Q96PC5 · MIA2_HUMAN
- ProteinMelanoma inhibitory activity protein 2
- GeneMIA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1412 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the secretion of lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their export from the endoplasmic reticulum (PubMed:27138255).
Thereby, may play a role in cholesterol and triglyceride homeostasis (By similarity).
Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites (PubMed:21525241, PubMed:25202031, PubMed:27170179).
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 exit site | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Molecular Function | cargo receptor activity | |
Molecular Function | enzyme activator activity | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | lipoprotein transport | |
Biological Process | protein exit from endoplasmic reticulum | |
Biological Process | protein localization to endoplasmic reticulum exit site | |
Biological Process | protein secretion | |
Biological Process | vesicle cargo loading |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMelanoma inhibitory activity protein 2
- Short namesMIA protein 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 accessionQ96PC5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, intramembrane, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-605 | Lumenal | ||||
Sequence: LESTKLLADLKKCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVFISEEIQMSTKESDFLCLLGVSYTFDNEDSELNGDYGENIYPYEEDKDEKSSIYESDFQIEPGFYATYESTLFEDQVPALEAPEDIGSTSESKDWEEVVVESMEQDRIPEVHVPPSSAVSGVKEWFGLGGEQAEEKAFESVIEPVQESSFRSRKIAVEDENDLEELNNGEPQTEHQQESESEIDSVPKTQSELASESEHIPKPQSTGWFGGGFTSYLGFGDEDTGLELIAEESNPPLQDFPNSISSDKEATVPCTEILTEKKDTITNDSLSLKPSWFDFGFAILGFAYAKEDKIMLDDRKNEEDGGADEHEHPLTSELDPEKEQEIETIKIIETEDQIDKKPVSEKTDESDTIPYLKKFLYNFDNPWNFQNIPKETELPFPKQILDQNNVIENEETGEFSIDNYPTDNTKVMIFKSSYSLSDMVSNIELPTRIHEEVYFEPSSSKDSDENSKPSVDTEGPALVEIDRSVENTLLNSQMVSTDNSLSSQNYISQKEDASEFQILK | ||||||
Intramembrane | 606-626 | |||||
Sequence: YLFQIDVYDFMNSAFSPIVIL | ||||||
Topological domain | 627-646 | Lumenal | ||||
Sequence: TERVVAALPEGMRPDSNLYG | ||||||
Transmembrane | 647-667 | Helical | ||||
Sequence: FPWELVICAAVVGFFAVLFFL | ||||||
Topological domain | 668-1412 | Cytoplasmic | ||||
Sequence: WRSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVPNTAFGREHSPYGPSPLGWPSSETRAFLSPPTLLEGPLRLSPLLPGGGGRGSRGPGNPLDHQITNERGESSCDRLTDPHRAPSDTGSLSPPWDQDRRMMFPPPGQSYPDSALPPQRQDRFCSNSGRLSGPAELRSFNMPSLDKMDGSMPSEMESSRNDTKDDLGNLNVPDSSLPAENEATGPGFVPPPLAPIRGPLFPVDARGPFLRRGPPFPPPPPGAMFGASRDYFPPGDFPGPPPAPFAMRNVYPPRGFPPYLPPRPGFFPPPPHSEGRSEFPSGLIPPSNEPATEHPEPQQET |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_082860 | 6 | In isoform Q96PC5-7; in dbSNP:rs7140561 | |||
Sequence: V → A | ||||||
Natural variant | VAR_082861 | 6 | In isoform Q96PC5-8; in dbSNP:rs7140561 | |||
Sequence: V → A | ||||||
Natural variant | VAR_082862 | 6 | In isoform Q96PC5-10; in dbSNP:rs7140561 | |||
Sequence: V → A | ||||||
Natural variant | VAR_082863 | 6 | In isoform Q96PC5-12; in dbSNP:rs7140561 | |||
Sequence: V → A | ||||||
Natural variant | VAR_082864 | 11 | In isoform Q96PC5-12; in dbSNP:rs17855895 | |||
Sequence: Y → D | ||||||
Natural variant | VAR_036460 | 437 | in a breast cancer sample; somatic mutation | |||
Sequence: D → H | ||||||
Mutagenesis | 679 | No effect on interaction with PERB. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 697 | Loss of interaction with PERB. Unable to recruit PERB to the endoplasmic reticulum exit sites. Loss of function in collagen VII transport. No effect on interaction with MIA3. | ||||
Sequence: K → A | ||||||
Mutagenesis | 705 | Decreased interaction with PERB. No effect on interaction with MIA3. | ||||
Sequence: S → A | ||||||
Mutagenesis | 720 | No effect on interaction with PERB. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_047891 | 813 | in dbSNP:rs17855896 | |||
Sequence: K → N | ||||||
Natural variant | VAR_047892 | 858 | in dbSNP:rs10162564 | |||
Sequence: K → E | ||||||
Natural variant | VAR_047893 | 968 | in dbSNP:rs1950952 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_047894 | 983 | in dbSNP:rs17109109 | |||
Sequence: N → S | ||||||
Natural variant | VAR_047895 | 1307 | in dbSNP:rs1140952 | |||
Sequence: I → V | ||||||
Natural variant | VAR_047896 | 1346 | in dbSNP:rs1060878 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,929 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-19 | UniProt | |||||
Sequence: MAKFGVHRILLLAISLTKC | |||||||
Chain | PRO_0000019031 | 20-1412 | UniProt | Melanoma inhibitory activity protein 2 | |||
Sequence: LESTKLLADLKKCGDLECEALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEVFISEEIQMSTKESDFLCLLGVSYTFDNEDSELNGDYGENIYPYEEDKDEKSSIYESDFQIEPGFYATYESTLFEDQVPALEAPEDIGSTSESKDWEEVVVESMEQDRIPEVHVPPSSAVSGVKEWFGLGGEQAEEKAFESVIEPVQESSFRSRKIAVEDENDLEELNNGEPQTEHQQESESEIDSVPKTQSELASESEHIPKPQSTGWFGGGFTSYLGFGDEDTGLELIAEESNPPLQDFPNSISSDKEATVPCTEILTEKKDTITNDSLSLKPSWFDFGFAILGFAYAKEDKIMLDDRKNEEDGGADEHEHPLTSELDPEKEQEIETIKIIETEDQIDKKPVSEKTDESDTIPYLKKFLYNFDNPWNFQNIPKETELPFPKQILDQNNVIENEETGEFSIDNYPTDNTKVMIFKSSYSLSDMVSNIELPTRIHEEVYFEPSSSKDSDENSKPSVDTEGPALVEIDRSVENTLLNSQMVSTDNSLSSQNYISQKEDASEFQILKYLFQIDVYDFMNSAFSPIVILTERVVAALPEGMRPDSNLYGFPWELVICAAVVGFFAVLFFLWRSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVPNTAFGREHSPYGPSPLGWPSSETRAFLSPPTLLEGPLRLSPLLPGGGGRGSRGPGNPLDHQITNERGESSCDRLTDPHRAPSDTGSLSPPWDQDRRMMFPPPGQSYPDSALPPQRQDRFCSNSGRLSGPAELRSFNMPSLDKMDGSMPSEMESSRNDTKDDLGNLNVPDSSLPAENEATGPGFVPPPLAPIRGPLFPVDARGPFLRRGPPFPPPPPGAMFGASRDYFPPGDFPGPPPAPFAMRNVYPPRGFPPYLPPRPGFFPPPPHSEGRSEFPSGLIPPSNEPATEHPEPQQET | |||||||
Glycosylation | 59 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 368 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 734 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 745 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 747 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1111 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1118 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1127 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1130 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1147 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1186 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1191 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1200 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1237 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1239 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1243 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1262 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1 is specifically expressed in lung, testis, small intestine, colon, pancreas, kidney, liver and prostate (PubMed:27138255).
Isoform 8 is expressed only in testis (at the protein level). Isoform 8 (at protein level) and isoform 9 are expressed in cutaneous T-cell lymphoma (CTCL) cell lines, colorectal carcinomas, breast carcinomas and melanoma. Isoform 9, but not isoform 5A, is expressed in head and neck squamous cell carcinoma (PubMed:12839582).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the COPII coat subunits SEC23A, SEC23B and maybe SEC24C (PubMed:21525241, PubMed:27551091).
Interacts with PREB; recruits PREB to endoplasmic reticulum exit sites (PubMed:25202031, PubMed:27170179).
Interacts with APOB (PubMed:27138255).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96PC5 | CCHCR1 Q8TD31-3 | 3 | EBI-1050253, EBI-10175300 | |
BINARY | Q96PC5 | CEP57 Q86XR8 | 3 | EBI-1050253, EBI-308614 | |
BINARY | Q96PC5 | EMILIN1 Q9Y6C2 | 3 | EBI-1050253, EBI-744586 | |
BINARY | Q96PC5 | MAGEB18 Q96M61 | 3 | EBI-1050253, EBI-741835 | |
BINARY | Q96PC5 | PSMA3 P25788 | 3 | EBI-1050253, EBI-348380 | |
BINARY | Q96PC5 | RASAL2 Q9UJF2 | 3 | EBI-1050253, EBI-359444 | |
BINARY | Q96PC5 | SS18L1 O75177 | 3 | EBI-1050253, EBI-744674 | |
BINARY | Q96PC5 | TLE5 Q08117 | 3 | EBI-1050253, EBI-717810 | |
BINARY | Q96PC5 | TTC23L Q6PF05-3 | 3 | EBI-1050253, EBI-10182647 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-101 | SH3 | ||||
Sequence: ALINRVSAMRDYRGPDCRYLNFTKGEEISVYVKLAGEREDLWAGSKGKEFGYFPRDAVQIEEV | ||||||
Region | 260-308 | Disordered | ||||
Sequence: DENDLEELNNGEPQTEHQQESESEIDSVPKTQSELASESEHIPKPQSTG | ||||||
Compositional bias | 269-283 | Basic and acidic residues | ||||
Sequence: NGEPQTEHQQESESE | ||||||
Compositional bias | 284-303 | Polar residues | ||||
Sequence: IDSVPKTQSELASESEHIPK | ||||||
Region | 401-424 | Disordered | ||||
Sequence: KNEEDGGADEHEHPLTSELDPEKE | ||||||
Compositional bias | 540-554 | Basic and acidic residues | ||||
Sequence: FEPSSSKDSDENSKP | ||||||
Region | 540-562 | Disordered | ||||
Sequence: FEPSSSKDSDENSKPSVDTEGPA | ||||||
Region | 669-1258 | Mediates interaction with MIA3 | ||||
Sequence: RSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVPNTAFGREHSPYGPSPLGWPSSETRAFLSPPTLLEGPLRLSPLLPGGGGRGSRGPGNPLDHQITNERGESSCDRLTDPHRAPSDTGSLSPPWDQDRRMMFPPPGQSYPDSALPPQRQDRFCSNSGRLSGPAELRSFNMPSLDK | ||||||
Coiled coil | 725-850 | |||||
Sequence: FEKEATEAQSLEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ | ||||||
Coiled coil | 948-1102 | |||||
Sequence: LSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELK | ||||||
Region | 1153-1304 | Disordered | ||||
Sequence: LRLSPLLPGGGGRGSRGPGNPLDHQITNERGESSCDRLTDPHRAPSDTGSLSPPWDQDRRMMFPPPGQSYPDSALPPQRQDRFCSNSGRLSGPAELRSFNMPSLDKMDGSMPSEMESSRNDTKDDLGNLNVPDSSLPAENEATGPGFVPPPL | ||||||
Compositional bias | 1181-1195 | Basic and acidic residues | ||||
Sequence: ERGESSCDRLTDPHR | ||||||
Compositional bias | 1225-1245 | Polar residues | ||||
Sequence: SALPPQRQDRFCSNSGRLSGP | ||||||
Region | 1259-1412 | Proline-rich domain (PRD); mediates interaction with the COPII coat subunits SEC23A and SEC23B | ||||
Sequence: MDGSMPSEMESSRNDTKDDLGNLNVPDSSLPAENEATGPGFVPPPLAPIRGPLFPVDARGPFLRRGPPFPPPPPGAMFGASRDYFPPGDFPGPPPAPFAMRNVYPPRGFPPYLPPRPGFFPPPPHSEGRSEFPSGLIPPSNEPATEHPEPQQET | ||||||
Region | 1316-1412 | Disordered | ||||
Sequence: ARGPFLRRGPPFPPPPPGAMFGASRDYFPPGDFPGPPPAPFAMRNVYPPRGFPPYLPPRPGFFPPPPHSEGRSEFPSGLIPPSNEPATEHPEPQQET | ||||||
Compositional bias | 1345-1359 | Pro residues | ||||
Sequence: PGDFPGPPPAPFAMR | ||||||
Compositional bias | 1365-1386 | Pro residues | ||||
Sequence: RGFPPYLPPRPGFFPPPPHSEG |
Domain
The coiled coil domains mediate interaction with MIA3 (PubMed:21525241).
The first coiled coil domain mediates interaction with PREB (PubMed:25202031).
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 12 isoforms produced by Alternative splicing.
Q96PC5-3
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
- SynonymsTALI
- NoteReadthrough transcript producing a functional fusion protein MIA2-CTAGE5 with similarity to MIA3.
- Length1,412
- Mass (Da)159,836
- Last updated2016-09-07 v4
- ChecksumE870056BF9D5A0B2
Q96PC5-2
- Name2
Q96PC5-5
- Name4
- Differences from canonical
- 1-637: Missing
- 1123-1165: Missing
Q96PC5-6
- Name5
- Differences from canonical
- 1-620: Missing
- 621-629: SPIVILTER → MELKSPEEE
- 711-736: Missing
- 1255-1325: Missing
- 1333-1355: Missing
Q96PC5-7
- Name6
- SynonymsMEA6
Q96PC5-8
- Name7
- SynonymsMEA11
- Differences from canonical
- 1-608: Missing
- 609-628: QIDVYDFMNSAFSPIVILTE → MEEPGVTPQPYLGLLLEELR
- 1123-1165: Missing
Q96PC5-9
- Name8
- Synonyms5A
- Differences from canonical
- 1-637: Missing
Q96PC5-10
- Name9
- Synonyms5B
- Differences from canonical
- 1-608: Missing
- 609-628: QIDVYDFMNSAFSPIVILTE → MEEPGVTPQPYLGLLLEELR
- 1358-1379: MRNVYPPRGFPPYLPPRPGFFP → SARSPPGAGAPASGRGLGGPQK
- 1380-1412: Missing
Q96PC5-11
- Name10
- Differences from canonical
- 1-688: Missing
Q96PC5-12
- Name11
Q96PC5-13
- Name12
Q96PC5-14
- Name13
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_060006 | 1-608 | in isoform 6, isoform 7, isoform 9 and isoform 11 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060005 | 1-620 | in isoform 5 and isoform 13 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060004 | 1-637 | in isoform 4 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060003 | 1-688 | in isoform 10 and isoform 12 | |||
Sequence: Missing | ||||||
Sequence conflict | 83 | in Ref. 9; AAL26990 | ||||
Sequence: Missing | ||||||
Compositional bias | 269-283 | Basic and acidic residues | ||||
Sequence: NGEPQTEHQQESESE | ||||||
Compositional bias | 284-303 | Polar residues | ||||
Sequence: IDSVPKTQSELASESEHIPK | ||||||
Compositional bias | 540-554 | Basic and acidic residues | ||||
Sequence: FEPSSSKDSDENSKP | ||||||
Alternative sequence | VSP_060007 | 609-628 | in isoform 6, isoform 7, isoform 9 and isoform 11 | |||
Sequence: QIDVYDFMNSAFSPIVILTE → MEEPGVTPQPYLGLLLEELR | ||||||
Alternative sequence | VSP_060008 | 621-629 | in isoform 5 and isoform 13 | |||
Sequence: SPIVILTER → MELKSPEEE | ||||||
Alternative sequence | VSP_058472 | 631-654 | in isoform 2 | |||
Sequence: VAALPEGMRPDSNLYGFPWELVIC → SLPFKPFAIILPILLNIRVATKYV | ||||||
Alternative sequence | VSP_058473 | 655-1412 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 698 | in Ref. 5; CAE45997 | ||||
Sequence: S → N | ||||||
Alternative sequence | VSP_060009 | 711-736 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060010 | 736 | in isoform 11 and isoform 12 | |||
Sequence: E → EVENQM | ||||||
Sequence conflict | 753 | in Ref. 5; CAE45997 | ||||
Sequence: I → M | ||||||
Sequence conflict | 803 | in Ref. 1; AAB86589/AAB86593 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 806 | in Ref. 1; AAB86593 | ||||
Sequence: Q → P | ||||||
Alternative sequence | VSP_060011 | 1123-1165 | in isoform 4 and isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 1154 | in Ref. 1; AAB86593 | ||||
Sequence: R → T | ||||||
Compositional bias | 1181-1195 | Basic and acidic residues | ||||
Sequence: ERGESSCDRLTDPHR | ||||||
Sequence conflict | 1197 | in Ref. 1; AAB86593 | ||||
Sequence: P → L | ||||||
Sequence conflict | 1202 | in Ref. 1; AAB86593 | ||||
Sequence: S → F | ||||||
Sequence conflict | 1212 | in Ref. 2; AAN77610 | ||||
Sequence: R → M | ||||||
Compositional bias | 1225-1245 | Polar residues | ||||
Sequence: SALPPQRQDRFCSNSGRLSGP | ||||||
Alternative sequence | VSP_060012 | 1255-1325 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060013 | 1333-1355 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 1345-1359 | Pro residues | ||||
Sequence: PGDFPGPPPAPFAMR | ||||||
Alternative sequence | VSP_060014 | 1358-1379 | in isoform 9 | |||
Sequence: MRNVYPPRGFPPYLPPRPGFFP → SARSPPGAGAPASGRGLGGPQK | ||||||
Compositional bias | 1365-1386 | Pro residues | ||||
Sequence: RGFPPYLPPRPGFFPPPPHSEG | ||||||
Alternative sequence | VSP_060015 | 1380-1412 | in isoform 9 | |||
Sequence: Missing | ||||||
Sequence conflict | 1384 | in Ref. 2; AAN77610 | ||||
Sequence: S → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73682 EMBL· GenBank· DDBJ | AAB86589.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U94780 EMBL· GenBank· DDBJ | AAB86593.1 EMBL· GenBank· DDBJ | mRNA | ||
AF338233 EMBL· GenBank· DDBJ | AAN77610.1 EMBL· GenBank· DDBJ | mRNA | ||
AF338234 EMBL· GenBank· DDBJ | AAN77611.1 EMBL· GenBank· DDBJ | mRNA | ||
KX388743 EMBL· GenBank· DDBJ | ANN89694.1 EMBL· GenBank· DDBJ | mRNA | ||
AK026057 EMBL· GenBank· DDBJ | BAB15339.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK091252 EMBL· GenBank· DDBJ | BAG52318.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298935 EMBL· GenBank· DDBJ | BAG61038.1 EMBL· GenBank· DDBJ | mRNA | ||
BX640994 EMBL· GenBank· DDBJ | CAE45997.1 EMBL· GenBank· DDBJ | mRNA | ||
AL132639 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL157791 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471078 EMBL· GenBank· DDBJ | EAW65808.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65812.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65813.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65814.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65818.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC051363 EMBL· GenBank· DDBJ | AAH51363.2 EMBL· GenBank· DDBJ | mRNA | ||
BC064355 EMBL· GenBank· DDBJ | AAH64355.1 EMBL· GenBank· DDBJ | mRNA | ||
BC130537 EMBL· GenBank· DDBJ | AAI30538.1 EMBL· GenBank· DDBJ | mRNA | ||
BC130563 EMBL· GenBank· DDBJ | AAI30564.1 EMBL· GenBank· DDBJ | mRNA | ||
AF390175 EMBL· GenBank· DDBJ | AAL26990.2 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |