Q7Z5J4 · RAI1_HUMAN

  • Protein
    Retinoic acid-induced protein 1
  • Gene
    RAI1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Transcriptional regulator of the circadian clock components: CLOCK, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively regulates the transcriptional activity of CLOCK a core component of the circadian clock. Regulates transcription through chromatin remodeling by interacting with other proteins in chromatin as well as proteins in the basic transcriptional machinery. May be important for embryonic and postnatal development. May be involved in neuronal differentiation.

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 Componentcytoplasm
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functionmetal ion binding
Biological Processcircadian regulation of gene expression
Biological Processnegative regulation of multicellular organism growth
Biological Processpositive regulation of DNA-templated transcription
Biological Processregulation of transcription by RNA polymerase II
Biological Processskeletal system development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Retinoic acid-induced protein 1

Gene names

    • Name
      RAI1
    • Synonyms
      KIAA1820

Organism names

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

Accessions

  • Primary accession
    Q7Z5J4
  • Secondary accessions
    • Q8N3B4
    • Q8ND08
    • Q8WU64
    • Q96JK5
    • Q9H1C1

Proteomes

Organism-specific databases

Subcellular Location

Note: In neurons, localized to neurites.

Keywords

Disease & Variants

Involvement in disease

Smith-Magenis syndrome (SMS)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    Characterized by intellectual disability associated with development and growth delays. Affected persons have characteristic behavioral abnormalities, including self-injurious behaviors and sleep disturbance, and distinct craniofacial and skeletal anomalies.
  • See also
    MIM:182290
Natural variants in SMS
Variant IDPosition(s)ChangeDescription
VAR_079636758-1906missingin SMS

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_05130090in dbSNP:rs3803763
Natural variantVAR_024344165in dbSNP:rs11649804
Natural variantVAR_079636758-1906in SMS
Natural variantVAR_051301939in dbSNP:rs1759075

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2,331 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00000971591-1906UniProtRetinoic acid-induced protein 1
Modified residue (large scale data)39PRIDEPhosphoserine
Modified residue (large scale data)65PRIDEPhosphothreonine
Modified residue (large scale data)105PRIDEPhosphoserine
Modified residue (large scale data)106PRIDEPhosphoserine
Modified residue339UniProtPhosphoserine
Modified residue (large scale data)339PRIDEPhosphoserine
Modified residue (large scale data)341PRIDEPhosphoserine
Modified residue345UniProtPhosphoserine
Modified residue (large scale data)345PRIDEPhosphoserine
Modified residue472UniProtPhosphothreonine
Modified residue (large scale data)528PRIDEPhosphoserine
Modified residue (large scale data)538PRIDEPhosphoserine
Modified residue (large scale data)560PRIDEPhosphoserine
Modified residue (large scale data)565PRIDEPhosphoserine
Modified residue568UniProtPhosphoserine
Modified residue (large scale data)568PRIDEPhosphoserine
Modified residue (large scale data)571PRIDEPhosphoserine
Modified residue (large scale data)574PRIDEPhosphoserine
Modified residue (large scale data)578PRIDEPhosphoserine
Modified residue (large scale data)600PRIDEPhosphoserine
Modified residue (large scale data)637PRIDEPhosphoserine
Modified residue (large scale data)642PRIDEPhosphoserine
Modified residue (large scale data)670PRIDEPhosphoserine
Modified residue683UniProtPhosphoserine
Modified residue (large scale data)683PRIDEPhosphoserine
Modified residue696UniProtPhosphothreonine
Modified residue (large scale data)696PRIDEPhosphothreonine
Modified residue (large scale data)776PRIDEPhosphoserine
Modified residue805UniProtPhosphoserine
Modified residue (large scale data)805PRIDEPhosphoserine
Cross-link811UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link819UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residue (large scale data)846PRIDEPhosphoserine
Modified residue880UniProtPhosphoserine
Modified residue (large scale data)880PRIDEPhosphoserine
Modified residue892UniProtPhosphoserine
Modified residue (large scale data)892PRIDEPhosphoserine
Cross-link901UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link901UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue (large scale data)916PRIDEPhosphoserine
Modified residue (large scale data)921PRIDEPhosphoserine
Modified residue (large scale data)924PRIDEPhosphoserine
Modified residue (large scale data)1013PRIDEPhosphoserine
Modified residue1064UniProtPhosphoserine
Modified residue (large scale data)1064PRIDEPhosphoserine
Modified residue1068UniProtPhosphothreonine
Modified residue (large scale data)1068PRIDEPhosphothreonine
Modified residue (large scale data)1075PRIDEPhosphothreonine
Modified residue (large scale data)1076PRIDEPhosphothreonine
Modified residue (large scale data)1077PRIDEPhosphothreonine
Modified residue (large scale data)1107PRIDEPhosphoserine
Modified residue (large scale data)1108PRIDEPhosphoserine
Modified residue (large scale data)1110PRIDEPhosphoserine
Modified residue (large scale data)1119PRIDEPhosphoserine
Modified residue (large scale data)1121PRIDEPhosphoserine
Modified residue1122UniProtPhosphoserine
Modified residue (large scale data)1122PRIDEPhosphoserine
Modified residue (large scale data)1126PRIDEPhosphoserine
Modified residue (large scale data)1133PRIDEPhosphoserine
Modified residue (large scale data)1135PRIDEPhosphoserine
Modified residue (large scale data)1136PRIDEPhosphothreonine
Modified residue (large scale data)1190PRIDEPhosphoserine
Modified residue (large scale data)1191PRIDEPhosphoserine
Modified residue (large scale data)1192PRIDEPhosphoserine
Modified residue (large scale data)1226PRIDEPhosphoserine
Modified residue (large scale data)1247PRIDEPhosphoserine
Modified residue (large scale data)1266PRIDEPhosphoserine
Modified residue1352UniProtPhosphoserine
Modified residue (large scale data)1352PRIDEPhosphoserine
Modified residue1358UniProtPhosphoserine
Modified residue (large scale data)1358PRIDEPhosphoserine
Modified residue (large scale data)1360PRIDEPhosphoserine
Modified residue (large scale data)1362PRIDEPhosphoserine
Modified residue1374UniProtPhosphoserine
Modified residue (large scale data)1374PRIDEPhosphoserine
Modified residue (large scale data)1387PRIDEPhosphothreonine
Modified residue (large scale data)1394PRIDEPhosphoserine
Cross-link1425UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1430PRIDEPhosphothreonine
Modified residue1431UniProtPhosphoserine
Modified residue (large scale data)1431PRIDEPhosphoserine
Modified residue (large scale data)1476PRIDEPhosphothreonine
Modified residue (large scale data)1533PRIDEPhosphoserine
Modified residue (large scale data)1550PRIDEPhosphoserine
Modified residue (large scale data)1590PRIDEPhosphoserine
Modified residue (large scale data)1616PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all tissues examined with higher expression in the heart and brain. No expression was seen in the corpus callosum of the brain.

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q7Z5J4PIN1 Q135264EBI-743815, EBI-714158

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-261Disordered
Compositional bias12-39Polar residues
Compositional bias192-261Polar residues
Region273-299Disordered
Region335-370Disordered
Region469-520Disordered
Compositional bias471-485Polar residues
Compositional bias496-514Polar residues
Region538-571Disordered
Region656-712Disordered
Region937-1299Disordered
Compositional bias989-1011Basic and acidic residues
Compositional bias1104-1151Polar residues
Motif1160-1177Nuclear localization signal
Compositional bias1184-1198Polar residues
Motif1223-1240Nuclear localization signal
Compositional bias1239-1255Polar residues
Region1344-1570Disordered
Compositional bias1407-1427Polar residues
Compositional bias1513-1534Polar residues
Region1613-1637Disordered
Region1746-1775Disordered
Zinc finger1780-1835C2HC pre-PHD-type
Region1794-1819Disordered
Zinc finger1855-1903PHD-type

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

Q7Z5J4-1

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.

  • Length
    1,906
  • Mass (Da)
    203,352
  • Last updated
    2004-07-19 v2
  • Checksum
    8D33A56C33BFE888
MQSFRERCGFHGKQQNYQQTSQETSRLENYRQPSQAGLSCDRQRLLAKDYYNPQPYPSYEGGAGTPSGTAAAVAADKYHRGSKALPTQQGLQGRPAFPGYGVQDSSPYPGRYAGEESLQAWGAPQPPPPQPQPLPAGVAKYDENLMKKTAVPPSRQYAEQGAQVPFRTHSLHVQQPPPPQQPLAYPKLQRQKLQNDIASPLPFPQGTHFPQHSQSFPTSSTYSSSVQGGGQGAHSYKSCTAPTAQPHDRPLTASSSLAPGQRVQNLHAYQSGRLSYDQQQQQQQQQQQQQQALQSRHHAQETLHYQNLAKYQHYGQQGQGYCQPDAAVRTPEQYYQTFSPSSSHSPARSVGRSPSYSSTPSPLMPNLENFPYSQQPLSTGAFPAGITDHSHFMPLLNPSPTDATSSVDTQAGNCKPLQKDKLPENLLSDLSLQSLTALTSQVENISNTVQQLLLSKAAVPQKKGVKNLVSRTPEQHKSQHCSPEGSGYSAEPAGTPLSEPPSSTPQSTHAEPQEADYLSGSEDPLERSFLYCNQARGSPARVNSNSKAKPESVSTCSVTSPDDMSTKSDDSFQSLHGSLPLDSFSKFVAGERDCPRLLLSALAQEDLASEILGLQEAIGEKADKAWAEAPSLVKDSSKPPFSLENHSACLDSVAKSAWPRPGEPEALPDSLQLDKGGNAKDFSPGLFEDPSVAFATPDPKKTTGPLSFGTKPTLGVPAPDPTTAAFDCFPDTTAASSADSANPFAWPEENLGDACPRWGLHPGELTKGLEQGGKASDGISKGDTHEASACLGFQEEDPPGEKVASLPGDFKQEEVGGVKEEAGGLLQCPEVAKADRWLEDSRHCCSTADFGDLPLLPPTSRKEDLEAEEEYSSLCELLGSPEQRPGMQDPLSPKAPLICTKEEVEEVLDSKAGWGSPCHLSGESVILLGPTVGTESKVQSWFESSLSHMKPGEEGPDGERAPGDSTTSDASLAQKPNKPAVPEAPIAKKEPVPRGKSLRSRRVHRGLPEAEDSPCRAPVLPKDLLLPESCTGPPQGQMEGAGAPGRGASEGLPRMCTRSLTALSEPRTPGPPGLTTTPAPPDKLGGKQRAAFKSGKRVGKPSPKAASSPSNPAALPVASDSSPMGSKTKETDSPSTPGKDQRSMILRSRTKTQEIFHSKRRRPSEGRLPNCRATKKLLDNSHLPATFKVSSSPQKEGRVSQRARVPKPGAGSKLSDRPLHALKRKSAFMAPVPTKKRNLVLRSRSSSSSNASGNGGDGKEERPEGSPTLFKRMSSPKKAKPTKGNGEPATKLPPPETPDACLKLASRAAFQGAMKTKVLPPRKGRGLKLEAIVQKITSPSLKKFACKAPGASPGNPLSPSLSDKDRGLKGAGGSPVGVEEGLVNVGTGQKLPTSGADPLCRNPTNRSLKGKLMNSKKLSSTDCFKTEAFTSPEALQPGGTALAPKKRSRKGRAGAHGLSKGPLEKRPYLGPALLLTPRDRASGTQGASEDNSGGGGKKPKMEELGLASQPPEGRPCQPQTRAQKQPGHTNYSSYSKRKRLTRGRAKNTTSSPCKGRAKRRRQQQVLPLDPAEPEIRLKYISSCKRLRSDSRTPAFSPFVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSFSLDAAGASLATLPGGSILQPRPSLPLSSTMHLGPVVSKALSTSCLVCCLCQNPANFKDLGDLCGPYYPEHCLPKKKPKLKEKVRPEGTCEEASLPLERTLKGPECAAAATAGKPPRPDGPADPAKQGPLRTSARGLSRRLQSCYCCDGREDGGEEAAPADKGRKHECSKEAPAEPGGEAQEHWVHEACAVWTGGVYLVAGKLFGLQEAMKVAVDMMCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP

Q7Z5J4-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 207-233: THFPQHSQSFPTSSTYSSSVQGGGQGA → WWAGG
    • 407-434: VDTQAGNCKPLQKDKLPENLLSDLSLQS → PAD
    • 1415-1479: Missing
    • 1803-1821: Missing
    • 1856-1906: MCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP → HGGTVALAPGDFSLPGLRFASLFQGPSWCDCPVLATSTPSSWSRCVPAAKKPGPPLGAATKDASTPTTTRVPAMQVRARPGTGGHWSPSKQSRGTLPGHSSPNPGPISLFSFPPLLPQQFFYPSVCLDLCWAMPGTWK

Q7Z5J4-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1598-1640: FVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSF → LEPSLGAQNPRSGQNAPPAPADARPLCTTRDRRAYSAREQGQR
    • 1641-1906: Missing

Q7Z5J4-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 947-966: SHMKPGEEGPDGERAPGDST → YSVYICIHIHIYNIYEDCKC
    • 967-1906: Missing

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A8MXE8A8MXE8_HUMANRAI1942
J3QLL5J3QLL5_HUMANRAI165
J3QR08J3QR08_HUMANRAI1156

Sequence caution

The sequence BAB47449.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

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

TypeIDPosition(s)Description
Compositional bias12-39Polar residues
Compositional bias192-261Polar residues
Alternative sequenceVSP_010995207-233in isoform 2
Alternative sequenceVSP_010996407-434in isoform 2
Sequence conflict440in Ref. 2; AAO31738
Compositional bias471-485Polar residues
Compositional bias496-514Polar residues
Alternative sequenceVSP_010997947-966in isoform 4
Alternative sequenceVSP_010998967-1906in isoform 4
Compositional bias989-1011Basic and acidic residues
Compositional bias1104-1151Polar residues
Compositional bias1184-1198Polar residues
Compositional bias1239-1255Polar residues
Sequence conflict1302in Ref. 2; AAO31738
Compositional bias1407-1427Polar residues
Alternative sequenceVSP_0109991415-1479in isoform 2
Sequence conflict1513in Ref. 2; AAO31738
Compositional bias1513-1534Polar residues
Alternative sequenceVSP_0110001598-1640in isoform 3
Alternative sequenceVSP_0110011641-1906in isoform 3
Sequence conflict1682in Ref. 5; CAD39144
Alternative sequenceVSP_0110021803-1821in isoform 2
Alternative sequenceVSP_0110031856-1906in isoform 2

Polymorphism

The poly-Gln tract is polymorphic and the number of Gln varies from 12 to 14 (PubMed:11404004).
The size of the poly-Gln region may influence the age at onset of spinocerebellar ataxia type 2 (SCA2) (PubMed:10915763).

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ271790
EMBL· GenBank· DDBJ
CAC20423.1
EMBL· GenBank· DDBJ
mRNA
AJ271791
EMBL· GenBank· DDBJ
CAC20424.1
EMBL· GenBank· DDBJ
Genomic DNA
AY172136
EMBL· GenBank· DDBJ
AAO31738.1
EMBL· GenBank· DDBJ
mRNA
AB058723
EMBL· GenBank· DDBJ
BAB47449.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC021209
EMBL· GenBank· DDBJ
AAH21209.1
EMBL· GenBank· DDBJ
mRNA
AL133649
EMBL· GenBank· DDBJ
CAB63768.1
EMBL· GenBank· DDBJ
mRNA
AL834468
EMBL· GenBank· DDBJ
CAD39127.1
EMBL· GenBank· DDBJ
mRNA
AL834486
EMBL· GenBank· DDBJ
CAD39144.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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