P04844 · RPN2_HUMAN
- ProteinDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- GeneRPN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids631 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc3Man9GlcNAc2 in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667).
N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity
N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity
Pathway
Protein modification; protein glycosylation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | nuclear body | |
Cellular Component | oligosaccharyltransferase complex | |
Biological Process | protein modification process | |
Biological Process | protein N-linked glycosylation | |
Biological Process | protein N-linked glycosylation via asparagine |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP04844
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-540 | Lumenal | ||||
Sequence: LTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTV | ||||||
Transmembrane | 541-561 | Helical | ||||
Sequence: VSNTFTALILSPLLLLFALWI | ||||||
Topological domain | 562-571 | Cytoplasmic | ||||
Sequence: RIGANVSNFT | ||||||
Transmembrane | 572-592 | Helical | ||||
Sequence: FAPSTIIFHLGHAAMLGLMYV | ||||||
Topological domain | 593-596 | Lumenal | ||||
Sequence: YWTQ | ||||||
Transmembrane | 597-617 | Helical | ||||
Sequence: LNMFQTLKYLAILGSVTFLAG | ||||||
Topological domain | 618-631 | Cytoplasmic | ||||
Sequence: NRMLAQQAVKRTAH |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_054040 | 597 | in dbSNP:rs34951322 | |||
Sequence: L → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 663 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MAPPGSSTVFLLALTIIASTWA | |||||||
Chain | PRO_0000022244 | 23-631 | UniProt | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 | |||
Sequence: LTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMFQTLKYLAILGSVTFLAGNRMLAQQAVKRTAH | |||||||
Glycosylation | 106 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Cross-link | 154 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues tested.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the oligosaccharyltransferase (OST) complex (PubMed:31831667).
OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits (PubMed:23606741, PubMed:25135935, PubMed:31831667).
STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity).
Interacts with DDI2 (PubMed:29290612).
Interacts with TMEM35A/NACHO (By similarity).
OST exists in two different complex forms which contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits, and form-specific accessory subunits (PubMed:23606741, PubMed:25135935, PubMed:31831667).
STT3A complex assembly occurs through the formation of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The STT3A complex can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity).
Interacts with DDI2 (PubMed:29290612).
Interacts with TMEM35A/NACHO (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P04844 | POMK Q9H5K3 | 2 | EBI-719731, EBI-11337900 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P04844-1
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.
- Name1
- Length631
- Mass (Da)69,284
- Last updated2000-12-01 v3
- ChecksumE24D7B3565141676
P04844-2
- Name2
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0Y5M1 | H0Y5M1_HUMAN | RPN2 | 147 | ||
Q5JYR3 | Q5JYR3_HUMAN | RPN2 | 138 | ||
Q5JYR4 | Q5JYR4_HUMAN | RPN2 | 166 | ||
Q5JYR7 | Q5JYR7_HUMAN | RPN2 | 344 | ||
A0A994J5J1 | A0A994J5J1_HUMAN | RPN2 | 654 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043051 | 70-101 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 197 | in Ref. 1; CAA68393 | ||||
Sequence: V → L | ||||||
Sequence conflict | 201 | in Ref. 1; CAA68393 | ||||
Sequence: F → C | ||||||
Sequence conflict | 260 | in Ref. 1; CAA68393 | ||||
Sequence: A → S | ||||||
Sequence conflict | 286 | in Ref. 4; CAG33180 | ||||
Sequence: A → S | ||||||
Sequence conflict | 423 | in Ref. 1; CAA68393 | ||||
Sequence: V → M | ||||||
Sequence conflict | 427 | in Ref. 4; CAG33180 | ||||
Sequence: A → V | ||||||
Sequence conflict | 571 | in Ref. 7; AAH13028 | ||||
Sequence: T → I | ||||||
Alternative sequence | VSP_043052 | 627 | in isoform 2 | |||
Sequence: K → KRIAAEQSSRLAKYRTL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y00282 EMBL· GenBank· DDBJ | CAA68393.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ237734 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237735 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237733 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237736 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237737 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237738 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237739 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237740 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237741 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237742 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237743 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237744 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237745 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237746 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237747 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237748 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ237749 EMBL· GenBank· DDBJ | CAB54801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK096243 EMBL· GenBank· DDBJ | BAG53237.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456899 EMBL· GenBank· DDBJ | CAG33180.1 EMBL· GenBank· DDBJ | mRNA | ||
AL031659 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002380 EMBL· GenBank· DDBJ | AAH02380.2 EMBL· GenBank· DDBJ | mRNA | ||
BC003560 EMBL· GenBank· DDBJ | AAH03560.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013028 EMBL· GenBank· DDBJ | AAH13028.2 EMBL· GenBank· DDBJ | mRNA | ||
BC020222 EMBL· GenBank· DDBJ | AAH20222.1 EMBL· GenBank· DDBJ | mRNA |