Q8TCT9 · HM13_HUMAN
- ProteinMinor histocompatibility antigen H13
- GeneHM13
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein (PubMed:12145199).
Involved in the intramembrane cleavage of the integral membrane protein PSEN1 (PubMed:11714810, PubMed:12077416, PubMed:14741365).
Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (PubMed:25239945).
May play a role in graft rejection (By similarity).
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 219 | |||||
Sequence: D | ||||||
Active site | 265 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasmic side of endoplasmic reticulum membrane | |
Cellular Component | Derlin-1 retrotranslocation complex | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | lumenal side of endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | rough endoplasmic reticulum | |
Molecular Function | aspartic endopeptidase activity, intramembrane cleaving | |
Molecular Function | peptidase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | cellular response to oxidative stress | |
Biological Process | in utero embryonic development | |
Biological Process | membrane protein proteolysis | |
Biological Process | membrane protein proteolysis involved in retrograde protein transport, ER to cytosol | |
Biological Process | signal peptide processing |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMinor histocompatibility antigen H13
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TCT9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 4
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-31 | Lumenal | ||||
Sequence: MDSALSDPHNGSAEAGGPTNSTTRPPSTPEG | ||||||
Transmembrane | 32-52 | Helical | ||||
Sequence: IALAYGSLLLMALLPIFFGAL | ||||||
Topological domain | 53-77 | Cytoplasmic | ||||
Sequence: RSVRCARGKNASDMPETITSRDAAR | ||||||
Transmembrane | 78-98 | Helical | ||||
Sequence: FPIIASCTLLGLYLFFKIFSQ | ||||||
Topological domain | 99-100 | Lumenal | ||||
Sequence: EY | ||||||
Transmembrane | 101-121 | Helical | ||||
Sequence: INLLLSMYFFVLGILALSHTI | ||||||
Topological domain | 122-157 | Cytoplasmic | ||||
Sequence: SPFMNKFFPASFPNRQYQLLFTQGSGENKEEIINYE | ||||||
Transmembrane | 158-178 | Helical | ||||
Sequence: FDTKDLVCLGLSSIVGVWYLL | ||||||
Topological domain | 179-181 | Lumenal | ||||
Sequence: RKH | ||||||
Transmembrane | 182-202 | Helical | ||||
Sequence: WIANNLFGLAFSLNGVELLHL | ||||||
Topological domain | 203-209 | Cytoplasmic | ||||
Sequence: NNVSTGC | ||||||
Transmembrane | 210-230 | Helical | ||||
Sequence: ILLGGLFIYDVFWVFGTNVMV | ||||||
Topological domain | 231-256 | Lumenal | ||||
Sequence: TVAKSFEAPIKLVFPQDLLEKGLEAN | ||||||
Transmembrane | 257-277 | Helical | ||||
Sequence: NFAMLGLGDVVIPGIFIALLL | ||||||
Topological domain | 278-290 | Cytoplasmic | ||||
Sequence: RFDISLKKNTHTY | ||||||
Transmembrane | 291-311 | Helical | ||||
Sequence: FYTSFAAYIFGLGLTIFIMHI | ||||||
Topological domain | 312-314 | Lumenal | ||||
Sequence: FKH | ||||||
Transmembrane | 315-335 | Helical | ||||
Sequence: AQPALLYLVPACIGFPVLVAL | ||||||
Topological domain | 336-377 | Cytoplasmic | ||||
Sequence: AKGEVTEMFSYEESNPKDPAAVTESKEGTEASASKGLEKKEK |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 10 | Abolishes N-glycosylation; when associated with Q-20. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 20 | Abolishes N-glycosylation; when associated with Q-10. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 219 | Abolishes proteolysis of PSEN1. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_014274 | 259 | in dbSNP:rs1044419 | |||
Sequence: A → P | ||||||
Mutagenesis | 264 | No effect on proteolysis of PSEN1. | ||||
Sequence: G → A | ||||||
Mutagenesis | 265 | No effect on inhibitor binding; abolishes catalytic activity. Abolishes proteolysis of PSEN1. Abolishes proteolysis of XBP1 isoform 1 and increases interaction with XBP1 isoform 1. | ||||
Sequence: D → A | ||||||
Mutagenesis | 317 | Abolishes proteolysis of PSEN1. | ||||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 363 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000073907 | 1-377 | UniProt | Minor histocompatibility antigen H13 | |||
Sequence: MDSALSDPHNGSAEAGGPTNSTTRPPSTPEGIALAYGSLLLMALLPIFFGALRSVRCARGKNASDMPETITSRDAARFPIIASCTLLGLYLFFKIFSQEYINLLLSMYFFVLGILALSHTISPFMNKFFPASFPNRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSIVGVWYLLRKHWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDVFWVFGTNVMVTVAKSFEAPIKLVFPQDLLEKGLEANNFAMLGLGDVVIPGIFIALLLRFDISLKKNTHTYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALAKGEVTEMFSYEESNPKDPAAVTESKEGTEASASKGLEKKEK | |||||||
Glycosylation | 10 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 20 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 367 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (PubMed:15385547, PubMed:15998642).
Interacts with RNF139 (PubMed:19720873, PubMed:25239945).
Interacts with DERL1 and XBP1 isoform 1 (PubMed:25239945).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TCT9 | DERL1 Q9BUN8 | 6 | EBI-347472, EBI-398977 | |
BINARY | Q8TCT9 | LZTS2 Q9BRK4 | 3 | EBI-347472, EBI-741037 | |
BINARY | Q8TCT9 | P4HB P07237 | 3 | EBI-347472, EBI-395883 | |
BINARY | Q8TCT9 | RNF139 Q8WU17 | 2 | EBI-347472, EBI-1551681 | |
BINARY | Q8TCT9 | XBP1 P17861-1 | 2 | EBI-347472, EBI-7631279 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-27 | Disordered | ||||
Sequence: MDSALSDPHNGSAEAGGPTNSTTRPPS | ||||||
Compositional bias | 13-27 | Polar residues | ||||
Sequence: AEAGGPTNSTTRPPS | ||||||
Motif | 317-319 | PAL | ||||
Sequence: PAL | ||||||
Region | 345-377 | Disordered | ||||
Sequence: SYEESNPKDPAAVTESKEGTEASASKGLEKKEK |
Domain
The PAL motif is required for normal active site conformation (By similarity).
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8TCT9-1
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
- Length377
- Mass (Da)41,488
- Last updated2002-06-01 v1
- Checksum322D231B52B33118
Q8TCT9-2
- Name2
- Differences from canonical
- 347-347: E → ESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAIYE
Q8TCT9-4
- Name4
- Differences from canonical
- 348-377: ESNPKDPAAVTESKEGTEASASKGLEKKEK → SSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAM
Q8TCT9-5
- Name5
- Differences from canonical
- 181-222: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0S2Z6F0 | A0A0S2Z6F0_HUMAN | HM13 | 345 | ||
A0A075B6F6 | A0A075B6F6_HUMAN | HM13 | 272 | ||
A0A3B3IT72 | A0A3B3IT72_HUMAN | HM13 | 365 | ||
A0A3B3IUB5 | A0A3B3IUB5_HUMAN | HM13 | 420 | ||
A0A087WVH6 | A0A087WVH6_HUMAN | HM13 | 50 | ||
A0A0C4DGU3 | A0A0C4DGU3_HUMAN | HM13 | 143 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 13-27 | Polar residues | ||||
Sequence: AEAGGPTNSTTRPPS | ||||||
Sequence conflict | 132 | in Ref. 1; AA sequence | ||||
Sequence: S → N | ||||||
Sequence conflict | 150 | in Ref. 8; BAC11519 | ||||
Sequence: K → R | ||||||
Sequence conflict | 159 | in Ref. 1; AA sequence | ||||
Sequence: D → A | ||||||
Alternative sequence | VSP_015082 | 181-222 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 235 | in Ref. 11; AAH08938/AAH08959 | ||||
Sequence: S → F | ||||||
Sequence conflict | 295 | in Ref. 7; AAQ13609 | ||||
Sequence: F → Y | ||||||
Alternative sequence | VSP_005196 | 347 | in isoform 2 | |||
Sequence: E → ESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAIYE | ||||||
Alternative sequence | VSP_015083 | 348-377 | in isoform 4 | |||
Sequence: ESNPKDPAAVTESKEGTEASASKGLEKKEK → SSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ420895 EMBL· GenBank· DDBJ | CAD13132.1 EMBL· GenBank· DDBJ | mRNA | ||
AF515663 EMBL· GenBank· DDBJ | AAN77099.1 EMBL· GenBank· DDBJ | mRNA | ||
AY169310 EMBL· GenBank· DDBJ | AAO12535.1 EMBL· GenBank· DDBJ | mRNA | ||
AY169311 EMBL· GenBank· DDBJ | AAO12536.1 EMBL· GenBank· DDBJ | mRNA | ||
AY169312 EMBL· GenBank· DDBJ | AAO12537.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ168450 EMBL· GenBank· DDBJ | ABA56163.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ345029 EMBL· GenBank· DDBJ | CAC87790.1 EMBL· GenBank· DDBJ | mRNA | ||
AF483215 EMBL· GenBank· DDBJ | AAM22076.1 EMBL· GenBank· DDBJ | mRNA | ||
AF172086 EMBL· GenBank· DDBJ | AAQ13609.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK074686 EMBL· GenBank· DDBJ | BAC11138.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK075283 EMBL· GenBank· DDBJ | BAC11519.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314410 EMBL· GenBank· DDBJ | BAG37032.1 EMBL· GenBank· DDBJ | mRNA | ||
AL110115 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL121751 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW76436.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW76437.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW76435.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW76438.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008938 EMBL· GenBank· DDBJ | AAH08938.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008959 EMBL· GenBank· DDBJ | AAH08959.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062595 EMBL· GenBank· DDBJ | AAH62595.1 EMBL· GenBank· DDBJ | mRNA |