ID   RAI1_HUMAN              Reviewed;        1906 AA.
AC   Q7Z5J4; Q8N3B4; Q8ND08; Q8WU64; Q96JK5; Q9H1C1; Q9H1C2; Q9UF69;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   05-OCT-2010, entry version 64.
DE   RecName: Full=Retinoic acid-induced protein 1;
GN   Name=RAI1; Synonyms=KIAA1820;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), POLYMORPHISM OF
RP   POLY-GLN REGION, AND INVOLVEMENT IN SMITH-MAGENIS SYNDROME.
RX   MEDLINE=21297181; PubMed=11404004; DOI=10.1016/S0378-1119(01)00415-2;
RA   Seranski P., Hoff C., Radelof U., Henning S., Reinhard R.,
RA   Schwartz C.E., Heiss N., Poustka A.;
RT   "RAI1 is a novel polyglutamine encoding gene that is deleted in Smith-
RT   Magenis syndrome patients.";
RL   Gene 270:69-76(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   MEDLINE=22721691; PubMed=12837267; DOI=10.1016/S0888-7543(03)00101-0;
RA   Toulouse A., Rochefort D., Roussel J., Joober R., Rouleau G.A.;
RT   "Molecular cloning and characterization of human RAI1, a gene
RT   associated with schizophrenia.";
RL   Genomics 82:162-171(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=21245130; PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 622-1906.
RC   TISSUE=Melanoma, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   INVOLVEMENT IN SMITH-MAGENIS SYNDROME.
RX   PubMed=12652298; DOI=10.1038/ng1126;
RA   Slager R.E., Newton T.L., Vlangos C.N., Finucane B., Elsea S.H.;
RT   "Mutations in RAI1 associated with Smith-Magenis syndrome.";
RL   Nat. Genet. 33:466-468(2003).
RN   [7]
RP   ROLE OF THE POLY-GLN REGION IN SPINOCEREBELLAR ATAXIA TYPE 2.
RX   PubMed=10915763; DOI=10.1093/hmg/9.12.1753;
RA   Hayes S., Turecki G., Brisebois K., Lopes-Cendes I., Gaspar C.,
RA   Riess O., Ranum L.P., Pulst S.M., Rouleau G.A.;
RT   "CAG repeat length in RAI1 is associated with age at onset variability
RT   in spinocerebellar ataxia type 2 (SCA2).";
RL   Hum. Mol. Genet. 9:1753-1758(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND
RP   SER-574, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1476, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT   cells and high confident phosphopeptide identification by cross-
RT   validation of MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; THR-696; SER-880;
RP   SER-892; SER-1108; SER-1122; SER-1352; SER-1358; SER-1374 AND
RP   SER-1431, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107; SER-1110;
RP   SER-1119; SER-1126; SER-1338; SER-1352; SER-1358 AND SER-1374, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; SER-1064; THR-1068
RP   AND SER-1374, AND MASS SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-774, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
CC   -!- FUNCTION: May function as a transcriptional regulator. Regulates
CC       transcription through chromatin remodeling by interacting with
CC       other proteins in chromatin as well as proteins in the basic
CC       transcriptional machinery. May be important for embryonic and
CC       postnatal development. May be involved in neuronal differentiation
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In neurons,
CC       localized to neurites (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q7Z5J4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z5J4-2; Sequence=VSP_010995, VSP_010996, VSP_010999,
CC                                  VSP_011002, VSP_011003;
CC       Name=3;
CC         IsoId=Q7Z5J4-3; Sequence=VSP_011000, VSP_011001;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q7Z5J4-4; Sequence=VSP_010997, VSP_010998;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined with higher
CC       expression in the heart and brain. No expression was seen in the
CC       corpus callosum of the brain.
CC   -!- POLYMORPHISM: The poly-Gln tract is polymorphic and the number of
CC       Gln varies from 12 to 14. The size of the poly-Gln region may
CC       influence the age at onset of spinocerebellar ataxia type 2
CC       (SCA2).
CC   -!- DISEASE: Defects in RAI1 are a cause of Smith-Magenis syndrome
CC       (SMS) [MIM:182290]. SMS is characterized by congenital mental
CC       retardation associated with development and growth delays.
CC       Affected persons have characteristic behavioral abnormalities,
CC       including self-injurious behaviors and sleep disturbance, and
CC       distinct craniofacial and skeletal anomalies.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47449.1; Type=Erroneous initiation;
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/RAI1";
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DR   EMBL; AJ271790; CAC20423.1; -; mRNA.
DR   EMBL; AJ271791; CAC20424.1; -; Genomic_DNA.
DR   EMBL; AY172136; AAO31738.1; -; mRNA.
DR   EMBL; AB058723; BAB47449.1; ALT_INIT; mRNA.
DR   EMBL; BC021209; AAH21209.1; -; mRNA.
DR   EMBL; AL133649; CAB63768.1; -; mRNA.
DR   EMBL; AL834468; CAD39127.1; -; mRNA.
DR   EMBL; AL834486; CAD39144.1; -; mRNA.
DR   IPI; IPI00449923; -.
DR   IPI; IPI00449924; -.
DR   IPI; IPI00449925; -.
DR   IPI; IPI00449926; -.
DR   PIR; T43490; T43490.
DR   RefSeq; NP_109590.3; -.
DR   UniGene; Hs.655395; -.
DR   ProteinModelPortal; Q7Z5J4; -.
DR   IntAct; Q7Z5J4; 3.
DR   MINT; MINT-1477867; -.
DR   STRING; Q7Z5J4; -.
DR   PhosphoSite; Q7Z5J4; -.
DR   PRIDE; Q7Z5J4; -.
DR   Ensembl; ENST00000353383; ENSP00000323074; ENSG00000108557.
DR   GeneID; 10743; -.
DR   KEGG; hsa:10743; -.
DR   UCSC; uc002grm.1; human.
DR   CTD; 10743; -.
DR   GeneCards; GC17P017525; -.
DR   H-InvDB; HIX0013588; -.
DR   HGNC; HGNC:9834; RAI1.
DR   MIM; 182290; phenotype.
DR   MIM; 607642; gene.
DR   Orphanet; 819; Smith-Magenis syndrome.
DR   PharmGKB; PA34188; -.
DR   eggNOG; prNOG18515; -.
DR   HOVERGEN; HBG056862; -.
DR   OrthoDB; EOG9K6JPN; -.
DR   PhylomeDB; Q7Z5J4; -.
DR   NextBio; 40793; -.
DR   ArrayExpress; Q7Z5J4; -.
DR   Bgee; Q7Z5J4; -.
DR   CleanEx; HS_RAI1; -.
DR   Genevestigator; Q7Z5J4; -.
DR   GermOnline; ENSG00000108557; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001965; Znf_PHD.
DR   SMART; SM00249; PHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW   Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Triplet repeat expansion; Zinc; Zinc-finger.
FT   CHAIN         1   1906       Retinoic acid-induced protein 1.
FT                                /FTId=PRO_0000097159.
FT   ZN_FING    1856   1903       PHD-type.
FT   MOTIF      1160   1177       Nuclear localization signal (Potential).
FT   MOTIF      1223   1240       Nuclear localization signal (Potential).
FT   COMPBIAS    124    135       Poly-Pro.
FT   COMPBIAS    156    336       Gln-rich.
FT   COMPBIAS    278    291       Poly-Gln.
FT   COMPBIAS   1243   1249       Poly-Ser.
FT   COMPBIAS   1493   1496       Poly-Gly.
FT   COMPBIAS   1628   1641       Ser-rich.
FT   COMPBIAS   1746   1751       Poly-Ala.
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     571    571       Phosphoserine.
FT   MOD_RES     574    574       Phosphoserine.
FT   MOD_RES     683    683       Phosphoserine.
FT   MOD_RES     696    696       Phosphothreonine.
FT   MOD_RES     774    774       N6-acetyllysine.
FT   MOD_RES     880    880       Phosphoserine.
FT   MOD_RES     892    892       Phosphoserine.
FT   MOD_RES    1064   1064       Phosphoserine.
FT   MOD_RES    1068   1068       Phosphothreonine.
FT   MOD_RES    1107   1107       Phosphoserine.
FT   MOD_RES    1108   1108       Phosphoserine.
FT   MOD_RES    1110   1110       Phosphoserine.
FT   MOD_RES    1119   1119       Phosphoserine.
FT   MOD_RES    1122   1122       Phosphoserine.
FT   MOD_RES    1126   1126       Phosphoserine.
FT   MOD_RES    1338   1338       Phosphoserine.
FT   MOD_RES    1352   1352       Phosphoserine.
FT   MOD_RES    1358   1358       Phosphoserine.
FT   MOD_RES    1374   1374       Phosphoserine.
FT   MOD_RES    1431   1431       Phosphoserine.
FT   MOD_RES    1476   1476       Phosphothreonine.
FT   VAR_SEQ     207    233       THFPQHSQSFPTSSTYSSSVQGGGQGA -> WWAGG (in
FT                                isoform 2).
FT                                /FTId=VSP_010995.
FT   VAR_SEQ     407    434       VDTQAGNCKPLQKDKLPENLLSDLSLQS -> PAD (in
FT                                isoform 2).
FT                                /FTId=VSP_010996.
FT   VAR_SEQ     947    966       SHMKPGEEGPDGERAPGDST -> YSVYICIHIHIYNIYED
FT                                CKC (in isoform 4).
FT                                /FTId=VSP_010997.
FT   VAR_SEQ     967   1906       Missing (in isoform 4).
FT                                /FTId=VSP_010998.
FT   VAR_SEQ    1415   1479       Missing (in isoform 2).
FT                                /FTId=VSP_010999.
FT   VAR_SEQ    1598   1640       FVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSS
FT                                SF -> LEPSLGAQNPRSGQNAPPAPADARPLCTTRDRRAY
FT                                SAREQGQR (in isoform 3).
FT                                /FTId=VSP_011000.
FT   VAR_SEQ    1641   1906       Missing (in isoform 3).
FT                                /FTId=VSP_011001.
FT   VAR_SEQ    1803   1821       Missing (in isoform 2).
FT                                /FTId=VSP_011002.
FT   VAR_SEQ    1856   1906       MCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFS
FT                                LKCPKHKRLP -> HGGTVALAPGDFSLPGLRFASLFQGPS
FT                                WCDCPVLATSTPSSWSRCVPAAKKPGPPLGAATKDASTPTT
FT                                TRVPAMQVRARPGTGGHWSPSKQSRGTLPGHSSPNPGPISL
FT                                FSFPPLLPQQFFYPSVCLDLCWAMPGTWK (in isoform
FT                                2).
FT                                /FTId=VSP_011003.
FT   VARIANT      90     90       G -> A (in dbSNP:rs3803763).
FT                                /FTId=VAR_051300.
FT   VARIANT     165    165       P -> T (in dbSNP:rs11649804).
FT                                /FTId=VAR_024344.
FT   VARIANT     939    939       Q -> P (in dbSNP:rs1759075).
FT                                /FTId=VAR_051301.
FT   CONFLICT    440    440       S -> L (in Ref. 2; AAO31738).
FT   CONFLICT   1302   1302       L -> F (in Ref. 2; AAO31738).
FT   CONFLICT   1513   1513       G -> A (in Ref. 2; AAO31738).
FT   CONFLICT   1682   1682       T -> A (in Ref. 5; CAD39144).
SQ   SEQUENCE   1906 AA;  203352 MW;  8D33A56C33BFE888 CRC64;
     MQSFRERCGF HGKQQNYQQT SQETSRLENY RQPSQAGLSC DRQRLLAKDY YNPQPYPSYE
     GGAGTPSGTA AAVAADKYHR GSKALPTQQG LQGRPAFPGY GVQDSSPYPG RYAGEESLQA
     WGAPQPPPPQ PQPLPAGVAK YDENLMKKTA VPPSRQYAEQ GAQVPFRTHS LHVQQPPPPQ
     QPLAYPKLQR QKLQNDIASP LPFPQGTHFP QHSQSFPTSS TYSSSVQGGG QGAHSYKSCT
     APTAQPHDRP LTASSSLAPG QRVQNLHAYQ SGRLSYDQQQ QQQQQQQQQQ QALQSRHHAQ
     ETLHYQNLAK YQHYGQQGQG YCQPDAAVRT PEQYYQTFSP SSSHSPARSV GRSPSYSSTP
     SPLMPNLENF PYSQQPLSTG AFPAGITDHS HFMPLLNPSP TDATSSVDTQ AGNCKPLQKD
     KLPENLLSDL SLQSLTALTS QVENISNTVQ QLLLSKAAVP QKKGVKNLVS RTPEQHKSQH
     CSPEGSGYSA EPAGTPLSEP PSSTPQSTHA EPQEADYLSG SEDPLERSFL YCNQARGSPA
     RVNSNSKAKP ESVSTCSVTS PDDMSTKSDD SFQSLHGSLP LDSFSKFVAG ERDCPRLLLS
     ALAQEDLASE ILGLQEAIGE KADKAWAEAP SLVKDSSKPP FSLENHSACL DSVAKSAWPR
     PGEPEALPDS LQLDKGGNAK DFSPGLFEDP SVAFATPDPK KTTGPLSFGT KPTLGVPAPD
     PTTAAFDCFP DTTAASSADS ANPFAWPEEN LGDACPRWGL HPGELTKGLE QGGKASDGIS
     KGDTHEASAC LGFQEEDPPG EKVASLPGDF KQEEVGGVKE EAGGLLQCPE VAKADRWLED
     SRHCCSTADF GDLPLLPPTS RKEDLEAEEE YSSLCELLGS PEQRPGMQDP LSPKAPLICT
     KEEVEEVLDS KAGWGSPCHL SGESVILLGP TVGTESKVQS WFESSLSHMK PGEEGPDGER
     APGDSTTSDA SLAQKPNKPA VPEAPIAKKE PVPRGKSLRS RRVHRGLPEA EDSPCRAPVL
     PKDLLLPESC TGPPQGQMEG AGAPGRGASE GLPRMCTRSL TALSEPRTPG PPGLTTTPAP
     PDKLGGKQRA AFKSGKRVGK PSPKAASSPS NPAALPVASD SSPMGSKTKE TDSPSTPGKD
     QRSMILRSRT KTQEIFHSKR RRPSEGRLPN CRATKKLLDN SHLPATFKVS SSPQKEGRVS
     QRARVPKPGA GSKLSDRPLH ALKRKSAFMA PVPTKKRNLV LRSRSSSSSN ASGNGGDGKE
     ERPEGSPTLF KRMSSPKKAK PTKGNGEPAT KLPPPETPDA CLKLASRAAF QGAMKTKVLP
     PRKGRGLKLE AIVQKITSPS LKKFACKAPG ASPGNPLSPS LSDKDRGLKG AGGSPVGVEE
     GLVNVGTGQK LPTSGADPLC RNPTNRSLKG KLMNSKKLSS TDCFKTEAFT SPEALQPGGT
     ALAPKKRSRK GRAGAHGLSK GPLEKRPYLG PALLLTPRDR ASGTQGASED NSGGGGKKPK
     MEELGLASQP PEGRPCQPQT RAQKQPGHTN YSSYSKRKRL TRGRAKNTTS SPCKGRAKRR
     RQQQVLPLDP AEPEIRLKYI SSCKRLRSDS RTPAFSPFVR VEKRDAFTTI CTVVNSPGDA
     PKPHRKPSSS ASSSSSSSSF SLDAAGASLA TLPGGSILQP RPSLPLSSTM HLGPVVSKAL
     STSCLVCCLC QNPANFKDLG DLCGPYYPEH CLPKKKPKLK EKVRPEGTCE EASLPLERTL
     KGPECAAAAT AGKPPRPDGP ADPAKQGPLR TSARGLSRRL QSCYCCDGRE DGGEEAAPAD
     KGRKHECSKE APAEPGGEAQ EHWVHEACAV WTGGVYLVAG KLFGLQEAMK VAVDMMCSSC
     QEAGATIGCC HKGCLHTYHY PCASDAGCIF IEENFSLKCP KHKRLP
//