Peptide loading complex

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Proteomics (795)
Unknown (229)
Transcriptomics (148)
Genomics (39)
Metabolomics (5)
Other (2)

Organisms

Homo sapiens (76)
Mus musculus (33)
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Schizosaccharomyces pombe (9)
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mixed sample (1)
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Organisms

Homo sapiens (6)
Saccharomyces cerevisiae (1)

Repository

pride (758)
biostudies-arrayexpress (180)
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geo (5)
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Tissue

Cell culture (173)
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Technology Type

Mass Spectrometry (758)
Shotgun proteomics (328)
Bottom-up proteomics (164)
Affinity purification coupled with mass spectrometry proteomics (156)
Data-dependent acquisition (119)
Gel-based experiment (64)
Chemical cross-linking coupled with mass spectrometry proteomics (38)
Data-independent acquisition (31)
SWATH MS (30)
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Mass spectrometry (5)
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MSE (1)

Instrument Platform

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Publication Date

2025 (151)
2023 (115)
2026 (98)
2024 (92)
2022 (85)
2021 (76)
2020 (68)
2019 (52)
2018 (37)
2014 (31)
2016 (28)
2010 (26)
2013 (25)
2017 (23)
2015 (23)
2012 (18)
2008 (7)
2011 (6)
2007 (5)
2009 (4)
2006 (3)
2005 (2)
2004 (2)

UNIPROT ID/AC

Q12337 (1)
P32874 (1)
P38431-2 (1)
P07263-2 (1)
P06208-2 (1)

CHEBI ID

CHEBI:17345 (3)
CHEBI:30915 (3)
CHEBI:17728 (2)
CHEBI:17781 (2)
CHEBI:30753 (2)
CHEBI:17521 (2)
CHEBI:36090 (2)
CHEBI:22652 (2)
CHEBI:30851 (2)
CHEBI:17724 (2)
CHEBI:17697 (2)
CHEBI:17016 (2)
CHEBI:4178 (2)
CHEBI:27956 (2)
CHEBI:16610 (2)
CHEBI:17895 (2)
CHEBI:16828 (2)
CHEBI:16643 (2)
CHEBI:30832 (2)
CHEBI:15603 (2)
CHEBI:17537 (2)
CHEBI:16119 (2)
CHEBI:16414 (2)
CHEBI:33198 (2)
CHEBI:9300 (2)
CHEBI:17015 (2)
CHEBI:17203 (2)
CHEBI:15971 (2)
CHEBI:16015 (2)
CHEBI:17385 (2)

Metabolite Name

5-Methylcytosine (3)
Riboflavin (3)
Adenosine (3)
L-Proline (3)
L-Methionine (3)
Xanthine (3)
L-Octanoylcarnitine (2)
1-Pyrroline-2-carboxylic acid (2)
1-Methylnicotinamide (2)
Betaine (2)
Homocysteine (2)
2-Oxoarginine (2)
Propionylcarnitine (2)
Thiamine (2)
Sphingosine (2)
N6-Acetyl-L-lysine (2)
Monoethylglycinexylidide (2)
Lumichrome (2)
Benzaldehyde (2)
5'-Methylthioadenosine (2)
1-Aminocyclopropanecarboxylic acid (2)
Pantothenol (2)
Nicotinic acid (2)
Kynurenic acid (2)
Serotonin (2)
Pyridoxamine (2)
Pantothenic acid (2)
L-Kynurenine (2)
L-Tyrosine (2)
Indole (2)

First Public Date

2026 (2)
2025 (2)
2024 (2)
2023 (1)
2019 (1)
2014 (1)

Modification

N6 (2)
2x(15)N labeled L-lysine (2)
4x(15)N labeled L-arginine (2)
N6-dimethyl-L-lysine (2)
Not available (2)
4-tetrahydrothiazine-3-carboxylic acid (1)

Study type

Transcription profiling by array (87)
ChIP-seq (24)
RNA-seq of coding RNA (22)
ChIP-chip by tiling array (11)
Other (6)
Proteomic profiling by array (6)
RNA-seq of coding RNA from single cells (4)
RNA-seq of non coding RNA (3)
Unknown experiment type (2)
CLIP-seq (2)
DNA-seq (2)
MNase-seq (1)
RNA-seq of non coding RNA from single cells (1)
RNAi profiling by array (1)
Comparative genomic hybridization by array (1)
Hi-C (1)
RIP-seq (1)
MicroRNA profiling by array (1)
Methylation profiling by array (1)
Methylation profiling by high throughput sequencing (1)
RNA-seq of total RNA (1)

Release Date

2014 (36)
2013 (33)
2023 (31)
2010 (31)
2015 (28)
2012 (28)
2022 (27)
2021 (19)
2020 (19)
2019 (19)
2016 (19)
2025 (18)
2024 (17)
2017 (16)
2011 (12)
2018 (11)
2008 (10)
2009 (8)
2026 (7)
2007 (7)
2006 (4)
2005 (4)
2004 (3)
2000 (1)
1997 (1)

Lab affiliation

University of Vienna, Faculty of Chemistry, Department of Analytical Chemistry (13)
Functional Proteomics, ICR (7)
Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg im Breisgau, Germany (6)
Division of Cell Matrix Biology & Regenerative Medicine (L5) / Division of Cell Matrix Biology & Regenerative Medicine, University of Manchester (5)
LMU Munich Plant Biochemistry and Physiology, Germany (5)
Ghent University, Department of Plant Biotechnology and Bioinformatics, Technologiepark 71, 9052 Ghent, Belgium VIB Center for Plant Systems Biology, Technologiepark 71, 9052 Ghent, Belgium (5)
Bioplatforms Australia (5)
ETHZ IMSB (4)
Dept. Oncology-Pathology, Scilifelab, Karolinska Institutet, Sweden (3)
Molecular Biosciences and the Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX, USA (3)
University Clinic for Poultry and Fish Medicine, University of Veterinary Medicine, Vienna, Austria (3)
Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK (3)
Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark (3)
University of Oxford (3)
EDyP (3)
Harvard Medical School (3)
The Institute of Cancer Research (3)
Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115 (2)
Proteomic Hematology Department of Experimental Medical Science Lund Stem Cell Center, Lund University (2)
Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) Technical University Munich (TUM) Gregor-Mendel-Strasse 4 85354 Freising GERMANY (2)
Chromosome and Plasmid Segregation Lab, Department of Biosciences and Bioengineering, IIT Bombay, Mumbai, India (2)
Department of Biochemistry and Microbiology, Ghent University, Belgium (2)
UAB CCC MS Proteomics Facility (2)
Department of Genetic Medicine and Development, Faculty of Medicine, University of Geneva, Switzerland (2)
Amphista Therapeutics Cambridge United Kingdom (2)
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences (2)
Max-Planck Institute of Biophysics (2)
Institut für Mikrobiologie, Universität Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald (2)
Molecular Biotechnology & Systems Biology, TU Kaiserslautern, Kaiserslautern, Germany (2)
Department of Biochemistry and Biotechnology, University of Thessaly, Biopolis, 41500 Larissa, Greece (2)

Tags

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xref:PubMed:41871810 (1)
xref:PubMed:18446792 (1)
xref:PubMed:39439221 (1)
xref:PubMed:39271725 (1)
xref:PubMed:42094418 (1)

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Cross-linking of the human MHC-I peptide-loading complex

The peptide-loading complex (PLC) is a transient, multisubunit membrane complex in the endoplasmic reticulum (ER), essential for establishing a hierarchical immune response. The PLC coordinates peptide translocation into the ER with loading and editing of major histocompatibility complex class I mol...

ORGANISM(S): Homo sapiens (Human)

2017-11-07 | PXD007928 | Pride

Viral immune evasions differentially impact cell surface presentation of MHC I allomorphs already at the peptide-loading complex

The transporter associated with antigen processing (TAP) translocates peptides from the cytosol into the endoplasmic reticulum (ER) where they are loaded onto major histocompatibility class I (MHC I) molecules. Stable peptide-MHC I complexes travel to the cell surface and present their antigenic car...

ORGANISM(S): Homo sapiens (Human)

2022-02-17 | PXD027408 | Pride

Er quality control Major histocompatibility complex class i Mass spectrometry Mhc i biogenesis Viral immune evasion Peptide-loading complex

Peptide loading genes

Unravelling the architecture of Major Histocompatibility Complex class II haplotypes in rhesus macaques

PRJEB71338 | ENA

Mechanical loading and gene expression - Microarray study

Skeletal integrity in humans and animals is maintained by daily mechanical loading. It has been widely accepted that osteocytes function as mechanosensors. Many biochemical signaling molecules are involved in the response of osteocytes to mechanical stimulation. The aim of this study was to identify...

ORGANISM(S): Rattus norvegicus

2013-11-21 | E-GEOD-50707 | biostudies-arrayexpress

Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.

Not available

S-EPMC3438949 | biostudies-literature

Molecular basis of MHC I quality control in the peptide loading complex.

Not available

S-EPMC9365787 | biostudies-literature

Light control of the peptide-loading complex synchronizes antigen translocation and MHC I trafficking.

Not available

S-EPMC8010092 | biostudies-literature

Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.