Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13127

- REST_HUMAN

UniProt

Q13127 - REST_HUMAN

Protein

RE1-silencing transcription factor

Gene

REST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells. Restricts the expression of neuronal genes by associating with two distinct corepressors, mSin3 and CoREST, which in turn recruit histone deacetylase to the promoters of REST-regulated genes. Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 18123C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri216 – 23823C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri248 – 27023C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 29823C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri304 – 32623C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri332 – 35524C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri361 – 38323C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri389 – 41224C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1060 – 108223C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. core promoter binding Source: UniProtKB
    3. core promoter sequence-specific DNA binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. outward rectifier potassium channel activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: UniProtKB
    8. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    9. transcription factor binding Source: UniProtKB
    10. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. cardiac muscle cell myoblast differentiation Source: UniProtKB
    2. cellular response to drug Source: UniProtKB
    3. cellular response to electrical stimulus Source: UniProtKB
    4. cellular response to glucocorticoid stimulus Source: UniProtKB
    5. histone H4 deacetylation Source: UniProtKB
    6. negative regulation by host of viral transcription Source: UniProtKB
    7. negative regulation of aldosterone biosynthetic process Source: UniProtKB
    8. negative regulation of amniotic stem cell differentiation Source: UniProtKB
    9. negative regulation of calcium ion-dependent exocytosis Source: UniProtKB
    10. negative regulation of cell proliferation Source: UniProtKB
    11. negative regulation of cortisol biosynthetic process Source: UniProtKB
    12. negative regulation of dense core granule biogenesis Source: UniProtKB
    13. negative regulation of gene expression Source: UniProtKB
    14. negative regulation of insulin secretion Source: UniProtKB
    15. negative regulation of mesenchymal stem cell differentiation Source: UniProtKB
    16. negative regulation of neurogenesis Source: UniProtKB
    17. negative regulation of neuron differentiation Source: UniProtKB
    18. negative regulation of transcription, DNA-templated Source: UniProtKB
    19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. positive regulation of apoptotic process Source: UniProtKB
    21. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    22. positive regulation of transcription, DNA-templated Source: UniProtKB
    23. potassium ion transmembrane transport Source: GOC
    24. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ13127.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RE1-silencing transcription factor
    Alternative name(s):
    Neural-restrictive silencer factor
    X2 box repressor
    Gene namesi
    Name:REST
    Synonyms:NRSF, XBR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9966. REST.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleus Source: UniProtKB
    3. transcriptional repressor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34334.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10971097RE1-silencing transcription factorPRO_0000269547Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei864 – 8641Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13127.
    PaxDbiQ13127.
    PRIDEiQ13127.

    PTM databases

    PhosphoSiteiQ13127.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed at higher levels in the tissues of the lymphocytic compartment, including spleen, thymus, peripheral blood lymphocytes and ovary.1 Publication

    Gene expression databases

    BgeeiQ13127.
    CleanExiHS_REST.
    GenevestigatoriQ13127.

    Organism-specific databases

    HPAiHPA006079.

    Interactioni

    Subunit structurei

    Interacts with SIN3A, SIN3B and RCOR1. Interacts with CDYL. Interacts with EHMT1 and EHMT2 only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMARCA4P515322EBI-926706,EBI-302489

    Protein-protein interaction databases

    BioGridi111910. 37 interactions.
    DIPiDIP-35264N.
    IntActiQ13127. 4 interactions.
    STRINGi9606.ENSP00000311816.

    Structurei

    Secondary structure

    1
    1097
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 5512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CZYNMR-B43-57[»]
    ProteinModelPortaliQ13127.
    SMRiQ13127. Positions 149-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13127.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 12291Interaction with SIN3AAdd
    BLAST
    Regioni43 – 5715Interaction with SIN3BAdd
    BLAST
    Regioni1009 – 108779Interaction with RCOR1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 144Poly-Gly
    Compositional biasi400 – 603204Lys-richAdd
    BLAST
    Compositional biasi595 – 815221Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 9 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri159 – 18123C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri216 – 23823C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri248 – 27023C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri276 – 29823C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri304 – 32623C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri332 – 35524C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri361 – 38323C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri389 – 41224C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1060 – 108223C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG271556.
    HOVERGENiHBG093893.
    InParanoidiQ13127.
    KOiK09222.
    OMAiVQKEPVQ.
    OrthoDBiEOG73FQM4.
    PhylomeDBiQ13127.
    TreeFamiTF332861.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR027775. C2H2_Znf_fam.
    IPR027757. REST.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PANTHERiPTHR10032. PTHR10032. 1 hit.
    PTHR10032:SF71. PTHR10032:SF71. 1 hit.
    SMARTiSM00355. ZnF_C2H2. 9 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 6 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q13127-1) [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

    MATQVMGQSS GGGGLFTSSG NIGMALPNDM YDLHDLSKAE LAAPQLIMLA     50
    NVALTGEVNG SCCDYLVGEE RQMAELMPVG DNNFSDSEEG EGLEESADIK 100
    GEPHGLENME LRSLELSVVE PQPVFEASGA PDIYSSNKDL PPETPGAEDK 150
    GKSSKTKPFR CKPCQYEAES EEQFVHHIRV HSAKKFFVEE SAEKQAKARE 200
    SGSSTAEEGD FSKGPIRCDR CGYNTNRYDH YTAHLKHHTR AGDNERVYKC 250
    IICTYTTVSE YHWRKHLRNH FPRKVYTCGK CNYFSDRKNN YVQHVRTHTG 300
    ERPYKCELCP YSSSQKTHLT RHMRTHSGEK PFKCDQCSYV ASNQHEVTRH 350
    ARQVHNGPKP LNCPHCDYKT ADRSNFKKHV ELHVNPRQFN CPVCDYAASK 400
    KCNLQYHFKS KHPTCPNKTM DVSKVKLKKT KKREADLPDN ITNEKTEIEQ 450
    TKIKGDVAGK KNEKSVKAEK RDVSKEKKPS NNVSVIQVTT RTRKSVTEVK 500
    EMDVHTGSNS EKFSKTKKSK RKLEVDSHSL HGPVNDEESS TKKKKKVESK 550
    SKNNSQEVPK GDSKVEENKK QNTCMKKSTK KKTLKNKSSK KSSKPPQKEP 600
    VEKGSAQMDP PQMGPAPTEA VQKGPVQVEP PPPMEHAQME GAQIRPAPDE 650
    PVQMEVVQEG PAQKELLPPV EPAQMVGAQI VLAHMELPPP METAQTEVAQ 700
    MGPAPMEPAQ MEVAQVESAP MQVVQKEPVQ MELSPPMEVV QKEPVQIELS 750
    PPMEVVQKEP VKIELSPPIE VVQKEPVQME LSPPMGVVQK EPAQREPPPP 800
    REPPLHMEPI SKKPPLRKDK KEKSNMQSER ARKEQVLIEV GLVPVKDSWL 850
    LKESVSTEDL SPPSPPLPKE NLREEASGDQ KLLNTGEGNK EAPLQKVGAE 900
    EADESLPGLA ANINESTHIS SSGQNLNTPE GETLNGKHQT DSIVCEMKMD 950
    TDQNTRENLT GINSTVEEPV SPMLPPSAVE EREAVSKTAL ASPPATMAAN 1000
    ESQEIDEDEG IHSHEGSDLS DNMSEGSDDS GLHGARPVPQ ESSRKNAKEA 1050
    LAVKAAKGDF VCIFCDRSFR KGKDYSKHLN RHLVNVYYLE EAAQGQE 1097
    Length:1,097
    Mass (Da):121,872
    Last modified:May 18, 2010 - v3
    Checksum:iEBC652EED19CA161
    GO
    Isoform 2 (identifier: Q13127-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         301-313: ERPYKCELCPYSS → KRSFLVHKFSSLF
         314-1097: Missing.

    Show »
    Length:313
    Mass (Da):35,048
    Checksum:i3B0F550EBD70F79D
    GO
    Isoform 3 (identifier: Q13127-3) [UniParc]FASTAAdd to Basket

    Also known as: N4

    The sequence of this isoform differs from the canonical sequence as follows:
         329-329: E → W
         330-1097: Missing.

    Show »
    Length:329
    Mass (Da):36,972
    Checksum:iAD25D9BAC94FCAF7
    GO
    Isoform 4 (identifier: Q13127-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         304-326: Missing.

    Show »
    Length:1,074
    Mass (Da):119,083
    Checksum:i7D5F7CBD2C74EC0A
    GO

    Sequence cautioni

    The sequence AAH38985.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAA98503.1 differs from that shown. Reason: Frameshift at positions 188, 198, 202, 212 and 1087.
    The sequence AAC50114.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAC50115.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAD92987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti295 – 2951V → L in AAC50114. (PubMed:7871435)Curated
    Sequence conflicti596 – 5994PQKE → SRNS in AAC50115. (PubMed:7871435)Curated
    Sequence conflicti630 – 6301P → L in AAB17211. (PubMed:7697725)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti626 – 6261V → I.1 Publication
    Corresponds to variant rs2228991 [ dbSNP | Ensembl ].
    VAR_029795
    Natural varianti692 – 6921E → D.
    Corresponds to variant rs2227902 [ dbSNP | Ensembl ].
    VAR_029796
    Natural varianti762 – 7621K → Q.
    Corresponds to variant rs2227903 [ dbSNP | Ensembl ].
    VAR_029797
    Natural varianti797 – 7971P → L.1 Publication
    Corresponds to variant rs3796529 [ dbSNP | Ensembl ].
    VAR_029798

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei301 – 31313ERPYK…CPYSS → KRSFLVHKFSSLF in isoform 2. 1 PublicationVSP_022064Add
    BLAST
    Alternative sequencei304 – 32623Missing in isoform 4. CuratedVSP_022067Add
    BLAST
    Alternative sequencei314 – 1097784Missing in isoform 2. 1 PublicationVSP_022065Add
    BLAST
    Alternative sequencei329 – 3291E → W in isoform 3. CuratedVSP_022066
    Alternative sequencei330 – 1097768Missing in isoform 3. CuratedVSP_022068Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22314 mRNA. Translation: AAB17211.1.
    U13877 mRNA. Translation: AAC50114.1. Different initiation.
    U13879 mRNA. Translation: AAC50115.1. Different initiation.
    U22680 mRNA. Translation: AAA98503.1. Frameshift.
    AB209750 mRNA. Translation: BAD92987.1. Different initiation.
    AC069307 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05517.1.
    BC038985 mRNA. Translation: AAH38985.1. Sequence problems.
    BC132859 mRNA. Translation: AAI32860.1.
    BC136491 mRNA. Translation: AAI36492.1.
    CCDSiCCDS3509.1. [Q13127-1]
    PIRiA56138.
    I38754.
    I38755.
    RefSeqiNP_001180437.1. NM_001193508.1. [Q13127-1]
    NP_005603.3. NM_005612.4. [Q13127-1]
    UniGeneiHs.307836.

    Genome annotation databases

    EnsembliENST00000309042; ENSP00000311816; ENSG00000084093. [Q13127-1]
    GeneIDi5978.
    KEGGihsa:5978.
    UCSCiuc003hch.3. human. [Q13127-1]
    uc031ser.1. human. [Q13127-2]
    uc031ses.1. human. [Q13127-3]
    uc031sex.1. human. [Q13127-4]

    Polymorphism databases

    DMDMi296452989.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22314 mRNA. Translation: AAB17211.1 .
    U13877 mRNA. Translation: AAC50114.1 . Different initiation.
    U13879 mRNA. Translation: AAC50115.1 . Different initiation.
    U22680 mRNA. Translation: AAA98503.1 . Frameshift.
    AB209750 mRNA. Translation: BAD92987.1 . Different initiation.
    AC069307 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05517.1 .
    BC038985 mRNA. Translation: AAH38985.1 . Sequence problems.
    BC132859 mRNA. Translation: AAI32860.1 .
    BC136491 mRNA. Translation: AAI36492.1 .
    CCDSi CCDS3509.1. [Q13127-1 ]
    PIRi A56138.
    I38754.
    I38755.
    RefSeqi NP_001180437.1. NM_001193508.1. [Q13127-1 ]
    NP_005603.3. NM_005612.4. [Q13127-1 ]
    UniGenei Hs.307836.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CZY NMR - B 43-57 [» ]
    ProteinModelPortali Q13127.
    SMRi Q13127. Positions 149-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111910. 37 interactions.
    DIPi DIP-35264N.
    IntActi Q13127. 4 interactions.
    STRINGi 9606.ENSP00000311816.

    PTM databases

    PhosphoSitei Q13127.

    Polymorphism databases

    DMDMi 296452989.

    Proteomic databases

    MaxQBi Q13127.
    PaxDbi Q13127.
    PRIDEi Q13127.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309042 ; ENSP00000311816 ; ENSG00000084093 . [Q13127-1 ]
    GeneIDi 5978.
    KEGGi hsa:5978.
    UCSCi uc003hch.3. human. [Q13127-1 ]
    uc031ser.1. human. [Q13127-2 ]
    uc031ses.1. human. [Q13127-3 ]
    uc031sex.1. human. [Q13127-4 ]

    Organism-specific databases

    CTDi 5978.
    GeneCardsi GC04P057689.
    H-InvDB HIX0031381.
    HGNCi HGNC:9966. REST.
    HPAi HPA006079.
    MIMi 600571. gene.
    neXtProti NX_Q13127.
    PharmGKBi PA34334.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271556.
    HOVERGENi HBG093893.
    InParanoidi Q13127.
    KOi K09222.
    OMAi VQKEPVQ.
    OrthoDBi EOG73FQM4.
    PhylomeDBi Q13127.
    TreeFami TF332861.

    Enzyme and pathway databases

    SignaLinki Q13127.

    Miscellaneous databases

    ChiTaRSi REST. human.
    EvolutionaryTracei Q13127.
    GeneWikii RE1-silencing_transcription_factor.
    GenomeRNAii 5978.
    NextBioi 23267.
    PROi Q13127.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13127.
    CleanExi HS_REST.
    Genevestigatori Q13127.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR027775. C2H2_Znf_fam.
    IPR027757. REST.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    PANTHERi PTHR10032. PTHR10032. 1 hit.
    PTHR10032:SF71. PTHR10032:SF71. 1 hit.
    SMARTi SM00355. ZnF_C2H2. 9 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "REST: a mammalian silencer protein that restricts sodium channel gene expression to neurons."
      Chong J.A., Tapia-Ramirez J., Kim S., Toledo-Aral J.J., Zheng Y., Boutros M.C., Altshuller Y.M., Frohman M.A., Kraner S.D., Mandel G.
      Cell 80:949-957(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. "The neuron-restrictive silencer factor (NRSF): a coordinate repressor of multiple neuron-specific genes."
      Schoenherr C.J., Anderson D.J.
      Science 267:1360-1363(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-599 (ISOFORM 1), FUNCTION.
    3. "A zinc finger protein that represses transcription of the human MHC class II gene, DPA."
      Scholl T., Stevens M.B., Mahanta S., Strominger J.L.
      J. Immunol. 156:1448-1457(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT LEU-797.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1), VARIANT ILE-626.
      Tissue: Testis and Uterus.
    8. "Neuron-specific splicing of zinc finger transcription factor REST/NRSF/XBR is frequent in neuroblastomas and conserved in human, mouse and rat."
      Palm K., Metsis M., Timmusk T.
      Brain Res. Mol. Brain Res. 72:30-39(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 3 AND 4).
    9. "CoREST: a functional corepressor required for regulation of neural-specific gene expression."
      Andres M.E., Burger C., Peral-Rubio M.J., Battaglioli E., Anderson M.E., Grimes J., Dallman J., Ballas N., Mandel G.
      Proc. Natl. Acad. Sci. U.S.A. 96:9873-9878(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RCOR1.
    10. "The co-repressor mSin3A is a functional component of the REST-CoREST repressor complex."
      Grimes J.A., Nielsen S.J., Battaglioli E., Miska E.A., Speh J.C., Berry D.L., Atouf F., Holdener B.C., Mandel G., Kouzarides T.
      J. Biol. Chem. 275:9461-9467(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RCOR1 AND SIN3A.
    11. Cited for: FUNCTION.
    12. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
      Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
      Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDYL; EHMT1 AND EHMT2, IDENTIFICATION IN A COMPLEX WITH CDYL; SETB1; EHMT1; EHMT2 AND WIZ.
    13. "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].
    14. "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-864, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix."
      Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y.
      J. Mol. Biol. 354:903-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 43-57 IN COMPLEX WITH SIN3B, INTERACTION WITH SIN3B.

    Entry informationi

    Entry nameiREST_HUMAN
    AccessioniPrimary (citable) accession number: Q13127
    Secondary accession number(s): A2RUE0
    , B9EGJ0, Q12956, Q12957, Q13134, Q59ER1, Q8IWI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3