PLXB1_HUMAN - dbPTM
PLXB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLXB1_HUMAN
UniProt AC O43157
Protein Name Plexin-B1
Gene Name PLXNB1
Organism Homo sapiens (Human).
Sequence Length 2135
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Secreted.
Isoform 3: Secreted.
Protein Description Receptor for SEMA4D. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration..
Protein Sequence MPALGPALLQALWAGWVLTLQPLPPTAFTPNGTYLQHLARDPTSGTLYLGATNFLFQLSPGLQLEATVSTGPVLDSRDCLPPVMPDECPQAQPTNNPNQLLLVSPGALVVCGSVHQGVCEQRRLGQLEQLLLRPERPGDTQYVAANDPAVSTVGLVAQGLAGEPLLFVGRGYTSRGVGGGIPPITTRALWPPDPQAAFSYEETAKLAVGRLSEYSHHFVSAFARGASAYFLFLRRDLQAQSRAFRAYVSRVCLRDQHYYSYVELPLACEGGRYGLIQAAAVATSREVAHGEVLFAAFSSAAPPTVGRPPSAAAGASGASALCAFPLDEVDRLANRTRDACYTREGRAEDGTEVAYIEYDVNSDCAQLPVDTLDAYPCGSDHTPSPMASRVPLEATPILEWPGIQLTAVAVTMEDGHTIAFLGDSQGQLHRVYLGPGSDGHPYSTQSIQQGSAVSRDLTFDGTFEHLYVMTQSTLLKVPVASCAQHLDCASCLAHRDPYCGWCVLLGRCSRRSECSRGQGPEQWLWSFQPELGCLQVAAMSPANISREETREVFLSVPDLPPLWPGESYSCHFGEHQSPALLTGSGVMCPSPDPSEAPVLPRGADYVSVSVELRFGAVVIAKTSLSFYDCVAVTELRPSAQCQACVSSRWGCNWCVWQHLCTHKASCDAGPMVASHQSPLVSPDPPARGGPSPSPPTAPKALATPAPDTLPVEPGAPSTATASDISPGASPSLLSPWGPWAGSGSISSPGSTGSPLHEEPSPPSPQNGPGTAVPAPTDFRPSATPEDLLASPLSPSEVAAVPPADPGPEALHPTVPLDLPPATVPATTFPGAMGSVKPALDWLTREGGELPEADEWTGGDAPAFSTSTLLSGDGDSAELEGPPAPLILPSSLDYQYDTPGLWELEEATLGASSCPCVESVQGSTLMPVHVEREIRLLGRNLHLFQDGPGDNECVMELEGLEVVVEARVECEPPPDTQCHVTCQQHQLSYEALQPELRVGLFLRRAGRLRVDSAEGLHVVLYDCSVGHGDCSRCQTAMPQYGCVWCEGERPRCVTREACGEAEAVATQCPAPLIHSVEPLTGPVDGGTRVTIRGSNLGQHVQDVLGMVTVAGVPCAVDAQEYEVSSSLVCITGASGEEVAGATAVEVPGRGRGVSEHDFAYQDPKVHSIFPARGPRAGGTRLTLNGSKLLTGRLEDIRVVVGDQPCHLLPEQQSEQLRCETSPRPTPATLPVAVWFGATERRLQRGQFKYTLDPNITSAGPTKSFLSGGREICVRGQNLDVVQTPRIRVTVVSRMLQPSQGLGRRRRVVPETACSLGPSCSSQQFEEPCHVNSSQLITCRTPALPGLPEDPWVRVEFILDNLVFDFATLNPTPFSYEADPTLQPLNPEDPTMPFRHKPGSVFSVEGENLDLAMSKEEVVAMIGDGPCVVKTLTRHHLYCEPPVEQPLPRHHALREAPDSLPEFTVQMGNLRFSLGHVQYDGESPGAFPVAAQVGLGVGTSLLALGVIIIVLMYRRKSKQALRDYKKVQIQLENLESSVRDRCKKEFTDLMTEMTDLTSDLLGSGIPFLDYKVYAERIFFPGHRESPLHRDLGVPESRRPTVEQGLGQLSNLLNSKLFLTKFIHTLESQRTFSARDRAYVASLLTVALHGKLEYFTDILRTLLSDLVAQYVAKNPKLMLRRTETVVEKLLTNWMSICLYTFVRDSVGEPLYMLFRGIKHQVDKGPVDSVTGKAKYTLNDNRLLREDVEYRPLTLNALLAVGPGAGEAQGVPVKVLDCDTISQAKEKMLDQLYKGVPLTQRPDPRTLDVEWRSGVAGHLILSDEDVTSEVQGLWRRLNTLQHYKVPDGATVALVPCLTKHVLRENQDYVPGERTPMLEDVDEGGIRPWHLVKPSDEPEPPRPRRGSLRGGERERAKAIPEIYLTRLLSMKGTLQKFVDDLFQVILSTSRPVPLAVKYFFDLLDEQAQQHGISDQDTIHIWKTNSLPLRFWINIIKNPQFVFDVQTSDNMDAVLLVIAQTFMDACTLADHKLGRDSPINKLLYARDIPRYKRMVERYYADIRQTVPASDQEMNSVLAELSWNYSGDLGARVALHELYKYINKYYDQIITALEEDGTAQKMQLGYRLQQIAAAVENKVTDL
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
19PhosphorylationLWAGWVLTLQPLPPT
HHHCCEEECCCCCCC		17.4624043423
26PhosphorylationTLQPLPPTAFTPNGT
ECCCCCCCCCCCCCC		32.2524043423
29PhosphorylationPLPPTAFTPNGTYLQ
CCCCCCCCCCCCEEH		17.2424043423
31N-linked_GlycosylationPPTAFTPNGTYLQHL
CCCCCCCCCCEEHHH		53.00UniProtKB CARBOHYD
33PhosphorylationTAFTPNGTYLQHLAR
CCCCCCCCEEHHHHC		27.9124043423
34PhosphorylationAFTPNGTYLQHLARD
CCCCCCCEEHHHHCC		13.0324043423
227PhosphorylationSAFARGASAYFLFLR
HHHHHHHHHHHHHHH		26.7330257219
229PhosphorylationFARGASAYFLFLRRD
HHHHHHHHHHHHHHH		9.7930257219
241PhosphorylationRRDLQAQSRAFRAYV
HHHHHHHHHHHHHHH		28.7030257219
334N-linked_GlycosylationDEVDRLANRTRDACY
HHHHHHHHHCCCCCC		50.91UniProtKB CARBOHYD
543N-linked_GlycosylationVAAMSPANISREETR
HHHCCCCCCCHHHHH		35.83UniProtKB CARBOHYD
674PhosphorylationDAGPMVASHQSPLVS
CCCCCCCCCCCCCCC		15.6221712546
677PhosphorylationPMVASHQSPLVSPDP
CCCCCCCCCCCCCCC		18.1221712546
691O-linked_GlycosylationPPARGGPSPSPPTAP
CCCCCCCCCCCCCCC		41.0863768519
691PhosphorylationPPARGGPSPSPPTAP
CCCCCCCCCCCCCCC		41.0821712546
693O-linked_GlycosylationARGGPSPSPPTAPKA
CCCCCCCCCCCCCCC		48.0955832677
693PhosphorylationARGGPSPSPPTAPKA
CCCCCCCCCCCCCCC		48.0923403867
696O-linked_GlycosylationGPSPSPPTAPKALAT
CCCCCCCCCCCCCCC		60.0055832681
696PhosphorylationGPSPSPPTAPKALAT
CCCCCCCCCCCCCCC		60.00-
790O-linked_GlycosylationTPEDLLASPLSPSEV
CHHHHHCCCCCHHHH		26.75OGP
795O-linked_GlycosylationLASPLSPSEVAAVPP
HCCCCCHHHHCCCCC		41.13OGP
834O-linked_GlycosylationTFPGAMGSVKPALDW
CCCCCCCCHHHHHHH		17.55OGP
1107PhosphorylationQDVLGMVTVAGVPCA
HHHHCCCEECCCCEE		8.8526074081
1183N-linked_GlycosylationGGTRLTLNGSKLLTG
CCEEEEECCCCCCCC		47.67UniProtKB CARBOHYD
1253N-linked_GlycosylationFKYTLDPNITSAGPT
CEEECCCCCCCCCCC		50.2419159218
1330N-linked_GlycosylationFEEPCHVNSSQLITC
CCCCCCCCHHHCEEE		16.5719159218
1524UbiquitinationQALRDYKKVQIQLEN
HHHHHHHHHHHHHHC		32.8929967540
1534PhosphorylationIQLENLESSVRDRCK
HHHHCHHHHHHHHHH		36.9824719451
1535PhosphorylationQLENLESSVRDRCKK
HHHCHHHHHHHHHHH		16.2828857561
1545PhosphorylationDRCKKEFTDLMTEMT
HHHHHHHHHHHHHHH		29.3422210691
1549PhosphorylationKEFTDLMTEMTDLTS
HHHHHHHHHHHHHHH		29.8725954137
1552PhosphorylationTDLMTEMTDLTSDLL
HHHHHHHHHHHHHHH		22.9422210691
1556PhosphorylationTEMTDLTSDLLGSGI
HHHHHHHHHHHCCCC		33.2925954137
1568PhosphorylationSGIPFLDYKVYAERI
CCCCCCCEEEEEEEC		12.4222210691
1583PhosphorylationFFPGHRESPLHRDLG
CCCCCCCCCCCCCCC		32.4923532336
1612PhosphorylationQLSNLLNSKLFLTKF
HHHHHHHHHHHHHHH		30.61-
1667PhosphorylationLSDLVAQYVAKNPKL
HHHHHHHHHHHCCCH		7.82-
1708PhosphorylationDSVGEPLYMLFRGIK
CCCCCHHHHHHHHHC		11.5019805522
1727PhosphorylationKGPVDSVTGKAKYTL
CCCCCCCCCEEEEEC		36.6023911959
1732PhosphorylationSVTGKAKYTLNDNRL
CCCCEEEEECCCCCC		22.7119805522
1855UbiquitinationALVPCLTKHVLRENQ
EHHHHHHHHHHHHCC		20.8329967540
1864PhosphorylationVLRENQDYVPGERTP
HHHHCCCCCCCCCCC		9.9728796482
1870PhosphorylationDYVPGERTPMLEDVD
CCCCCCCCCCCCCCC		14.56-
1902PhosphorylationPPRPRRGSLRGGERE
CCCCCCCCCCCCHHH		17.0622817900
1928PhosphorylationRLLSMKGTLQKFVDD
HHHHCCHHHHHHHHH		22.09-
1980PhosphorylationIHIWKTNSLPLRFWI
EEEEECCCCCEEEEE		36.2724719451
2001PhosphorylationQFVFDVQTSDNMDAV
CEEEEECCCCCHHHH		37.5927251275
2002PhosphorylationFVFDVQTSDNMDAVL
EEEEECCCCCHHHHH		15.1927251275
2051MethylationRYKRMVERYYADIRQ
HHHHHHHHHHHHHHH		20.5324383357
2131UbiquitinationIAAAVENKVTDL---
HHHHHHHHCCCC---		32.7629967540
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
1708YPhosphorylationKinaseERBB2P04626
GPS
1732YPhosphorylationKinaseERBB2P04626
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLXB1_HUMAN !!
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 PLXB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RND1_HUMANRND1physical
12730235
RND2_HUMANRND2physical
12730235
RND3_HUMANRND3physical
12730235
ARHGB_HUMANARHGEF11physical
12730235
ARHGB_HUMANARHGEF11physical
12123608
ARHGB_HUMANARHGEF11physical
12220504
ARHGC_HUMANARHGEF12physical
12220504
RHOA_HUMANRHOAphysical
19805522
AKT1_HUMANAKT1physical
19805522
GRB2_HUMANGRB2physical
19805522
PLCG1_HUMANPLCG1physical
19805522
PLCG2_HUMANPLCG2physical
19805522
SMPX_HUMANSMPXphysical
28514442
HBB_HUMANHBBphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLXB1_HUMAN

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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-1253, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253 AND ASN-1330, ANDMASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253, AND MASSSPECTROMETRY.

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