Q86UR5 · RIMS1_HUMAN

  • Protein
    Regulating synaptic membrane exocytosis protein 1
  • Gene
    RIMS1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Rab effector involved in exocytosis (By similarity).
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.

116922004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Binding site116Zn2+ 1 (UniProtKB | ChEBI)
Binding site119Zn2+ 1 (UniProtKB | ChEBI)
Binding site132Zn2+ 2 (UniProtKB | ChEBI)
Binding site135Zn2+ 2 (UniProtKB | ChEBI)
Binding site140Zn2+ 1 (UniProtKB | ChEBI)
Binding site143Zn2+ 1 (UniProtKB | ChEBI)
Binding site162Zn2+ 2 (UniProtKB | ChEBI)
Binding site165Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell projection
Cellular Componentcytoskeleton of presynaptic active zone
Cellular Componentcytosol
Cellular Componentplasma membrane
Cellular Componentpresynaptic active zone
Cellular Componentpresynaptic membrane
Molecular FunctionGTPase regulator activity
Molecular Functionmetal ion binding
Molecular FunctionRNA binding
Molecular Functionsmall GTPase binding
Molecular Functiontransmembrane transporter binding
Biological Processacrosomal vesicle exocytosis
Biological Processcalcium ion-regulated exocytosis of neurotransmitter
Biological Processcalcium-ion regulated exocytosis
Biological Processcell differentiation
Biological Processintracellular protein transport
Biological Processmembrane fusion
Biological Processpositive regulation of dendrite extension
Biological Processpositive regulation of excitatory postsynaptic potential
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of inhibitory postsynaptic potential
Biological Processpositive regulation of synaptic transmission
Biological Processprotein-containing complex assembly
Biological Processregulated exocytosis
Biological Processregulation of membrane potential
Biological Processregulation of neurotransmitter secretion
Biological Processregulation of synaptic plasticity
Biological Processregulation of synaptic vesicle exocytosis
Biological Processsecretion
Biological Processsynaptic vesicle exocytosis
Biological Processvisual perception

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Regulating synaptic membrane exocytosis protein 1
  • Alternative names
    • Rab-3-interacting molecule 1 (RIM 1)
    • Rab-3-interacting protein 2

Gene names

    • Name
      RIMS1
    • Synonyms
      KIAA0340, RAB3IP2, RIM1
    • ORF names
      Nbla00761

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q86UR5
  • Secondary accessions
    • A7MBN6
    • B7Z2M0
    • B7Z2Q9
    • B7Z3S3
    • B7Z6S2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis796-797Abolishes interaction with SYT1 and CACNA1B.
Natural variantVAR_016804820found in a family with cone-rod dystrophy; uncertain significance; dbSNP:rs121918302
Mutagenesis1591-1592Abolishes interaction with SYT1 and CACNA1B.

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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00001901981-1692UniProtRegulating synaptic membrane exocytosis protein 1
Modified residue (large scale data)324PRIDEPhosphoserine
Modified residue (large scale data)391PRIDEPhosphoserine
Modified residue (large scale data)448PRIDEPhosphoserine
Modified residue500UniProtPhosphoserine
Modified residue578UniProtPhosphoserine
Modified residue728UniProtPhosphoserine
Modified residue (large scale data)728PRIDEPhosphoserine
Modified residue731UniProtPhosphoserine
Modified residue (large scale data)731PRIDEPhosphoserine
Modified residue881UniProtPhosphoserine
Modified residue (large scale data)881PRIDEPhosphoserine
Modified residue977UniProtPhosphoserine
Modified residue (large scale data)977PRIDEPhosphoserine
Modified residue (large scale data)999PRIDEPhosphoserine
Modified residue1031UniProtPhosphoserine
Modified residue1252UniProtPhosphoserine
Modified residue1254UniProtPhosphothreonine
Modified residue (large scale data)1254PRIDEPhosphothreonine
Modified residue1256UniProtPhosphoserine
Modified residue1308UniProtPhosphoserine
Modified residue1310UniProtPhosphoserine
Modified residue1311UniProtPhosphoserine
Modified residue (large scale data)1311PRIDEPhosphoserine
Modified residue (large scale data)1331PRIDEPhosphoserine
Modified residue1339UniProtPhosphoserine
Modified residue1340UniProtPhosphoserine
Modified residue1342UniProtPhosphoserine
Modified residue (large scale data)1407PRIDEPhosphothreonine
Modified residue1416UniProtPhosphoserine
Modified residue (large scale data)1416PRIDEPhosphoserine
Modified residue (large scale data)1450PRIDEPhosphoserine
Modified residue (large scale data)1486PRIDEPhosphoserine
Modified residue (large scale data)1489PRIDEPhosphoserine
Modified residue (large scale data)1490PRIDEPhosphothreonine
Modified residue (large scale data)1613PRIDEPhosphoserine
Modified residue1677UniProtPhosphoserine
Modified residue (large scale data)1677PRIDEPhosphoserine
Modified residue (large scale data)1679PRIDEPhosphoserine
Modified residue1680UniProtPhosphoserine
Modified residue (large scale data)1680PRIDEPhosphoserine
Modified residue1683UniProtPhosphoserine
Modified residue (large scale data)1683PRIDEPhosphoserine
Modified residue1692UniProtPhosphoserine
Modified residue (large scale data)1692PRIDEPhosphoserine

Post-translational modification

Phosphorylated by BRSK1.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in melanocytes (PubMed:23999003).
Detected in brain and retina (PubMed:23999003).

Gene expression databases

Organism-specific databases

Interaction

Subunit

Binds RAB3A, RAB3B and RAB3D that have been activated by GTP-binding. Interacts with RAB3C, RAB10, RAB26 and RAB37. Binds UNC13A. Interacts with TSPOAP1 and RIMBP2. Interacts with PPFIA3 and PPFIA4. Interacts with ERC1 (By similarity).
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

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain, zinc finger, compositional bias.

TypeIDPosition(s)Description
Region1-26Disordered
Domain22-182RabBD
Zinc finger110-170FYVE-type
Compositional bias183-199Polar residues
Region183-555Disordered
Compositional bias216-231Polar residues
Compositional bias262-277Basic and acidic residues
Compositional bias284-356Basic and acidic residues
Compositional bias373-395Basic and acidic residues
Compositional bias482-497Basic and acidic residues
Compositional bias498-512Polar residues
Domain605-691PDZ
Region698-732Disordered
Compositional bias704-730Polar residues
Domain742-865C2 1
Region870-1013Disordered
Compositional bias889-910Basic and acidic residues
Compositional bias929-944Polar residues
Compositional bias945-964Basic and acidic residues
Compositional bias993-1013Basic and acidic residues
Region1118-1222Disordered
Compositional bias1125-1142Basic and acidic residues
Compositional bias1155-1172Basic and acidic residues
Region1235-1278Disordered
Compositional bias1247-1278Polar residues
Region1332-1394Disordered
Compositional bias1333-1375Polar residues
Region1408-1428Disordered
Compositional bias1445-1460Polar residues
Region1445-1495Disordered
Domain1538-1656C2 2

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete

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.

  • Name
    1
  • Synonyms
    RIM1 alpha
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,692
  • Mass (Da)
    189,073
  • Last updated
    2003-06-01 v1
  • Checksum
    0A96642DC832C15E
MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEKGDLDYYWLDPATWHSRETSPISSHPVTWQPSKEGDRLIGRVILNKRTTMPKDSGALLGLKVVGGKMTDLGRLGAFITKVKKGSLADVVGHLRAGDEVLEWNGKPLPGATNEEVYNIILESKSEPQVEIIVSRPIGDIPRIPESSHPPLESSSSSFESQKMERPSISVISPTSPGALKDAPQVLPGQLSVKLWYDKVGHQLIVNVLQATDLPARVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKILEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQEEESEFLGEILIELETALLDDEPHWYKLQTHDESSLPLPQPSPFMPRRHIHGESSSKKLQRSQRISDSDISDYEVDDGIGVVPPVGYRSSARESKSTTLTVPEQQRTTHHRSRSVSPHRGNDQGKPRSRLPNVPLQRSLDEIHPTRRSRSPTRHHDASRSPVDHRTRDVDSQYLSEQDSELLMLPRAKRGRSAECLHTTRHLVRHYKTLPPKMPLLQSSSHWNIYSSILPAHTKTKSVTRQDISLHHECFNSTVLRFTDEILVSELQPFLDRARSASTNCLRPDTSLHSPERERGRWSPSLDRRRPPSPRIQIQHASPENDRHSRKSERSSIQKQTRKGTASDAERVLPTCLSRRGHAAPRATDQPVIRGKHPARSRSSEHSSIRTLCSMHHLVPGGSAPPSPLLTRMHRQRSPTQSPPADTSFSSRRGRQLPQVPVRSGSIEQASLVVEERTRQMKMKVHRFKQTTGSGSSQELDREQYSKYNIHKDQYRSCDNVSAKSSDSDVSDVSAISRTSSASRLSSTSFMSEQSERPRGRISSFTPKMQGRRMGTSGRSIMKSTSVSGEMYTLEHNDGSQSDTAVGTVGAGGKKRRSSLSAKVVAIVSRRSRSTSQLSQTESGHKKLKSTIQRSTETGMAAEMRKMVRQPSRESTDGSINSYSSEGNLIFPGVRLGADSQFSDFLDGLGPAQLVGRQTLATPAMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQILLEELDLSSMVIGWYKLFPPSSLVDPTLTPLTRRASQSSLESSTGPPCIRS

Q86UR5-2

  • Name
    2
  • Synonyms
    RIM short form
  • Note
    May be due to intron retention.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86UR5-3

  • Name
    3
  • Synonyms
    RIM long form, Rab3 interacting protein variant 2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86UR5-4

  • Name
    4
  • Synonyms
    Rab3 interacting protein variant 1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86UR5-5

  • Name
    5
  • Synonyms
    Rab3 interacting protein variant 3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86UR5-6

Q86UR5-7

Q86UR5-8

  • Name
    8
  • Synonyms
    Rab3 interacting protein variant 6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86UR5-9

Q86UR5-10

Q86UR5-11

  • Name
    11
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86UR5-12

  • Name
    12
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-559: MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEAMLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQEILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASSQDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKSERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRKEEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPEGKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELKAQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGKKRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEK → MCAPGIHVSSEGWEEVRSVDSEEGTIEARRAVA
    • 924-924: Missing
    • 1039-1102: Missing
    • 1133-1160: Missing
    • 1185-1245: Missing

Q86UR5-13

  • Name
    13
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • 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

View all
EntryEntry nameGene nameLength
H0YBU6H0YBU6_HUMANRIMS11038
H0YBE7H0YBE7_HUMANRIMS1610
A0A8V8TKU9A0A8V8TKU9_HUMANRIMS11515
E5RGM0E5RGM0_HUMANRIMS1753
A0A0C4DFV1A0A0C4DFV1_HUMANRIMS1740

Sequence caution

The sequence BAA20798.1 differs from that shown. Reason: Erroneous initiation
The sequence CAI39600.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAI42135.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0431771-18in isoform 9
Alternative sequenceVSP_0467961-559in isoform 12 and isoform 13
Alternative sequenceVSP_0454861-607in isoform 10
Alternative sequenceVSP_0454851-1473in isoform 11
Alternative sequenceVSP_04317819-559in isoform 9
Sequence conflict157in Ref. 5; CAI16961
Compositional bias183-199Polar residues
Compositional bias216-231Polar residues
Compositional bias262-277Basic and acidic residues
Compositional bias284-356Basic and acidic residues
Compositional bias373-395Basic and acidic residues
Compositional bias482-497Basic and acidic residues
Sequence conflict484-494in Ref. 2; BAB87121/BAB87242, 3; BAA20798 and 6; AAI51854/AAI52436
Compositional bias498-512Polar residues
Compositional bias704-730Polar residues
Compositional bias889-910Basic and acidic residues
Alternative sequenceVSP_008161924in isoform 5, isoform 7, isoform 8 and isoform 12
Compositional bias929-944Polar residues
Compositional bias945-964Basic and acidic residues
Compositional bias993-1013Basic and acidic residues
Alternative sequenceVSP_0081621018-1245in isoform 8
Alternative sequenceVSP_0081631038-1244in isoform 5
Alternative sequenceVSP_0081641039-1102in isoform 3, isoform 6, isoform 7, isoform 9, isoform 10, isoform 12 and isoform 13
Alternative sequenceVSP_0081651040-1692in isoform 2
Alternative sequenceVSP_0081661065-1102in isoform 4
Compositional bias1125-1142Basic and acidic residues
Alternative sequenceVSP_0431791133-1160in isoform 9, isoform 10 and isoform 12
Alternative sequenceVSP_0081671133-1245in isoform 3, isoform 4, isoform 7 and isoform 13
Compositional bias1155-1172Basic and acidic residues
Alternative sequenceVSP_0081681161-1245in isoform 6
Alternative sequenceVSP_0431801185-1245in isoform 9, isoform 10 and isoform 12
Compositional bias1247-1278Polar residues
Sequence conflict1272in Ref. 4; BAH11945
Alternative sequenceVSP_0081691284-1455in isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 13
Compositional bias1333-1375Polar residues
Alternative sequenceVSP_0081701377-1385in isoform 5
Compositional bias1445-1460Polar residues
Alternative sequenceVSP_0081711540-1573in isoform 3
Sequence conflict1606in Ref. 4; BAH11906
Sequence conflict1609in Ref. 4; BAH13358
Sequence conflict1662in Ref. 4; AK309185

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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