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O43157

- PLXB1_HUMAN

UniProt

O43157 - PLXB1_HUMAN

Protein

Plexin-B1

Gene

PLXNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (31 Aug 2004)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1305 – 13062Cleavage; by proprotein convertases
    Sitei1815 – 18151Important for interaction with RAC1 and RND1

    GO - Molecular functioni

    1. GTPase activating protein binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. receptor activity Source: ProtInc
    4. semaphorin receptor activity Source: UniProtKB
    5. semaphorin receptor binding Source: UniProtKB
    6. transmembrane signaling receptor activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell migration Source: UniProtKB
    3. intracellular signal transduction Source: UniProtKB
    4. negative regulation of cell adhesion Source: UniProtKB
    5. negative regulation of osteoblast proliferation Source: BHF-UCL
    6. neuron projection morphogenesis Source: UniProtKB
    7. ossification involved in bone maturation Source: BHF-UCL
    8. positive regulation of axonogenesis Source: Ensembl
    9. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    10. positive regulation of Rho GTPase activity Source: UniProtKB
    11. regulation of cell shape Source: UniProtKB
    12. regulation of cytoskeleton organization Source: UniProtKB
    13. semaphorin-plexin signaling pathway Source: UniProtKB
    14. semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis Source: BHF-UCL
    15. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_18407. G alpha (12/13) signalling events.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plexin-B1
    Alternative name(s):
    Semaphorin receptor SEP
    Gene namesi
    Name:PLXNB1
    Synonyms:KIAA0407, PLXN5, SEP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9103. PLXNB1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: UniProtKB
    3. intracellular Source: InterPro
    4. plasma membrane Source: Reactome
    5. semaphorin receptor complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391D → K: Strongly reduced interaction with SEMA4D. 1 Publication
    Mutagenesisi1302 – 13054RRRR → AAAA: Abolishes cleavage by proprotein convertases.
    Mutagenesisi1815 – 18151L → F or P: Abolishes interaction with RAC1 and RND1. 1 Publication
    Mutagenesisi1884 – 18852WH → SS: Loss of cytoskeleton remodeling in response to SEMA4D.

    Organism-specific databases

    PharmGKBiPA33429.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 21352116Plexin-B1PRO_0000024671Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi79 ↔ 88PROSITE-ProRule annotation
    Disulfide bondi111 ↔ 119PROSITE-ProRule annotation
    Disulfide bondi252 ↔ 377PROSITE-ProRule annotation
    Disulfide bondi268 ↔ 322PROSITE-ProRule annotation
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi340 ↔ 364PROSITE-ProRule annotation
    Disulfide bondi482 ↔ 499PROSITE-ProRule annotation
    Disulfide bondi488 ↔ 533PROSITE-ProRule annotation
    Disulfide bondi491 ↔ 508PROSITE-ProRule annotation
    Disulfide bondi502 ↔ 514PROSITE-ProRule annotation
    Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi570 ↔ 588PROSITE-ProRule annotation
    Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1253 – 12531N-linked (GlcNAc...)3 Publications
    Glycosylationi1330 – 13301N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D binding.2 Publications
    Proteolytic processing favors heterodimerization with PLXNB2 and SEMA4D binding.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO43157.
    PaxDbiO43157.
    PRIDEiO43157.

    PTM databases

    PhosphoSiteiO43157.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal kidney, and at slightly lower levels in fetal brain, lung and liver.1 Publication

    Gene expression databases

    ArrayExpressiO43157.
    BgeeiO43157.
    CleanExiHS_PLXNB1.
    GenevestigatoriO43157.

    Organism-specific databases

    HPAiHPA040586.

    Interactioni

    Subunit structurei

    Monomer, and heterodimer with PLXNB2 after proteolytic processing. Binds RAC1 that has been activated by GTP binding. Interaction with SEMA4D promotes binding of cytoplasmic ligands. Binds PLXNA1 By similarity. Interacts with ARHGEF11, ARHGEF12, ERBB2, MET, MST1R, RRAS, RHOD, RND1, NRP1 and NRP2.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    METP085817EBI-1111488,EBI-1039152
    MST1RQ049123EBI-1111488,EBI-2637518
    RND1Q927302EBI-1111488,EBI-448618

    Protein-protein interaction databases

    BioGridi111377. 11 interactions.
    DIPiDIP-36742N.
    IntActiO43157. 11 interactions.
    MINTiMINT-245604.
    STRINGi9606.ENSP00000296440.

    Structurei

    Secondary structure

    1
    2135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 283
    Beta strandi35 – 406
    Turni42 – 443
    Beta strandi47 – 515
    Beta strandi54 – 585
    Beta strandi64 – 696
    Beta strandi73 – 753
    Turni85 – 873
    Beta strandi92 – 943
    Beta strandi98 – 1036
    Beta strandi105 – 11410
    Helixi115 – 1173
    Beta strandi119 – 1235
    Beta strandi126 – 1327
    Helixi139 – 1413
    Beta strandi152 – 1587
    Beta strandi164 – 1707
    Beta strandi183 – 1908
    Helixi194 – 1963
    Beta strandi202 – 2054
    Helixi211 – 2144
    Beta strandi217 – 2248
    Beta strandi227 – 2359
    Beta strandi244 – 25411
    Beta strandi262 – 2687
    Turni269 – 2724
    Beta strandi275 – 2839
    Beta strandi291 – 2988
    Helixi314 – 3163
    Beta strandi319 – 3257
    Helixi326 – 34217
    Turni344 – 3463
    Beta strandi348 – 3503
    Beta strandi354 – 3563
    Helixi371 – 3744
    Beta strandi385 – 3906
    Beta strandi397 – 4004
    Beta strandi405 – 4139
    Beta strandi416 – 4238
    Beta strandi426 – 4327
    Beta strandi434 – 4363
    Beta strandi442 – 4487
    Beta strandi463 – 4697
    Beta strandi474 – 4796
    Helixi482 – 4843
    Helixi488 – 4936
    Beta strandi500 – 5023
    Turni503 – 5064
    Beta strandi507 – 5093
    Helixi511 – 5133
    Beta strandi523 – 5253
    Helixi1568 – 15769
    Beta strandi1580 – 15823
    Helixi1593 – 15953
    Helixi1596 – 161015
    Helixi1613 – 162513
    Beta strandi1627 – 16293
    Helixi1631 – 164414
    Turni1645 – 16473
    Helixi1649 – 166820
    Helixi1672 – 16743
    Beta strandi1677 – 16793
    Helixi1682 – 170120
    Helixi1704 – 171916
    Turni1725 – 17273
    Beta strandi1730 – 17323
    Beta strandi1736 – 17394
    Beta strandi1748 – 17558
    Beta strandi1757 – 17593
    Beta strandi1767 – 17726
    Helixi1777 – 178812
    Turni1789 – 17913
    Helixi1794 – 17963
    Helixi1800 – 18023
    Beta strandi1803 – 18086
    Beta strandi1810 – 18123
    Beta strandi1814 – 18174
    Beta strandi1819 – 18213
    Beta strandi1825 – 18273
    Beta strandi1830 – 18323
    Helixi1836 – 18394
    Beta strandi1846 – 18516
    Beta strandi1882 – 18876
    Helixi1916 – 194126
    Beta strandi1943 – 19453
    Helixi1949 – 196416
    Helixi1970 – 198011
    Turni1981 – 19855
    Helixi1986 – 19916
    Helixi1993 – 19953
    Helixi2003 – 202018
    Helixi2033 – 20375
    Turni2038 – 20414
    Helixi2042 – 205817
    Helixi2064 – 207613
    Helixi2084 – 209714
    Helixi2099 – 21079
    Helixi2110 – 21145
    Helixi2117 – 212812
    Beta strandi2132 – 21343

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JPHNMR-A1743-1862[»]
    2OS6NMR-B2128-2135[»]
    2R2OX-ray2.00A/B1743-1862[»]
    2REXX-ray2.30A/C1743-1862[»]
    3HM6X-ray2.40X1511-2135[»]
    3OL2X-ray2.99B20-535[»]
    3SU8X-ray3.20X1533-2135[»]
    3SUAX-ray4.39D/E/F1511-2135[»]
    ProteinModelPortaliO43157.
    SMRiO43157. Positions 23-533, 1560-2129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43157.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 14901471ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1512 – 2135624CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1491 – 151121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 479460SemaPROSITE-ProRule annotationAdd
    BLAST
    Domaini1070 – 116091IPT/TIG 1Add
    BLAST
    Domaini1162 – 124988IPT/TIG 2Add
    BLAST
    Domaini1252 – 1375124IPT/TIG 3Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1507 – 153933Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi678 – 829152Pro-richAdd
    BLAST
    Compositional biasi1302 – 13054Poly-Arg

    Sequence similaritiesi

    Belongs to the plexin family.Curated
    Contains 3 IPT/TIG domains.Curated
    Contains 1 Sema domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG254546.
    HOGENOMiHOG000231376.
    HOVERGENiHBG053404.
    InParanoidiO43157.
    KOiK06821.
    OMAiGVMCPSP.
    OrthoDBiEOG7Q8CM9.
    PhylomeDBiO43157.
    TreeFamiTF312962.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    2.60.40.10. 4 hits.
    InterProiIPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR016201. Plexin-like_fold.
    IPR013548. Plexin_cytoplasmic_RasGAP_dom.
    IPR002165. Plexin_repeat.
    IPR008936. Rho_GTPase_activation_prot.
    IPR001627. Semap_dom.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF08337. Plexin_cytopl. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view]
    SMARTiSM00429. IPT. 3 hits.
    SM00423. PSI. 3 hits.
    SM00630. Sema. 1 hit.
    [Graphical view]
    SUPFAMiSSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF48350. SSF48350. 2 hits.
    SSF81296. SSF81296. 4 hits.
    PROSITEiPS51004. SEMA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43157-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPALGPALLQ ALWAGWVLTL QPLPPTAFTP NGTYLQHLAR DPTSGTLYLG     50
    ATNFLFQLSP GLQLEATVST GPVLDSRDCL PPVMPDECPQ AQPTNNPNQL 100
    LLVSPGALVV CGSVHQGVCE QRRLGQLEQL LLRPERPGDT QYVAANDPAV 150
    STVGLVAQGL AGEPLLFVGR GYTSRGVGGG IPPITTRALW PPDPQAAFSY 200
    EETAKLAVGR LSEYSHHFVS AFARGASAYF LFLRRDLQAQ SRAFRAYVSR 250
    VCLRDQHYYS YVELPLACEG GRYGLIQAAA VATSREVAHG EVLFAAFSSA 300
    APPTVGRPPS AAAGASGASA LCAFPLDEVD RLANRTRDAC YTREGRAEDG 350
    TEVAYIEYDV NSDCAQLPVD TLDAYPCGSD HTPSPMASRV PLEATPILEW 400
    PGIQLTAVAV TMEDGHTIAF LGDSQGQLHR VYLGPGSDGH PYSTQSIQQG 450
    SAVSRDLTFD GTFEHLYVMT QSTLLKVPVA SCAQHLDCAS CLAHRDPYCG 500
    WCVLLGRCSR RSECSRGQGP EQWLWSFQPE LGCLQVAAMS PANISREETR 550
    EVFLSVPDLP PLWPGESYSC HFGEHQSPAL LTGSGVMCPS PDPSEAPVLP 600
    RGADYVSVSV ELRFGAVVIA KTSLSFYDCV AVTELRPSAQ CQACVSSRWG 650
    CNWCVWQHLC THKASCDAGP MVASHQSPLV SPDPPARGGP SPSPPTAPKA 700
    LATPAPDTLP VEPGAPSTAT ASDISPGASP SLLSPWGPWA GSGSISSPGS 750
    TGSPLHEEPS PPSPQNGPGT AVPAPTDFRP SATPEDLLAS PLSPSEVAAV 800
    PPADPGPEAL HPTVPLDLPP ATVPATTFPG AMGSVKPALD WLTREGGELP 850
    EADEWTGGDA PAFSTSTLLS GDGDSAELEG PPAPLILPSS LDYQYDTPGL 900
    WELEEATLGA SSCPCVESVQ GSTLMPVHVE REIRLLGRNL HLFQDGPGDN 950
    ECVMELEGLE VVVEARVECE PPPDTQCHVT CQQHQLSYEA LQPELRVGLF 1000
    LRRAGRLRVD SAEGLHVVLY DCSVGHGDCS RCQTAMPQYG CVWCEGERPR 1050
    CVTREACGEA EAVATQCPAP LIHSVEPLTG PVDGGTRVTI RGSNLGQHVQ 1100
    DVLGMVTVAG VPCAVDAQEY EVSSSLVCIT GASGEEVAGA TAVEVPGRGR 1150
    GVSEHDFAYQ DPKVHSIFPA RGPRAGGTRL TLNGSKLLTG RLEDIRVVVG 1200
    DQPCHLLPEQ QSEQLRCETS PRPTPATLPV AVWFGATERR LQRGQFKYTL 1250
    DPNITSAGPT KSFLSGGREI CVRGQNLDVV QTPRIRVTVV SRMLQPSQGL 1300
    GRRRRVVPET ACSLGPSCSS QQFEEPCHVN SSQLITCRTP ALPGLPEDPW 1350
    VRVEFILDNL VFDFATLNPT PFSYEADPTL QPLNPEDPTM PFRHKPGSVF 1400
    SVEGENLDLA MSKEEVVAMI GDGPCVVKTL TRHHLYCEPP VEQPLPRHHA 1450
    LREAPDSLPE FTVQMGNLRF SLGHVQYDGE SPGAFPVAAQ VGLGVGTSLL 1500
    ALGVIIIVLM YRRKSKQALR DYKKVQIQLE NLESSVRDRC KKEFTDLMTE 1550
    MTDLTSDLLG SGIPFLDYKV YAERIFFPGH RESPLHRDLG VPESRRPTVE 1600
    QGLGQLSNLL NSKLFLTKFI HTLESQRTFS ARDRAYVASL LTVALHGKLE 1650
    YFTDILRTLL SDLVAQYVAK NPKLMLRRTE TVVEKLLTNW MSICLYTFVR 1700
    DSVGEPLYML FRGIKHQVDK GPVDSVTGKA KYTLNDNRLL REDVEYRPLT 1750
    LNALLAVGPG AGEAQGVPVK VLDCDTISQA KEKMLDQLYK GVPLTQRPDP 1800
    RTLDVEWRSG VAGHLILSDE DVTSEVQGLW RRLNTLQHYK VPDGATVALV 1850
    PCLTKHVLRE NQDYVPGERT PMLEDVDEGG IRPWHLVKPS DEPEPPRPRR 1900
    GSLRGGERER AKAIPEIYLT RLLSMKGTLQ KFVDDLFQVI LSTSRPVPLA 1950
    VKYFFDLLDE QAQQHGISDQ DTIHIWKTNS LPLRFWINII KNPQFVFDVQ 2000
    TSDNMDAVLL VIAQTFMDAC TLADHKLGRD SPINKLLYAR DIPRYKRMVE 2050
    RYYADIRQTV PASDQEMNSV LAELSWNYSG DLGARVALHE LYKYINKYYD 2100
    QIITALEEDG TAQKMQLGYR LQQIAAAVEN KVTDL 2135
    Length:2,135
    Mass (Da):232,298
    Last modified:August 31, 2004 - v3
    Checksum:i12A81B68AF1D340F
    GO
    Isoform 2 (identifier: O43157-2) [UniParc]FASTAAdd to Basket

    Also known as: Isoform R

    The sequence of this isoform differs from the canonical sequence as follows:
         688-870: Missing.

    Show »
    Length:1,952
    Mass (Da):214,411
    Checksum:iFCAD0630E128EE9C
    GO
    Isoform 3 (identifier: O43157-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         677-729: SPLVSPDPPA...TASDISPGAS → VMETQQSLRA...PVWRAFRAPR
         730-2135: Missing.

    Show »
    Length:729
    Mass (Da):78,395
    Checksum:i4AE56E0EDBAE6D75
    GO

    Sequence cautioni

    The sequence BAA23703.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1297 – 12971S → N in CAB57277. (PubMed:8570614)Curated
    Sequence conflicti1625 – 16251S → T in CAB57277. (PubMed:8570614)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti389 – 3891R → W.
    Corresponds to variant rs34050056 [ dbSNP | Ensembl ].
    VAR_050598
    Natural varianti753 – 7531S → L.
    Corresponds to variant rs35592743 [ dbSNP | Ensembl ].
    VAR_050599
    Natural varianti1891 – 18911D → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036074

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei677 – 72953SPLVS…SPGAS → VMETQQSLRALPPPSSSRPA STTSMTPPGSGSWKRRPWGQ APAPVWRAFRAPR in isoform 3. 1 PublicationVSP_011513Add
    BLAST
    Alternative sequencei688 – 870183Missing in isoform 2. 1 PublicationVSP_011514Add
    BLAST
    Alternative sequencei730 – 21351406Missing in isoform 3. 1 PublicationVSP_011515Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007867 mRNA. Translation: BAA23703.2. Different initiation.
    AJ011414 mRNA. Translation: CAB56221.1.
    AJ011415 mRNA. Translation: CAB56222.1.
    X87904 mRNA. Translation: CAB57277.1.
    CH471055 Genomic DNA. Translation: EAW64865.1.
    BC146793 mRNA. Translation: AAI46794.1.
    CCDSiCCDS2765.1. [O43157-1]
    RefSeqiNP_001123554.1. NM_001130082.2. [O43157-1]
    NP_002664.2. NM_002673.5. [O43157-1]
    UniGeneiHs.476209.

    Genome annotation databases

    EnsembliENST00000296440; ENSP00000296440; ENSG00000164050. [O43157-1]
    ENST00000358536; ENSP00000351338; ENSG00000164050. [O43157-1]
    ENST00000449094; ENSP00000395987; ENSG00000164050. [O43157-3]
    ENST00000456774; ENSP00000414199; ENSG00000164050. [O43157-2]
    GeneIDi5364.
    KEGGihsa:5364.
    UCSCiuc003csu.2. human. [O43157-2]
    uc003csw.2. human. [O43157-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007867 mRNA. Translation: BAA23703.2 . Different initiation.
    AJ011414 mRNA. Translation: CAB56221.1 .
    AJ011415 mRNA. Translation: CAB56222.1 .
    X87904 mRNA. Translation: CAB57277.1 .
    CH471055 Genomic DNA. Translation: EAW64865.1 .
    BC146793 mRNA. Translation: AAI46794.1 .
    CCDSi CCDS2765.1. [O43157-1 ]
    RefSeqi NP_001123554.1. NM_001130082.2. [O43157-1 ]
    NP_002664.2. NM_002673.5. [O43157-1 ]
    UniGenei Hs.476209.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JPH NMR - A 1743-1862 [» ]
    2OS6 NMR - B 2128-2135 [» ]
    2R2O X-ray 2.00 A/B 1743-1862 [» ]
    2REX X-ray 2.30 A/C 1743-1862 [» ]
    3HM6 X-ray 2.40 X 1511-2135 [» ]
    3OL2 X-ray 2.99 B 20-535 [» ]
    3SU8 X-ray 3.20 X 1533-2135 [» ]
    3SUA X-ray 4.39 D/E/F 1511-2135 [» ]
    ProteinModelPortali O43157.
    SMRi O43157. Positions 23-533, 1560-2129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111377. 11 interactions.
    DIPi DIP-36742N.
    IntActi O43157. 11 interactions.
    MINTi MINT-245604.
    STRINGi 9606.ENSP00000296440.

    PTM databases

    PhosphoSitei O43157.

    Proteomic databases

    MaxQBi O43157.
    PaxDbi O43157.
    PRIDEi O43157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296440 ; ENSP00000296440 ; ENSG00000164050 . [O43157-1 ]
    ENST00000358536 ; ENSP00000351338 ; ENSG00000164050 . [O43157-1 ]
    ENST00000449094 ; ENSP00000395987 ; ENSG00000164050 . [O43157-3 ]
    ENST00000456774 ; ENSP00000414199 ; ENSG00000164050 . [O43157-2 ]
    GeneIDi 5364.
    KEGGi hsa:5364.
    UCSCi uc003csu.2. human. [O43157-2 ]
    uc003csw.2. human. [O43157-1 ]

    Organism-specific databases

    CTDi 5364.
    GeneCardsi GC03M048420.
    HGNCi HGNC:9103. PLXNB1.
    HPAi HPA040586.
    MIMi 601053. gene.
    neXtProti NX_O43157.
    PharmGKBi PA33429.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG254546.
    HOGENOMi HOG000231376.
    HOVERGENi HBG053404.
    InParanoidi O43157.
    KOi K06821.
    OMAi GVMCPSP.
    OrthoDBi EOG7Q8CM9.
    PhylomeDBi O43157.
    TreeFami TF312962.

    Enzyme and pathway databases

    Reactomei REACT_18407. G alpha (12/13) signalling events.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Miscellaneous databases

    EvolutionaryTracei O43157.
    GeneWikii PLXNB1.
    GenomeRNAii 5364.
    NextBioi 20792.
    PROi O43157.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43157.
    Bgeei O43157.
    CleanExi HS_PLXNB1.
    Genevestigatori O43157.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    2.60.40.10. 4 hits.
    InterProi IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002909. IPT.
    IPR016201. Plexin-like_fold.
    IPR013548. Plexin_cytoplasmic_RasGAP_dom.
    IPR002165. Plexin_repeat.
    IPR008936. Rho_GTPase_activation_prot.
    IPR001627. Semap_dom.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF08337. Plexin_cytopl. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    PF01833. TIG. 3 hits.
    [Graphical view ]
    SMARTi SM00429. IPT. 3 hits.
    SM00423. PSI. 3 hits.
    SM00630. Sema. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    SSF48350. SSF48350. 2 hits.
    SSF81296. SSF81296. 4 hits.
    PROSITEi PS51004. SEMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
      Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Plexins are a large family of receptors for transmembrane, secreted and GPI-anchored semaphorins in vertebrates."
      Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L., Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., Tessier-Lavigne M., Comoglio P.M.
      Cell 99:71-80(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SEMA4D; NRP1 AND NRP2.
      Tissue: Gastric carcinoma.
    3. "A family of transmembrane proteins with homology to the MET-hepatocyte growth factor receptor."
      Maestrini E., Tamagnone L., Longati P., Cremona O., Gulisano M., Bione S., Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.
      Proc. Natl. Acad. Sci. U.S.A. 93:674-678(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner."
      Vikis H.G., Li W., He Z., Guan K.-L.
      Proc. Natl. Acad. Sci. U.S.A. 97:12457-12462(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAC1.
    7. "The semaphorin 4D receptor controls invasive growth by coupling with Met."
      Giordano S., Corso S., Conrotto P., Artigiani S., Gilestro G., Barberis D., Tamagnone L., Comoglio P.M.
      Nat. Cell Biol. 4:720-724(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEMA4D AND MET, FUNCTION.
    8. "The semaphorin receptor plexin-B1 signals through a direct interaction with the Rho-specific nucleotide exchange factor, LARG."
      Aurandt J., Vikis H.G., Gutkind J.S., Ahn N., Guan K.-L.
      Proc. Natl. Acad. Sci. U.S.A. 99:12085-12090(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF11 AND ARHGEF12, FUNCTION.
    9. Cited for: HETERODIMERIZATION WITH PLXNB2, MUTAGENESIS OF 1302-ARG--ARG-1305, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
    10. "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells."
      Oinuma I., Katoh H., Harada A., Negishi M.
      J. Biol. Chem. 278:25671-25677(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RND1.
    11. "Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor tyrosine kinase ErbB-2."
      Swiercz J.M., Kuner R., Offermanns S.
      J. Cell Biol. 165:869-880(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB2, PHOSPHORYLATION, FUNCTION.
    12. "Interplay between scatter factor receptors and B plexins controls invasive growth."
      Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.
      Oncogene 23:5131-5137(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MET AND MST1R.
    13. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253.
      Tissue: Plasma.
    14. "Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253 AND ASN-1330.
      Tissue: Liver.
    15. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1253.
      Tissue: Leukemic T-cell.
    16. "Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain."
      Tong Y., Chugha P., Hota P.K., Alviani R.S., Li M., Tempel W., Shen L., Park H.W., Buck M.
      J. Biol. Chem. 282:37215-37224(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1743-1862, SUBUNIT, INTERACTION WITH RAC1; RND1 AND RHOD.
    17. "Conformational change upon ligand binding and dynamics of the PDZ domain from leukemia-associated Rho guanine nucleotide exchange factor."
      Liu J., Zhang J., Yang Y., Huang H., Shen W., Hu Q., Wang X., Wu J., Shi Y.
      Protein Sci. 17:1003-1014(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2128-2135 IN COMPLEX WITH ARHGEF12, SUBUNIT.
    18. "Insights into oncogenic mutations of plexin-B1 based on the solution structure of the Rho GTPase binding domain."
      Tong Y., Hota P.K., Hamaneh M.B., Buck M.
      Structure 16:246-258(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1743-1862, MUTAGENESIS OF LEU-1815, SUBUNIT, INTERACTION WITH RAC1 AND RND1.
    19. "Structure and function of the intracellular region of the plexin-B1 transmembrane receptor."
      Tong Y., Hota P.K., Penachioni J.Y., Hamaneh M.B., Kim S., Alviani R.S., Shen L., He H., Tempel W., Tamagnone L., Park H.W., Buck M.
      J. Biol. Chem. 284:35962-35972(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1511-2135 IN COMPLEX WITH RND1, FUNCTION, SUBUNIT, INTERACTION WITH SEMA4D; RND1; RAC1 AND RRAS, MUTAGENESIS OF 1884-TRP-HIS-1885.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 20-535 IN COMPLEX WITH SEMA4D, FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-139, GLYCOSYLATION AT ASN-334, DISULFIDE BONDS.
    21. "A dual binding mode for RhoGTPases in plexin signalling."
      Bell C.H., Aricescu A.R., Jones E.Y., Siebold C.
      PLoS Biol. 9:E1001134-E1001134(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1533-2135 IN COMPLEX WITH RAC1, SUBUNIT, FUNCTION.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1891.

    Entry informationi

    Entry nameiPLXB1_HUMAN
    AccessioniPrimary (citable) accession number: O43157
    Secondary accession number(s): A6H8Y2
    , Q6NY20, Q9UIV7, Q9UJ92, Q9UJ93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: August 31, 2004
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3