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Protein

Plexin-B2

Gene

PLXNB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Plexin-B2
Alternative name(s):
MM1
Gene namesi
Name:PLXNB2
Synonyms:KIAA0315
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:9104. PLXNB2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 11971178ExtracellularSequence analysisAdd
BLAST
Transmembranei1198 – 121821HelicalSequence analysisAdd
BLAST
Topological domaini1219 – 1838620CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • semaphorin receptor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1161 – 11644RQKR → AQKA: Abolishes cleavage by proprotein convertases. 1 Publication

Organism-specific databases

PharmGKBiPA33430.

Polymorphism and mutation databases

BioMutaiPLXNB2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 18381819Plexin-B2PRO_0000024673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi78 ↔ 87PROSITE-ProRule annotation
Disulfide bondi112 ↔ 120PROSITE-ProRule annotation
Glycosylationi127 – 1271N-linked (GlcNAc...)2 Publications
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi250 ↔ 364PROSITE-ProRule annotation
Disulfide bondi266 ↔ 312PROSITE-ProRule annotation
Disulfide bondi330 ↔ 351PROSITE-ProRule annotation
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi469 ↔ 486PROSITE-ProRule annotation
Disulfide bondi475 ↔ 518PROSITE-ProRule annotation
Disulfide bondi478 ↔ 495PROSITE-ProRule annotation
Disulfide bondi489 ↔ 501PROSITE-ProRule annotation
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi555 ↔ 574PROSITE-ProRule annotation
Glycosylationi733 – 7331N-linked (GlcNAc...)1 Publication
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence analysis
Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence analysis
Glycosylationi844 – 8441N-linked (GlcNAc...)Sequence analysis
Glycosylationi1002 – 10021N-linked (GlcNAc...)Sequence analysis
Glycosylationi1049 – 10491N-linked (GlcNAc...)Sequence analysis
Glycosylationi1068 – 10681N-linked (GlcNAc...)Sequence analysis
Glycosylationi1099 – 10991N-linked (GlcNAc...)Sequence analysis
Modified residuei1236 – 12361PhosphoserineBy similarity
Modified residuei1244 – 12441PhosphoserineBy similarity
Modified residuei1570 – 15701PhosphoserineBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1164 – 11652Cleavage; by proprotein convertases

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO15031.
MaxQBiO15031.
PaxDbiO15031.
PRIDEiO15031.

PTM databases

iPTMnetiO15031.
PhosphoSiteiO15031.
SwissPalmiO15031.

Expressioni

Gene expression databases

BgeeiO15031.
CleanExiHS_PLXNB2.
ExpressionAtlasiO15031. baseline and differential.
GenevisibleiO15031. HS.

Organism-specific databases

HPAiHPA003100.

Interactioni

Subunit structurei

Monomer, and heterodimer with PLXNB1. Interacts with SEMA4C, SEMA4D and SEMA4G (By similarity). Binds MET, ARHGEF11 and ARHGEF12. May also interact with MST1R.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
METP085812EBI-722004,EBI-1039152
MST1RQ049122EBI-722004,EBI-2637518

Protein-protein interaction databases

BioGridi117178. 35 interactions.
IntActiO15031. 12 interactions.
MINTiMINT-5000789.
STRINGi9606.ENSP00000352288.

Structurei

Secondary structure

1
1838
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1462 – 14698Combined sources
Beta strandi1477 – 14826Combined sources
Helixi1487 – 149812Combined sources
Beta strandi1512 – 15176Combined sources
Helixi1545 – 15484Combined sources
Beta strandi1555 – 15606Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E71X-ray2.26A1452-1562[»]
ProteinModelPortaliO15031.
SMRiO15031. Positions 1459-1561.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 466447SemaPROSITE-ProRule annotationAdd
BLAST
Domaini803 – 89391IPT/TIG 1Add
BLAST
Domaini895 – 98086IPT/TIG 2Add
BLAST
Domaini983 – 1092110IPT/TIG 3Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IN3E. Eukaryota.
ENOG411131Q. LUCA.
GeneTreeiENSGT00760000119048.
HOGENOMiHOG000231376.
HOVERGENiHBG053404.
InParanoidiO15031.
KOiK06821.
OMAiEPKQGPQ.
OrthoDBiEOG7Q8CM9.
PhylomeDBiO15031.
TreeFamiTF312962.

Family and domain databases

Gene3Di1.10.506.10. 2 hits.
2.130.10.10. 1 hit.
2.60.40.10. 3 hits.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR031148. Plexin.
IPR016201. Plexin-like_fold.
IPR013548. Plexin_cytoplasmic_RasGAP_dom.
IPR002165. Plexin_repeat.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR001627. Semap_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR22625. PTHR22625. 2 hits.
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. 3 hits.
PROSITEiPS51004. SEMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O15031-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALQLWALTL LGLLGAGASL RPRKLDFFRS EKELNHLAVD EASGVVYLGA
60 70 80 90 100
VNALYQLDAK LQLEQQVATG PALDNKKCTP PIEASQCHEA EMTDNVNQLL
110 120 130 140 150
LLDPPRKRLV ECGSLFKGIC ALRALSNISL RLFYEDGSGE KSFVASNDEG
160 170 180 190 200
VATVGLVSST GPGGDRVLFV GKGNGPHDNG IIVSTRLLDR TDSREAFEAY
210 220 230 240 250
TDHATYKAGY LSTNTQQFVA AFEDGPYVFF VFNQQDKHPA RNRTLLARMC
260 270 280 290 300
REDPNYYSYL EMDLQCRDPD IHAAAFGTCL AASVAAPGSG RVLYAVFSRD
310 320 330 340 350
SRSSGGPGAG LCLFPLDKVH AKMEANRNAC YTGTREARDI FYKPFHGDIQ
360 370 380 390 400
CGGHAPGSSK SFPCGSEHLP YPLGSRDGLR GTAVLQRGGL NLTAVTVAAE
410 420 430 440 450
NNHTVAFLGT SDGRILKVYL TPDGTSSEYD SILVEINKRV KRDLVLSGDL
460 470 480 490 500
GSLYAMTQDK VFRLPVQECL SYPTCTQCRD SQDPYCGWCV VEGRCTRKAE
510 520 530 540 550
CPRAEEASHW LWSRSKSCVA VTSAQPQNMS RRAQGEVQLT VSPLPALSEE
560 570 580 590 600
DELLCLFGES PPHPARVEGE AVICNSPSSI PVTPPGQDHV AVTIQLLLRR
610 620 630 640 650
GNIFLTSYQY PFYDCRQAMS LEENLPCISC VSNRWTCQWD LRYHECREAS
660 670 680 690 700
PNPEDGIVRA HMEDSCPQFL GPSPLVIPMN HETDVNFQGK NLDTVKGSSL
710 720 730 740 750
HVGSDLLKFM EPVTMQESGT FAFRTPKLSH DANETLPLHL YVKSYGKNID
760 770 780 790 800
SKLHVTLYNC SFGRSDCSLC RAANPDYRCA WCGGQSRCVY EALCNTTSEC
810 820 830 840 850
PPPVITRIQP ETGPLGGGIR ITILGSNLGV QAGDIQRISV AGRNCSFQPE
860 870 880 890 900
RYSVSTRIVC VIEAAETPFT GGVEVDVFGK LGRSPPNVQF TFQQPKPLSV
910 920 930 940 950
EPQQGPQAGG TTLTIHGTHL DTGSQEDVRV TLNGVPCKVT KFGAQLQCVT
960 970 980 990 1000
GPQATRGQML LEVSYGGSPV PNPGIFFTYR ENPVLRAFEP LRSFASGGRS
1010 1020 1030 1040 1050
INVTGQGFSL IQRFAMVVIA EPLQSWQPPR EAESLQPMTV VGTDYVFHND
1060 1070 1080 1090 1100
TKVVFLSPAV PEEPEAYNLT VLIEMDGHRA LLRTEAGAFE YVPDPTFENF
1110 1120 1130 1140 1150
TGGVKKQVNK LIHARGTNLN KAMTLQEAEA FVGAERCTMK TLTETDLYCE
1160 1170 1180 1190 1200
PPEVQPPPKR RQKRDTTHNL PEFIVKFGSR EWVLGRVEYD TRVSDVPLSL
1210 1220 1230 1240 1250
ILPLVIVPMV VVIAVSVYCY WRKSQQAERE YEKIKSQLEG LEESVRDRCK
1260 1270 1280 1290 1300
KEFTDLMIEM EDQTNDVHEA GIPVLDYKTY TDRVFFLPSK DGDKDVMITG
1310 1320 1330 1340 1350
KLDIPEPRRP VVEQALYQFS NLLNSKSFLI NFIHTLENQR EFSARAKVYF
1360 1370 1380 1390 1400
ASLLTVALHG KLEYYTDIMH TLFLELLEQY VVAKNPKLML RRSETVVERM
1410 1420 1430 1440 1450
LSNWMSICLY QYLKDSAGEP LYKLFKAIKH QVEKGPVDAV QKKAKYTLND
1460 1470 1480 1490 1500
TGLLGDDVEY APLTVSVIVQ DEGVDAIPVK VLNCDTISQV KEKIIDQVYR
1510 1520 1530 1540 1550
GQPCSCWPRP DSVVLEWRPG STAQILSDLD LTSQREGRWK RVNTLMHYNV
1560 1570 1580 1590 1600
RDGATLILSK VGVSQQPEDS QQDLPGERHA LLEEENRVWH LVRPTDEVDE
1610 1620 1630 1640 1650
GKSKRGSVKE KERTKAITEI YLTRLLSVKG TLQQFVDNFF QSVLAPGHAV
1660 1670 1680 1690 1700
PPAVKYFFDF LDEQAEKHNI QDEDTIHIWK TNSLPLRFWV NILKNPHFIF
1710 1720 1730 1740 1750
DVHVHEVVDA SLSVIAQTFM DACTRTEHKL SRDSPSNKLL YAKEISTYKK
1760 1770 1780 1790 1800
MVEDYYKGIR QMVQVSDQDM NTHLAEISRA HTDSLNTLVA LHQLYQYTQK
1810 1820 1830
YYDEIINALE EDPAAQKMQL AFRLQQIAAA LENKVTDL
Length:1,838
Mass (Da):205,127
Last modified:February 20, 2007 - v3
Checksum:i4AE43003828BC769
GO

Sequence cautioni

The sequence BAA21571.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1535 – 15351R → Q in AAH04542 (PubMed:15489334).Curated
Sequence conflicti1535 – 15351R → Q in AAP35533 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti318 – 3181K → E.Combined sources
Corresponds to variant rs28379706 [ dbSNP | Ensembl ].
VAR_050600
Natural varianti823 – 8231I → V.
Corresponds to variant rs11547731 [ dbSNP | Ensembl ].
VAR_061537

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002313 mRNA. Translation: BAA21571.1. Different initiation.
BX649592, AL022328 Genomic DNA. Translation: CAO03498.1.
BC004542 mRNA. Translation: AAH04542.2.
BT006887 mRNA. Translation: AAP35533.1.
CCDSiCCDS43035.1.
RefSeqiNP_036533.2. NM_012401.3.
XP_005261966.1. XM_005261909.1.
XP_005261967.1. XM_005261910.1.
XP_005261968.1. XM_005261911.3.
XP_006724476.1. XM_006724413.1.
XP_011528985.1. XM_011530683.1.
UniGeneiHs.3989.
Hs.736016.

Genome annotation databases

EnsembliENST00000359337; ENSP00000352288; ENSG00000196576.
ENST00000449103; ENSP00000409171; ENSG00000196576.
GeneIDi23654.
KEGGihsa:23654.
UCSCiuc003bkv.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002313 mRNA. Translation: BAA21571.1. Different initiation.
BX649592, AL022328 Genomic DNA. Translation: CAO03498.1.
BC004542 mRNA. Translation: AAH04542.2.
BT006887 mRNA. Translation: AAP35533.1.
CCDSiCCDS43035.1.
RefSeqiNP_036533.2. NM_012401.3.
XP_005261966.1. XM_005261909.1.
XP_005261967.1. XM_005261910.1.
XP_005261968.1. XM_005261911.3.
XP_006724476.1. XM_006724413.1.
XP_011528985.1. XM_011530683.1.
UniGeneiHs.3989.
Hs.736016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E71X-ray2.26A1452-1562[»]
ProteinModelPortaliO15031.
SMRiO15031. Positions 1459-1561.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117178. 35 interactions.
IntActiO15031. 12 interactions.
MINTiMINT-5000789.
STRINGi9606.ENSP00000352288.

PTM databases

iPTMnetiO15031.
PhosphoSiteiO15031.
SwissPalmiO15031.

Polymorphism and mutation databases

BioMutaiPLXNB2.

Proteomic databases

EPDiO15031.
MaxQBiO15031.
PaxDbiO15031.
PRIDEiO15031.

Protocols and materials databases

DNASUi23654.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359337; ENSP00000352288; ENSG00000196576.
ENST00000449103; ENSP00000409171; ENSG00000196576.
GeneIDi23654.
KEGGihsa:23654.
UCSCiuc003bkv.4. human.

Organism-specific databases

CTDi23654.
GeneCardsiPLXNB2.
HGNCiHGNC:9104. PLXNB2.
HPAiHPA003100.
MIMi604293. gene.
neXtProtiNX_O15031.
PharmGKBiPA33430.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN3E. Eukaryota.
ENOG411131Q. LUCA.
GeneTreeiENSGT00760000119048.
HOGENOMiHOG000231376.
HOVERGENiHBG053404.
InParanoidiO15031.
KOiK06821.
OMAiEPKQGPQ.
OrthoDBiEOG7Q8CM9.
PhylomeDBiO15031.
TreeFamiTF312962.

Miscellaneous databases

ChiTaRSiPLXNB2. human.
GeneWikiiPLXNB2.
GenomeRNAii23654.
NextBioi46489.
PROiO15031.
SOURCEiSearch...

Gene expression databases

BgeeiO15031.
CleanExiHS_PLXNB2.
ExpressionAtlasiO15031. baseline and differential.
GenevisibleiO15031. HS.

Family and domain databases

Gene3Di1.10.506.10. 2 hits.
2.130.10.10. 1 hit.
2.60.40.10. 3 hits.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR031148. Plexin.
IPR016201. Plexin-like_fold.
IPR013548. Plexin_cytoplasmic_RasGAP_dom.
IPR002165. Plexin_repeat.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR001627. Semap_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR22625. PTHR22625. 2 hits.
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. 3 hits.
PROSITEiPS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 1364-1838.
    Tissue: Ovary.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1369-1838.
  5. "Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF."
    Perrot V., Vazquez-Prado J., Gutkind J.S.
    J. Biol. Chem. 277:43115-43120(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF11 AND ARHGEF12, FUNCTION.
  6. Cited for: HETERODIMERIZATION WITH PLXNB1, MUTAGENESIS OF 1161-ARG--ARG-1164, PROTEOLYTIC PROCESSING, FUNCTION, SUBCELLULAR LOCATION.
  7. "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, FUNCTION.
  8. "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-127 AND ASN-733.
    Tissue: Liver.
  9. "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-127.
    Tissue: Leukemic T-cell.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPLXB2_HUMAN
AccessioniPrimary (citable) accession number: O15031
Secondary accession number(s): A6QRH0, Q7KZU3, Q9BSU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 20, 2007
Last modified: March 16, 2016
This is version 136 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 22
    Human chromosome 22: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.