PLXB2_MOUSE - dbPTM
PLXB2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXB2_MOUSE
UniProt AC B2RXS4
Protein Name Plexin-B2
Gene Name Plxnb2
Organism Mus musculus (Mouse).
Sequence Length 1842
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling. Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development. Regulates the migration of cerebellar granule cells in the developing brain. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May modulate the activity of RAC1 and CDC42. Down-regulates macrophage migration in wound-healing assays (in vitro)..
Protein Sequence MALPLWALTFLGLTGLGLSLRSRKPESFRSETELNHLAVDEVTGVVYVGAVNALYQLSADLHVQQHVVTGPFMDNKKCTPPIEASQCHEAVLTDNFNQLLLLDPPGKRLVECGSLFKGICALRAMSNISVRLFYEDGSGEKSFVASNDERVATVGLVTSTRPDGERVLFVGKGNGPHDNGIIVSTRLLDRAEGREAFEAYSDHTTFKAGYLSTNTQQFVAAFEDDFYVFFVFNHQDKHPAKNRTLLARMCKDDPSYYSYVEMDLQCQDPSDPQDSAFGTCLAASVATSGAGRALYAVFSRDGRSTGGPGAGLCVFPLDKVREKIEANRNACYTGAREAGRTIFYKPFHGEIQCGGHLIGASESFPCGSEHLPYPLGSRDGLVATAVLHRGGLNLTAVTVTAENDHTVAFLGTSDGRILKVYLAPDGTSAEYGSIPVDINKKIKQDLALSGNLSSLYAMTQDKVFRLPVQECLSYVTCAQCRDSQDPYCGWCVIEGRCTRKSECSRAEETGHWLWSREKSCVAITDAFPQNMSRRAQGEVRLSVSPLPTLTEDDELLCLFGDSPPHPARVEDDTVICNSPSSIPSTPPGQDHVDVSIQLLLKSGSVFLTSHQYPFYDCREAMSLVENLPCISCASNRWTCQWDLQYYECREASPNPEEGIIRAHMEDNCPQFLAPDPLVIPMNHETEVTFQGKNLETVKVSSLYVGSELLNFEETVTMHESDTFSFRTPKLSHDGNETLPLHLYVKSFGKNIDSKLQVTLYNCSFGRSDCSLCLAADPAYRCVWCRGQNRCVYEALCSNVTSECPPPVITRIQPETGPLGGGILVTIHGSNLGVKADDVKKITVAGQNCAFEPRGYSVSTRIVCAIEASEMPFTGGIEVDVNGKLGHSPPHVQFTYQQPQPLSVEPRQGPQAGGTTLTINGTHLDTGSKEDVRVTLNDVPCEVTKFGAQLQCVTGQQLAPGQVTLEIYYGGSRVPSPGISFTYCENPMIRAFEPLRSFVSGGRSINVTGQGFSLIQKFAMVVIAEPLRSWRRRRREAGALERVTVEGMEYVFYNDTKVVFLSPAVPEEPEAYNLTVLIRMDGHCAPLRTEAGVFEYVADPTFENFTGGVKKQVNKLIHARGTNLNKAMTLEEAEAFVGAERCIMKTLTETDLYCEPPEVQPPPKRRQKRDTAHNLPEFIVKFGSREWVLGRVEYDTRASDVPLSLILPLVMVPMVFIIVVSIYCYWRKSQQAEREYEKIKSQLEGLEESVRDRCKKEFTDLMIEMEDQTNDVHEAGIPTLDYKTYTDRVFFLPSKDGDKDVMITGKLDIPESRRPIVEQALYQFSNLLNSKSFLINFIHTLENQREFSARAKVYFASLLTVALHGKLEYYTDIMRTLFLELMEQYVVAKNPKLMLRRSETVVERMLSNWMSICLYQYLKDSAGEPLYKLFKAIKHQVEKGPVDAVQKKAKYTLNDTGLLGDDVEYAPLTVSVIVQDEGIDAIPVKVLNCDTISQVKEKIIDQVYRTQPCSCWPKPDSVVLEWRPGSTAQILSDLDLTSQREGRWKRINTLMHYNVRDGATLILSKVGVSQQPEDSQQDLPGERHALLEEENRVWHLVRPTDEVDEGKSKRGSMKEKERTKAITEIYLTRLLSVKGTLQQFVDNFFQSVLAPGHAVPPAVKYFFDFLDEQAEKHDIRDEDTIHIWKTNSLPLRFWVNILKNPHFIFDVHVHEVVDASLSVIAQTFMDACTRTEHKLSRDSPSNKLLYAKEISTYKKMVEDYYKGIRQMVQVSDQDMNTHLAEISRAHTDSLNTLVALHQLYQYTQKYYDEIINALEEDPAAQKMQLAFRLQQIAAALENKVTDL
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
127N-linked_GlycosylationCALRAMSNISVRLFY
HHHHHHCCEEEEEEE		19.92-
242N-linked_GlycosylationQDKHPAKNRTLLARM
CCCCCCCCCHHHHHH		44.25-
393N-linked_GlycosylationVLHRGGLNLTAVTVT
EEECCCCCEEEEEEE		38.3219349973
421PhosphorylationDGRILKVYLAPDGTS
CCCEEEEEECCCCCC		8.78-
427PhosphorylationVYLAPDGTSAEYGSI
EEECCCCCCCCCCCC		31.95-
428PhosphorylationYLAPDGTSAEYGSIP
EECCCCCCCCCCCCC		25.32-
431PhosphorylationPDGTSAEYGSIPVDI
CCCCCCCCCCCCCCC		18.85-
451N-linked_GlycosylationQDLALSGNLSSLYAM
HHHHHCCCHHHHHHH		33.11-
617S-palmitoylationHQYPFYDCREAMSLV
CCCCCCCHHHHHHHH		2.6328680068
798N-linked_GlycosylationVYEALCSNVTSECPP
HHHHHHCCCCCCCCC		39.84-
815PhosphorylationITRIQPETGPLGGGI
EEEECCCCCCCCCEE		51.2720047950
825PhosphorylationLGGGILVTIHGSNLG
CCCEEEEEECCCCCC		12.1020047950
829PhosphorylationILVTIHGSNLGVKAD
EEEEECCCCCCCCHH		18.0820047950
917PhosphorylationQAGGTTLTINGTHLD
CCCCCEEEECCEECC		15.42-
919N-linked_GlycosylationGGTTLTINGTHLDTG
CCCEEEECCEECCCC		44.04-
921PhosphorylationTTLTINGTHLDTGSK
CEEEECCEECCCCCC		18.12-
925PhosphorylationINGTHLDTGSKEDVR
ECCEECCCCCCCCEE		50.11-
927PhosphorylationGTHLDTGSKEDVRVT
CEECCCCCCCCEEEE		34.66-
1053N-linked_GlycosylationGMEYVFYNDTKVVFL
CEEEEEECCCEEEEE		38.72-
1072N-linked_GlycosylationPEEPEAYNLTVLIRM
CCCCCCCCEEEEEEE		35.96-
1239UbiquitinationEREYEKIKSQLEGLE
HHHHHHHHHHHHHHH		43.1222790023
1240PhosphorylationREYEKIKSQLEGLEE
HHHHHHHHHHHHHHH		43.3919144319
1248PhosphorylationQLEGLEESVRDRCKK
HHHHHHHHHHHHHHH		17.0530352176
1305UbiquitinationKDVMITGKLDIPESR
CCEEEEEECCCCHHH		34.0422790023
1331PhosphorylationSNLLNSKSFLINFIH
HHHHCCHHHHHHHHH		25.7122817900
1339PhosphorylationFLINFIHTLENQREF
HHHHHHHHHHHHHCH		30.8321183079
1509PhosphorylationVYRTQPCSCWPKPDS
HHHCCCCCCCCCCCC		26.3728418008
1525PhosphorylationVLEWRPGSTAQILSD
EEEECCCCHHHHHHH		24.2128066266
1526PhosphorylationLEWRPGSTAQILSDL
EEECCCCHHHHHHHC		28.6128066266
1568PhosphorylationILSKVGVSQQPEDSQ
EEEECCCCCCCCCCC		19.7128066266
1574PhosphorylationVSQQPEDSQQDLPGE
CCCCCCCCCCCCCCC		28.2526824392
1622PhosphorylationKERTKAITEIYLTRL
HHHHHHHHHHHHHHH		22.6128285833
1627PhosphorylationAITEIYLTRLLSVKG
HHHHHHHHHHHHCCH		11.4228285833
1738PhosphorylationEHKLSRDSPSNKLLY
CCCCCCCCCCCCEEE		29.1720531401
1745PhosphorylationSPSNKLLYAKEISTY
CCCCCEEEHHHHHHH		26.5120531401
1747UbiquitinationSNKLLYAKEISTYKK
CCCEEEHHHHHHHHH		41.8622790023
1750PhosphorylationLLYAKEISTYKKMVE
EEEHHHHHHHHHHHH		27.1221454597
1751PhosphorylationLYAKEISTYKKMVED
EEHHHHHHHHHHHHH		45.0521454597
1752PhosphorylationYAKEISTYKKMVEDY
EHHHHHHHHHHHHHH		11.21-
1821UbiquitinationEEDPAAQKMQLAFRL
HHCHHHHHHHHHHHH		24.7222790023
1838UbiquitinationIAAALENKVTDL---
HHHHHHHHCCCC---		36.8222790023
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 PLXB2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXB2_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 PLXB2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLXB2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLXB2_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-393, AND MASSSPECTROMETRY.
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-1248, AND MASSSPECTROMETRY.

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