE		27.6524719451
1002PhosphorylationGGRPCSFSWRNSREI
CCEECCEECCCCCEE		14.6128059163
1041N-linked_GlycosylationSNPEVKYNYTEDPTI
CCCCCCCCCCCCCCE		31.3719349973
1047PhosphorylationYNYTEDPTILRIDPE
CCCCCCCCEEEECCC		44.9926824392
1185N-linked_GlycosylationAPGNSRLNYTVLIGS
CCCCCCCCEEEEECC		29.35-
1210N-linked_GlycosylationQLLCEAPNLTGQHKV
EEEEECCCCCCCCEE		58.23-
1351UbiquitinationEVQANVEKSLTLFGQ
EECCHHHHHHHHHHH		46.6222790023
1354PhosphorylationANVEKSLTLFGQLLT
CHHHHHHHHHHHHHH		27.42-
1361PhosphorylationTLFGQLLTKKHFLLT
HHHHHHHHHHHHHHH		46.79-
1416UbiquitinationLLSDLIEKNLESKNH
HHHHHHHHHHHCCCC		60.8922790023
1433PhosphorylationLLLRRTESVAEKMLT
HHHHCCHHHHHHHHH		26.4719144319
1573PhosphorylationLQDEDVTTKIDNDWK
ECCCCCCCCCCCCHH		26.3326643407
1588PhosphorylationRLNTLAHYQVTDGSS
HHHCCEEEEECCCCC		10.0821454597
1606PhosphorylationVPKQTSAYNISNSST
EECCCCCCCCCCCHH		16.8829514104
1609PhosphorylationQTSAYNISNSSTFTK
CCCCCCCCCCHHHHH		27.3325338131
1611PhosphorylationSAYNISNSSTFTKSL
CCCCCCCCHHHHHHH		24.7829514104
1612PhosphorylationAYNISNSSTFTKSLS
CCCCCCCHHHHHHHH		31.6124719451
1613PhosphorylationYNISNSSTFTKSLSR
CCCCCCHHHHHHHHH		34.8329899451
1615PhosphorylationISNSSTFTKSLSRYE
CCCCHHHHHHHHHHH		21.5829899451
1616UbiquitinationSNSSTFTKSLSRYES
CCCHHHHHHHHHHHH		45.2522790023
1617PhosphorylationNSSTFTKSLSRYESM
CCHHHHHHHHHHHHH		28.6429514104
1619PhosphorylationSTFTKSLSRYESMLR
HHHHHHHHHHHHHHH		39.6522942356
1621PhosphorylationFTKSLSRYESMLRTA
HHHHHHHHHHHHHHC		14.6929514104
1623PhosphorylationKSLSRYESMLRTASS
HHHHHHHHHHHHCCC		17.7422817900
1627PhosphorylationRYESMLRTASSPDSL
HHHHHHHHCCCCHHH		27.2530635358
1629PhosphorylationESMLRTASSPDSLRS
HHHHHHCCCCHHHHC		41.6222817900
1630PhosphorylationSMLRTASSPDSLRSR
HHHHHCCCCHHHHCC		30.2030635358
1633PhosphorylationRTASSPDSLRSRTPM
HHCCCCHHHHCCCCC		29.1230635358
1636PhosphorylationSSPDSLRSRTPMITP
CCCHHHHCCCCCCCC		45.8829514104
1638PhosphorylationPDSLRSRTPMITPDL
CHHHHCCCCCCCCCC		20.6029514104
1642PhosphorylationRSRTPMITPDLESGT
HCCCCCCCCCCHHCC		12.4229899451
1670PhosphorylationQREGDRGSKMVSEIY
HCCCCHHHHHHHHHH		20.6224719451
1677PhosphorylationSKMVSEIYLTRLLAT
HHHHHHHHHHHHHCC		9.6625177544
1793PhosphorylationEHKLGKDSPSNKLLY
CCCCCCCCCCCCEEE		33.4422817900
1795PhosphorylationKLGKDSPSNKLLYAK
CCCCCCCCCCEEEEC		51.0222817900
1814PhosphorylationYKSWVERYYADIAKM
HHHHHHHHHHHHHCC		6.9025168779
1815PhosphorylationKSWVERYYADIAKMP
HHHHHHHHHHHHCCC		12.2025168779
1825PhosphorylationIAKMPAISDQDMSAY
HHCCCCCCCHHHHHH		31.1825168779
1830PhosphorylationAISDQDMSAYLAEQS
CCCCHHHHHHHHHHH		23.2725168779
1832PhosphorylationSDQDMSAYLAEQSRL
CCHHHHHHHHHHHHH		10.1125168779
1837PhosphorylationSAYLAEQSRLHLSQF
HHHHHHHHHHCHHHH		28.4525168779
1842PhosphorylationEQSRLHLSQFNSMSA
HHHHHCHHHHCCHHH		23.21-
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 PLXA1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXA1_MOUSE !!
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 PLXA1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NRP1_MOUSENrp1physical
10520994
NRP2_MOUSENrp2physical
10520994
ANPRA_MOUSENpr1physical
10520994
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLXA1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1041, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-120, AND MASSSPECTROMETRY.

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