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Q7Z5J4

- RAI1_HUMAN

UniProt

Q7Z5J4 - RAI1_HUMAN

Protein

Retinoic acid-induced protein 1

Gene

RAI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Transcriptional regulator of the circadian clock components: CLOCK, ARNTL/BMAL1, ARNTL2/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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1856 – 190348PHD-typeAdd
    BLAST

    GO - Molecular functioni

    1. enhancer binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. circadian regulation of gene expression Source: UniProtKB
    2. negative regulation of multicellular organism growth Source: Ensembl
    3. positive regulation of transcription, DNA-templated Source: UniProtKB
    4. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. skeletal system development Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Biological rhythms

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoic acid-induced protein 1
    Gene namesi
    Name:RAI1
    Synonyms:KIAA1820
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9834. RAI1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: In neurons, localized to neurites.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Smith-Magenis syndrome (SMS) [MIM:182290]: Characterized by congenital mental retardation 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi182290. phenotype.
    Orphaneti1713. 17p11.2 microduplication syndrome.
    819. Smith-Magenis syndrome.
    PharmGKBiPA34188.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19061906Retinoic acid-induced protein 1PRO_0000097159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei568 – 5681Phosphoserine1 Publication
    Modified residuei683 – 6831Phosphoserine3 Publications
    Modified residuei696 – 6961Phosphothreonine1 Publication
    Modified residuei880 – 8801Phosphoserine1 Publication
    Modified residuei892 – 8921Phosphoserine1 Publication
    Modified residuei1064 – 10641Phosphoserine1 Publication
    Modified residuei1068 – 10681Phosphothreonine1 Publication
    Modified residuei1122 – 11221Phosphoserine1 Publication
    Modified residuei1352 – 13521Phosphoserine2 Publications
    Modified residuei1358 – 13581Phosphoserine2 Publications
    Modified residuei1374 – 13741Phosphoserine3 Publications
    Modified residuei1431 – 14311Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z5J4.
    PaxDbiQ7Z5J4.
    PRIDEiQ7Z5J4.

    PTM databases

    PhosphoSiteiQ7Z5J4.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined with higher expression in the heart and brain. No expression was seen in the corpus callosum of the brain.1 Publication

    Gene expression databases

    ArrayExpressiQ7Z5J4.
    BgeeiQ7Z5J4.
    CleanExiHS_RAI1.
    GenevestigatoriQ7Z5J4.

    Organism-specific databases

    HPAiHPA023898.
    HPA054906.

    Interactioni

    Protein-protein interaction databases

    BioGridi115966. 21 interactions.
    IntActiQ7Z5J4. 10 interactions.
    MINTiMINT-1477867.
    STRINGi9606.ENSP00000323074.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z5J4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1160 – 117718Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi1223 – 124018Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi124 – 13512Poly-ProAdd
    BLAST
    Compositional biasi156 – 336181Gln-richAdd
    BLAST
    Compositional biasi278 – 29114Poly-GlnAdd
    BLAST
    Compositional biasi1243 – 12497Poly-Ser
    Compositional biasi1493 – 14964Poly-Gly
    Compositional biasi1628 – 164114Ser-richAdd
    BLAST
    Compositional biasi1746 – 17516Poly-Ala

    Sequence similaritiesi

    Contains 1 PHD-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1856 – 190348PHD-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG146768.
    HOVERGENiHBG056862.
    OMAiPRMCTRS.
    OrthoDBiEOG7G4QDB.
    PhylomeDBiQ7Z5J4.
    TreeFamiTF331317.

    Family and domain databases

    InterProiIPR001965. Znf_PHD.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z5J4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MQSFRERCGF HGKQQNYQQT SQETSRLENY RQPSQAGLSC DRQRLLAKDY     50
    YNPQPYPSYE GGAGTPSGTA AAVAADKYHR GSKALPTQQG LQGRPAFPGY 100
    GVQDSSPYPG RYAGEESLQA WGAPQPPPPQ PQPLPAGVAK YDENLMKKTA 150
    VPPSRQYAEQ GAQVPFRTHS LHVQQPPPPQ QPLAYPKLQR QKLQNDIASP 200
    LPFPQGTHFP QHSQSFPTSS TYSSSVQGGG QGAHSYKSCT APTAQPHDRP 250
    LTASSSLAPG QRVQNLHAYQ SGRLSYDQQQ QQQQQQQQQQ QALQSRHHAQ 300
    ETLHYQNLAK YQHYGQQGQG YCQPDAAVRT PEQYYQTFSP SSSHSPARSV 350
    GRSPSYSSTP SPLMPNLENF PYSQQPLSTG AFPAGITDHS HFMPLLNPSP 400
    TDATSSVDTQ AGNCKPLQKD KLPENLLSDL SLQSLTALTS QVENISNTVQ 450
    QLLLSKAAVP QKKGVKNLVS RTPEQHKSQH CSPEGSGYSA EPAGTPLSEP 500
    PSSTPQSTHA EPQEADYLSG SEDPLERSFL YCNQARGSPA RVNSNSKAKP 550
    ESVSTCSVTS PDDMSTKSDD SFQSLHGSLP LDSFSKFVAG ERDCPRLLLS 600
    ALAQEDLASE ILGLQEAIGE KADKAWAEAP SLVKDSSKPP FSLENHSACL 650
    DSVAKSAWPR PGEPEALPDS LQLDKGGNAK DFSPGLFEDP SVAFATPDPK 700
    KTTGPLSFGT KPTLGVPAPD PTTAAFDCFP DTTAASSADS ANPFAWPEEN 750
    LGDACPRWGL HPGELTKGLE QGGKASDGIS KGDTHEASAC LGFQEEDPPG 800
    EKVASLPGDF KQEEVGGVKE EAGGLLQCPE VAKADRWLED SRHCCSTADF 850
    GDLPLLPPTS RKEDLEAEEE YSSLCELLGS PEQRPGMQDP LSPKAPLICT 900
    KEEVEEVLDS KAGWGSPCHL SGESVILLGP TVGTESKVQS WFESSLSHMK 950
    PGEEGPDGER APGDSTTSDA SLAQKPNKPA VPEAPIAKKE PVPRGKSLRS 1000
    RRVHRGLPEA EDSPCRAPVL PKDLLLPESC TGPPQGQMEG AGAPGRGASE 1050
    GLPRMCTRSL TALSEPRTPG PPGLTTTPAP PDKLGGKQRA AFKSGKRVGK 1100
    PSPKAASSPS NPAALPVASD SSPMGSKTKE TDSPSTPGKD QRSMILRSRT 1150
    KTQEIFHSKR RRPSEGRLPN CRATKKLLDN SHLPATFKVS SSPQKEGRVS 1200
    QRARVPKPGA GSKLSDRPLH ALKRKSAFMA PVPTKKRNLV LRSRSSSSSN 1250
    ASGNGGDGKE ERPEGSPTLF KRMSSPKKAK PTKGNGEPAT KLPPPETPDA 1300
    CLKLASRAAF QGAMKTKVLP PRKGRGLKLE AIVQKITSPS LKKFACKAPG 1350
    ASPGNPLSPS LSDKDRGLKG AGGSPVGVEE GLVNVGTGQK LPTSGADPLC 1400
    RNPTNRSLKG KLMNSKKLSS TDCFKTEAFT SPEALQPGGT ALAPKKRSRK 1450
    GRAGAHGLSK GPLEKRPYLG PALLLTPRDR ASGTQGASED NSGGGGKKPK 1500
    MEELGLASQP PEGRPCQPQT RAQKQPGHTN YSSYSKRKRL TRGRAKNTTS 1550
    SPCKGRAKRR RQQQVLPLDP AEPEIRLKYI SSCKRLRSDS RTPAFSPFVR 1600
    VEKRDAFTTI CTVVNSPGDA PKPHRKPSSS ASSSSSSSSF SLDAAGASLA 1650
    TLPGGSILQP RPSLPLSSTM HLGPVVSKAL STSCLVCCLC QNPANFKDLG 1700
    DLCGPYYPEH CLPKKKPKLK EKVRPEGTCE EASLPLERTL KGPECAAAAT 1750
    AGKPPRPDGP ADPAKQGPLR TSARGLSRRL QSCYCCDGRE DGGEEAAPAD 1800
    KGRKHECSKE APAEPGGEAQ EHWVHEACAV WTGGVYLVAG KLFGLQEAMK 1850
    VAVDMMCSSC QEAGATIGCC HKGCLHTYHY PCASDAGCIF IEENFSLKCP 1900
    KHKRLP 1906
    Length:1,906
    Mass (Da):203,352
    Last modified:July 19, 2004 - v2
    Checksum:i8D33A56C33BFE888
    GO
    Isoform 2 (identifier: Q7Z5J4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         207-233: THFPQHSQSFPTSSTYSSSVQGGGQGA → WWAGG
         407-434: VDTQAGNCKPLQKDKLPENLLSDLSLQS → PAD
         1415-1479: Missing.
         1803-1821: Missing.
         1856-1906: MCSSCQEAGA...LKCPKHKRLP → HGGTVALAPG...LCWAMPGTWK

    Show »
    Length:1,862
    Mass (Da):198,392
    Checksum:i9C4D9E4EF917A911
    GO
    Isoform 3 (identifier: Q7Z5J4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1598-1640: FVRVEKRDAF...ASSSSSSSSF → LEPSLGAQNP...AYSAREQGQR
         1641-1906: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,640
    Mass (Da):175,343
    Checksum:iA178ECCDECEDA431
    GO
    Isoform 4 (identifier: Q7Z5J4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         947-966: SHMKPGEEGPDGERAPGDST → YSVYICIHIHIYNIYEDCKC
         967-1906: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:966
    Mass (Da):104,319
    Checksum:iEBD2A4453EADBA58
    GO

    Sequence cautioni

    The sequence BAB47449.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti440 – 4401S → L in AAO31738. (PubMed:12837267)Curated
    Sequence conflicti1302 – 13021L → F in AAO31738. (PubMed:12837267)Curated
    Sequence conflicti1513 – 15131G → A in AAO31738. (PubMed:12837267)Curated
    Sequence conflicti1682 – 16821T → A in CAD39144. (PubMed:17974005)Curated

    Polymorphismi

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901G → A.
    Corresponds to variant rs3803763 [ dbSNP | Ensembl ].
    VAR_051300
    Natural varianti165 – 1651P → T.
    Corresponds to variant rs11649804 [ dbSNP | Ensembl ].
    VAR_024344
    Natural varianti939 – 9391Q → P.
    Corresponds to variant rs1759075 [ dbSNP | Ensembl ].
    VAR_051301

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei207 – 23327THFPQ…GGQGA → WWAGG in isoform 2. 1 PublicationVSP_010995Add
    BLAST
    Alternative sequencei407 – 43428VDTQA…LSLQS → PAD in isoform 2. 1 PublicationVSP_010996Add
    BLAST
    Alternative sequencei947 – 96620SHMKP…PGDST → YSVYICIHIHIYNIYEDCKC in isoform 4. 1 PublicationVSP_010997Add
    BLAST
    Alternative sequencei967 – 1906940Missing in isoform 4. 1 PublicationVSP_010998Add
    BLAST
    Alternative sequencei1415 – 147965Missing in isoform 2. 1 PublicationVSP_010999Add
    BLAST
    Alternative sequencei1598 – 164043FVRVE…SSSSF → LEPSLGAQNPRSGQNAPPAP ADARPLCTTRDRRAYSAREQ GQR in isoform 3. 1 PublicationVSP_011000Add
    BLAST
    Alternative sequencei1641 – 1906266Missing in isoform 3. 1 PublicationVSP_011001Add
    BLAST
    Alternative sequencei1803 – 182119Missing in isoform 2. 1 PublicationVSP_011002Add
    BLAST
    Alternative sequencei1856 – 190651MCSSC…HKRLP → HGGTVALAPGDFSLPGLRFA SLFQGPSWCDCPVLATSTPS SWSRCVPAAKKPGPPLGAAT KDASTPTTTRVPAMQVRARP GTGGHWSPSKQSRGTLPGHS SPNPGPISLFSFPPLLPQQF FYPSVCLDLCWAMPGTWK in isoform 2. 1 PublicationVSP_011003Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271790 mRNA. Translation: CAC20423.1.
    AJ271791 Genomic DNA. Translation: CAC20424.1.
    AY172136 mRNA. Translation: AAO31738.1.
    AB058723 mRNA. Translation: BAB47449.1. Different initiation.
    BC021209 mRNA. Translation: AAH21209.1.
    AL133649 mRNA. Translation: CAB63768.1.
    AL834468 mRNA. Translation: CAD39127.1.
    AL834486 mRNA. Translation: CAD39144.1.
    CCDSiCCDS11188.1. [Q7Z5J4-1]
    PIRiT43490.
    RefSeqiNP_109590.3. NM_030665.3. [Q7Z5J4-1]
    UniGeneiHs.655395.
    Hs.727059.

    Genome annotation databases

    EnsembliENST00000353383; ENSP00000323074; ENSG00000108557. [Q7Z5J4-1]
    GeneIDi10743.
    KEGGihsa:10743.
    UCSCiuc002grm.3. human. [Q7Z5J4-1]

    Polymorphism databases

    DMDMi50400978.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271790 mRNA. Translation: CAC20423.1 .
    AJ271791 Genomic DNA. Translation: CAC20424.1 .
    AY172136 mRNA. Translation: AAO31738.1 .
    AB058723 mRNA. Translation: BAB47449.1 . Different initiation.
    BC021209 mRNA. Translation: AAH21209.1 .
    AL133649 mRNA. Translation: CAB63768.1 .
    AL834468 mRNA. Translation: CAD39127.1 .
    AL834486 mRNA. Translation: CAD39144.1 .
    CCDSi CCDS11188.1. [Q7Z5J4-1 ]
    PIRi T43490.
    RefSeqi NP_109590.3. NM_030665.3. [Q7Z5J4-1 ]
    UniGenei Hs.655395.
    Hs.727059.

    3D structure databases

    ProteinModelPortali Q7Z5J4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115966. 21 interactions.
    IntActi Q7Z5J4. 10 interactions.
    MINTi MINT-1477867.
    STRINGi 9606.ENSP00000323074.

    PTM databases

    PhosphoSitei Q7Z5J4.

    Polymorphism databases

    DMDMi 50400978.

    Proteomic databases

    MaxQBi Q7Z5J4.
    PaxDbi Q7Z5J4.
    PRIDEi Q7Z5J4.

    Protocols and materials databases

    DNASUi 10743.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353383 ; ENSP00000323074 ; ENSG00000108557 . [Q7Z5J4-1 ]
    GeneIDi 10743.
    KEGGi hsa:10743.
    UCSCi uc002grm.3. human. [Q7Z5J4-1 ]

    Organism-specific databases

    CTDi 10743.
    GeneCardsi GC17P017525.
    GeneReviewsi RAI1.
    H-InvDB HIX0013588.
    HGNCi HGNC:9834. RAI1.
    HPAi HPA023898.
    HPA054906.
    MIMi 182290. phenotype.
    607642. gene.
    neXtProti NX_Q7Z5J4.
    Orphaneti 1713. 17p11.2 microduplication syndrome.
    819. Smith-Magenis syndrome.
    PharmGKBi PA34188.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146768.
    HOVERGENi HBG056862.
    OMAi PRMCTRS.
    OrthoDBi EOG7G4QDB.
    PhylomeDBi Q7Z5J4.
    TreeFami TF331317.

    Miscellaneous databases

    ChiTaRSi RAI1. human.
    GenomeRNAii 10743.
    NextBioi 40793.
    PROi Q7Z5J4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z5J4.
    Bgeei Q7Z5J4.
    CleanExi HS_RAI1.
    Genevestigatori Q7Z5J4.

    Family and domain databases

    InterProi IPR001965. Znf_PHD.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RAI1 is a novel polyglutamine encoding gene that is deleted in Smith-Magenis syndrome patients."
      Seranski P., Hoff C., Radelof U., Henning S., Reinhard R., Schwartz C.E., Heiss N., Poustka A.
      Gene 270:69-76(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), POLYMORPHISM OF POLY-GLN REGION, INVOLVEMENT IN SMITH-MAGENIS SYNDROME.
    2. "Molecular cloning and characterization of human RAI1, a gene associated with schizophrenia."
      Toulouse A., Rochefort D., Roussel J., Joober R., Rouleau G.A.
      Genomics 82:162-171(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Muscle.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 622-1906.
      Tissue: Melanoma and Testis.
    6. "Mutations in RAI1 associated with Smith-Magenis syndrome."
      Slager R.E., Newton T.L., Vlangos C.N., Finucane B., Elsea S.H.
      Nat. Genet. 33:466-468(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SMITH-MAGENIS SYNDROME.
    7. "CAG repeat length in RAI1 is associated with age at onset variability in spinocerebellar ataxia type 2 (SCA2)."
      Hayes S., Turecki G., Brisebois K., Lopes-Cendes I., Gaspar C., Riess O., Ranum L.P., Pulst S.M., Rouleau G.A.
      Hum. Mol. Genet. 9:1753-1758(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF THE POLY-GLN REGION IN SPINOCEREBELLAR ATAXIA TYPE 2.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; THR-696; SER-880; SER-892; SER-1122; SER-1352; SER-1358; SER-1374 AND SER-1431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; SER-1064; THR-1068 AND SER-1374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-683; SER-1352; SER-1358 AND SER-1374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Smith-Magenis syndrome results in disruption of CLOCK gene transcription and reveals an integral role for RAI1 in the maintenance of circadian rhythmicity."
      Williams S.R., Zies D., Mullegama S.V., Grotewiel M.S., Elsea S.H.
      Am. J. Hum. Genet. 90:941-949(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiRAI1_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z5J4
    Secondary accession number(s): Q8N3B4
    , Q8ND08, Q8WU64, Q96JK5, Q9H1C1, Q9H1C2, Q9UF69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3