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O43157 (PLXB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plexin-B1
Alternative name(s):
Semaphorin receptor SEP
Gene names
Name:PLXNB1
Synonyms:KIAA0407, PLXN5, SEP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.12 Ref.20 Ref.21 Ref.22

Subunit structure

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. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.2 Ref.10.

Isoform 2: Secreted Ref.2 Ref.10.

Isoform 3: Secreted Ref.2 Ref.10.

Tissue specificity

Highly expressed in fetal kidney, and at slightly lower levels in fetal brain, lung and liver. Ref.4

Post-translational modification

Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D binding. Ref.2 Ref.12

Proteolytic processing favors heterodimerization with PLXNB2 and SEMA4D binding.

Sequence similarities

Belongs to the plexin family.

Contains 3 IPT/TIG domains.

Contains 1 Sema domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cell migration

Non-traceable author statement Ref.2. Source: UniProtKB

intracellular signal transduction

Non-traceable author statement Ref.2. Source: UniProtKB

negative regulation of osteoblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

ossification involved in bone maturation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of Rho GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of cytoskeleton organization

Inferred from direct assay Ref.20. Source: UniProtKB

semaphorin-plexin signaling pathway

Inferred from direct assay Ref.20. Source: UniProtKB

semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

Traceable author statement Ref.4. Source: ProtInc

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from direct assay Ref.20. Source: UniProtKB

intracellular

Inferred from electronic annotation. Source: InterPro

plasma membrane

Traceable author statement. Source: Reactome

semaphorin receptor complex

Inferred from direct assay Ref.20. Source: UniProtKB

   Molecular_functionGTPase activating protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor activity

Traceable author statement Ref.4. Source: ProtInc

semaphorin receptor activity

Inferred from direct assay Ref.20. Source: UniProtKB

semaphorin receptor binding

Traceable author statement Ref.2. Source: UniProtKB

transmembrane signaling receptor activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43157-1)

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.
Isoform 2 (identifier: O43157-2)

Also known as: Isoform R;

The sequence of this isoform differs from the canonical sequence as follows:
     688-870: Missing.
Isoform 3 (identifier: O43157-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 21352116Plexin-B1
PRO_0000024671

Regions

Topological domain20 – 14901471Extracellular Potential
Transmembrane1491 – 151121Helical; Potential
Topological domain1512 – 2135624Cytoplasmic Potential
Domain20 – 479460Sema
Domain1070 – 116091IPT/TIG 1
Domain1162 – 124988IPT/TIG 2
Domain1252 – 1375124IPT/TIG 3
Coiled coil1507 – 153933 Potential
Compositional bias678 – 829152Pro-rich
Compositional bias1302 – 13054Poly-Arg

Sites

Site1305 – 13062Cleavage; by proprotein convertases
Site18151Important for interaction with RAC1 and RND1

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation5431N-linked (GlcNAc...) Potential
Glycosylation11831N-linked (GlcNAc...) Potential
Glycosylation12531N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16
Glycosylation13301N-linked (GlcNAc...) Ref.15
Disulfide bond79 ↔ 88 By similarity
Disulfide bond111 ↔ 119 By similarity
Disulfide bond252 ↔ 377 By similarity
Disulfide bond268 ↔ 322 By similarity
Disulfide bond340 ↔ 364 By similarity
Disulfide bond482 ↔ 499 By similarity
Disulfide bond488 ↔ 533 By similarity
Disulfide bond491 ↔ 508 By similarity
Disulfide bond502 ↔ 514 By similarity
Disulfide bond570 ↔ 588 By similarity

Natural variations

Alternative sequence677 – 72953SPLVS…SPGAS → VMETQQSLRALPPPSSSRPA STTSMTPPGSGSWKRRPWGQ APAPVWRAFRAPR in isoform 3.
VSP_011513
Alternative sequence688 – 870183Missing in isoform 2.
VSP_011514
Alternative sequence730 – 21351406Missing in isoform 3.
VSP_011515
Natural variant3891R → W.
Corresponds to variant rs34050056 [ dbSNP | Ensembl ].
VAR_050598
Natural variant7531S → L.
Corresponds to variant rs35592743 [ dbSNP | Ensembl ].
VAR_050599
Natural variant18911D → V in a breast cancer sample; somatic mutation. Ref.23
VAR_036074

Experimental info

Mutagenesis1391D → K: Strongly reduced interaction with SEMA4D. Ref.20 Ref.21
Mutagenesis1302 – 13054RRRR → AAAA: Abolishes cleavage by proprotein convertases. Ref.10 Ref.20
Mutagenesis18151L → F or P: Abolishes interaction with RAC1 and RND1. Ref.19 Ref.20
Mutagenesis1884 – 18852WH → SS: Loss of cytoskeleton remodeling in response to SEMA4D. Ref.20
Sequence conflict12971S → N in CAB57277. Ref.4
Sequence conflict16251S → T in CAB57277. Ref.4

Secondary structure

............................................................................................................................................................................................ 2135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 31, 2004. Version 3.
Checksum: 12A81B68AF1D340F

FASTA2,135232,298
        10         20         30         40         50         60 
MPALGPALLQ ALWAGWVLTL QPLPPTAFTP NGTYLQHLAR DPTSGTLYLG ATNFLFQLSP 

        70         80         90        100        110        120 
GLQLEATVST GPVLDSRDCL PPVMPDECPQ AQPTNNPNQL LLVSPGALVV CGSVHQGVCE 

       130        140        150        160        170        180 
QRRLGQLEQL LLRPERPGDT QYVAANDPAV STVGLVAQGL AGEPLLFVGR GYTSRGVGGG 

       190        200        210        220        230        240 
IPPITTRALW PPDPQAAFSY EETAKLAVGR LSEYSHHFVS AFARGASAYF LFLRRDLQAQ 

       250        260        270        280        290        300 
SRAFRAYVSR VCLRDQHYYS YVELPLACEG GRYGLIQAAA VATSREVAHG EVLFAAFSSA 

       310        320        330        340        350        360 
APPTVGRPPS AAAGASGASA LCAFPLDEVD RLANRTRDAC YTREGRAEDG TEVAYIEYDV 

       370        380        390        400        410        420 
NSDCAQLPVD TLDAYPCGSD HTPSPMASRV PLEATPILEW PGIQLTAVAV TMEDGHTIAF 

       430        440        450        460        470        480 
LGDSQGQLHR VYLGPGSDGH PYSTQSIQQG SAVSRDLTFD GTFEHLYVMT QSTLLKVPVA 

       490        500        510        520        530        540 
SCAQHLDCAS CLAHRDPYCG WCVLLGRCSR RSECSRGQGP EQWLWSFQPE LGCLQVAAMS 

       550        560        570        580        590        600 
PANISREETR EVFLSVPDLP PLWPGESYSC HFGEHQSPAL LTGSGVMCPS PDPSEAPVLP 

       610        620        630        640        650        660 
RGADYVSVSV ELRFGAVVIA KTSLSFYDCV AVTELRPSAQ CQACVSSRWG CNWCVWQHLC 

       670        680        690        700        710        720 
THKASCDAGP MVASHQSPLV SPDPPARGGP SPSPPTAPKA LATPAPDTLP VEPGAPSTAT 

       730        740        750        760        770        780 
ASDISPGASP SLLSPWGPWA GSGSISSPGS TGSPLHEEPS PPSPQNGPGT AVPAPTDFRP 

       790        800        810        820        830        840 
SATPEDLLAS PLSPSEVAAV PPADPGPEAL HPTVPLDLPP ATVPATTFPG AMGSVKPALD 

       850        860        870        880        890        900 
WLTREGGELP EADEWTGGDA PAFSTSTLLS GDGDSAELEG PPAPLILPSS LDYQYDTPGL 

       910        920        930        940        950        960 
WELEEATLGA SSCPCVESVQ GSTLMPVHVE REIRLLGRNL HLFQDGPGDN ECVMELEGLE 

       970        980        990       1000       1010       1020 
VVVEARVECE PPPDTQCHVT CQQHQLSYEA LQPELRVGLF LRRAGRLRVD SAEGLHVVLY 

      1030       1040       1050       1060       1070       1080 
DCSVGHGDCS RCQTAMPQYG CVWCEGERPR CVTREACGEA EAVATQCPAP LIHSVEPLTG 

      1090       1100       1110       1120       1130       1140 
PVDGGTRVTI RGSNLGQHVQ DVLGMVTVAG VPCAVDAQEY EVSSSLVCIT GASGEEVAGA 

      1150       1160       1170       1180       1190       1200 
TAVEVPGRGR GVSEHDFAYQ DPKVHSIFPA RGPRAGGTRL TLNGSKLLTG RLEDIRVVVG 

      1210       1220       1230       1240       1250       1260 
DQPCHLLPEQ QSEQLRCETS PRPTPATLPV AVWFGATERR LQRGQFKYTL DPNITSAGPT 

      1270       1280       1290       1300       1310       1320 
KSFLSGGREI CVRGQNLDVV QTPRIRVTVV SRMLQPSQGL GRRRRVVPET ACSLGPSCSS 

      1330       1340       1350       1360       1370       1380 
QQFEEPCHVN SSQLITCRTP ALPGLPEDPW VRVEFILDNL VFDFATLNPT PFSYEADPTL 

      1390       1400       1410       1420       1430       1440 
QPLNPEDPTM PFRHKPGSVF SVEGENLDLA MSKEEVVAMI GDGPCVVKTL TRHHLYCEPP 

      1450       1460       1470       1480       1490       1500 
VEQPLPRHHA LREAPDSLPE FTVQMGNLRF SLGHVQYDGE SPGAFPVAAQ VGLGVGTSLL 

      1510       1520       1530       1540       1550       1560 
ALGVIIIVLM YRRKSKQALR DYKKVQIQLE NLESSVRDRC KKEFTDLMTE MTDLTSDLLG 

      1570       1580       1590       1600       1610       1620 
SGIPFLDYKV YAERIFFPGH RESPLHRDLG VPESRRPTVE QGLGQLSNLL NSKLFLTKFI 

      1630       1640       1650       1660       1670       1680 
HTLESQRTFS ARDRAYVASL LTVALHGKLE YFTDILRTLL SDLVAQYVAK NPKLMLRRTE 

      1690       1700       1710       1720       1730       1740 
TVVEKLLTNW MSICLYTFVR DSVGEPLYML FRGIKHQVDK GPVDSVTGKA KYTLNDNRLL 

      1750       1760       1770       1780       1790       1800 
REDVEYRPLT LNALLAVGPG AGEAQGVPVK VLDCDTISQA KEKMLDQLYK GVPLTQRPDP 

      1810       1820       1830       1840       1850       1860 
RTLDVEWRSG VAGHLILSDE DVTSEVQGLW RRLNTLQHYK VPDGATVALV PCLTKHVLRE 

      1870       1880       1890       1900       1910       1920 
NQDYVPGERT PMLEDVDEGG IRPWHLVKPS DEPEPPRPRR GSLRGGERER AKAIPEIYLT 

      1930       1940       1950       1960       1970       1980 
RLLSMKGTLQ KFVDDLFQVI LSTSRPVPLA VKYFFDLLDE QAQQHGISDQ DTIHIWKTNS 

      1990       2000       2010       2020       2030       2040 
LPLRFWINII KNPQFVFDVQ TSDNMDAVLL VIAQTFMDAC TLADHKLGRD SPINKLLYAR 

      2050       2060       2070       2080       2090       2100 
DIPRYKRMVE RYYADIRQTV PASDQEMNSV LAELSWNYSG DLGARVALHE LYKYINKYYD 

      2110       2120       2130 
QIITALEEDG TAQKMQLGYR LQQIAAAVEN KVTDL 

« Hide

Isoform 2 (Isoform R) [UniParc].

Checksum: FCAD0630E128EE9C
Show »

FASTA1,952214,411
Isoform 3 [UniParc].

Checksum: 4AE56E0EDBAE6D75
Show »

FASTA72978,395

References

« Hide 'large scale' references
[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]Erratum
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 104:321-321(2001)
[4]"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.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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).
[7]"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.
[8]"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.
[9]"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.
[10]"Functional regulation of semaphorin receptors by proprotein convertases."
Artigiani S., Barberis D., Fazzari P., Longati P., Angelini P., van de Loo J.-W., Comoglio P.M., Tamagnone L.
J. Biol. Chem. 278:10094-10101(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH PLXNB2, MUTAGENESIS OF 1302-ARG--ARG-1305, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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) [PubMed] [Europe PMC] [Abstract]
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.
[22]"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.
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1891.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001123554.1. NM_001130082.2.
NP_002664.2. NM_002673.5.
UniGeneHs.476209.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO43157.
SMRO43157. Positions 23-533, 1560-2129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111377. 11 interactions.
DIPDIP-36742N.
IntActO43157. 11 interactions.
MINTMINT-245604.
STRING9606.ENSP00000296440.

PTM databases

PhosphoSiteO43157.

Proteomic databases

PaxDbO43157.
PRIDEO43157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296440; ENSP00000296440; ENSG00000164050. [O43157-1]
ENST00000358459; ENSP00000351242; ENSG00000164050. [O43157-2]
ENST00000358536; ENSP00000351338; ENSG00000164050. [O43157-1]
ENST00000449094; ENSP00000395987; ENSG00000164050. [O43157-3]
ENST00000456774; ENSP00000414199; ENSG00000164050. [O43157-2]
GeneID5364.
KEGGhsa:5364.
UCSCuc003csu.2. human. [O43157-2]
uc003csw.2. human. [O43157-1]

Organism-specific databases

CTD5364.
GeneCardsGC03M048420.
HGNCHGNC:9103. PLXNB1.
HPAHPA040586.
MIM601053. gene.
neXtProtNX_O43157.
PharmGKBPA33429.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254546.
HOGENOMHOG000231376.
HOVERGENHBG053404.
InParanoidO43157.
KOK06821.
OMAGVMCPSP.
OrthoDBEOG7Q8CM9.
PhylomeDBO43157.
TreeFamTF312962.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO43157.
BgeeO43157.
CleanExHS_PLXNB1.
GenevestigatorO43157.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.60.40.10. 4 hits.
InterProIPR013783. 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]
PfamPF08337. Plexin_cytopl. 1 hit.
PF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
PF01833. TIG. 3 hits.
[Graphical view]
SMARTSM00429. IPT. 3 hits.
SM00423. PSI. 3 hits.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF48350. SSF48350. 2 hits.
SSF81296. SSF81296. 4 hits.
PROSITEPS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43157.
GeneWikiPLXNB1.
GenomeRNAi5364.
NextBio20792.
PROO43157.
SOURCESearch...

Entry information

Entry namePLXB1_HUMAN
AccessionPrimary (citable) accession number: O43157
Secondary accession number(s): A6H8Y2 expand/collapse secondary AC list , Q6NY20, Q9UIV7, Q9UJ92, Q9UJ93
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM