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P70207

- PLXA2_MOUSE

UniProt

P70207 - PLXA2_MOUSE

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Protein

Plexin-A2

Gene

Plxna2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.3 Publications

GO - Molecular functioni

  1. semaphorin receptor activity Source: UniProtKB

GO - Biological processi

  1. cell surface receptor signaling pathway Source: MGI
  2. centrosome localization Source: MGI
  3. cerebellar granule cell precursor tangential migration Source: MGI
  4. limb bud formation Source: BHF-UCL
  5. neural tube development Source: BHF-UCL
  6. pharyngeal system development Source: BHF-UCL
  7. regulation of cell migration Source: UniProtKB
  8. semaphorin-plexin signaling pathway Source: UniProtKB
  9. somitogenesis Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_231928. Other semaphorin interactions.
REACT_244852. CRMPs in Sema3A signaling.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_254306. Sema3A PAK dependent Axon repulsion.

Names & Taxonomyi

Protein namesi
Recommended name:
Plexin-A2
Short name:
Plex 2
Short name:
Plexin-2
Gene namesi
Name:Plxna2
Synonyms:Kiaa0463
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:107684. Plxna2.

Subcellular locationi

Cell membrane 2 Publications; Single-pass type I membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 12371203ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1238 – 125821HelicalSequence AnalysisAdd
BLAST
Topological domaini1259 – 1894636CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: UniProtKB
  2. intracellular Source: InterPro
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi193 – 1931D → K: Abolishes interaction with SEMA6A. 1 Publication
Mutagenesisi221 – 2211F → A or R: Abolishes interaction with SEMA6A. 2 Publications
Mutagenesisi396 – 3961A → E: Abolishes interaction with SEMA6A. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 18941860Plexin-A2PRO_0000232748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi15 – 151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi76 – 761N-linked (GlcNAc...)2 Publications
Disulfide bondi94 ↔ 103
Disulfide bondi129 ↔ 137
Glycosylationi163 – 1631N-linked (GlcNAc...)1 Publication
Disulfide bondi284 ↔ 405
Disulfide bondi300 ↔ 356
Glycosylationi327 – 3271N-linked (GlcNAc...)1 Publication
Disulfide bondi374 ↔ 393
Disulfide bondi511 ↔ 528
Disulfide bondi517 ↔ 559
Disulfide bondi520 ↔ 537
Disulfide bondi531 ↔ 543
Disulfide bondi594 ↔ 613
Glycosylationi598 – 5981N-linked (GlcNAc...)1 Publication
Glycosylationi696 – 6961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1180 – 11801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1205 – 12051N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP70207.
PaxDbiP70207.
PRIDEiP70207.

PTM databases

PhosphoSiteiP70207.

Expressioni

Gene expression databases

BgeeiP70207.
CleanExiMM_PLXNA2.
ExpressionAtlasiP70207. baseline and differential.
GenevestigatoriP70207.

Interactioni

Subunit structurei

Homodimer. Interacts with RND1 (By similarity). Interacts directly with NRP1 and NRP2. The PLXNA2 homodimer interacts with a SEMA6A homodimer, giving rise to a heterotetramer.By similarity4 Publications

Protein-protein interaction databases

BioGridi202262. 1 interaction.
DIPiDIP-32252N.
IntActiP70207. 1 interaction.

Structurei

Secondary structure

1
1894
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 423Combined sources
Beta strandi44 – 485Combined sources
Beta strandi50 – 556Combined sources
Turni57 – 593Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 735Combined sources
Beta strandi79 – 846Combined sources
Beta strandi88 – 903Combined sources
Turni98 – 1003Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi114 – 1207Combined sources
Helixi121 – 1233Combined sources
Beta strandi125 – 1328Combined sources
Turni133 – 1353Combined sources
Beta strandi137 – 1415Combined sources
Turni142 – 1443Combined sources
Beta strandi147 – 1493Combined sources
Helixi155 – 1573Combined sources
Beta strandi165 – 1739Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1867Combined sources
Turni192 – 1943Combined sources
Beta strandi197 – 2037Combined sources
Turni210 – 2134Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi223 – 2264Combined sources
Helixi230 – 2356Combined sources
Beta strandi242 – 2498Combined sources
Beta strandi252 – 2609Combined sources
Beta strandi275 – 28612Combined sources
Beta strandi294 – 3029Combined sources
Beta strandi305 – 31612Combined sources
Helixi320 – 3267Combined sources
Beta strandi334 – 34411Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi353 – 3597Combined sources
Helixi360 – 37516Combined sources
Helixi384 – 3874Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi422 – 4309Combined sources
Beta strandi432 – 4409Combined sources
Beta strandi443 – 4508Combined sources
Beta strandi453 – 46210Combined sources
Turni463 – 4653Combined sources
Beta strandi466 – 4749Combined sources
Beta strandi492 – 4987Combined sources
Beta strandi500 – 5089Combined sources
Helixi511 – 5133Combined sources
Helixi517 – 5204Combined sources
Beta strandi529 – 5313Combined sources
Turni532 – 5354Combined sources
Beta strandi536 – 5383Combined sources
Helixi540 – 5423Combined sources
Turni544 – 5474Combined sources
Beta strandi551 – 5533Combined sources
Helixi557 – 5615Combined sources
Beta strandi577 – 5837Combined sources
Beta strandi592 – 5965Combined sources
Turni597 – 5993Combined sources
Beta strandi600 – 6034Combined sources
Beta strandi605 – 6073Combined sources
Beta strandi610 – 6145Combined sources
Turni618 – 6203Combined sources
Beta strandi630 – 63910Combined sources
Turni640 – 6423Combined sources
Beta strandi645 – 65410Combined sources
Helixi656 – 6583Combined sources
Helixi662 – 6665Combined sources
Beta strandi673 – 6753Combined sources
Turni676 – 6794Combined sources
Beta strandi680 – 6834Combined sources
Helixi685 – 6873Combined sources
Beta strandi688 – 6903Combined sources
Helixi691 – 6933Combined sources
Helixi698 – 7003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AL8X-ray3.60B31-561[»]
3AL9X-ray2.10A/B31-561[»]
3OKTX-ray2.30A35-703[»]
3OKYX-ray2.20A35-703[»]
4GZAX-ray7.00A/B/C/D/E/F33-703[»]
ProteinModelPortaliP70207.
SMRiP70207. Positions 36-702, 809-1040, 1273-1890.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70207.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 508474SemaPROSITE-ProRule annotationAdd
BLAST
Domaini858 – 95194IPT/TIG 1Add
BLAST
Domaini954 – 103784IPT/TIG 2Add
BLAST
Domaini1041 – 113999IPT/TIG 3Add
BLAST
Domaini1143 – 122886IPT/TIG 4Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1261 – 131050Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the plexin family.Curated
Contains 4 IPT/TIG domains.Curated
Contains 1 Sema domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG254546.
GeneTreeiENSGT00760000119048.
HOGENOMiHOG000231377.
HOVERGENiHBG105711.
InParanoidiP70207.
KOiK06820.
OMAiCKDDPKF.
OrthoDBiEOG7Q8CM9.
PhylomeDBiP70207.
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. 3 hits.
PF01403. Sema. 1 hit.
PF01833. TIG. 4 hits.
[Graphical view]
SMARTiSM00429. IPT. 4 hits.
SM00423. PSI. 3 hits.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 2 hits.
SSF48350. SSF48350. 2 hits.
SSF81296. SSF81296. 4 hits.
PROSITEiPS51004. SEMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70207-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQRRFYLRA MQADNLSVVL LSVAWLLLAR GTTGMPQYST FHSENRDWTF
60 70 80 90 100
NHLTVHRRTG AVYVGAINRV YKLTGNLTIQ VAHKTGPEED NKACYPPLIV
110 120 130 140 150
QPCSEVLTLT NNVNKLLIID YSENRLLACG SLYQGVCKLL RLDDLFILVE
160 170 180 190 200
PSHKKEHYLS SVNKTGTMYG VIVRSEGEDG KLFIGTAVDG KQDYFPTLSS
210 220 230 240 250
RKLPRDPESS AMLDYELHSD FVSSLIKIPS DTLALVSHFD IFYIYGFASG
260 270 280 290 300
GFVYFLTVQP ETPDGMAINS AGDLFYTSRI VRLCKDDPKF HSYVSLPFGC
310 320 330 340 350
TRAGVEYRLL QAAYLAKPGE ALAQAFNISS DEDVLFAIFS KGQKQYHHPP
360 370 380 390 400
DDSALCAFPI RAINLQIKER LQSCYHGEGN LELNWLLGKD VQCTKAPVPI
410 420 430 440 450
DDNFCGLDIN QPLGGSTPVE GLTLYTTSRD RLTSVASYVY NGYSVVFVGT
460 470 480 490 500
KSGKLKKIRA DGPPHGGVQY EMVSVFKDGS PILRDMAFSI NQLYLYVMSE
510 520 530 540 550
RQVTRVPVES CEQYTTCGEC LSSGDPHCGW CALHNMCSRR DKCQRAWEAN
560 570 580 590 600
RFAASISQCM SLEVHPNSIS VSDHSRLLSL VVNDAPNLSE GIACAFGNLT
610 620 630 640 650
EVEGQVSGSQ VICISPGPKD VPVIPLDQDW FGLELQLRSK ETGKIFVSTE
660 670 680 690 700
FKFYNCSAHQ LCLSCVNSAF RCHWCKYRNL CTHDPTTCSF QEGRINVSED
710 720 730 740 750
CPQLVPTEEI LIPVGEVKPI TLKARNLPQP QSGQRGYECV LSIQGAVHRV
760 770 780 790 800
PALRFNSSSV QCQNSSYQYD GMDISNLAVD FAVVWNGNFI IDNPQDLKVH
810 820 830 840 850
LYKCAAQRES CGLCLKADHK FECGWCSGER RCTLHQHCPS TSSPWLDWSS
860 870 880 890 900
HNVKCSNPQI TEILTVSGPP EGGTRVTIHG VNLGLDFSEI AHHVQVAGVP
910 920 930 940 950
CTPIPGEYII AEQIVCEMGH AVIGTTSGPV RLCIGECKPE FMTKSHQQYT
960 970 980 990 1000
FVNPSVLSLS PIRGPESGGT MVTITGHYLG AGSSVAVYLG NQTCEFYGRS
1010 1020 1030 1040 1050
MNEIVCVSPP SSNGLGPVPV SVSVDRARVD SSLQFEYIDD PRVQRIEPEW
1060 1070 1080 1090 1100
SITSGHTPLT ITGFNLDVIQ EPRVRVKFNG KESVNVCTVV NTTTLTCLAP
1110 1120 1130 1140 1150
SLTSDYRPGL DTVERPDEFG FLFNNVQSLL IYNDTKFIYY PNPTFELLSP
1160 1170 1180 1190 1200
TGILDQKPGS PIILKGKNLC PPASGGAKLN YTVMIGETPC TVTVSETQLL
1210 1220 1230 1240 1250
CEPPNLTGQH KVMVHVGGMV FSPGSVSVIS DSLLTLPAII SIAAGGSLLL
1260 1270 1280 1290 1300
IIVIIVLIAY KRKSRENDLT LKRLQMQMDN LESRVALECK EAFAELQTDI
1310 1320 1330 1340 1350
NELTSDLDRS GIPYLDYRTY AMRVLFPGIE DHPVLRELEV QGNGQQHVEK
1360 1370 1380 1390 1400
ALKLFAQLIN NKVFLLTFIR TLELQRSFSM RDRGNVASLI MTGLQGRLEY
1410 1420 1430 1440 1450
ATDVLKQLLS DLIDKNLENK NHPKLLLRRT ESVAEKMLTN WFAFLLHKFL
1460 1470 1480 1490 1500
KECAGEPLFM LYCAIKQQME KGPIDAITGE ARYSLSEDKL IRQQIEYKTL
1510 1520 1530 1540 1550
ILNCVNPDNE NSPEIPVKVL NCDTITQVKE KILDAVYKNV PYSQRPRAVD
1560 1570 1580 1590 1600
MDLEWRQGRI ARVVLQDEDI TTKIEGDWKR LNTLMHYQVS DRSVVALVPK
1610 1620 1630 1640 1650
QTSSYNIPAS ASISRTSISR YDSSFRYTGS PDSLRSRVPM ITPDLESGVK
1660 1670 1680 1690 1700
VWHLVKNHDH GDQKEGDRGS KMVSEIYLTR LLATKGTLQK FVDDLFETLF
1710 1720 1730 1740 1750
STVHRGSALP LAIKYMFDFL DEQADRHSIH DTDVRHTWKS NCLPLRFWVN
1760 1770 1780 1790 1800
VIKNPQFVFD IHKGSITDAC LSVVAQTFMD SCSTSEHRLG KDSPSNKLLY
1810 1820 1830 1840 1850
AKDIPSYKNW VERYYADIAK LPAISDQDMN AYLAEQSRLH ATEFNMLSAL
1860 1870 1880 1890
NEIYSYVSKY SEELIGALEQ DEQARRQRLA YKVEHLINAM SIES
Length:1,894
Mass (Da):211,535
Last modified:July 7, 2009 - v2
Checksum:i9F6C34F48BC29CEE
GO

Sequence cautioni

The sequence AAH68155.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA13189.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111A → P in AAH68155. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86949 mRNA. Translation: BAA13189.1. Different initiation.
BC024509 mRNA. Translation: AAH24509.1.
BC056475 mRNA. Translation: AAH56475.1.
BC068155 mRNA. Translation: AAH68155.1. Different initiation.
AK122289 mRNA. Translation: BAC65571.1.
CCDSiCCDS35827.1.
PIRiJC4975.
RefSeqiNP_032908.2. NM_008882.2.
UniGeneiMm.2251.

Genome annotation databases

EnsembliENSMUST00000027952; ENSMUSP00000027952; ENSMUSG00000026640.
GeneIDi18845.
KEGGimmu:18845.
UCSCiuc007een.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86949 mRNA. Translation: BAA13189.1 . Different initiation.
BC024509 mRNA. Translation: AAH24509.1 .
BC056475 mRNA. Translation: AAH56475.1 .
BC068155 mRNA. Translation: AAH68155.1 . Different initiation.
AK122289 mRNA. Translation: BAC65571.1 .
CCDSi CCDS35827.1.
PIRi JC4975.
RefSeqi NP_032908.2. NM_008882.2.
UniGenei Mm.2251.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AL8 X-ray 3.60 B 31-561 [» ]
3AL9 X-ray 2.10 A/B 31-561 [» ]
3OKT X-ray 2.30 A 35-703 [» ]
3OKY X-ray 2.20 A 35-703 [» ]
4GZA X-ray 7.00 A/B/C/D/E/F 33-703 [» ]
ProteinModelPortali P70207.
SMRi P70207. Positions 36-702, 809-1040, 1273-1890.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202262. 1 interaction.
DIPi DIP-32252N.
IntActi P70207. 1 interaction.

PTM databases

PhosphoSitei P70207.

Proteomic databases

MaxQBi P70207.
PaxDbi P70207.
PRIDEi P70207.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027952 ; ENSMUSP00000027952 ; ENSMUSG00000026640 .
GeneIDi 18845.
KEGGi mmu:18845.
UCSCi uc007een.1. mouse.

Organism-specific databases

CTDi 5362.
MGIi MGI:107684. Plxna2.
Rougei Search...

Phylogenomic databases

eggNOGi NOG254546.
GeneTreei ENSGT00760000119048.
HOGENOMi HOG000231377.
HOVERGENi HBG105711.
InParanoidi P70207.
KOi K06820.
OMAi CKDDPKF.
OrthoDBi EOG7Q8CM9.
PhylomeDBi P70207.
TreeFami TF312962.

Enzyme and pathway databases

Reactomei REACT_231928. Other semaphorin interactions.
REACT_244852. CRMPs in Sema3A signaling.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_254306. Sema3A PAK dependent Axon repulsion.

Miscellaneous databases

ChiTaRSi Plxna2. mouse.
EvolutionaryTracei P70207.
NextBioi 295220.
PROi P70207.
SOURCEi Search...

Gene expression databases

Bgeei P70207.
CleanExi MM_PLXNA2.
ExpressionAtlasi P70207. baseline and differential.
Genevestigatori P70207.

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. 3 hits.
PF01403. Sema. 1 hit.
PF01833. TIG. 4 hits.
[Graphical view ]
SMARTi SM00429. IPT. 4 hits.
SM00423. PSI. 3 hits.
SM00630. Sema. 1 hit.
[Graphical view ]
SUPFAMi SSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 2 hits.
SSF48350. SSF48350. 2 hits.
SSF81296. SSF81296. 4 hits.
PROSITEi PS51004. SEMA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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].
    Strain: C57BL/6.
    Tissue: Brain and Colon.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1894.
    Tissue: Brain.
  4. "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors."
    Takahashi T., Fournier A., Nakamura F., Wang L.-H., Murakami Y., Kalb R.G., Fujisawa H., Strittmatter S.M.
    Cell 99:59-69(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NRP1 AND SEMA3A.
  5. "Plexin/neuropilin complexes mediate repulsion by the axonal guidance signal semaphorin 3A."
    Rohm B., Ottemeyer A., Lohrum M., Pueschel A.W.
    Mech. Dev. 93:95-104(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NRP1; NRP2 AND SEMA3A.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 35-701 IN COMPLEX WITH SEMA6A, INTERACTION WITH SEMA6A, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-76; ASN-163; ASN-327 AND ASN-598, MUTAGENESIS OF PHE-221 AND ALA-396, DISULFIDE BONDS.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-561 IN COMPLEX WITH SEMA6A, INTERACTION WITH SEMA6A, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-76, MUTAGENESIS OF ASP-193; PHE-221 AND ALA-396, DISULFIDE BONDS.

Entry informationi

Entry nameiPLXA2_MOUSE
AccessioniPrimary (citable) accession number: P70207
Secondary accession number(s): Q6NVE6
, Q6PHN4, Q80TZ7, Q8R1I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: July 7, 2009
Last modified: November 26, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3