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Index > Protein center > TRPC4AP(Gene name) > Human
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  • TRPC4AP (Gene name),
  • Short transient receptor potential channel 4-associated protein (Protein name ),  TP4AP_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • 3D
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  • Predicted Eptitope
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  • Vaild Sequence
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  • Gene name:
    TRPC4AP(C20orf188;TRRP4AP);
    Protein name:
    Short transient receptor potential channel 4-associated protein(Trp4-associated protein;Trpc4-associated protein);
    Alternative:
    TNF-receptor ubiquitous scaffolding/signaling protein(Protein TRUSS);Protein TAP1;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Constitutively associated with TNFRSF1A. Directly interacts with TRADD, TRAF2, CHUK, IKBKB and IKBKG. Interacts with TRPC1, TRPC4 and TRPC5 (By similarity). Component of the DCX(TRUSS) E3 ubiquitin ligase complex, at least composed of CUL4A, DDB1, TRPC4AP/TRUSS and RBX1. Interacts with MYC.
    Function:
    Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRUSS) complex specifically mediates the polyubiquitination and subsequent degradation of MYC. Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1.
    Subcellular Location:
    N/A
    Protein Attributes:
    Sequence length:
    797
    Sequence:
    50:
    MAAAPVAAGS | GAGRGRRSAA | TVAAWGGWGG | RPRPGNILLQ | LRQGQLTGRG | 
    100:
    LVRAVQFTET | FLTERDKQSK | WSGIPQLLLK | LHTTSHLHSD | FVECQNILKE | 
    150:
    ISPLLSMEAM | AFVTEERKLT | QETTYPNTYI | FDLFGGVDLL | VEILMRPTIS | 
    200:
    IRGQKLKISD | EMSKDCLSIL | YNTCVCTEGV | TKRLAEKNDF | VIFLFTLMTS | 
    250:
    KKTFLQTATL | IEDILGVKKE | MIRLDEVPNL | SSLVSNFDQQ | QLANFCRILA | 
    300:
    VTISEMDTGN | DDKHTLLAKN | AQQKKSLSLG | PSAAEINQAA | LLSIPGFVER | 
    350:
    LCKLATRKVS | ESTGTASFLQ | ELEEWYTWLD | NALVLDALMR | VANEESEHNQ | 
    400:
    ASIVFPPPGA | SEENGLPHTS | ARTQLPQSMK | IMHEIMYKLE | VLYVLCVLLM | 
    450:
    GRQRNQVHRM | IAEFKLIPGL | NNLFDKLIWR | KHSASALVLH | GHNQNCDCSP | 
    500:
    DITLKIQFLR | LLQSFSDHHE | NKYLLLNNQE | LNELSAISLK | ANIPEVEAVL | 
    550:
    NTDRSLVCDG | KRGLLTRLLQ | VMKKEPAESS | FRFWQARAVE | SFLRGTTSYA | 
    600:
    DQMFLLKRGL | LEHILYCIVD | SECKSRDVLQ | SYFDLLGELM | KFNVDAFKRF | 
    650:
    NKYINTDAKF | QVFLKQINSS | LVDSNMLVRC | VTLSLDRFEN | QVDMKVAEVL | 
    700:
    SECRLLAYIS | QVPTQMSFLF | RLINIIHVQT | LTQENVSCLN | TSLVILMLAR | 
    750:
    RKERLPLYLR | LLQRMEHSKK | YPGFLLNNFH | NLLRFWQQHY | LHKDKDSTCL | 
    797:
    ENSSCISFSY | WKETVSILLN | PDRQSPSALV | SYIEEPYMDI | DRDFTEE
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    String:
    UniGene:
    Pfam:
    MIM:
    KEGG:
    Uniprot:
     
    FOR
    ELISA Kit for Human Trp4-associated protein
    ELISA Kit for Human Trp4-associated protein
    CLIA Kit for Human Trp4-associated protein
    CLIA Kit for Human Trp4-associated protein
    Polyclonal Antibody for Human Trp4-associated protein
    Polyclonal Antibody for Human Trp4-associated protein
    Monoclonal Antibody for Human Trp4-associated protein
    Monoclonal Antibody for Human Trp4-associated protein
    Protein for Human Trp4-associated protein
    Protein for Human Trp4-associated protein

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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "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. , more...
      Nat. Genet.36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3)
    2. 2.
      "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P. , Matthews L.H. , Ashurst J.L. , Burton J. , Gilbert J.G.R. , Jones M. , Stavrides G. , Almeida J.P. , Babbage A.K. , Bagguley C.L. , Bailey J. , Barlow K.F. , Bates K.N. , Beard L.M. , Beare D.M. , Beasley O.P. , Bird C.P. , Blakey S.E. , more...
      Nature414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
    3. 3.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
    4. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
      tissue: Cervix.
      tissue: Muscle.
      tissue: Prostate.
    5. 5.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-797 (ISOFORM 1)
      tissue: Mammary cancer.
    6. 6.
      "Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."
      Choi S.H. , Wright J.B. , Gerber S.A. , Cole M.D.
      Genes Dev.24:1236-1241(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX;INTERACTION WITH MYC
    7. 7.
      "A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery."
      Li T. , Robert E.I. , van Breugel P.C. , Strubin M. , Zheng N.
      Nat. Struct. Mol. Biol.17:105-111(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH DDB1
    8. 8.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
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