PLXA2_MOUSE - dbPTM
PLXA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXA2_MOUSE
UniProt AC P70207
Protein Name Plexin-A2
Gene Name Plxna2
Organism Mus musculus (Mouse).
Sequence Length 1894
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and 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 MEQRRFYLRAMQADNLSVVLLSVAWLLLARGTTGMPQYSTFHSENRDWTFNHLTVHRRTGAVYVGAINRVYKLTGNLTIQVAHKTGPEEDNKACYPPLIVQPCSEVLTLTNNVNKLLIIDYSENRLLACGSLYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKTGTMYGVIVRSEGEDGKLFIGTAVDGKQDYFPTLSSRKLPRDPESSAMLDYELHSDFVSSLIKIPSDTLALVSHFDIFYIYGFASGGFVYFLTVQPETPDGMAINSAGDLFYTSRIVRLCKDDPKFHSYVSLPFGCTRAGVEYRLLQAAYLAKPGEALAQAFNISSDEDVLFAIFSKGQKQYHHPPDDSALCAFPIRAINLQIKERLQSCYHGEGNLELNWLLGKDVQCTKAPVPIDDNFCGLDINQPLGGSTPVEGLTLYTTSRDRLTSVASYVYNGYSVVFVGTKSGKLKKIRADGPPHGGVQYEMVSVFKDGSPILRDMAFSINQLYLYVMSERQVTRVPVESCEQYTTCGECLSSGDPHCGWCALHNMCSRRDKCQRAWEANRFAASISQCMSLEVHPNSISVSDHSRLLSLVVNDAPNLSEGIACAFGNLTEVEGQVSGSQVICISPGPKDVPVIPLDQDWFGLELQLRSKETGKIFVSTEFKFYNCSAHQLCLSCVNSAFRCHWCKYRNLCTHDPTTCSFQEGRINVSEDCPQLVPTEEILIPVGEVKPITLKARNLPQPQSGQRGYECVLSIQGAVHRVPALRFNSSSVQCQNSSYQYDGMDISNLAVDFAVVWNGNFIIDNPQDLKVHLYKCAAQRESCGLCLKADHKFECGWCSGERRCTLHQHCPSTSSPWLDWSSHNVKCSNPQITEILTVSGPPEGGTRVTIHGVNLGLDFSEIAHHVQVAGVPCTPIPGEYIIAEQIVCEMGHAVIGTTSGPVRLCIGECKPEFMTKSHQQYTFVNPSVLSLSPIRGPESGGTMVTITGHYLGAGSSVAVYLGNQTCEFYGRSMNEIVCVSPPSSNGLGPVPVSVSVDRARVDSSLQFEYIDDPRVQRIEPEWSITSGHTPLTITGFNLDVIQEPRVRVKFNGKESVNVCTVVNTTTLTCLAPSLTSDYRPGLDTVERPDEFGFLFNNVQSLLIYNDTKFIYYPNPTFELLSPTGILDQKPGSPIILKGKNLCPPASGGAKLNYTVMIGETPCTVTVSETQLLCEPPNLTGQHKVMVHVGGMVFSPGSVSVISDSLLTLPAIISIAAGGSLLLIIVIIVLIAYKRKSRENDLTLKRLQMQMDNLESRVALECKEAFAELQTDINELTSDLDRSGIPYLDYRTYAMRVLFPGIEDHPVLRELEVQGNGQQHVEKALKLFAQLINNKVFLLTFIRTLELQRSFSMRDRGNVASLIMTGLQGRLEYATDVLKQLLSDLIDKNLENKNHPKLLLRRTESVAEKMLTNWFAFLLHKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIEYKTLILNCVNPDNENSPEIPVKVLNCDTITQVKEKILDAVYKNVPYSQRPRAVDMDLEWRQGRIARVVLQDEDITTKIEGDWKRLNTLMHYQVSDRSVVALVPKQTSSYNIPASASISRTSISRYDSSFRYTGSPDSLRSRVPMITPDLESGVKVWHLVKNHDHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETLFSTVHRGSALPLAIKYMFDFLDEQADRHSIHDTDVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKGSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKNWVERYYADIAKLPAISDQDMNAYLAEQSRLHATEFNMLSALNEIYSYVSKYSEELIGALEQDEQARRQRLAYKVEHLINAMSIES
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
15N-linked_GlycosylationLRAMQADNLSVVLLS
HHHHHCCCHHHHHHH		36.91-
76N-linked_GlycosylationRVYKLTGNLTIQVAH
EEEEECCCEEEEEEE		28.8620877282
163N-linked_GlycosylationEHYLSSVNKTGTMYG
CEEEECCCCCCCEEE		37.8120877282
293PhosphorylationDDPKFHSYVSLPFGC
CCCCCCCEECCCCCC		5.86-
327N-linked_GlycosylationEALAQAFNISSDEDV
HHHHHHHCCCCCHHH		35.9320877282
542AcetylationNMCSRRDKCQRAWEA
HHHHCHHHHHHHHHH		30.387618933
598N-linked_GlycosylationGIACAFGNLTEVEGQ
HEEEECCCCEEEEEE		37.0220877282
615PhosphorylationGSQVICISPGPKDVP
CCEEEEECCCCCCCC		21.2825159016
648PhosphorylationETGKIFVSTEFKFYN
CCCCEEEECEEEEEE		16.09-
649PhosphorylationTGKIFVSTEFKFYNC
CCCEEEECEEEEEEC		39.89-
668PhosphorylationLCLSCVNSAFRCHWC
HHHHHHHHHHHCCCC		14.37-
696N-linked_GlycosylationSFQEGRINVSEDCPQ
CCCCCCCCCCCCCCC		29.87-
756N-linked_GlycosylationRVPALRFNSSSVQCQ
ECCEEEECCCCEEEC		34.25-
1180N-linked_GlycosylationASGGAKLNYTVMIGE
CCCCCEEEEEEEECC		29.71-
1205N-linked_GlycosylationQLLCEPPNLTGQHKV
EEEECCCCCCCCCEE		62.03-
1264PhosphorylationLIAYKRKSRENDLTL
HHHHHHHCCCCCHHH		49.19-
1272UbiquitinationRENDLTLKRLQMQMD
CCCCHHHHHHHHHHH		45.9127667366
1305PhosphorylationTDINELTSDLDRSGI
HHHHHHHCCCHHCCC		49.12-
1415UbiquitinationLLSDLIDKNLENKNH
HHHHHHHHCCCCCCC		57.3422790023
1422PhosphorylationKNLENKNHPKLLLRR
HCCCCCCCHHHHHHC		23.6019144319
1432PhosphorylationLLLRRTESVAEKMLT
HHHHCCHHHHHHHHH		26.4719144319
1593PhosphorylationHYQVSDRSVVALVPK
EEECCCCEEEEEEEC		26.4025159016
1602PhosphorylationVALVPKQTSSYNIPA
EEEEECCCCCCCCCC		26.2625159016
1603PhosphorylationALVPKQTSSYNIPAS
EEEECCCCCCCCCCC		28.4725159016
1604PhosphorylationLVPKQTSSYNIPASA
EEECCCCCCCCCCCC		26.1125159016
1605PhosphorylationVPKQTSSYNIPASAS
EECCCCCCCCCCCCE		19.5129514104
1610PhosphorylationSSYNIPASASISRTS
CCCCCCCCCEECCCE		19.7329899451
1610O-linked_GlycosylationSSYNIPASASISRTS
CCCCCCCCCEECCCE		19.7355413429
1612PhosphorylationYNIPASASISRTSIS
CCCCCCCEECCCEEE		20.7125159016
1614PhosphorylationIPASASISRTSISRY
CCCCCEECCCEEECC		27.3229899451
1617PhosphorylationSASISRTSISRYDSS
CCEECCCEEECCCCC		19.9125338131
1620PhosphorylationISRTSISRYDSSFRY
ECCCEEECCCCCCCC		37.2919144319
1621PhosphorylationSRTSISRYDSSFRYT
CCCEEECCCCCCCCC		17.2429899451
1623PhosphorylationTSISRYDSSFRYTGS
CEEECCCCCCCCCCC		23.5715572359
1624PhosphorylationSISRYDSSFRYTGSP
EEECCCCCCCCCCCC		15.7319060867
1627PhosphorylationRYDSSFRYTGSPDSL
CCCCCCCCCCCCHHH		17.2829899451
1628PhosphorylationYDSSFRYTGSPDSLR
CCCCCCCCCCCHHHH		27.2529899451
1630PhosphorylationSSFRYTGSPDSLRSR
CCCCCCCCCHHHHHC		20.1025521595
1633PhosphorylationRYTGSPDSLRSRVPM
CCCCCCHHHHHCCCE		29.1221082442
1636PhosphorylationGSPDSLRSRVPMITP
CCCHHHHHCCCEECC		42.8122324799
1642PhosphorylationRSRVPMITPDLESGV
HHCCCEECCCHHHCC		12.4229899451
1670PhosphorylationQKEGDRGSKMVSEIY
CCCCCHHHHHHHHHH		20.62-
1677PhosphorylationSKMVSEIYLTRLLAT
HHHHHHHHHHHHHHC		9.6625177544
1793PhosphorylationEHRLGKDSPSNKLLY
CCCCCCCCCCCCEEE		33.4422817900
1795PhosphorylationRLGKDSPSNKLLYAK
CCCCCCCCCCEEEEC		51.0220415495
1802UbiquitinationSNKLLYAKDIPSYKN
CCCEEEECCCHHHHH		42.51-
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 PLXA2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXA2_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 PLXA2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLXA2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLXA2_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis for semaphorin signalling through the plexinreceptor.";
Nogi T., Yasui N., Mihara E., Matsunaga Y., Noda M., Yamashita N.,Toyofuku T., Uchiyama S., Goshima Y., Kumanogoh A., Takagi J.;
Nature 467:1123-1127(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-561 IN COMPLEX WITHSEMA6A, INTERACTION WITH SEMA6A, SUBUNIT, SUBCELLULAR LOCATION,GLYCOSYLATION AT ASN-76, MUTAGENESIS OF ASP-193; PHE-221 AND ALA-396,AND DISULFIDE BONDS.
"Structural basis of semaphorin-plexin signalling.";
Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H.,Mitchell K.J., Siebold C., Jones E.Y.;
Nature 467:1118-1122(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 35-701 IN COMPLEX WITHSEMA6A, INTERACTION WITH SEMA6A, FUNCTION, SUBCELLULAR LOCATION,GLYCOSYLATION AT ASN-76; ASN-163; ASN-327 AND ASN-598, MUTAGENESIS OFPHE-221 AND ALA-396, AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1432, AND MASSSPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1630 AND SER-1633, ANDMASS SPECTROMETRY.

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