Ambox notice.png

GONUTS is under stress! The website is currently experiencing long-wait times and frequent time-outs due to the record number of students, groups, and annotations related to CACAO this semester. We are currently working on increasing performance -- please accept our apologies for the technical difficulties.

You can help reduce stress on the server by:

  1. not reloading pages frequently - this just adds
  2. opening links in new windows (so you can read the old page)

RAT:NRX1B

From GONUTS
Jump to: navigation, search

Contents

Species (Taxon ID) Rattus norvegicus (Rat). (taxon:10116)
Gene Name(s) Nrxn1
Protein Name(s)
  • Neurexin-1-beta
  • Neurexin I-beta
External Links
UniProt Identifier NRX1B_RAT
UniProt Accessions Q63373,
EMBL M96375,
PIR B40228,
PDB 1C4R, 2R1B, 2R1D, 2WQZ, 2XB6,
IntAct Q63373,
Pfam PF02210,

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005102

receptor binding

PMID:15797875[1]

IPI: Inferred from Physical Interaction

UniProtKB:Q62765

F

GO:0005509

calcium ion binding

PMID:18334216[2]

IDA: Inferred from Direct Assay

F

GO:0005515

protein binding

PMID:18093521[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q8N0W4

F

GO:0005515

protein binding

PMID:18093522[4]

IPI: Inferred from Physical Interaction

RGD:621117

F

GO:0005515

protein binding

PMID:18423203[5]

IPI: Inferred from Physical Interaction

UniProtKB:O14936

F

GO:0005886

plasma membrane

PMID:18755801[6]

IDA: Inferred from Direct Assay

C

GO:0007155

cell adhesion

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0130

P

GO:0009986

cell surface

PMID:15797875[1]

IDA: Inferred from Direct Assay

C

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

GO:0016020

membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0162

C

GO:0016021

integral to membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0812

C

GO:0030139

endocytic vesicle

PMID:15797875[1]

IDA: Inferred from Direct Assay

C

GO:0050839

cell adhesion molecule binding

PMID:15797875[1]

IPI: Inferred from Physical Interaction

UniProtKB:Q62765

F

GO:0051290

protein heterotetramerization

PMID:18093522[4]

IDA: Inferred from Direct Assay

P

GO:0042734

presynaptic membrane

PMID:17868325[7]

IDA: Inferred from Direct Assay

C

See Fig 5. Neurexin is largely presynaptic and binds with neuroligin normally to form trans-synaptic complexes and transduce bidirectional signals across the membrane.

complete

GO:0001525

angiogenesis

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:D0PRN2

P

GO:0005102

receptor binding

PMID:15797875[1]

IPI: Inferred from Physical Interaction

UniProtKB:Q62765

F

GO:0005509

calcium ion binding

PMID:18334216[2]

IDA: Inferred from Direct Assay

F

GO:0005515

protein binding

PMID:18093521[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q8N0W4

F

GO:0005515

protein binding

PMID:18093522[4]

IPI: Inferred from Physical Interaction

RGD:621117

F

GO:0005515

protein binding

PMID:18423203[5]

IPI: Inferred from Physical Interaction

UniProtKB:O14936

F

GO:0005886

plasma membrane

PMID:18755801[6]

IDA: Inferred from Direct Assay

C

GO:0007155

cell adhesion

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0130

P

GO:0009986

cell surface

PMID:15797875[1]

IDA: Inferred from Direct Assay

C

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

GO:0016020

membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0162

C

GO:0016021

integral to membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0812

C

GO:0030139

endocytic vesicle

PMID:15797875[1]

IDA: Inferred from Direct Assay

C

GO:0050839

cell adhesion molecule binding

PMID:15797875[1]

IPI: Inferred from Physical Interaction

UniProtKB:Q62765

F

GO:0051290

protein heterotetramerization

PMID:18093522[4]

IDA: Inferred from Direct Assay

P


Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Chubykin AA et al. (2005) Dissection of synapse induction by neuroligins: effect of a neuroligin mutation associated with autism. J Biol Chem 280: 22365-74 PubMed GONUTS page
  2. 2.0 2.1 Koehnke J et al. (2008) Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4. Structure 16: 410-21 PubMed GONUTS page
  3. 3.0 3.1 Fabrichny IP et al. (2007) Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron 56: 979-91 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Araç D et al. (2007) Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. Neuron 56: 992-1003 PubMed GONUTS page
  5. 5.0 5.1 Mukherjee K et al. (2008) CASK Functions as a Mg2+-independent neurexin kinase. Cell 133: 328-39 PubMed GONUTS page
  6. 6.0 6.1 Suckow AT et al. (2008) Expression of neurexin, neuroligin, and their cytoplasmic binding partners in the pancreatic beta-cells and the involvement of neuroligin in insulin secretion. Endocrinology 149: 6006-17 PubMed GONUTS page
  7. Berninghausen O et al. (2007) Neurexin Ibeta and neuroligin are localized on opposite membranes in mature central synapses. J Neurochem 103: 1855-63 PubMed GONUTS page
Personal tools
Namespaces
Variants
Actions
Navigation
Cacao
Journal Clubs
page contributors
Toolbox