Q86UR5 · RIMS1_HUMAN
- ProteinRegulating synaptic membrane exocytosis protein 1
- GeneRIMS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1692 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity).
Plays a role in dendrite formation by melanocytes (PubMed:23999003).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 116 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 119 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 132 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 135 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 140 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 143 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 162 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 165 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
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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Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegulating synaptic membrane exocytosis 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 accessionQ86UR5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 796-797 | Abolishes interaction with SYT1 and CACNA1B. | ||||
Sequence: RR → AA | ||||||
Natural variant | VAR_016804 | 820 | found in a family with cone-rod dystrophy; uncertain significance; dbSNP:rs121918302 | |||
Sequence: R → H | ||||||
Mutagenesis | 1591-1592 | Abolishes interaction with SYT1 and CACNA1B. | ||||
Sequence: KK → AA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,169 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
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_0000190198 | 1-1692 | UniProt | Regulating synaptic membrane exocytosis protein 1 | |||
Sequence: MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEKGDLDYYWLDPATWHSRETSPISSHPVTWQPSKEGDRLIGRVILNKRTTMPKDSGALLGLKVVGGKMTDLGRLGAFITKVKKGSLADVVGHLRAGDEVLEWNGKPLPGATNEEVYNIILESKSEPQVEIIVSRPIGDIPRIPESSHPPLESSSSSFESQKMERPSISVISPTSPGALKDAPQVLPGQLSVKLWYDKVGHQLIVNVLQATDLPARVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKILEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQEEESEFLGEILIELETALLDDEPHWYKLQTHDESSLPLPQPSPFMPRRHIHGESSSKKLQRSQRISDSDISDYEVDDGIGVVPPVGYRSSARESKSTTLTVPEQQRTTHHRSRSVSPHRGNDQGKPRSRLPNVPLQRSLDEIHPTRRSRSPTRHHDASRSPVDHRTRDVDSQYLSEQDSELLMLPRAKRGRSAECLHTTRHLVRHYKTLPPKMPLLQSSSHWNIYSSILPAHTKTKSVTRQDISLHHECFNSTVLRFTDEILVSELQPFLDRARSASTNCLRPDTSLHSPERERGRWSPSLDRRRPPSPRIQIQHASPENDRHSRKSERSSIQKQTRKGTASDAERVLPTCLSRRGHAAPRATDQPVIRGKHPARSRSSEHSSIRTLCSMHHLVPGGSAPPSPLLTRMHRQRSPTQSPPADTSFSSRRGRQLPQVPVRSGSIEQASLVVEERTRQMKMKVHRFKQTTGSGSSQELDREQYSKYNIHKDQYRSCDNVSAKSSDSDVSDVSAISRTSSASRLSSTSFMSEQSERPRGRISSFTPKMQGRRMGTSGRSIMKSTSVSGEMYTLEHNDGSQSDTAVGTVGAGGKKRRSSLSAKVVAIVSRRSRSTSQLSQTESGHKKLKSTIQRSTETGMAAEMRKMVRQPSRESTDGSINSYSSEGNLIFPGVRLGADSQFSDFLDGLGPAQLVGRQTLATPAMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQILLEELDLSSMVIGWYKLFPPSSLVDPTLTPLTRRASQSSLESSTGPPCIRS | |||||||
Modified residue (large scale data) | 324 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 448 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 500 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 578 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 728 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 731 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 731 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 881 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 881 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 977 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 977 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 999 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1031 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1252 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1254 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1254 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1256 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1308 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1310 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1311 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1331 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1339 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1340 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1342 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1407 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1416 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1416 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1450 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1489 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1490 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1613 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1677 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1677 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1679 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1680 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1683 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1683 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1692 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1692 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds SNAP25, SYT1 and CACNA1B. Interaction with SYT1 is enhanced by calcium ions. Interaction with SNAP25 is weaker in the presence of calcium ions
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86UR5 | ABL1 P00519 | 2 | EBI-1043236, EBI-375543 | |
BINARY | Q86UR5 | FXR1 P51114 | 2 | EBI-1043236, EBI-713291 | |
BINARY | Q86UR5 | FYN P06241 | 2 | EBI-1043236, EBI-515315 | |
BINARY | Q86UR5 | GABBR2 O75899 | 2 | EBI-1043236, EBI-715469 | |
BINARY | Q86UR5 | MARK3 P27448 | 3 | EBI-1043236, EBI-707595 | |
BINARY | Q86UR5 | RALY Q9UKM9 | 2 | EBI-1043236, EBI-714796 | |
BINARY | Q86UR5 | SRPK2 P78362 | 3 | EBI-1043236, EBI-593303 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MSSAVGPRGPRPPTVPPPMQELPDLS | ||||||
Domain | 22-182 | RabBD | ||||
Sequence: LPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGS | ||||||
Zinc finger | 110-170 | FYVE-type | ||||
Sequence: KDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQE | ||||||
Compositional bias | 183-199 | Polar residues | ||||
Sequence: GPQQTSQDGTLSDTATG | ||||||
Region | 183-555 | Disordered | ||||
Sequence: GPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESES | ||||||
Compositional bias | 216-231 | Polar residues | ||||
Sequence: SRSQTPLSTAAASSQD | ||||||
Compositional bias | 262-277 | Basic and acidic residues | ||||
Sequence: RSRSEPPRERKKTPGL | ||||||
Compositional bias | 284-356 | Basic and acidic residues | ||||
Sequence: GALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYR | ||||||
Compositional bias | 373-395 | Basic and acidic residues | ||||
Sequence: QQMRMHARVSRARHERRHSDVAL | ||||||
Compositional bias | 482-497 | Basic and acidic residues | ||||
Sequence: VLMRKAKREKVETMLR | ||||||
Compositional bias | 498-512 | Polar residues | ||||
Sequence: NDSLSSDQSESVRPS | ||||||
Domain | 605-691 | PDZ | ||||
Sequence: RTTMPKDSGALLGLKVVGGKMTDLGRLGAFITKVKKGSLADVVGHLRAGDEVLEWNGKPLPGATNEEVYNIILESKSEPQVEIIVSR | ||||||
Region | 698-732 | Disordered | ||||
Sequence: RIPESSHPPLESSSSSFESQKMERPSISVISPTSP | ||||||
Compositional bias | 704-730 | Polar residues | ||||
Sequence: HPPLESSSSSFESQKMERPSISVISPT | ||||||
Domain | 742-865 | C2 1 | ||||
Sequence: LPGQLSVKLWYDKVGHQLIVNVLQATDLPARVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKILEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQEEESEFLGEILIELETALLDDEPHWY | ||||||
Region | 870-1013 | Disordered | ||||
Sequence: HDESSLPLPQPSPFMPRRHIHGESSSKKLQRSQRISDSDISDYEVDDGIGVVPPVGYRSSARESKSTTLTVPEQQRTTHHRSRSVSPHRGNDQGKPRSRLPNVPLQRSLDEIHPTRRSRSPTRHHDASRSPVDHRTRDVDSQYL | ||||||
Compositional bias | 889-910 | Basic and acidic residues | ||||
Sequence: IHGESSSKKLQRSQRISDSDIS | ||||||
Compositional bias | 929-944 | Polar residues | ||||
Sequence: SARESKSTTLTVPEQQ | ||||||
Compositional bias | 945-964 | Basic and acidic residues | ||||
Sequence: RTTHHRSRSVSPHRGNDQGK | ||||||
Compositional bias | 993-1013 | Basic and acidic residues | ||||
Sequence: HHDASRSPVDHRTRDVDSQYL | ||||||
Region | 1118-1222 | Disordered | ||||
Sequence: NCLRPDTSLHSPERERGRWSPSLDRRRPPSPRIQIQHASPENDRHSRKSERSSIQKQTRKGTASDAERVLPTCLSRRGHAAPRATDQPVIRGKHPARSRSSEHSS | ||||||
Compositional bias | 1125-1142 | Basic and acidic residues | ||||
Sequence: SLHSPERERGRWSPSLDR | ||||||
Compositional bias | 1155-1172 | Basic and acidic residues | ||||
Sequence: ASPENDRHSRKSERSSIQ | ||||||
Region | 1235-1278 | Disordered | ||||
Sequence: GGSAPPSPLLTRMHRQRSPTQSPPADTSFSSRRGRQLPQVPVRS | ||||||
Compositional bias | 1247-1278 | Polar residues | ||||
Sequence: MHRQRSPTQSPPADTSFSSRRGRQLPQVPVRS | ||||||
Region | 1332-1394 | Disordered | ||||
Sequence: CDNVSAKSSDSDVSDVSAISRTSSASRLSSTSFMSEQSERPRGRISSFTPKMQGRRMGTSGRS | ||||||
Compositional bias | 1333-1375 | Polar residues | ||||
Sequence: DNVSAKSSDSDVSDVSAISRTSSASRLSSTSFMSEQSERPRGR | ||||||
Region | 1408-1428 | Disordered | ||||
Sequence: LEHNDGSQSDTAVGTVGAGGK | ||||||
Compositional bias | 1445-1460 | Polar residues | ||||
Sequence: RSRSTSQLSQTESGHK | ||||||
Region | 1445-1495 | Disordered | ||||
Sequence: RSRSTSQLSQTESGHKKLKSTIQRSTETGMAAEMRKMVRQPSRESTDGSIN | ||||||
Domain | 1538-1656 | C2 2 | ||||
Sequence: AMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQILLEELDLSSMVIGWY |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 13 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q86UR5-1
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
- SynonymsRIM1 alpha
- Length1,692
- Mass (Da)189,073
- Last updated2003-06-01 v1
- Checksum0A96642DC832C15E
Q86UR5-2
- Name2
- SynonymsRIM short form
- NoteMay be due to intron retention.
- Differences from canonical
- 1040-1692: Missing
Q86UR5-3
- Name3
- SynonymsRIM long form, Rab3 interacting protein variant 2
- Differences from canonical
- 1039-1102: Missing
- 1133-1245: Missing
- 1540-1573: Missing
Q86UR5-4
- Name4
- SynonymsRab3 interacting protein variant 1
- Differences from canonical
- 1065-1102: Missing
- 1133-1245: Missing
Q86UR5-5
- Name5
- SynonymsRab3 interacting protein variant 3
- Differences from canonical
- 924-924: Missing
- 1038-1244: Missing
- 1377-1385: Missing
Q86UR5-6
- Name6
- SynonymsRab3 interacting protein variant 4
- Differences from canonical
- 1039-1102: Missing
- 1161-1245: Missing
- 1284-1455: Missing
Q86UR5-7
- Name7
- SynonymsRab3 interacting protein variant 5
- Differences from canonical
- 924-924: Missing
- 1039-1102: Missing
- 1133-1245: Missing
- 1284-1455: Missing
Q86UR5-8
- Name8
- SynonymsRab3 interacting protein variant 6
- Differences from canonical
- 924-924: Missing
- 1018-1245: Missing
- 1284-1455: Missing
Q86UR5-9
- Name9
- Differences from canonical
- 1-18: MSSAVGPRGPRPPTVPPP → MFAGFLQFLLLHTLHSGT
- 19-559: Missing
- 1039-1102: Missing
- 1133-1160: Missing
- 1185-1245: Missing
- 1284-1455: Missing
Q86UR5-10
- Name10
- Differences from canonical
- 1-607: Missing
- 1039-1102: Missing
- 1133-1160: Missing
- 1185-1245: Missing
- 1284-1455: Missing
Q86UR5-11
- Name11
- Differences from canonical
- 1-1473: Missing
Q86UR5-12
- Name12
- Differences from canonical
- 1-559: MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEK → MCAPGIHVSSEGWEEVRSVDSEEGTIEARRAVA
- 924-924: Missing
- 1039-1102: Missing
- 1133-1160: Missing
- 1185-1245: Missing
Q86UR5-13
- Name13
- Differences from canonical
- 1-559: MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEK → MCAPGIHVSSEGWEEVRSVDSEEGTIEARRAVA
- 1039-1102: Missing
- 1133-1245: Missing
- 1284-1455: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YBU6 | H0YBU6_HUMAN | RIMS1 | 1038 | ||
H0YBE7 | H0YBE7_HUMAN | RIMS1 | 610 | ||
A0A8V8TKU9 | A0A8V8TKU9_HUMAN | RIMS1 | 1515 | ||
E5RGM0 | E5RGM0_HUMAN | RIMS1 | 753 | ||
A0A0C4DFV1 | A0A0C4DFV1_HUMAN | RIMS1 | 740 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043177 | 1-18 | in isoform 9 | |||
Sequence: MSSAVGPRGPRPPTVPPP → MFAGFLQFLLLHTLHSGT | ||||||
Alternative sequence | VSP_046796 | 1-559 | in isoform 12 and isoform 13 | |||
Sequence: MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEK → MCAPGIHVSSEGWEEVRSVDSEEGTIEARRAVA | ||||||
Alternative sequence | VSP_045486 | 1-607 | in isoform 10 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045485 | 1-1473 | in isoform 11 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043178 | 19-559 | in isoform 9 | |||
Sequence: Missing | ||||||
Sequence conflict | 157 | in Ref. 5; CAI16961 | ||||
Sequence: V → Y | ||||||
Compositional bias | 183-199 | Polar residues | ||||
Sequence: GPQQTSQDGTLSDTATG | ||||||
Compositional bias | 216-231 | Polar residues | ||||
Sequence: SRSQTPLSTAAASSQD | ||||||
Compositional bias | 262-277 | Basic and acidic residues | ||||
Sequence: RSRSEPPRERKKTPGL | ||||||
Compositional bias | 284-356 | Basic and acidic residues | ||||
Sequence: GALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYR | ||||||
Compositional bias | 373-395 | Basic and acidic residues | ||||
Sequence: QQMRMHARVSRARHERRHSDVAL | ||||||
Compositional bias | 482-497 | Basic and acidic residues | ||||
Sequence: VLMRKAKREKVETMLR | ||||||
Sequence conflict | 484-494 | in Ref. 2; BAB87121/BAB87242, 3; BAA20798 and 6; AAI51854/AAI52436 | ||||
Sequence: Missing | ||||||
Compositional bias | 498-512 | Polar residues | ||||
Sequence: NDSLSSDQSESVRPS | ||||||
Compositional bias | 704-730 | Polar residues | ||||
Sequence: HPPLESSSSSFESQKMERPSISVISPT | ||||||
Compositional bias | 889-910 | Basic and acidic residues | ||||
Sequence: IHGESSSKKLQRSQRISDSDIS | ||||||
Alternative sequence | VSP_008161 | 924 | in isoform 5, isoform 7, isoform 8 and isoform 12 | |||
Sequence: Missing | ||||||
Compositional bias | 929-944 | Polar residues | ||||
Sequence: SARESKSTTLTVPEQQ | ||||||
Compositional bias | 945-964 | Basic and acidic residues | ||||
Sequence: RTTHHRSRSVSPHRGNDQGK | ||||||
Compositional bias | 993-1013 | Basic and acidic residues | ||||
Sequence: HHDASRSPVDHRTRDVDSQYL | ||||||
Alternative sequence | VSP_008162 | 1018-1245 | in isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008163 | 1038-1244 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008164 | 1039-1102 | in isoform 3, isoform 6, isoform 7, isoform 9, isoform 10, isoform 12 and isoform 13 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008165 | 1040-1692 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008166 | 1065-1102 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 1125-1142 | Basic and acidic residues | ||||
Sequence: SLHSPERERGRWSPSLDR | ||||||
Alternative sequence | VSP_043179 | 1133-1160 | in isoform 9, isoform 10 and isoform 12 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008167 | 1133-1245 | in isoform 3, isoform 4, isoform 7 and isoform 13 | |||
Sequence: Missing | ||||||
Compositional bias | 1155-1172 | Basic and acidic residues | ||||
Sequence: ASPENDRHSRKSERSSIQ | ||||||
Alternative sequence | VSP_008168 | 1161-1245 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043180 | 1185-1245 | in isoform 9, isoform 10 and isoform 12 | |||
Sequence: Missing | ||||||
Compositional bias | 1247-1278 | Polar residues | ||||
Sequence: MHRQRSPTQSPPADTSFSSRRGRQLPQVPVRS | ||||||
Sequence conflict | 1272 | in Ref. 4; BAH11945 | ||||
Sequence: P → S | ||||||
Alternative sequence | VSP_008169 | 1284-1455 | in isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 13 | |||
Sequence: Missing | ||||||
Compositional bias | 1333-1375 | Polar residues | ||||
Sequence: DNVSAKSSDSDVSDVSAISRTSSASRLSSTSFMSEQSERPRGR | ||||||
Alternative sequence | VSP_008170 | 1377-1385 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 1445-1460 | Polar residues | ||||
Sequence: RSRSTSQLSQTESGHK | ||||||
Alternative sequence | VSP_008171 | 1540-1573 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1606 | in Ref. 4; BAH11906 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 1609 | in Ref. 4; BAH13358 | ||||
Sequence: V → A | ||||||
Sequence conflict | 1662 | in Ref. 4; AK309185 | ||||
Sequence: S → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY190519 EMBL· GenBank· DDBJ | AAO38848.1 EMBL· GenBank· DDBJ | mRNA | ||
AB045726 EMBL· GenBank· DDBJ | BAB87121.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051866 EMBL· GenBank· DDBJ | BAB87242.1 EMBL· GenBank· DDBJ | mRNA | ||
AB002338 EMBL· GenBank· DDBJ | BAA20798.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK296303 EMBL· GenBank· DDBJ | BAH12309.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294868 EMBL· GenBank· DDBJ | BAH11906.1 EMBL· GenBank· DDBJ | mRNA | ||
AK295001 EMBL· GenBank· DDBJ | BAH11945.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300853 EMBL· GenBank· DDBJ | BAH13358.1 EMBL· GenBank· DDBJ | mRNA | ||
AK309185 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AL160405 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL590011 EMBL· GenBank· DDBJ | CAI16961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL034373 EMBL· GenBank· DDBJ | CAI16961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL390056 EMBL· GenBank· DDBJ | CAI16961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445256 EMBL· GenBank· DDBJ | CAI16961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL034373 EMBL· GenBank· DDBJ | CAI20558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL390056 EMBL· GenBank· DDBJ | CAI20558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445256 EMBL· GenBank· DDBJ | CAI20558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL590011 EMBL· GenBank· DDBJ | CAI20558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL390056 EMBL· GenBank· DDBJ | CAI21554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL034373 EMBL· GenBank· DDBJ | CAI21554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445256 EMBL· GenBank· DDBJ | CAI21554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL590011 EMBL· GenBank· DDBJ | CAI21554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445256 EMBL· GenBank· DDBJ | CAI39598.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL034373 EMBL· GenBank· DDBJ | CAI39598.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL390056 EMBL· GenBank· DDBJ | CAI39598.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL590011 EMBL· GenBank· DDBJ | CAI39598.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445256 EMBL· GenBank· DDBJ | CAI39600.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL035633 EMBL· GenBank· DDBJ | CAI39600.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL445256 EMBL· GenBank· DDBJ | CAI39604.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL035633 EMBL· GenBank· DDBJ | CAI39604.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL035633 EMBL· GenBank· DDBJ | CAI42135.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL445256 EMBL· GenBank· DDBJ | CAI42135.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL035633 EMBL· GenBank· DDBJ | CAI42139.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL445256 EMBL· GenBank· DDBJ | CAI42139.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC151853 EMBL· GenBank· DDBJ | AAI51854.1 EMBL· GenBank· DDBJ | mRNA | ||
BC152435 EMBL· GenBank· DDBJ | AAI52436.1 EMBL· GenBank· DDBJ | mRNA | ||
AF263305 EMBL· GenBank· DDBJ | AAG23162.1 EMBL· GenBank· DDBJ | mRNA | ||
AF263306 EMBL· GenBank· DDBJ | AAG23163.1 EMBL· GenBank· DDBJ | mRNA | ||
AF263307 EMBL· GenBank· DDBJ | AAG23164.1 EMBL· GenBank· DDBJ | mRNA | ||
AF263308 EMBL· GenBank· DDBJ | AAG23165.1 EMBL· GenBank· DDBJ | mRNA | ||
AF263309 EMBL· GenBank· DDBJ | AAG23166.1 EMBL· GenBank· DDBJ | mRNA | ||
AF263310 EMBL· GenBank· DDBJ | AAG23167.1 EMBL· GenBank· DDBJ | mRNA |