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Index > Protein center > FICD(Gene name) > Human
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  • FICD (Gene name),
  • Adenosine monophosphate-protein transferase FICD (Protein name ),  FICD_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:
    FICD(UNQ3041/PRO9857;HIP13;HYPE);
    Protein name:
    Adenosine monophosphate-protein transferase FICD;
    Alternative:
    FIC domain-containing protein;AMPylator FICD;Huntingtin-interacting protein 13(HIP-13);Huntingtin yeast partner E;Huntingtin-interacting protein E;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Interacts with HD.
    Function:
    Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.
    Subcellular Location:
    Membrane Single-pass membrane protein
    Protein Attributes:
    Sequence length:
    458
    Sequence:
    50:
    MMLIPMASVM | AVTEPKWVSV | WSRFLWVTLL | SMVLGSLLAL | LLPLGAVEEQ | 
    100:
    CLAVLKGLYL | LRSKPDRAQH | AATKCTSPST | ELSITSRGAT | LLVAKTKASP | 
    150:
    AGKLEARAAL | NQALEMKRQG | KREKAQKLFM | HALKMDPDFV | DALTEFGIFS | 
    200:
    EEDKDIIQAD | YLYTRALTIS | PYHEKALVNR | DRTLPLVEEI | DQRYFSIIDS | 
    250:
    KVKKVMSIPK | GNSALRRVME | ETYYHHIYHT | VAIEGNTLTL | SEIRHILETR | 
    300:
    YAVPGKSLEE | QNEVIGMHAA | MKYINTTLVS | RIGSVTISDV | LEIHRRVLGY | 
    350:
    VDPVEAGRFR | TTQVLVGHHI | PPHPQDVEKQ | MQEFVQWLNS | EEAMNLHPVE | 
    400:
    FAALAHYKLV | YIHPFIDGNG | RTSRLLMNLI | LMQAGYPPIT | IRKEQRSDYY | 
    450:
    HVLEAANEGD | VRPFIRFIAK | CTETTLDTLL | FATTEYSVAL | PEAQPNHSGF | 
    458:
    KETLPVKP
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
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    Related Databases
    SMR:
    KEGG:
    UniGene:
    String:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Human Adenosine monophosphate-protein transferase FICD
    ELISA Kit for Human Adenosine monophosphate-protein transferase FICD
    ELISA Kit for Human Adenosine monophosphate-protein transferase FICD
    CLIA Kit for Human Adenosine monophosphate-protein transferase FICD
    CLIA Kit for Human Adenosine monophosphate-protein transferase FICD
    CLIA Kit for Human Adenosine monophosphate-protein transferase FICD
    Polyclonal Antibody for Human Adenosine monophosphate-protein transferase FICD
    Polyclonal Antibody for Human Adenosine monophosphate-protein transferase FICD
    Polyclonal Antibody for Human Adenosine monophosphate-protein transferase FICD
    Monoclonal Antibody for Human Adenosine monophosphate-protein transferase FICD
    Monoclonal Antibody for Human Adenosine monophosphate-protein transferase FICD
    Monoclonal Antibody for Human Adenosine monophosphate-protein transferase FICD
    Protein for Human Adenosine monophosphate-protein transferase FICD
    Protein for Human Adenosine monophosphate-protein transferase FICD
    Protein for Human Adenosine monophosphate-protein transferase FICD

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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
      Clark H.F. , Gurney A.L. , Abaya E. , Baker K. , Baldwin D.T. , Brush J. , Chen J. , Chow B. , Chui C. , Crowley C. , Currell B. , Deuel B. , Dowd P. , Eaton D. , Foster J.S. , Grimaldi C. , Gu Q. , Hass P.E. , more...
      Genome Res.13:2265-2270(2003) [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]
    2. 2.
      [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.
      "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]
      tissue: Cervix.
    4. 4.
      "Huntingtin interacts with a family of WW domain proteins."
      Faber P.W. , Barnes G.T. , Srinidhi J. , Chen J. , Gusella J.F. , MacDonald M.E.
      Hum. Mol. Genet.7:1463-1474(1998) [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 [MRNA] OF 275-458;INTERACTION WITH HD
      tissue: Frontal cortex.
    5. 5.
      "The fic domain: regulation of cell signaling by adenylylation."
      Worby C.A. , Mattoo S. , Kruger R.P. , Corbeil L.B. , Koller A. , Mendez J.C. , Zekarias B. , Lazar C. , Dixon J.E.
      Mol. Cell34:93-103(2009) [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;CATALYTIC ACTIVITY;TISSUE SPECIFICITY;MUTAGENESIS OF HIS-363
    6. 6.
      "Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins."
      Engel P. , Goepfert A. , Stanger F.V. , Harms A. , Schmidt A. , Schirmer T. , Dehio C.
      Nature482:107-110(2012) [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;ENZYME REGULATION;MUTAGENESIS OF GLU-234
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