Q96QZ7 · MAGI1_HUMAN
- ProteinMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- GeneMAGI1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1491 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in coupling actin fibers to cell junctions in endothelial cells, via its interaction with AMOTL2 and CDH5 (By similarity).
May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity).
May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface (By similarity).
Features
Showing features for binding site.
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 | adherens junction | |
Cellular Component | bicellular tight junction | |
Cellular Component | cell junction | |
Cellular Component | cell periphery | |
Cellular Component | cell projection | |
Cellular Component | cell-cell junction | |
Cellular Component | cytoplasm | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | alpha-actinin binding | |
Molecular Function | ATP binding | |
Biological Process | cell adhesion | |
Biological Process | cell surface receptor signaling pathway | |
Biological Process | endothelial cell morphogenesis | |
Biological Process | positive regulation of cell-cell adhesion | |
Biological Process | protein-containing complex assembly | |
Biological Process | signal transduction |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96QZ7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Localizes to epithelial cells tight junctions.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000094589 | 1-1491 | UniProt | Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 | |||
Sequence: MSKVIQKKNHWTSRVHECTVKRGPQGELGVTVLGGAEHGEFPYVGAVAAVEAAGLPGGGEGPRLGEGELLLEVQGVRVSGLPRYDVLGVIDSCKEAVTFKAVRQGGRLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQQQQQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGEREREINSTNFGECPIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKTENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYDPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQAERAAAANGPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKECSTDLSI | |||||||
Modified residue | 357 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 730 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 730 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 741 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 800 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 938 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1071 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1361 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1412 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1490 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed with the exception of skeletal muscle. Isoform 1, isoform 2 and isoform 6 are highly expressed in colon, kidney, lung, liver, and pancreas. Isoform 5 is predominantly expressed in brain and heart. Isoform 3 and isoform 4 are highly expressed in pancreas and brain.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of a complex composed of AMOTL2, MAGI1 and CDH5, within the complex AMOTL2 acts as a scaffold protein for the interaction of MAGI1 with CDH5 (By similarity).
The complex is required for coupling actin fibers to cell junctions in endothelial cells (By similarity).
Interacts through its WW 2 domain with SYNPO and through its PDZ 5 domain with ACTN4 (PubMed:12042308).
Interacts with cytoplasmic domain of ADGRB1 (PubMed:9647739).
Interacts via its WW domains with DRPLA (PubMed:9647693).
Interacts with ESAM, LRP2 and CXADR (By similarity).
May interact with CTNNB1 (By similarity).
Interacts through its PDZ 1 domain with NET1 (By similarity).
Interacts with ASIC3 and AMOT (PubMed:15317815, PubMed:16043488).
Interacts with FCHSD2 (PubMed:14627983).
Interacts with IGSF5/JAM4 and through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex (By similarity) (PubMed:12773569).
Interacts with DDN (PubMed:16751601).
Interacts with DLL1 (By similarity).
Interacts with KCNJ10 and possibly with KCNJ10/KCNJ16 heterodimer; this interaction may facilitate KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane in kidney tubular cells. Interacts with PRRG4 (via cytoplasmic domain) (PubMed:23873930).
The complex is required for coupling actin fibers to cell junctions in endothelial cells (By similarity).
Interacts through its WW 2 domain with SYNPO and through its PDZ 5 domain with ACTN4 (PubMed:12042308).
Interacts with cytoplasmic domain of ADGRB1 (PubMed:9647739).
Interacts via its WW domains with DRPLA (PubMed:9647693).
Interacts with ESAM, LRP2 and CXADR (By similarity).
May interact with CTNNB1 (By similarity).
Interacts through its PDZ 1 domain with NET1 (By similarity).
Interacts with ASIC3 and AMOT (PubMed:15317815, PubMed:16043488).
Interacts with FCHSD2 (PubMed:14627983).
Interacts with IGSF5/JAM4 and through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex (By similarity) (PubMed:12773569).
Interacts with DDN (PubMed:16751601).
Interacts with DLL1 (By similarity).
Interacts with KCNJ10 and possibly with KCNJ10/KCNJ16 heterodimer; this interaction may facilitate KCNJ10/KCNJ16 potassium channel expression at the basolateral membrane in kidney tubular cells. Interacts with PRRG4 (via cytoplasmic domain) (PubMed:23873930).
Isoform 3
Interacts (via PDZ domain) with RAPGEF2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q96QZ7 | E6 P03126 | 2 | EBI-924464, EBI-1177242 | |
XENO | Q96QZ7 | E6 P06463 | 4 | EBI-924464, EBI-1186926 | |
BINARY | Q96QZ7 | FCHSD2 O94868 | 5 | EBI-924464, EBI-1215612 | |
BINARY | Q96QZ7 | IQGAP1 P46940 | 4 | EBI-924464, EBI-297509 | |
BINARY | Q96QZ7 | KIF1B O60333-3 | 3 | EBI-924464, EBI-465669 | |
XENO | Q96QZ7 | M P0DOF2 | 2 | EBI-924464, EBI-25567776 | |
BINARY | Q96QZ7 | PRRG4 Q9BZD6 | 2 | EBI-924464, EBI-3918643 | |
BINARY | Q96QZ7-3 | RAPGEF2 Q9Y4G8 | 2 | EBI-8769674, EBI-307079 | |
BINARY | Q96QZ7-3 | RASL11B Q9BPW5 | 3 | EBI-8769674, EBI-745409 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-105 | PDZ 1 | ||||
Sequence: ECTVKRGPQGELGVTVLGGAEHGEFPYVGAVAAVEAAGLPGGGEGPRLGEGELLLEVQGVRVSGLPRYDVLGVIDSCKEAVTFKAVRQG | ||||||
Domain | 96-287 | Guanylate kinase-like | ||||
Sequence: AVTFKAVRQGGRLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKF | ||||||
Region | 236-267 | Disordered | ||||
Sequence: AENEEEDDVPEMNSSFTADSGEQEEHTLQETA | ||||||
Domain | 300-333 | WW 1 | ||||
Sequence: GPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRC | ||||||
Domain | 359-392 | WW 2 | ||||
Sequence: LELPAGWEKIEDPVYGIYYVDHINRKTQYENPVL | ||||||
Compositional bias | 411-427 | Polar residues | ||||
Sequence: QQQQQQQQQQQTEEWTE | ||||||
Region | 411-462 | Disordered | ||||
Sequence: QQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRN | ||||||
Domain | 472-554 | PDZ 2 | ||||
Sequence: HTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCR | ||||||
Region | 586-623 | Disordered | ||||
Sequence: QETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHG | ||||||
Compositional bias | 587-601 | Polar residues | ||||
Sequence: ETYDSPASHSSKTGK | ||||||
Domain | 643-721 | PDZ 3 | ||||
Sequence: TVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQR | ||||||
Region | 720-832 | Disordered | ||||
Sequence: QRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGEREREINSTNFGEC | ||||||
Compositional bias | 737-766 | Polar residues | ||||
Sequence: ERKDSQNSSQHSVSSHRSLHTASPSHSTQV | ||||||
Domain | 813-895 | PDZ 4 | ||||
Sequence: SGLSKGEREREINSTNFGECPIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTP | ||||||
Region | 932-987 | Disordered | ||||
Sequence: TENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGS | ||||||
Compositional bias | 935-982 | Polar residues | ||||
Sequence: EVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSG | ||||||
Domain | 970-1066 | PDZ 5 | ||||
Sequence: SSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCS | ||||||
Region | 970-1066 | Interaction with FCHSD2 | ||||
Sequence: SSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCS | ||||||
Region | 1112-1143 | Disordered | ||||
Sequence: TTTHTPSQQGTQETRNTTKPKQESQFEFKAPQ | ||||||
Domain | 1124-1206 | PDZ 6 | ||||
Sequence: ETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGET | ||||||
Region | 1234-1491 | Disordered | ||||
Sequence: DGSVPEYDPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQAERAAAANGPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKECSTDLSI | ||||||
Compositional bias | 1281-1338 | Basic and acidic residues | ||||
Sequence: KSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQA | ||||||
Compositional bias | 1346-1485 | Basic and acidic residues | ||||
Sequence: GPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKEC |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q96QZ7-1
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
- SynonymsMAGI-1C-alpha-beta1
- Length1,491
- Mass (Da)164,581
- Last updated2009-12-15 v3
- Checksum4B2EE05243A6FA65
Q96QZ7-2
- Name2
- SynonymsMAGI-1C-beta
- Differences from canonical
- 806-834: PMSPSPASGLSKGEREREINSTNFGECPI → L
- 1027-1027: Missing
Q96QZ7-3
- Name3
- SynonymsMAGI-1A-alpha-beta1
- Differences from canonical
- 1241-1256: DPSSDRHGPATGPQGV → GGSNYENIPSFPGMTP
- 1257-1288: Missing
- 1289-1491: Missing
Q96QZ7-4
- Name4
- SynonymsMAGI-1A-alpha
- Differences from canonical
- 806-834: PMSPSPASGLSKGEREREINSTNFGECPI → L
- 1027-1027: Missing
- 1028-1038: Missing
- 1039-1094: Missing
- 1241-1256: DPSSDRHGPATGPQGV → GGSNYENIPSFPGMTP
- 1257-1288: Missing
- 1289-1491: Missing
Q96QZ7-5
- Name5
- SynonymsMAGI-1B-alpha-beta
- Differences from canonical
- 1027-1027: Missing
- 1241-1288: DPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEK → AMIPPNIAACMRNEKLGEACFYLMGHNQTTTPAATATAPPPVHKVFRK
- 1289-1491: Missing
Q96QZ7-6
- Name6
- SynonymsMAGI-1C-beta2
- Differences from canonical
- 806-834: PMSPSPASGLSKGEREREINSTNFGECPI → L
- 1027-1027: Missing
- 1028-1038: Missing
Q96QZ7-7
- Name7
- SynonymsMAGI-1C-beta3
- Differences from canonical
- 806-834: PMSPSPASGLSKGEREREINSTNFGECPI → L
- 1023-1099: GTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNA → VMQCQPPSWCHSALGGSKHCNSVMGAASLEVQIYSCNNP
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H7C5T8 | H7C5T8_HUMAN | MAGI1 | 1014 | ||
H7C4U7 | H7C4U7_HUMAN | MAGI1 | 1131 | ||
H7C4S7 | H7C4S7_HUMAN | MAGI1 | 185 | ||
H7C535 | H7C535_HUMAN | MAGI1 | 1136 | ||
A0A087WT53 | A0A087WT53_HUMAN | MAGI1 | 1155 | ||
A0A087WXD2 | A0A087WXD2_HUMAN | MAGI1 | 980 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 124 | in Ref. 1; BAA32002 and 2; AAK94064/AAK94065/AAK94066/AAC51326 | ||||
Sequence: S → F | ||||||
Compositional bias | 411-427 | Polar residues | ||||
Sequence: QQQQQQQQQQQTEEWTE | ||||||
Sequence conflict | 428 | in Ref. 3; BAF82492 | ||||
Sequence: D → H | ||||||
Compositional bias | 587-601 | Polar residues | ||||
Sequence: ETYDSPASHSSKTGK | ||||||
Compositional bias | 737-766 | Polar residues | ||||
Sequence: ERKDSQNSSQHSVSSHRSLHTASPSHSTQV | ||||||
Sequence conflict | 775 | in Ref. 5; AAC04844 | ||||
Sequence: A → G | ||||||
Alternative sequence | VSP_011664 | 806-834 | in isoform 2, isoform 4, isoform 6 and isoform 7 | |||
Sequence: PMSPSPASGLSKGEREREINSTNFGECPI → L | ||||||
Compositional bias | 935-982 | Polar residues | ||||
Sequence: EVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSG | ||||||
Sequence conflict | 1001 | in Ref. 3; BAF82492 | ||||
Sequence: I → T | ||||||
Alternative sequence | VSP_011665 | 1023-1099 | in isoform 7 | |||
Sequence: GTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNA → VMQCQPPSWCHSALGGSKHCNSVMGAASLEVQIYSCNNP | ||||||
Alternative sequence | VSP_011666 | 1027 | in isoform 2, isoform 4, isoform 5 and isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011667 | 1028-1038 | in isoform 4 and isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011668 | 1039-1094 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011670 | 1241-1256 | in isoform 3 and isoform 4 | |||
Sequence: DPSSDRHGPATGPQGV → GGSNYENIPSFPGMTP | ||||||
Alternative sequence | VSP_011669 | 1241-1288 | in isoform 5 | |||
Sequence: DPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEK → AMIPPNIAACMRNEKLGEACFYLMGHNQTTTPAATATAPPPVHKVFRK | ||||||
Alternative sequence | VSP_011671 | 1257-1288 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 1281-1338 | Basic and acidic residues | ||||
Sequence: KSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQA | ||||||
Alternative sequence | VSP_011672 | 1289-1491 | in isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 1346-1485 | Basic and acidic residues | ||||
Sequence: GPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKEC |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB010894 EMBL· GenBank· DDBJ | BAA32002.1 EMBL· GenBank· DDBJ | mRNA | ||
AF401655 EMBL· GenBank· DDBJ | AAK94065.1 EMBL· GenBank· DDBJ | mRNA | ||
AF401656 EMBL· GenBank· DDBJ | AAK94066.1 EMBL· GenBank· DDBJ | mRNA | ||
AF401654 EMBL· GenBank· DDBJ | AAK94064.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289803 EMBL· GenBank· DDBJ | BAF82492.1 EMBL· GenBank· DDBJ | mRNA | ||
AC104438 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC112516 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC121493 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC145425 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
U80754 EMBL· GenBank· DDBJ | AAC04844.1 EMBL· GenBank· DDBJ | mRNA | ||
U96115 EMBL· GenBank· DDBJ | AAC51326.1 EMBL· GenBank· DDBJ | mRNA | Different termination. |