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Q9ULB1 (NRX1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurexin-1
Alternative name(s):
Neurexin I-alpha
Neurexin-1-alpha
Gene names
Name:NRXN1
Synonyms:KIAA0578
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca2+-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca2+-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their calcium-dependent interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom By similarity.

Subunit structure

Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer interacts with one NRXN1 dimer. Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1, NLGN2, NLGN3, NLGN4X and NLGN4Y; these interactions are calcium-dependent. Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 By similarity. Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 By similarity. Alpha-type isoforms (neurexin-1-alpha) interact (via laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-latrotoxin from spider venom. The cytoplasmic C-terminal region binds to CASK, CASKIN1 and APBA1. Interacts with SYT13 and SYTL1 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein Probable. Cell junctionsynapse Probable. Note: Localized on the pre-synaptic membrane By similarity.

Tissue specificity

Brain. Ref.3

Post-translational modification

N-glycosylated By similarity.

O-glycosylated By similarity.

Sequence similarities

Belongs to the neurexin family.

Contains 3 EGF-like domains.

Contains 6 laminin G-like domains.

Sequence caution

The sequence BAA25504.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult behavior

Inferred from mutant phenotype PubMed 19896112. Source: BHF-UCL

axon guidance

Traceable author statement PubMed 1621094. Source: ProtInc

extracellular matrix organization

Traceable author statement. Source: Reactome

gephyrin clustering

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

learning

Inferred from mutant phenotype PubMed 19896112. Source: BHF-UCL

neuroligin clustering

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

neuromuscular process controlling balance

Inferred from sequence or structural similarity PubMed 19822762. Source: BHF-UCL

neuron cell-cell adhesion

Traceable author statement PubMed 18923512. Source: BHF-UCL

neurotransmitter secretion

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

positive regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity PubMed 19822762. Source: BHF-UCL

positive regulation of synapse assembly

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

positive regulation of synapse maturation

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

positive regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity PubMed 19822762. Source: BHF-UCL

postsynaptic density protein 95 clustering

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

postsynaptic membrane assembly

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

prepulse inhibition

Inferred from electronic annotation. Source: Ensembl

regulation of grooming behavior

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from mutant phenotype PubMed 18057082PubMed 19896112. Source: BHF-UCL

synapse assembly

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

synaptic transmission

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

vocal learning

Inferred from mutant phenotype PubMed 19896112. Source: BHF-UCL

vocalization behavior

Inferred from mutant phenotype PubMed 18057082PubMed 19896112. Source: BHF-UCL

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 21424692. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement PubMed 1621094. Source: ProtInc

plasma membrane

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

presynaptic membrane

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

   Molecular_functionacetylcholine receptor binding

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

calcium channel regulator activity

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

calcium ion binding

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

cell adhesion molecule binding

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

neuroligin family protein binding

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

protein binding

Inferred from physical interaction PubMed 11152476. Source: UniProtKB

receptor activity

Traceable author statement PubMed 1621094. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: A number of isoforms are produced by alternative promoter usage including the alpha-type and beta-type isoforms which differ in their N-terminus. Additional isoforms may be produced by alternative splicing.
Isoform 1a (identifier: Q9ULB1-1)

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 2a (identifier: Q9ULB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     379-386: Missing.
     1240-1240: G → GNNDNERLAIARQRIPYRLGRVVDEWLLDKG
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 3a (identifier: Q9ULB1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     258-258: E → EIKFGLQCVLPVLLHDNDQGKYCCINTAKPLTEK
     386-386: M → MVNKLHCS
     1239-1239: A → AGNNDNERLAIARQRIPYRLGRVVDEWLLDK
Note: Produced by alternative splicing.
Isoform 1b (identifier: P58400-1)

The sequence of this isoform can be found in the external entry P58400.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 By similarity
Chain31 – 14771447Neurexin-1
PRO_0000019490

Regions

Topological domain31 – 14011371Extracellular Potential
Transmembrane1402 – 142221Helical; Potential
Topological domain1423 – 147755Cytoplasmic Potential
Domain31 – 217187Laminin G-like 1
Domain213 – 25644EGF-like 1
Domain283 – 473191Laminin G-like 2
Domain480 – 672193Laminin G-like 3
Domain676 – 71338EGF-like 2
Domain718 – 891174Laminin G-like 4
Domain905 – 1080176Laminin G-like 5
Domain1083 – 112038EGF-like 3
Domain1126 – 1294169Laminin G-like 6
Compositional bias1324 – 13274Poly-Thr
Compositional bias1409 – 14124Poly-Ala

Sites

Metal binding3291Calcium By similarity
Metal binding3291Calcium 1 By similarity
Metal binding3461Calcium 1; via carbonyl oxygen By similarity
Metal binding4071Calcium 1; via carbonyl oxygen By similarity
Metal binding7651Calcium 2 By similarity
Metal binding7821Calcium 2; via carbonyl oxygen By similarity
Metal binding8411Calcium 2; via carbonyl oxygen By similarity
Metal binding11761Calcium 3 By similarity
Metal binding11931Calcium 3; via carbonyl oxygen By similarity
Metal binding12451Calcium 3; via carbonyl oxygen By similarity
Metal binding12471Calcium 3 By similarity

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation7901N-linked (GlcNAc...) Potential
Glycosylation12231N-linked (GlcNAc...) Potential
Disulfide bond228 ↔ 243 By similarity
Disulfide bond245 ↔ 255 By similarity
Disulfide bond437 ↔ 473 By similarity
Disulfide bond643 ↔ 672 By similarity
Disulfide bond680 ↔ 691 By similarity
Disulfide bond685 ↔ 700 By similarity
Disulfide bond702 ↔ 712 By similarity
Disulfide bond1052 ↔ 1080 By similarity
Disulfide bond1087 ↔ 1098 By similarity
Disulfide bond1092 ↔ 1107 By similarity
Disulfide bond1109 ↔ 1119 By similarity

Natural variations

Alternative sequence2581E → EIKFGLQCVLPVLLHDNDQG KYCCINTAKPLTEK in isoform 3a.
VSP_041353
Alternative sequence379 – 3868Missing in isoform 2a.
VSP_014541
Alternative sequence3861M → MVNKLHCS in isoform 3a.
VSP_041354
Alternative sequence12391A → AGNNDNERLAIARQRIPYRL GRVVDEWLLDK in isoform 3a.
VSP_041355
Alternative sequence12401G → GNNDNERLAIARQRIPYRLG RVVDEWLLDKG in isoform 2a.
VSP_014542
Natural variant281G → A. Ref.7
VAR_070274
Natural variant4001Y → N.
Corresponds to variant rs17040901 [ dbSNP | Ensembl ].
VAR_050265

Experimental info

Sequence conflict1373 – 13753Missing in BAA25504. Ref.2

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: FF845FB428B1A683

FASTA1,477161,883
        10         20         30         40         50         60 
MGTALLQRGG CFLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT 

        70         80         90        100        110        120 
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR 

       130        140        150        160        170        180 
RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF 

       190        200        210        220        230        240 
KGWIRDVRVN SSQVLPVDSG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ 

       250        260        270        280        290        300 
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP 

       310        320        330        340        350        360 
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG 

       370        380        390        400        410        420 
KFNDNAWHDV KVTRNLRQHS GIGHAMVTIS VDGILTTTGY TQEDYTMLGS DDFFYVGGSP 

       430        440        450        460        470        480 
STADLPGSPV SNNFMGCLKE VVYKNNDVRL ELSRLAKQGD PKMKIHGVVA FKCENVATLD 

       490        500        510        520        530        540 
PITFETPESF ISLPKWNAKK TGSISFDFRT TEPNGLILFS HGKPRHQKDA KHPQMIKVDF 

       550        560        570        580        590        600 
FAIEMLDGHL YLLLDMGSGT IKIKALLKKV NDGEWYHVDF QRDGRSGTIS VNTLRTPYTA 

       610        620        630        640        650        660 
PGESEILDLD DELYLGGLPE NKAGLVFPTE VWTALLNYGY VGCIRDLFID GQSKDIRQMA 

       670        680        690        700        710        720 
EVQSTAGVKP SCSKETAKPC LSNPCKNNGM CRDGWNRYVC DCSGTGYLGR SCEREATVLS 

       730        740        750        760        770        780 
YDGSMFMKIQ LPVVMHTEAE DVSLRFRSQR AYGILMATTS RDSADTLRLE LDAGRVKLTV 

       790        800        810        820        830        840 
NLDCIRINCN SSKGPETLFA GYNLNDNEWH TVRVVRRGKS LKLTVDDQQA MTGQMAGDHT 

       850        860        870        880        890        900 
RLEFHNIETG IITERRYLSS VPSNFIGHLQ SLTFNGMAYI DLCKNGDIDY CELNARFGFR 

       910        920        930        940        950        960 
NIIADPVTFK TKSSYVALAT LQAYTSMHLF FQFKTTSLDG LILYNSGDGN DFIVVELVKG 

       970        980        990       1000       1010       1020 
YLHYVFDLGN GANLIKGSSN KPLNDNQWHN VMISRDTSNL HTVKIDTKIT TQITAGARNL 

      1030       1040       1050       1060       1070       1080 
DLKSDLYIGG VAKETYKSLP KLVHAKEGFQ GCLASVDLNG RLPDLISDAL FCNGQIERGC 

      1090       1100       1110       1120       1130       1140 
EGPSTTCQED SCSNQGVCLQ QWDGFSCDCS MTSFSGPLCN DPGTTYIFSK GGGQITYKWP 

      1150       1160       1170       1180       1190       1200 
PNDRPSTRAD RLAIGFSTVQ KEAVLVRVDS SSGLGDYLEL HIHQGKIGVK FNVGTDDIAI 

      1210       1220       1230       1240       1250       1260 
EESNAIINDG KYHVVRFTRS GGNATLQVDS WPVIERYPAG RQLTIFNSQA TIIIGGKEQG 

      1270       1280       1290       1300       1310       1320 
QPFQGQLSGL YYNGLKVLNM AAENDANIAI VGNVRLVGEV PSSMTTESTA TAMQSEMSTS 

      1330       1340       1350       1360       1370       1380 
IMETTTTLAT STARRGKPPT KEPISQTTDD ILVASAECPS DDEDIDPCEP SSGGLANPTR 

      1390       1400       1410       1420       1430       1440 
AGGREPYPGS AEVIRESSST TGMVVGIVAA AALCILILLY AMYKYRNRDE GSYHVDESRN 

      1450       1460       1470 
YISNSAQSNG AVVKEKQPSS AKSSNKNKKN KDKEYYV 

« Hide

Isoform 2a [UniParc].

Checksum: F8481191C84C9CD7
Show »

FASTA1,499164,655
Isoform 3a [UniParc].

Checksum: 2F6A3FBB6E53AA2E
Show »

FASTA1,547169,913
Isoform 1b [UniParc].

See P58400.

References

« Hide 'large scale' references
[1]"Disruption of neurexin 1 associated with autism spectrum disorder."
Kim H.G., Kishikawa S., Higgins A.W., Seong I.S., Donovan D.J., Shen Y., Lally E., Weiss L.A., Najm J., Kutsche K., Descartes M., Holt L., Braddock S., Troxell R., Kaplan L., Volkmar F., Klin A., Tsatsanis K. expand/collapse author list , Harris D.J., Noens I., Pauls D.L., Daly M.J., MacDonald M.E., Morton C.C., Quade B.J., Gusella J.F.
Am. J. Hum. Genet. 82:199-207(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3A).
[2]"Human neurexin I-alpha."
Seki N., Yoshikawa T., Azuma T., Saito T., Muramatsu M.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
Tissue: Brain.
[3]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A), TISSUE SPECIFICITY.
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, ALTERNATIVE SPLICING.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity."
Rowen L., Young J., Birditt B., Kaur A., Madan A., Philipps D.L., Qin S., Minx P., Wilson R.K., Hood L., Graveley B.R.
Genomics 79:587-597(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[7]"Prevalence of SHANK3 variants in patients with different subtypes of autism spectrum disorders."
Boccuto L., Lauri M., Sarasua S.M., Skinner C.D., Buccella D., Dwivedi A., Orteschi D., Collins J.S., Zollino M., Visconti P., Dupont B., Tiziano D., Schroer R.J., Neri G., Stevenson R.E., Gurrieri F., Schwartz C.E.
Eur. J. Hum. Genet. 21:310-316(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-28.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF539882 mRNA. Translation: ABS86974.1.
AB035356 mRNA. Translation: BAA87821.1.
AB011150 mRNA. Translation: BAA25504.2. Different initiation.
AC007462 Genomic DNA. Translation: AAF03536.1.
AC007682 Genomic DNA. Translation: AAY14894.1.
AC009234 Genomic DNA. Translation: AAY14944.1.
AC068725 Genomic DNA. Translation: AAG59602.1.
AC069550 Genomic DNA. Translation: AAG38120.1.
AC078994 Genomic DNA. Translation: AAK06387.1.
AC068715 Genomic DNA. Translation: AAG59642.1.
CCDSCCDS46282.1. [Q9ULB1-3]
CCDS54360.1. [Q9ULB1-1]
RefSeqNP_001129131.1. NM_001135659.1. [Q9ULB1-3]
NP_004792.1. NM_004801.4. [Q9ULB1-1]
NP_620072.1. NM_138735.2.
UniGeneHs.637685.

3D structure databases

ProteinModelPortalQ9ULB1.
SMRQ9ULB1. Positions 209-257, 281-1300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114779. 11 interactions.
IntActQ9ULB1. 4 interactions.

PTM databases

PhosphoSiteQ9ULB1.

Polymorphism databases

DMDM17369704.

Proteomic databases

PaxDbQ9ULB1.
PRIDEQ9ULB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000404971; ENSP00000385142; ENSG00000179915. [Q9ULB1-3]
ENST00000405472; ENSP00000434015; ENSG00000179915. [Q9ULB1-2]
ENST00000406316; ENSP00000384311; ENSG00000179915. [Q9ULB1-1]
GeneID9378.
KEGGhsa:9378.
UCSCuc021vhg.1. human. [Q9ULB1-3]
uc021vhh.1. human. [Q9ULB1-1]

Organism-specific databases

CTD9378.
GeneCardsGC02M050145.
HGNCHGNC:8008. NRXN1.
MIM600565. gene.
neXtProtNX_Q9ULB1.
PharmGKBPA31786.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302266.
HOVERGENHBG052670.
KOK07377.
OMADCSQEIK.
OrthoDBEOG7XWPMM.
PhylomeDBQ9ULB1.
TreeFamTF321302.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9ULB1.
BgeeQ9ULB1.
CleanExHS_NRXN1.
GenevestigatorQ9ULB1.

Family and domain databases

Gene3D2.60.120.200. 6 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR001791. Laminin_G.
IPR003585. Neurexin-like.
IPR027789. Syndecan/Neurexin_dom.
[Graphical view]
PfamPF02210. Laminin_G_2. 6 hits.
PF01034. Syndecan. 1 hit.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
SM00181. EGF. 3 hits.
SM00282. LamG. 6 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 6 hits.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS50026. EGF_3. 3 hits.
PS50025. LAM_G_DOMAIN. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNRXN1. human.
GenomeRNAi9378.
NextBio35134.
PROQ9ULB1.
SOURCESearch...

Entry information

Entry nameNRX1A_HUMAN
AccessionPrimary (citable) accession number: Q9ULB1
Secondary accession number(s): A7KRL9 expand/collapse secondary AC list , O60323, Q53TJ9, Q53TQ1, Q9C079, Q9C080, Q9C081, Q9H3M2, Q9UDM6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 143 of the entry and version 1 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM