Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neuroligin-2

Gene

Nlgn2

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

Functioni

Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion (By similarity). Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures.By similarity6 Publications

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: GO_Central
  • cell adhesion molecule binding Source: BHF-UCL
  • neurexin family protein binding Source: BHF-UCL
  • receptor activity Source: GO_Central

GO - Biological processi

  • gephyrin clustering involved in postsynaptic density assembly Source: BHF-UCL
  • inhibitory synapse assembly Source: ParkinsonsUK-UCL
  • jump response Source: BHF-UCL
  • locomotory exploration behavior Source: BHF-UCL
  • modulation of synaptic transmission Source: MGI
  • neuromuscular process controlling balance Source: BHF-UCL
  • neuron cell-cell adhesion Source: BHF-UCL
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • positive regulation of inhibitory postsynaptic potential Source: BHF-UCL
  • positive regulation of insulin secretion Source: MGI
  • positive regulation of protein localization to synapse Source: MGI
  • 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: BHF-UCL
  • postsynaptic density protein 95 clustering Source: BHF-UCL
  • postsynaptic membrane assembly Source: BHF-UCL
  • presynaptic membrane assembly Source: BHF-UCL
  • protein 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 respiratory gaseous exchange by neurological system process Source: MGI
  • sensory perception of pain Source: BHF-UCL
  • social behavior Source: BHF-UCL
  • synapse assembly Source: BHF-UCL
  • synapse organization Source: BHF-UCL
  • terminal button organization Source: BHF-UCL
  • thigmotaxis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Protein family/group databases

ESTHERimouse-2neur. Neuroligin.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroligin-2
Gene namesi
Name:Nlgn2
Synonyms:Kiaa1366
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2681835. Nlgn2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini15 – 678664ExtracellularSequence analysisAdd
BLAST
Transmembranei679 – 69921HelicalSequence analysisAdd
BLAST
Topological domaini700 – 836137CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: BHF-UCL
  • excitatory synapse Source: BHF-UCL
  • inhibitory synapse Source: BHF-UCL
  • integral component of plasma membrane Source: BHF-UCL
  • postsynaptic membrane Source: UniProtKB-SubCell
  • presynaptic membrane Source: UniProtKB-SubCell
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

No obvious phenotype, but mice present subtle behavorial changes. Signaling from inhibitory synapses is impaired. In addition, mice have reduced brain volume. Mice lacking both NLGN1 and NLGN2, or NLGN2 and NLGN3, are viable, but have impaired breathing, drastically reduced reproduction rates and striking deficits in raising their offspring. Mice lacking NLGN1, NLGN2 and NLGN3 are born at the expected Mendelian rate, but die shortly after birth due to respiratory failure. They do not show a significant change in the number of synapses, but synapse function is strongly impaired.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414By similarityAdd
BLAST
Chaini15 – 836822Neuroligin-2PRO_0000041879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi98 – 981N-linked (GlcNAc...)1 Publication
Disulfide bondi106 ↔ 1411 Publication
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi317 ↔ 3281 Publication
Disulfide bondi487 ↔ 5211 Publication
Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence analysis
Modified residuei714 – 7141PhosphoserineCombined sources
Modified residuei719 – 7191PhosphoserineCombined sources
Modified residuei770 – 7701PhosphotyrosineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ69ZK9.
PaxDbiQ69ZK9.
PeptideAtlasiQ69ZK9.
PRIDEiQ69ZK9.

PTM databases

iPTMnetiQ69ZK9.
PhosphoSiteiQ69ZK9.

Expressioni

Tissue specificityi

Brain and arteries. Detected in the retina outer plexiform layer (at protein level). Widely expressed. Detected in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.5 Publications

Gene expression databases

BgeeiQ69ZK9.
CleanExiMM_NLGN2.
ExpressionAtlasiQ69ZK9. baseline and differential.
GenevisibleiQ69ZK9. MM.

Interactioni

Subunit structurei

Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with INADL (By similarity). Interacts with MDGA2 (By similarity). Interacts with GPHN (PubMed:19755106). Interacts with MDGA1 (PubMed:23358245). Found in a complex with MAGI2 and IGSF9B, where it interacts with MAGI2 (via WW 1, WW 2 and PDZ 2 domains) (PubMed:23751499).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPRTO145222EBI-775065,EBI-728180From a different organism.

GO - Molecular functioni

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

Protein-protein interaction databases

DIPiDIP-29702N.
IntActiQ69ZK9. 3 interactions.
STRINGi10090.ENSMUSP00000053097.

Structurei

Secondary structure

1
836
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 635Combined sources
Beta strandi66 – 738Combined sources
Turni81 – 844Combined sources
Beta strandi94 – 974Combined sources
Beta strandi110 – 1123Combined sources
Turni116 – 1183Combined sources
Helixi121 – 1255Combined sources
Helixi127 – 1315Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi143 – 1497Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi177 – 1837Combined sources
Beta strandi186 – 1905Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 2057Combined sources
Beta strandi207 – 2126Combined sources
Helixi217 – 2215Combined sources
Helixi233 – 24816Combined sources
Helixi249 – 2524Combined sources
Beta strandi254 – 26411Combined sources
Helixi266 – 27611Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi286 – 2916Combined sources
Beta strandi294 – 2963Combined sources
Turni297 – 2993Combined sources
Helixi304 – 31512Combined sources
Helixi322 – 3298Combined sources
Helixi334 – 3385Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi357 – 3604Combined sources
Helixi364 – 3707Combined sources
Beta strandi377 – 3837Combined sources
Helixi390 – 3945Combined sources
Beta strandi396 – 4005Combined sources
Helixi403 – 41614Combined sources
Helixi424 – 43512Combined sources
Helixi444 – 45916Combined sources
Helixi461 – 47313Combined sources
Beta strandi478 – 4847Combined sources
Turni500 – 5034Combined sources
Helixi504 – 5085Combined sources
Helixi510 – 5134Combined sources
Beta strandi517 – 5193Combined sources
Helixi525 – 54420Combined sources
Beta strandi549 – 5513Combined sources
Helixi564 – 5663Combined sources
Beta strandi575 – 5773Combined sources
Beta strandi579 – 5868Combined sources
Beta strandi589 – 5924Combined sources
Helixi595 – 6028Combined sources
Turni603 – 6053Combined sources
Helixi606 – 6083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL8X-ray3.30A/B/C/D42-612[»]
ProteinModelPortaliQ69ZK9.
SMRiQ69ZK9. Positions 42-609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ69ZK9.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ69ZK9.
KOiK07378.
OMAiSTEAVEC.
OrthoDBiEOG7RBZ7R.
PhylomeDBiQ69ZK9.
TreeFamiTF326187.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Nlgn.
IPR030023. NLGN2.
[Graphical view]
PANTHERiPTHR11559:SF53. PTHR11559:SF53. 2 hits.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q69ZK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR
60 70 80 90 100
VRGVRRELNN EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT
110 120 130 140 150
TLPPACPQNL HGALPAIMLP VWFTDNLEAA ATYVQNQSED CLYLNLYVPT
160 170 180 190 200
EDGPLTKKRD EATLNPPDTD IRDSGKKPVM LFLHGGSYME GTGNMFDGSV
210 220 230 240 250
LAAYGNVIVV TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ ALRWLSENIA
260 270 280 290 300
HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV
310 320 330 340 350
NYQPLKYTRL LAAKVGCDRE DSTEAVECLR RKSSRELVDQ DVQPARYHIA
360 370 380 390 400
FGPVVDGDVV PDDPEILMQQ GEFLNYDMLI GVNQGEGLKF VEDSAESEDG
410 420 430 440 450
VSASAFDFTV SNFVDNLYGY PEGKDVLRET IKFMYTDWAD RDNGEMRRKT
460 470 480 490 500
LLALFTDHQW VAPAVATAKL HADYQSPVYF YTFYHHCQAE GRPEWADAAH
510 520 530 540 550
GDELPYVFGV PMVGATDLFP CNFSKNDVML SAVVMTYWTN FAKTGDPNQP
560 570 580 590 600
VPQDTKFIHT KPNRFEEVVW SKFNSKEKQY LHIGLKPRVR DNYRANKVAF
610 620 630 640 650
WLELVPHLHN LHTELFTTTT RLPPYATRWP PRTPGPGTSG TRRPPPPATL
660 670 680 690 700
PPESDIDLGP RAYDRFPGDS RDYSTELSVT VAVGASLLFL NILAFAALYY
710 720 730 740 750
KRDRRQELRC RRLSPPGGSG SGVPGGGPLL PTAGRELPPE EELVSLQLKR
760 770 780 790 800
GGGVGADPAE ALRPACPPDY TLALRRAPDD VPLLAPGALT LLPSGLGPPP
810 820 830
PPPPPSLHPF GPFPPPPPTA TSHNNTLPHP HSTTRV
Length:836
Mass (Da):90,989
Last modified:September 13, 2005 - v2
Checksum:i4C03297F4F1A1F14
GO

Sequence cautioni

The sequence BAD32437.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101V → A in BAD32437 (PubMed:15368895).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173159 mRNA. Translation: BAD32437.1. Different initiation.
AL603707 Genomic DNA. Translation: CAI51964.1.
CCDSiCCDS24914.1.
RefSeqiNP_942562.2. NM_198862.2.
XP_006532964.1. XM_006532901.1.
UniGeneiMm.151293.

Genome annotation databases

EnsembliENSMUST00000056484; ENSMUSP00000053097; ENSMUSG00000051790.
ENSMUST00000108634; ENSMUSP00000104274; ENSMUSG00000051790.
GeneIDi216856.
KEGGimmu:216856.
UCSCiuc007jrw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173159 mRNA. Translation: BAD32437.1. Different initiation.
AL603707 Genomic DNA. Translation: CAI51964.1.
CCDSiCCDS24914.1.
RefSeqiNP_942562.2. NM_198862.2.
XP_006532964.1. XM_006532901.1.
UniGeneiMm.151293.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL8X-ray3.30A/B/C/D42-612[»]
ProteinModelPortaliQ69ZK9.
SMRiQ69ZK9. Positions 42-609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29702N.
IntActiQ69ZK9. 3 interactions.
STRINGi10090.ENSMUSP00000053097.

Protein family/group databases

ESTHERimouse-2neur. Neuroligin.

PTM databases

iPTMnetiQ69ZK9.
PhosphoSiteiQ69ZK9.

Proteomic databases

MaxQBiQ69ZK9.
PaxDbiQ69ZK9.
PeptideAtlasiQ69ZK9.
PRIDEiQ69ZK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056484; ENSMUSP00000053097; ENSMUSG00000051790.
ENSMUST00000108634; ENSMUSP00000104274; ENSMUSG00000051790.
GeneIDi216856.
KEGGimmu:216856.
UCSCiuc007jrw.1. mouse.

Organism-specific databases

CTDi57555.
MGIiMGI:2681835. Nlgn2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000231424.
HOVERGENiHBG008839.
InParanoidiQ69ZK9.
KOiK07378.
OMAiSTEAVEC.
OrthoDBiEOG7RBZ7R.
PhylomeDBiQ69ZK9.
TreeFamiTF326187.

Miscellaneous databases

ChiTaRSiNlgn2. mouse.
EvolutionaryTraceiQ69ZK9.
PROiQ69ZK9.
SOURCEiSearch...

Gene expression databases

BgeeiQ69ZK9.
CleanExiMM_NLGN2.
ExpressionAtlasiQ69ZK9. baseline and differential.
GenevisibleiQ69ZK9. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR000460. Nlgn.
IPR030023. NLGN2.
[Graphical view]
PANTHERiPTHR11559:SF53. PTHR11559:SF53. 2 hits.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR01090. NEUROLIGIN.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons."
    Scheiffele P., Fan J., Choih J., Fetter R., Serafini T.
    Cell 101:657-669(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "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.
  5. Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  6. "Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses."
    Budreck E.C., Scheiffele P.
    Eur. J. Neurosci. 26:1738-1748(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLGN3.
  7. Cited for: TISSUE SPECIFICITY.
  8. "Neuroligin 2 controls the maturation of GABAergic synapses and information processing in the retina."
    Hoon M., Bauer G., Fritschy J.M., Moser T., Falkenburger B.H., Varoqueaux F.
    J. Neurosci. 29:8039-8050(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION.
  9. "Neuroligin-2 deletion selectively decreases inhibitory synaptic transmission originating from fast-spiking but not from somatostatin-positive interneurons."
    Gibson J.R., Huber K.M., Sudhof T.C.
    J. Neurosci. 29:13883-13897(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  10. "Neuroligin 2 drives postsynaptic assembly at perisomatic inhibitory synapses through gephyrin and collybistin."
    Poulopoulos A., Aramuni G., Meyer G., Soykan T., Hoon M., Papadopoulos T., Zhang M., Paarmann I., Fuchs C., Harvey K., Jedlicka P., Schwarzacher S.W., Betz H., Harvey R.J., Brose N., Zhang W., Varoqueaux F.
    Neuron 63:628-642(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPHN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "The synaptic proteins neurexins and neuroligins are widely expressed in the vascular system and contribute to its functions."
    Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B., Cera M.R., Mascia L., Bussolino F., Arese M.
    Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714 AND SER-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  13. "Synaptic localization of neuroligin 2 in the rodent retina: comparative study with the dystroglycan-containing complex."
    Lui L., Levinson J.N., Noel G., Handrigan G.R., Richman J.M., El-Husseini A., Moukhles H.
    J. Neurosci. Res. 88:837-849(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  14. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  15. "Interaction between autism-linked MDGAs and neuroligins suppresses inhibitory synapse development."
    Pettem K.L., Yokomaku D., Takahashi H., Ge Y., Craig A.M.
    J. Cell Biol. 200:321-336(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDGA1.
  16. "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to promote inhibitory synapse development."
    Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J., Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S., Craig A.M., Kim E.
    J. Cell Biol. 201:929-944(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH MAGI2 AND IGSF9B.
  17. "Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2."
    Koehnke J., Jin X., Budreck E.C., Posy S., Scheiffele P., Honig B., Shapiro L.
    Proc. Natl. Acad. Sci. U.S.A. 105:1873-1878(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 42-612, DISULFIDE BONDS, GLYCOSYLATION AT ASN-98.

Entry informationi

Entry nameiNLGN2_MOUSE
AccessioniPrimary (citable) accession number: Q69ZK9
Secondary accession number(s): Q5F288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: July 6, 2016
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

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.