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Protein

Neuroligin-1

Gene

Nlgn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (By similarity).By similarity2 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • neurexin family protein binding Source: UniProtKB
  • protein dimerization activity Source: BHF-UCL
  • receptor activity Source: BHF-UCL

GO - Biological processi

  • AMPA glutamate receptor clustering Source: BHF-UCL
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • cytoskeletal matrix organization at active zone Source: BHF-UCL
  • establishment of protein localization Source: BHF-UCL
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: BHF-UCL
  • long-term synaptic potentiation Source: RGD
  • negative regulation of dendritic spine morphogenesis Source: BHF-UCL
  • nervous system development Source: UniProtKB
  • neurexin clustering involved in presynaptic membrane assembly Source: BHF-UCL
  • neuronal ion channel clustering Source: UniProtKB
  • neuron cell-cell adhesion Source: BHF-UCL
  • neuron projection development Source: Ensembl
  • NMDA glutamate receptor clustering Source: BHF-UCL
  • positive regulation of circadian sleep/wake cycle, wakefulness Source: UniProtKB
  • positive regulation of dendritic spine development Source: BHF-UCL
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • positive regulation of filopodium assembly Source: BHF-UCL
  • positive regulation of intracellular signal transduction Source: BHF-UCL
  • positive regulation of protein localization to synapse Source: RGD
  • positive regulation of ruffle assembly Source: BHF-UCL
  • positive regulation of synapse assembly Source: BHF-UCL
  • positive regulation of synaptic transmission, GABAergic Source: BHF-UCL
  • positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
  • positive regulation of synaptic vesicle clustering Source: Ensembl
  • positive regulation of synaptic vesicle endocytosis Source: BHF-UCL
  • positive regulation of synaptic vesicle exocytosis Source: BHF-UCL
  • postsynaptic density protein 95 clustering Source: BHF-UCL
  • postsynaptic membrane assembly Source: BHF-UCL
  • presynaptic membrane assembly Source: BHF-UCL
  • protein heterotetramerization Source: RGD
  • protein homooligomerization Source: BHF-UCL
  • protein localization to synapse Source: BHF-UCL
  • protein targeting Source: UniProtKB
  • receptor localization to synapse Source: BHF-UCL
  • regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
  • regulation of neuron differentiation Source: UniProtKB
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  • regulation of respiratory gaseous exchange by neurological system process Source: Ensembl
  • rhythmic process Source: UniProtKB-KW
  • synapse assembly Source: UniProtKB
  • synapse organization Source: MGI
  • synaptic vesicle clustering Source: BHF-UCL
  • synaptic vesicle targeting Source: UniProtKB
  • synaptic vesicle transport Source: CACAO
  • terminal button organization Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Biological rhythms, Cell adhesion

Protein family/group databases

ESTHERiratno-1neur. Neuroligin.
MEROPSiS09.994.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroligin-1
Alternative name(s):
Neuroligin I
Gene namesi
Name:Nlgn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi621117. Nlgn1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini46 – 697652ExtracellularSequence analysisAdd
BLAST
Transmembranei698 – 71821HelicalSequence analysisAdd
BLAST
Topological domaini719 – 843125CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: BHF-UCL
  • dendrite Source: BHF-UCL
  • dendritic shaft Source: RGD
  • dendritic spine Source: BHF-UCL
  • excitatory synapse Source: BHF-UCL
  • external side of plasma membrane Source: Ensembl
  • filopodium tip Source: BHF-UCL
  • Golgi apparatus Source: BHF-UCL
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: BHF-UCL
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-KW
  • presynapse Source: GOC
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4545Sequence analysisAdd
BLAST
Chaini46 – 843798Neuroligin-1PRO_0000008642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi109 – 1091N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi117 ↔ 153
Disulfide bondi172 ↔ 181
Glycosylationi303 – 3031N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi342 ↔ 353
Glycosylationi343 – 3431N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi512 ↔ 546
Glycosylationi547 – 5471N-linked (GlcNAc...)1 Publication
Glycosylationi683 – 6831O-linked (GalNAc...)1 Publication
Glycosylationi686 – 6861O-linked (GalNAc...)1 Publication
Modified residuei733 – 7331PhosphoserineBy similarity
Modified residuei782 – 7821PhosphotyrosineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ62765.
PRIDEiQ62765.

PTM databases

UniCarbKBiQ62765.

Expressioni

Tissue specificityi

Expressed in brain, almost exclusively in neurons, and spinal chord. Detected in pancreas islet beta cells.4 Publications

Developmental stagei

Expression is low in embryonic brains (E12-E16) but increases dramatically after birth (postnatal days P0-P3) and reaches a plateau during the period when most synapses are formed (P5-P8).1 Publication

Gene expression databases

ExpressionAtlasiQ62765. baseline.

Interactioni

Subunit structurei

Interacts with NRXN1, NRXN2 and NRXN3. Interacts with NLGN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with GOPC (By similarity). Interacts with AIP1 and PDZRN3.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nrxn1Q633735EBI-7281118,EBI-1780696

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • neurexin family protein binding Source: UniProtKB
  • protein dimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi250532. 12 interactions.
DIPiDIP-44832N.
IntActiQ62765. 4 interactions.
MINTiMINT-1526995.
STRINGi10116.ENSRNOP00000049486.

Structurei

Secondary structure

1
843
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 574Combined sources
Beta strandi60 – 634Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 745Combined sources
Beta strandi77 – 848Combined sources
Helixi91 – 933Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi122 – 1243Combined sources
Turni128 – 1303Combined sources
Helixi133 – 1364Combined sources
Helixi139 – 1457Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi155 – 1617Combined sources
Helixi169 – 1746Combined sources
Helixi179 – 1824Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi202 – 2065Combined sources
Helixi209 – 2113Combined sources
Helixi215 – 2217Combined sources
Beta strandi224 – 2285Combined sources
Helixi233 – 2375Combined sources
Beta strandi241 – 2444Combined sources
Helixi249 – 26416Combined sources
Helixi265 – 2684Combined sources
Beta strandi270 – 28011Combined sources
Helixi282 – 29110Combined sources
Helixi294 – 2963Combined sources
Beta strandi311 – 3166Combined sources
Beta strandi319 – 3213Combined sources
Helixi329 – 34012Combined sources
Helixi347 – 3548Combined sources
Helixi359 – 3635Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi382 – 3854Combined sources
Helixi389 – 3946Combined sources
Beta strandi402 – 4087Combined sources
Turni409 – 4124Combined sources
Helixi413 – 4164Combined sources
Turni417 – 4193Combined sources
Helixi428 – 44316Combined sources
Beta strandi445 – 4484Combined sources
Helixi452 – 4598Combined sources
Helixi463 – 4653Combined sources
Helixi469 – 48416Combined sources
Helixi486 – 49813Combined sources
Beta strandi503 – 5086Combined sources
Beta strandi515 – 5173Combined sources
Turni525 – 5284Combined sources
Helixi529 – 5324Combined sources
Helixi535 – 5384Combined sources
Beta strandi542 – 5443Combined sources
Helixi550 – 56920Combined sources
Beta strandi574 – 5763Combined sources
Helixi582 – 5843Combined sources
Turni589 – 5924Combined sources
Turni600 – 6023Combined sources
Beta strandi604 – 6118Combined sources
Beta strandi613 – 6175Combined sources
Helixi620 – 6278Combined sources
Helixi629 – 6346Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BIWX-ray3.50A/B/C/D46-638[»]
3BIXX-ray1.80A/B/C/D46-638[»]
3VKFX-ray3.30A/B45-638[»]
ProteinModelPortaliQ62765.
SMRiQ62765. Positions 52-631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62765.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ62765.
KOiK07378.
OMAiKFVELIV.
OrthoDBiEOG7RBZ7R.
PhylomeDBiQ62765.
TreeFamiTF326187.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Nlgn.
IPR030022. NLGN1.
[Graphical view]
PANTHERiPTHR11559:SF52. PTHR11559:SF52. 2 hits.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62765-1) [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

        10         20         30         40         50
MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD
60 70 80 90 100
VDPLVTTNFG KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP
110 120 130 140 150
PSPWSDIRNA TQFAPVCPQN IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS
160 170 180 190 200
EDCLYLNIYV PTEDVKRISK ECARKPGKKI CRKGDIRDSG GPKPVMVYIH
210 220 230 240 250
GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG
260 270 280 290 300
LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR
310 320 330 340 350
WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL
360 370 380 390 400
VECLQKKPYK ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN
410 420 430 440 450
YDIMLGVNQG EGLKFVENIV DSDDGVSASD FDFAVSNFVD NLYGYPEGKD
460 470 480 490 500
VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG
510 520 530 540 550
SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK
560 570 580 590 600
NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ
610 620 630 640 650
KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP
660 670 680 690 700
STDITLRPTR KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI
710 720 730 740 750
AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI
760 770 780 790 800
MSLQMKHTDL DHECESIHPH EVVLRTACPP DYTLAMRRSP DDVPLMTPNT
810 820 830 840
ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST TRV
Length:843
Mass (Da):94,294
Last modified:November 1, 1996 - v1
Checksum:i90A18540245B789D
GO
Isoform 2 (identifier: Q62765-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-184: Missing.
     298-306: Missing.

Note: No experimental confirmation available.
Show »
Length:814
Mass (Da):90,995
Checksum:iBA0F19EB618C46F2
GO
Isoform 3 (identifier: Q62765-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     298-306: Missing.

Show »
Length:834
Mass (Da):93,263
Checksum:iC48D369CCB6AEAAA
GO
Isoform 4 (identifier: Q62765-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-184: Missing.

Show »
Length:823
Mass (Da):92,026
Checksum:iB3D07E1FF1AB1FD8
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 18420Missing in isoform 2 and isoform 4. 1 PublicationVSP_007531Add
BLAST
Alternative sequencei298 – 3069Missing in isoform 2 and isoform 3. 1 PublicationVSP_007532

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22952 mRNA. Translation: AAA85720.1.
RefSeqiNP_446320.1. NM_053868.2. [Q62765-1]
UniGeneiRn.10173.

Genome annotation databases

EnsembliENSRNOT00000092660; ENSRNOP00000075793; ENSRNOG00000032576. [Q62765-1]
GeneIDi116647.
KEGGirno:116647.
UCSCiRGD:621117. rat. [Q62765-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22952 mRNA. Translation: AAA85720.1.
RefSeqiNP_446320.1. NM_053868.2. [Q62765-1]
UniGeneiRn.10173.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BIWX-ray3.50A/B/C/D46-638[»]
3BIXX-ray1.80A/B/C/D46-638[»]
3VKFX-ray3.30A/B45-638[»]
ProteinModelPortaliQ62765.
SMRiQ62765. Positions 52-631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250532. 12 interactions.
DIPiDIP-44832N.
IntActiQ62765. 4 interactions.
MINTiMINT-1526995.
STRINGi10116.ENSRNOP00000049486.

Protein family/group databases

ESTHERiratno-1neur. Neuroligin.
MEROPSiS09.994.

PTM databases

UniCarbKBiQ62765.

Proteomic databases

PaxDbiQ62765.
PRIDEiQ62765.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000092660; ENSRNOP00000075793; ENSRNOG00000032576. [Q62765-1]
GeneIDi116647.
KEGGirno:116647.
UCSCiRGD:621117. rat. [Q62765-1]

Organism-specific databases

CTDi22871.
RGDi621117. Nlgn1.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ62765.
KOiK07378.
OMAiKFVELIV.
OrthoDBiEOG7RBZ7R.
PhylomeDBiQ62765.
TreeFamiTF326187.

Miscellaneous databases

EvolutionaryTraceiQ62765.
NextBioi619391.
PROiQ62765.

Gene expression databases

ExpressionAtlasiQ62765. baseline.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Nlgn.
IPR030022. NLGN1.
[Graphical view]
PANTHERiPTHR11559:SF52. PTHR11559:SF52. 2 hits.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Neuroligin 1: a splice site-specific ligand for beta-neurexins."
    Ichtchenko K., Hata Y., Nguyen T., Ullrich B., Missler M., Moomaw C., Suedhof T.C.
    Cell 81:435-443(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, INTERACTION WITH NEUREXIN 1-BETA.
    Tissue: Brain.
  2. "Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules."
    Nguyen T., Suedhof T.C.
    J. Biol. Chem. 272:26032-26039(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEUREXIN 1-BETA, FUNCTION.
  3. "Structures, alternative splicing, and neurexin binding of multiple neuroligins."
    Ichtchenko K., Nguyen T., Suedhof T.C.
    J. Biol. Chem. 271:2676-2682(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: BLOCKAGE OF N-TERMINUS, INTERACTION WITH NEUREXIN 1-BETA; NEUREXIN 2-BETA AND NEUREXIN 3-BETA.
  4. "Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses."
    Song J.-Y., Ichtchenko K., Suedhof T.C., Brose N.
    Proc. Natl. Acad. Sci. U.S.A. 96:1100-1105(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  5. "A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins."
    Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., Toyoda A., Suedhof T.C., Takai Y.
    J. Biol. Chem. 273:21105-21110(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AIP1.
  6. "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory ensheathing glia, a growth-promoting class of macroglia."
    Gilbert M., Smith J., Roskams A.J., Auld V.J.
    Glia 34:151-164(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Structural characterization of recombinant soluble rat neuroligin 1: mapping of secondary structure and glycosylation by mass spectrometry."
    Hoffman R.C., Jennings L.L., Tsigelny I., Comoletti D., Flynn R.E., Suedhof T.C., Taylor P.
    Biochemistry 43:1496-1506(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION.
  8. "Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins."
    Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M.
    Cell 119:1013-1026(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "The complexity of PDZ domain-mediated interactions at glutamatergic synapses: a case study on neuroligin."
    Meyer G., Varoqueaux F., Neeb A., Oschlies M., Brose N.
    Neuropharmacology 47:724-733(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDZRN3.
  10. "Expression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretion."
    Suckow A.T., Comoletti D., Waldrop M.A., Mosedale M., Egodage S., Taylor P., Chessler S.D.
    Endocrinology 149:6006-6017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
  11. Cited for: SUBCELLULAR LOCATION.
  12. "Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4."
    Koehnke J., Jin X., Trbovic N., Katsamba P.S., Brasch J., Ahlsen G., Scheiffele P., Honig B., Palmer A.G. III, Shapiro L.
    Structure 16:410-421(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRXN1.
  13. "Splice form dependence of beta-neurexin/neuroligin binding interactions."
    Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B., Shapiro L., Jin X.
    Neuron 67:61-74(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRXN1.
  14. "Postsynaptic scaffolding molecules modulate the localization of neuroligins."
    Levinson J.N., Li R., Kang R., Moukhles H., El-Husseini A., Bamji S.X.
    Neuroscience 165:782-793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  15. "Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions."
    Arac D., Boucard A.A., Ozkan E., Strop P., Newell E., Sudhof T.C., Brunger A.T.
    Neuron 56:992-1003(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 46-638 IN COMPLEX WITH NRXN1, GLYCOSYLATION AT ASN-109 AND ASN-343, DISULFIDE BONDS.

Entry informationi

Entry nameiNLGN1_RAT
AccessioniPrimary (citable) accession number: Q62765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.