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Q15650

- TRIP4_HUMAN

UniProt

Q15650 - TRIP4_HUMAN

Protein

Activating signal cointegrator 1

Gene

TRIP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 4 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Transcription coactivator of nuclear receptors which functions in conjunction with CBP-p300 and SRC-1 and may play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B. Plays a role in androgen receptor transactivation and in testicular function By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri171 – 18717C4-typeAdd
    BLAST

    GO - Molecular functioni

    1. ligand-dependent nuclear receptor binding Source: UniProtKB
    2. transcription coactivator activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: UniProtKB
    2. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activating signal cointegrator 1
    Short name:
    ASC-1
    Alternative name(s):
    Thyroid receptor-interacting protein 4
    Short name:
    TR-interacting protein 4
    Short name:
    TRIP-4
    Gene namesi
    Name:TRIP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:12310. TRIP4.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Cytoplasmic under conditions of serum deprivation. Colocalizes with NEK6 in the centrosome.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36988.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 581580Activating signal cointegrator 1PRO_0000065631Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei289 – 2891PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated by NEK6.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15650.
    PaxDbiQ15650.
    PeptideAtlasiQ15650.
    PRIDEiQ15650.

    PTM databases

    PhosphoSiteiQ15650.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15650.
    BgeeiQ15650.
    CleanExiHS_TRIP4.
    GenevestigatoriQ15650.

    Organism-specific databases

    HPAiHPA016605.
    HPA050666.

    Interactioni

    Subunit structurei

    Specifically interacts with the ligand binding domain of the thyroid receptor (TR). This interaction requires the presence of thyroid hormone. Exists as a steady-state complex associated with ASCC1, ASCC2 and HELIC1. Interacts with the androgen receptor androgen (AR) in an androgen, testosterone and dihydrotestosterone-dependent manner By similarity. Interacts with NEK6.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi114735. 33 interactions.
    IntActiQ15650. 4 interactions.
    STRINGi9606.ENSP00000261884.

    Structurei

    Secondary structure

    1
    581
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi435 – 4395
    Helixi443 – 4486
    Beta strandi454 – 4596
    Beta strandi465 – 4717
    Helixi478 – 49215
    Beta strandi504 – 51815
    Helixi521 – 5255
    Turni530 – 5323
    Beta strandi535 – 54612
    Beta strandi557 – 5615
    Helixi564 – 5729
    Helixi573 – 5753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E5ONMR-A435-581[»]
    ProteinModelPortaliQ15650.
    SMRiQ15650. Positions 434-581.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15650.

    Family & Domainsi

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri171 – 18717C4-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG248556.
    HOGENOMiHOG000006873.
    HOVERGENiHBG061618.
    InParanoidiQ15650.
    OMAiMSGTENS.
    OrthoDBiEOG7RZ5PP.
    PhylomeDBiQ15650.
    TreeFamiTF314842.

    Family and domain databases

    InterProiIPR007374. ASCH_domain.
    IPR015947. PUA-like_domain.
    IPR009349. Znf_C2HC5.
    [Graphical view]
    PfamiPF04266. ASCH. 1 hit.
    PF06221. zf-C2HC5. 1 hit.
    [Graphical view]
    SMARTiSM01022. ASCH. 1 hit.
    [Graphical view]
    SUPFAMiSSF88697. SSF88697. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q15650-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVAGAVSGE PLVHWCTQQL RKTFGLDVSE EIIQYVLSIE SAEEIREYVT    50
    DLLQGNEGKK GQFIEELITK WQKNDQELIS DPLQQCFKKD EILDGQKSGD 100
    HLKRGRKKGR NRQEVPAFTE PDTTAEVKTP FDLAKAQENS NSVKKKTKFV 150
    NLYTREGQDR LAVLLPGRHP CDCLGQKHKL INNCLICGRI VCEQEGSGPC 200
    LFCGTLVCTH EEQDILQRDS NKSQKLLKKL MSGVENSGKV DISTKDLLPH 250
    QELRIKSGLE KAIKHKDKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK 300
    LERETLQKRE EELRELRHAS RLSKKVTIDF AGRKILEEEN SLAEYHSRLD 350
    ETIQAIANGT LNQPLTKLDR SSEEPLGVLV NPNMYQSPPQ WVDHTGAASQ 400
    KKAFRSSGFG LEFNSFQHQL RIQDQEFQEG FDGGWCLSVH QPWASLLVRG 450
    IKRVEGRSWY TPHRGRLWIA ATAKKPSPQE VSELQATYRL LRGKDVEFPN 500
    DYPSGCLLGC VDLIDCLSQK QFKEQFPDIS QESDSPFVFI CKNPQEMVVK 550
    FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V 581
    Length:581
    Mass (Da):66,146
    Last modified:October 17, 2006 - v4
    Checksum:iDADD3994533A808E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571G → R in AAF01278. (PubMed:10454579)Curated
    Sequence conflicti157 – 1571G → R in AAC41738. (PubMed:7776974)Curated
    Sequence conflicti164 – 1641L → A in AAF01278. (PubMed:10454579)Curated
    Sequence conflicti392 – 41019VDHTG…SSGFG → LTTQVQPHRRRLSVLQDLD(PubMed:7776974)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168418 mRNA. Translation: AAF01278.1.
    AK314319 mRNA. Translation: BAG36967.1.
    CH471082 Genomic DNA. Translation: EAW77685.1.
    BC012448 mRNA. Translation: AAH12448.1.
    L40371 mRNA. Translation: AAC41738.1.
    CCDSiCCDS10194.1.
    RefSeqiNP_057297.2. NM_016213.4.
    UniGeneiHs.500340.

    Genome annotation databases

    EnsembliENST00000261884; ENSP00000261884; ENSG00000103671.
    GeneIDi9325.
    KEGGihsa:9325.
    UCSCiuc002anm.3. human.

    Polymorphism databases

    DMDMi116242828.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168418 mRNA. Translation: AAF01278.1 .
    AK314319 mRNA. Translation: BAG36967.1 .
    CH471082 Genomic DNA. Translation: EAW77685.1 .
    BC012448 mRNA. Translation: AAH12448.1 .
    L40371 mRNA. Translation: AAC41738.1 .
    CCDSi CCDS10194.1.
    RefSeqi NP_057297.2. NM_016213.4.
    UniGenei Hs.500340.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E5O NMR - A 435-581 [» ]
    ProteinModelPortali Q15650.
    SMRi Q15650. Positions 434-581.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114735. 33 interactions.
    IntActi Q15650. 4 interactions.
    STRINGi 9606.ENSP00000261884.

    PTM databases

    PhosphoSitei Q15650.

    Polymorphism databases

    DMDMi 116242828.

    Proteomic databases

    MaxQBi Q15650.
    PaxDbi Q15650.
    PeptideAtlasi Q15650.
    PRIDEi Q15650.

    Protocols and materials databases

    DNASUi 9325.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261884 ; ENSP00000261884 ; ENSG00000103671 .
    GeneIDi 9325.
    KEGGi hsa:9325.
    UCSCi uc002anm.3. human.

    Organism-specific databases

    CTDi 9325.
    GeneCardsi GC15P064876.
    HGNCi HGNC:12310. TRIP4.
    HPAi HPA016605.
    HPA050666.
    MIMi 604501. gene.
    neXtProti NX_Q15650.
    PharmGKBi PA36988.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248556.
    HOGENOMi HOG000006873.
    HOVERGENi HBG061618.
    InParanoidi Q15650.
    OMAi MSGTENS.
    OrthoDBi EOG7RZ5PP.
    PhylomeDBi Q15650.
    TreeFami TF314842.

    Miscellaneous databases

    EvolutionaryTracei Q15650.
    GeneWikii TRIP4.
    GenomeRNAii 9325.
    NextBioi 34931.
    PROi Q15650.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15650.
    Bgeei Q15650.
    CleanExi HS_TRIP4.
    Genevestigatori Q15650.

    Family and domain databases

    InterProi IPR007374. ASCH_domain.
    IPR015947. PUA-like_domain.
    IPR009349. Znf_C2HC5.
    [Graphical view ]
    Pfami PF04266. ASCH. 1 hit.
    PF06221. zf-C2HC5. 1 hit.
    [Graphical view ]
    SMARTi SM01022. ASCH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF88697. SSF88697. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation."
      Kim H.J., Yi J.Y., Sung H.S., Moore D.D., Jhun B.H., Lee Y.C., Lee J.W.
      Mol. Cell. Biol. 19:6323-6332(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Lung.
    5. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
      Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
      Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-410.
    6. "Novel transcription coactivator complex containing activating signal cointegrator 1."
      Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.
      Mol. Cell. Biol. 22:5203-5211(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ASCC1; ASCC2 AND HELIC1.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
      Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
      J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION BY NEK6.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRIP4_HUMAN
    AccessioniPrimary (citable) accession number: Q15650
    Secondary accession number(s): B2RAS0, Q96ED7, Q9UKH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 127 of the entry and version 4 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 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3