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Q14140

- SRTD2_HUMAN

UniProt

Q14140 - SRTD2_HUMAN

Protein

SERTA domain-containing protein 2

Gene

SERTAD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. May act as coactivator as well as corepressor of E2F1-TFDP1 and E2F4-TFDP1 complexes on E2F consensus binding sites, which would activate or inhibit E2F-target genes expression. Modulates fat storage by down-regulating the expression of key genes involved in adipocyte lipolysis, thermogenesis and oxidative metabolism.1 Publication

    GO - Molecular functioni

    1. transcription coactivator activity Source: Ensembl

    GO - Biological processi

    1. negative regulation of cell growth Source: MGI
    2. positive regulation of transcription, DNA-templated Source: Ensembl
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SERTA domain-containing protein 2
    Alternative name(s):
    Transcriptional regulator interacting with the PHD-bromodomain 2
    Short name:
    TRIP-Br2
    Gene namesi
    Name:SERTAD2
    Synonyms:KIAA0127
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:30784. SERTAD2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Exported out of the nucleus via its NES in a XPO1-dependent manner. Once in the cytoplasm, is degraded by the proteasome.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi238 – 2381L → A: Abolishes the interaction with XPO1 as well as the nuclear export and the subsequent proteasomal degradation. 1 Publication
    Mutagenesisi241 – 2411L → A: Slight resistance to proteasomal degradation, no effect on the interaction with XPO1 neither on nuclear export. 1 Publication
    Mutagenesisi243 – 2431L → A: Slight decrease of interaction with XPO1 and resistance to proteasomal degradation, no effect on nuclear export. 1 Publication

    Organism-specific databases

    PharmGKBiPA134948884.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314SERTA domain-containing protein 2PRO_0000191613Add
    BLAST

    Post-translational modificationi

    Polyubiquitinated, which promotes proteasomal degradation.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ14140.
    PRIDEiQ14140.

    PTM databases

    PhosphoSiteiQ14140.

    Expressioni

    Tissue specificityi

    Expressed in adipose tissue.1 Publication

    Developmental stagei

    Transcript levels remain constant in all phases of the cell cycle. In contrast, protein levels accumulate at the G1/S phase boundary and decrease progressively through S phase until G2/M phase is reached, residual expression is observed in the G2/M and early G1 phases.1 Publication

    Gene expression databases

    BgeeiQ14140.
    CleanExiHS_SERTAD2.
    GenevestigatoriQ14140.

    Organism-specific databases

    HPAiHPA019021.
    HPA020904.

    Interactioni

    Subunit structurei

    Interacts with XPO1; which mediates nuclear export. Interacts with TFDP1; modulates transactivation activity of TFDP1/E2F complexes.2 Publications

    Protein-protein interaction databases

    BioGridi115136. 9 interactions.
    IntActiQ14140. 1 interaction.
    STRINGi9606.ENSP00000326933.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14140.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 8048SERTAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni235 – 31177Required for transactivation activityAdd
    BLAST
    Regioni238 – 2436Nuclear export signal (NES)

    Sequence similaritiesi

    Contains 1 SERTA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG47551.
    HOGENOMiHOG000111497.
    HOVERGENiHBG097654.
    InParanoidiQ14140.
    OMAiPCDLGST.
    OrthoDBiEOG7VTDNP.
    PhylomeDBiQ14140.
    TreeFamiTF331620.

    Family and domain databases

    InterProiIPR009263. SERTA_dom.
    [Graphical view]
    PfamiPF06031. SERTA. 1 hit.
    [Graphical view]
    PROSITEiPS51053. SERTA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14140-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGKGGKRKF DEHEDGLEGK IVSPCDGPSK VSYTLQRQTI FNISLMKLYN    50
    HRPLTEPSLQ KTVLINNMLR RIQEELKQEG SLRPMFTPSS QPTTEPSDSY 100
    REAPPAFSHL ASPSSHPCDL GSTTPLEACL TPASLLEDDD DTFCTSQAMQ 150
    PTAPTKLSPP ALLPEKDSFS SALDEIEELC PTSTSTEAAT AATDSVKGTS 200
    SEAGTQKLDG PQESRADDSK LMDSLPGNFE ITTSTGFLTD LTLDDILFAD 250
    IDTSMYDFDP CTSSSGTASK MAPVSADDLL KTLAPYSSQP VTPSQPFKMD 300
    LTELDHIMEV LVGS 314
    Length:314
    Mass (Da):33,897
    Last modified:November 1, 1996 - v1
    Checksum:iE43107FC565AAC31
    GO

    Sequence cautioni

    The sequence BAA09476.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50917 mRNA. Translation: BAA09476.2. Different initiation.
    AC007365 Genomic DNA. Translation: AAY14766.1.
    BC074788 mRNA. Translation: AAH74788.1.
    BC074789 mRNA. Translation: AAH74789.1.
    BC101639 mRNA. Translation: AAI01640.1.
    BC101641 mRNA. Translation: AAI01642.1.
    CCDSiCCDS33210.1.
    RefSeqiNP_055570.1. NM_014755.2.
    XP_005264726.1. XM_005264669.1.
    UniGeneiHs.591569.

    Genome annotation databases

    EnsembliENST00000313349; ENSP00000326933; ENSG00000179833.
    GeneIDi9792.
    KEGGihsa:9792.
    UCSCiuc002sde.2. human.

    Polymorphism databases

    DMDMi3123047.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50917 mRNA. Translation: BAA09476.2 . Different initiation.
    AC007365 Genomic DNA. Translation: AAY14766.1 .
    BC074788 mRNA. Translation: AAH74788.1 .
    BC074789 mRNA. Translation: AAH74789.1 .
    BC101639 mRNA. Translation: AAI01640.1 .
    BC101641 mRNA. Translation: AAI01642.1 .
    CCDSi CCDS33210.1.
    RefSeqi NP_055570.1. NM_014755.2.
    XP_005264726.1. XM_005264669.1.
    UniGenei Hs.591569.

    3D structure databases

    ProteinModelPortali Q14140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115136. 9 interactions.
    IntActi Q14140. 1 interaction.
    STRINGi 9606.ENSP00000326933.

    PTM databases

    PhosphoSitei Q14140.

    Polymorphism databases

    DMDMi 3123047.

    Proteomic databases

    PaxDbi Q14140.
    PRIDEi Q14140.

    Protocols and materials databases

    DNASUi 9792.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313349 ; ENSP00000326933 ; ENSG00000179833 .
    GeneIDi 9792.
    KEGGi hsa:9792.
    UCSCi uc002sde.2. human.

    Organism-specific databases

    CTDi 9792.
    GeneCardsi GC02M064770.
    HGNCi HGNC:30784. SERTAD2.
    HPAi HPA019021.
    HPA020904.
    neXtProti NX_Q14140.
    PharmGKBi PA134948884.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47551.
    HOGENOMi HOG000111497.
    HOVERGENi HBG097654.
    InParanoidi Q14140.
    OMAi PCDLGST.
    OrthoDBi EOG7VTDNP.
    PhylomeDBi Q14140.
    TreeFami TF331620.

    Miscellaneous databases

    GenomeRNAii 9792.
    NextBioi 36874.
    PROi Q14140.

    Gene expression databases

    Bgeei Q14140.
    CleanExi HS_SERTAD2.
    Genevestigatori Q14140.

    Family and domain databases

    InterProi IPR009263. SERTA_dom.
    [Graphical view ]
    Pfami PF06031. SERTA. 1 hit.
    [Graphical view ]
    PROSITEi PS51053. SERTA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    2. "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].
    3. "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].
      Tissue: Brain and Brain cortex.
    4. "TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting proteins that regulate the transcriptional activity of E2F-1/DP-1."
      Hsu S.-I., Yang C.M., Sim K.G., Hentschel D.M., O'Leary E., Bonventre J.V.
      EMBO J. 20:2273-2285(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COREGULATOR, INTERACTION WITH TFDP1.
    5. "CRM1-mediated nuclear export is required for 26 S proteasome-dependent degradation of the TRIP-Br2 proto-oncoprotein."
      Cheong J.K., Gunaratnam L., Hsu S.I.
      J. Biol. Chem. 283:11661-11676(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XPO1, DEVELOPMENTAL STAGE, NUCLEAR EXPORT SIGNAL, UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-238; LEU-241 AND LEU-243.
    6. "Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and oxidative metabolism, prevents diet-induced obesity and insulin resistance."
      Liew C.W., Boucher J., Cheong J.K., Vernochet C., Koh H.J., Mallol C., Townsend K., Langin D., Kawamori D., Hu J., Tseng Y.H., Hellerstein M.K., Farmer S.R., Goodyear L., Doria A., Blueher M., Hsu S.I., Kulkarni R.N.
      Nat. Med. 19:217-226(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiSRTD2_HUMAN
    AccessioniPrimary (citable) accession number: Q14140
    Secondary accession number(s): Q53TS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3