Q96N21 · AP4AT_HUMAN
- ProteinAP-4 complex accessory subunit Tepsin
- GeneTEPSIN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids525 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Associates with the adapter-like complex 4 (AP-4) and may therefore play a role in vesicular trafficking of proteins at the trans-Golgi network.
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 | coated vesicle membrane | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extrinsic component of organelle membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | organelle membrane | |
Cellular Component | trans-Golgi network membrane | |
Molecular Function | protein-containing complex binding |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAP-4 complex accessory subunit Tepsin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96N21
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein
Note: Extensively colocalizes with AP-4 which mediates the recruitment of TEPSIN to the trans-Golgi network.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 467 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: R → A | ||||||
Mutagenesis | 468 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: D → A | ||||||
Mutagenesis | 469 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: S → A or P | ||||||
Mutagenesis | 470 | Loss of interaction with AP4B1 n vitro. | ||||
Sequence: L → A | ||||||
Mutagenesis | 470 | Loss of interaction with AP4B1 in vitro; when associated with S-471. | ||||
Sequence: L → S | ||||||
Mutagenesis | 471 | Loss of interaction with AP4B1 in vitro. | ||||
Sequence: F → A | ||||||
Mutagenesis | 471 | Loss of interaction with AP4B1 in vitro; when associated with S-470. | ||||
Sequence: F → S | ||||||
Mutagenesis | 472 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: A → D or P | ||||||
Mutagenesis | 473 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: G → A | ||||||
Mutagenesis | 473 | Loss of interaction with AP4B1 in vitro; when associated with Q-474. | ||||
Sequence: G → I | ||||||
Mutagenesis | 474 | Decreased interaction with AP4B1 in vitro. | ||||
Sequence: M → A | ||||||
Mutagenesis | 474 | Decreased interaction with AP4B1 in vitro; when associated with A-476. | ||||
Sequence: M → D | ||||||
Mutagenesis | 474 | Loss of interaction with AP4B1 in vitro; when associated with I-473. | ||||
Sequence: M → Q | ||||||
Mutagenesis | 475 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: E → A | ||||||
Mutagenesis | 476 | No effect on interaction with AP4B1 in vitro. Decreased interaction with AP4B1; when associated with D-474. | ||||
Sequence: L → A | ||||||
Mutagenesis | 476 | Decreased interaction with AP4B1 in vitro; when associated with S-477. | ||||
Sequence: L → S | ||||||
Mutagenesis | 477 | No effect on interaction with AP4B1 in vitro. | ||||
Sequence: V → A | ||||||
Mutagenesis | 477 | Decreased interaction with AP4B1 in vitro; when associated with S-476. | ||||
Sequence: V → S | ||||||
Mutagenesis | 516 | No effect on interaction with AP4E1 in vitro. | ||||
Sequence: E → A | ||||||
Mutagenesis | 517 | No effect on interaction with AP4E1 in vitro. | ||||
Sequence: P → A | ||||||
Mutagenesis | 518 | Loss of interaction with AP4E1 in vitro. | ||||
Sequence: S → A | ||||||
Mutagenesis | 519 | Loss of interaction with AP4E1 in vitro. | ||||
Sequence: A → D | ||||||
Mutagenesis | 520 | Loss of interaction with AP4E1 in vitro. | ||||
Sequence: F → A | ||||||
Mutagenesis | 521 | No effect on interaction with AP4E1 in vitro. | ||||
Sequence: A → D | ||||||
Mutagenesis | 522 | Loss of interaction with AP4E1 in vitro. | ||||
Sequence: F → A | ||||||
Mutagenesis | 523 | Loss of interaction with AP4E1 in vitro. | ||||
Sequence: L → A | ||||||
Mutagenesis | 524 | Decreased interaction with AP4E1 in vitro. | ||||
Sequence: N → A | ||||||
Mutagenesis | 525 | No effect on interaction with AP4E1 in vitro. | ||||
Sequence: A → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 692 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000286678 | 1-525 | UniProt | AP-4 complex accessory subunit Tepsin | |||
Sequence: MAAAPPLRDRLSFLHRLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRTAVRHQPGQAGGGWDELDSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSGASREPGDLAERVEVVALSDCQQELSLVRTVTRGPRAFLSREEAQHFIKACGLLNCEAVLQLLTCHLRGTSECTQLRALCAIASLGSSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPSEAEARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPGSEPSAFAFLNA | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 333 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 356 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 455 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with AP4B1 and AP4E1; the interaction is direct and mediates the association of TEPSIN with the adapter-like complex 4 (AP-4), a heterotetramer composed of AP4B1, AP4E1, AP4M1 and AP4S1.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-141 | ENTH | ||||
Sequence: RDRLSFLHRLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAP | ||||||
Region | 139-229 | Disordered | ||||
Sequence: LAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRTAVRHQPGQAGGGWDELDSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSGASREPG | ||||||
Compositional bias | 148-163 | Polar residues | ||||
Sequence: PPATGMGSQARPHSTL | ||||||
Compositional bias | 192-223 | Polar residues | ||||
Sequence: DSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSG | ||||||
Region | 355-465 | Disordered | ||||
Sequence: LSPARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPSEAEARLAESRRWRPERIPGGTDSPKRGPSSCAW | ||||||
Compositional bias | 389-408 | Polar residues | ||||
Sequence: VFLQPLSSTPVSSRSPAPSS | ||||||
Compositional bias | 409-427 | Pro residues | ||||
Sequence: GMPSSPVPTPPPDASPIPA | ||||||
Compositional bias | 435-452 | Basic and acidic residues | ||||
Sequence: EARLAESRRWRPERIPGG | ||||||
Region | 467-477 | Interaction with AP4B1 | ||||
Sequence: RDSLFAGMELV | ||||||
Region | 487-525 | Disordered | ||||
Sequence: AAAGESCPDAPRAPQTSSQRTAAKEPPGSEPSAFAFLNA | ||||||
Compositional bias | 497-511 | Polar residues | ||||
Sequence: PRAPQTSSQRTAAKE | ||||||
Region | 515-525 | Interaction with AP4E1 | ||||
Sequence: SEPSAFAFLNA |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q96N21-1
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
- Length525
- Mass (Da)55,137
- Last updated2001-12-01 v1
- ChecksumB79970A37B801549
Q96N21-2
- Name2
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1B0GV70 | A0A1B0GV70_HUMAN | TEPSIN | 593 | ||
I3L4S7 | I3L4S7_HUMAN | TEPSIN | 113 | ||
I3L4J0 | I3L4J0_HUMAN | TEPSIN | 97 | ||
I3L3R3 | I3L3R3_HUMAN | TEPSIN | 183 | ||
I3L3N1 | I3L3N1_HUMAN | TEPSIN | 52 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_025141 | 1-85 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 22 | In isoform Q96N21-2; in Ref. 1; BAC87593 | ||||
Sequence: R → H | ||||||
Alternative sequence | VSP_025142 | 86-175 | in isoform 2 | |||
Sequence: FFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRT → MGSQARPHSTLQGFGYSKEHGRTGSAGEAFLSTIQKAAEVVASAMRPGPESPSTRRLLPRGDTYQPAMMPSASHGPPTLGNLLPGAIPGPR | ||||||
Compositional bias | 148-163 | Polar residues | ||||
Sequence: PPATGMGSQARPHSTL | ||||||
Compositional bias | 192-223 | Polar residues | ||||
Sequence: DSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSG | ||||||
Compositional bias | 389-408 | Polar residues | ||||
Sequence: VFLQPLSSTPVSSRSPAPSS | ||||||
Compositional bias | 409-427 | Pro residues | ||||
Sequence: GMPSSPVPTPPPDASPIPA | ||||||
Compositional bias | 435-452 | Basic and acidic residues | ||||
Sequence: EARLAESRRWRPERIPGG | ||||||
Compositional bias | 497-511 | Polar residues | ||||
Sequence: PRAPQTSSQRTAAKE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK056090 EMBL· GenBank· DDBJ | BAB71091.1 EMBL· GenBank· DDBJ | mRNA | ||
AK127221 EMBL· GenBank· DDBJ | BAC86888.1 EMBL· GenBank· DDBJ | mRNA | ||
AK128728 EMBL· GenBank· DDBJ | BAC87593.1 EMBL· GenBank· DDBJ | mRNA | ||
BC064483 EMBL· GenBank· DDBJ | AAH64483.1 EMBL· GenBank· DDBJ | mRNA |