CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000350
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Plexin-B2 
Protein Synonyms/Alias
 MM1 
Gene Name
 PLXNB2 
Gene Synonyms/Alias
 KIAA0315 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76TGPALDNKKCTPPIEubiquitination[1]
696GKNLDTVKGSSLHVGubiquitination[1]
1105ENFTGGVKKQVNKLIubiquitination[1, 2]
1121ARGTNLNKAMTLQEAubiquitination[1]
1235EREYEKIKSQLEGLEubiquitination[1]
1423SAGEPLYKLFKAIKHubiquitination[3, 4]
1560GATLILSKVGVSQQPubiquitination[1, 2]
1743SNKLLYAKEISTYKKubiquitination[5]
1817EEDPAAQKMQLAFRLubiquitination[1, 2, 6]
1834IAAALENKVTDL***ubiquitination[1, 2, 7]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional 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) (By similarity). 
Sequence Annotation
 DOMAIN 20 466 Sema.
 DOMAIN 803 893 IPT/TIG 1.
 DOMAIN 895 980 IPT/TIG 2.
 DOMAIN 983 1092 IPT/TIG 3.
 MOD_RES 1244 1244 Phosphoserine (By similarity).
 CARBOHYD 127 127 N-linked (GlcNAc...).
 CARBOHYD 242 242 N-linked (GlcNAc...) (Potential).
 CARBOHYD 391 391 N-linked (GlcNAc...) (Potential).
 CARBOHYD 402 402 N-linked (GlcNAc...) (Potential).
 CARBOHYD 528 528 N-linked (GlcNAc...) (Potential).
 CARBOHYD 733 733 N-linked (GlcNAc...).
 CARBOHYD 759 759 N-linked (GlcNAc...) (Potential).
 CARBOHYD 795 795 N-linked (GlcNAc...) (Potential).
 CARBOHYD 844 844 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1002 1002 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1049 1049 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1068 1068 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1099 1099 N-linked (GlcNAc...) (Potential).
 DISULFID 78 87 By similarity.
 DISULFID 112 120 By similarity.
 DISULFID 250 364 By similarity.
 DISULFID 266 312 By similarity.
 DISULFID 330 351 By similarity.
 DISULFID 469 486 By similarity.
 DISULFID 475 518 By similarity.
 DISULFID 478 495 By similarity.
 DISULFID 489 501 By similarity.
 DISULFID 555 574 By similarity.  
Keyword
 3D-structure; Cell membrane; Complete proteome; Developmental protein; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1838 AA 
Protein Sequence
MALQLWALTL LGLLGAGASL RPRKLDFFRS EKELNHLAVD EASGVVYLGA VNALYQLDAK 60
LQLEQQVATG PALDNKKCTP PIEASQCHEA EMTDNVNQLL LLDPPRKRLV ECGSLFKGIC 120
ALRALSNISL RLFYEDGSGE KSFVASNDEG VATVGLVSST GPGGDRVLFV GKGNGPHDNG 180
IIVSTRLLDR TDSREAFEAY TDHATYKAGY LSTNTQQFVA AFEDGPYVFF VFNQQDKHPA 240
RNRTLLARMC REDPNYYSYL EMDLQCRDPD IHAAAFGTCL AASVAAPGSG RVLYAVFSRD 300
SRSSGGPGAG LCLFPLDKVH AKMEANRNAC YTGTREARDI FYKPFHGDIQ CGGHAPGSSK 360
SFPCGSEHLP YPLGSRDGLR GTAVLQRGGL NLTAVTVAAE NNHTVAFLGT SDGRILKVYL 420
TPDGTSSEYD SILVEINKRV KRDLVLSGDL GSLYAMTQDK VFRLPVQECL SYPTCTQCRD 480
SQDPYCGWCV VEGRCTRKAE CPRAEEASHW LWSRSKSCVA VTSAQPQNMS RRAQGEVQLT 540
VSPLPALSEE DELLCLFGES PPHPARVEGE AVICNSPSSI PVTPPGQDHV AVTIQLLLRR 600
GNIFLTSYQY PFYDCRQAMS LEENLPCISC VSNRWTCQWD LRYHECREAS PNPEDGIVRA 660
HMEDSCPQFL GPSPLVIPMN HETDVNFQGK NLDTVKGSSL HVGSDLLKFM EPVTMQESGT 720
FAFRTPKLSH DANETLPLHL YVKSYGKNID SKLHVTLYNC SFGRSDCSLC RAANPDYRCA 780
WCGGQSRCVY EALCNTTSEC PPPVITRIQP ETGPLGGGIR ITILGSNLGV QAGDIQRISV 840
AGRNCSFQPE RYSVSTRIVC VIEAAETPFT GGVEVDVFGK LGRSPPNVQF TFQQPKPLSV 900
EPQQGPQAGG TTLTIHGTHL DTGSQEDVRV TLNGVPCKVT KFGAQLQCVT GPQATRGQML 960
LEVSYGGSPV PNPGIFFTYR ENPVLRAFEP LRSFASGGRS INVTGQGFSL IQRFAMVVIA 1020
EPLQSWQPPR EAESLQPMTV VGTDYVFHND TKVVFLSPAV PEEPEAYNLT VLIEMDGHRA 1080
LLRTEAGAFE YVPDPTFENF TGGVKKQVNK LIHARGTNLN KAMTLQEAEA FVGAERCTMK 1140
TLTETDLYCE PPEVQPPPKR RQKRDTTHNL PEFIVKFGSR EWVLGRVEYD TRVSDVPLSL 1200
ILPLVIVPMV VVIAVSVYCY WRKSQQAERE YEKIKSQLEG LEESVRDRCK KEFTDLMIEM 1260
EDQTNDVHEA GIPVLDYKTY TDRVFFLPSK DGDKDVMITG KLDIPEPRRP VVEQALYQFS 1320
NLLNSKSFLI NFIHTLENQR EFSARAKVYF ASLLTVALHG KLEYYTDIMH TLFLELLEQY 1380
VVAKNPKLML RRSETVVERM LSNWMSICLY QYLKDSAGEP LYKLFKAIKH QVEKGPVDAV 1440
QKKAKYTLND TGLLGDDVEY APLTVSVIVQ DEGVDAIPVK VLNCDTISQV KEKIIDQVYR 1500
GQPCSCWPRP DSVVLEWRPG STAQILSDLD LTSQREGRWK RVNTLMHYNV RDGATLILSK 1560
VGVSQQPEDS QQDLPGERHA LLEEENRVWH LVRPTDEVDE GKSKRGSVKE KERTKAITEI 1620
YLTRLLSVKG TLQQFVDNFF QSVLAPGHAV PPAVKYFFDF LDEQAEKHNI QDEDTIHIWK 1680
TNSLPLRFWV NILKNPHFIF DVHVHEVVDA SLSVIAQTFM DACTRTEHKL SRDSPSNKLL 1740
YAKEISTYKK MVEDYYKGIR QMVQVSDQDM NTHLAEISRA HTDSLNTLVA LHQLYQYTQK 1800
YYDEIINALE EDPAAQKMQL AFRLQQIAAA LENKVTDL 1838 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005096; F:GTPase activator activity; IEA:InterPro.
 GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
 GO:0007420; P:brain development; ISS:UniProtKB.
 GO:0001843; P:neural tube closure; ISS:UniProtKB.
 GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
 GO:0050772; P:positive regulation of axonogenesis; IEA:Compara.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
 GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
 GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
 GO:0032319; P:regulation of Rho GTPase activity; ISS:UniProtKB. 
Interpro
 IPR013783; Ig-like_fold.
 IPR014756; Ig_E-set.
 IPR002909; IPT_TIG_rcpt.
 IPR003659; Plexin-like.
 IPR016201; Plexin-like_fold.
 IPR013548; Plexin_cytoplasmic_RasGAP_dom.
 IPR002165; Plexin_repeat.
 IPR001936; RasGAP.
 IPR008936; Rho_GTPase_activation_prot.
 IPR001627; Semaphorin/CD100_Ag.
 IPR015943; WD40/YVTN_repeat-like_dom. 
Pfam
 PF08337; Plexin_cytopl
 PF01437; PSI
 PF01403; Sema
 PF01833; TIG 
SMART
 SM00429; IPT
 SM00423; PSI
 SM00630; Sema 
PROSITE
 PS51004; SEMA 
PRINTS