about
Insulin receptorKeratin 1Keratin 10Annexin A2Polycystin 1, transient receptor poteintial channel interactingCarbonyl reductase 4Decaprenyl diphosphate synthase subunit 2Nucleoporin 54Phenylalanyl-tRNA synthetase subunit alphaCyclic nucleotide gated channel subunit beta 1Ribonucleotide reductase regulatory subunit M2H3 clustered histone 10H3.4 histoneCD74 moleculeDecaprenyl diphosphate synthase subunit 1Putative annexin A2-like proteinGlutamate ionotropic receptor NMDA type subunit 2BCleavage and polyadenylation specific factor 7X-ray repair cross complementing 6Cleavage and polyadenylation specific factor 6Hydroxysteroid 17-beta dehydrogenase 8Regulator of chromosome condensation 1Glutamate ionotropic receptor NMDA type subunit 1LDL receptor related protein 4Ribonucleotide reductase catalytic subunit M1Neuroligin 1Phenylalanyl-tRNA synthetase subunit betaNudix hydrolase 21S100 calcium binding protein A10CD74 antigen (invariant polypeptide of major histocompatibility complex, class II antigen-associated)AgrinNucleoporin 54Nucleoporin 58S100 calcium binding protein A10 (calpactin)Neurexin IPrenyl (solanesyl) diphosphate synthase, subunit 2Glutamate receptor, ionotropic, NMDA2B (epsilon 2)H2-K region expressed gene 6Carbonyl reductase 4Cyclic nucleotide gated channel alpha 4
P682
Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patternsThe X-Ray Crystal Structure of the Keratin 1-Keratin 10 Helix 2B Heterodimer Reveals Molecular Surface Properties and Biochemical Insights into Human Skin Disease.Structure of the human PKD1-PKD2 complex
P921
Q14863366-1856BF02-6ADC-433E-B0A5-1933DF60F118Q14864150-B34C5665-35A8-4DD0-A32A-986038B21E78Q14864191-C6A6E612-E765-4C05-96CC-1B60A451AF70Q14908237-3E4894B3-60A7-413D-B95A-A84E581BA8B3Q14908237-F18CDAE9-B46A-403D-94A5-13F682E3EBB7Q14914569-BAD25E38-3FDF-4358-B9E7-6742D80163E5Q14914569-CDD9EB96-242D-4802-B8C0-F177B602F191Q21102252-E41E3B4A-C35B-43CA-871D-B9A1919644AAQ21102637-86F5F382-F1C3-4D2D-BFAA-D74C94B70EADQ21103322-68B0DD17-C809-4E5B-8B41-B9D640C54F82Q21104906-6FFCD147-658B-4658-BBB5-504CD94C2652Q21105651-6821B1B8-E7B3-4C09-AF68-B3E8815232FEQ21108338-12F5D1A9-740C-44AE-A044-0A7975026F1FQ21109291-8C41CAA2-6C4A-43BB-8750-56911527A96FQ21110983-EA817DF2-8210-41B1-8598-5B507C184A26Q21113110-5BF3DB7F-3800-4627-A9CC-A3126C1D08FBQ21113207-C9279F0D-9A50-4599-8094-F47F185E6C36Q21115367-077541D8-5CAB-40D1-B4E4-C8D9EB6C81F3Q21115816-A9DCB3B4-0DC2-43D8-A6C9-C59DBDA1E6D2Q21116398-C6B4DDC7-0FA0-495C-8B49-5B0BFB6595F3Q21116645-5EA4F27B-3D11-4515-B1BE-616DF414BCE0Q21116713-124E00D3-3B36-4AFD-A53D-7A5DA42A7020Q21117491-649DC52B-9041-4BFE-BB3B-FEEF54161EABQ21117726-31235734-A4C9-4D45-8BB6-EE44003992E2Q21118862-65426830-AC7F-4631-9E9C-79BCADEBDC3BQ21119936-1C6F1EB1-B41F-45C0-BC4D-83F37A0F4EDCQ21121233-BAE917FF-7FC4-4C71-9161-78EE8357D287Q21123113-13CB2699-643F-4B33-9322-6C41213F83C4Q21123450-2CD343F4-D6AB-4704-903F-672C7AC04704Q21132119-555E3586-75F1-4B12-BA28-AF3DDC18F59FQ21154867-A352965C-8159-4133-8F09-B7F76AD5C97DQ21428393-EF4FA955-65B3-4402-8544-ADE60BEA8CC9Q21428623-2C68C83F-4907-46B3-B2CA-55C1B508E000Q21433614-C0AA8701-750E-4CA5-8AA7-9B9F265BE60BQ21433615-AF8BAEA8-B2C2-4D60-A80A-9ABAF8D2C821Q21494839-328C4D0E-10B8-4AAF-8149-F1565FFF812BQ21494945-5A9AABD3-8250-4D1F-9215-5F1EDAE28404Q21495526-A6D47B81-5664-450C-8CBA-301619DAE19DQ21496048-F9A5AA35-9949-4B4A-ADD8-E8AAB4B50EA0Q21497481-4A156D2B-1683-474D-8DD2-09F1FC6A59A7
P682
description
The formation of a protein het ...... f which not all are identical.
@en
biologisch proces
@nl
name
protein heterotetramerization
@en
type
label
protein heterotetramerization
@en
altLabel
GO:0051290
@en
protein heterotetramer assembly
@en
protein heterotetramer biosynthesis
@en
protein heterotetramer biosynthetic process
@en
protein heterotetramer formation
@en
prefLabel
protein heterotetramerization
@en
P2888
P686
GO:0051290