GRINL1A
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Official Full Name
glutamate receptor, ionotropic, N-methyl D-aspartate-like 1A -
Overview
This gene (GRINL1A) is part of a complex transcript unit that includes the gene for GRINL1A combined protein (Gcom1). Transcription of this gene occurs at a downstream promoter, with at least three different alternatively spliced variants, grouped together as Gdown for GRINL1A downstream transcripts. The Gcom1 gene uses an upstream promoter for transcription and also has multiple alternatively spliced variants. -
Synonyms
glutamate receptor, ionotropic, N-methyl D-aspartate-like 1A;Glutamate receptor-like protein 1A;DKFZp586F1918;GRINL1A downstream protein Gdown4;protein GRINL1A;protein GRINL1A, isoforms 4/5;OTTHUMP00000163345;OTTHUMP00000163421
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Involved Pathway
GRINL1A involved in several pathways and played different roles in them. We selected most pathways GRINL1A participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with GRINL1A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Protein Function
GRINL1A has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by GRINL1A itself. We selected most functions GRINL1A had, and list some proteins which have the same functions with GRINL1A. You can find most of the proteins on our site.
Function | Related Protein |
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Interacting Protein
GRINL1A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with GRINL1A here. Most of them are supplied by our site. Hope this information will be useful for your research of GRINL1A.
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References
- Davis, MAM; Guo, JN; et al. Functional Interactions of the RNA Polymerase II-interacting Proteins Gdown1 and TFIIF. JOURNAL OF BIOLOGICAL CHEMISTRY 289:11143-11152(2014).
- Huo, L; Wen, WY; et al. Cdc42-dependent formation of the ZO-1/MRCK beta complex at the leading edge controls cell migration. EMBO JOURNAL 30:665-678(2011).