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Index > Protein center > XPC(Gene name) > Human
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  • XPC (Gene name),
  • DNA repair protein complementing XP-C cells (Protein name ),  XPC_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Predicted Eptitope
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  • Vaild Sequence
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  • Gene name:
    XPC(XPCC);
    Protein name:
    DNA repair protein complementing XP-C cells;
    Alternative:
    p125;Xeroderma pigmentosum group C-complementing protein;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with RAD23A; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with TDG; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with SMUG1; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and ERCC3.
    Function:
    The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
    Subcellular Location:
    Nucleus Cytoplasm Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions.
    Protein Attributes:
    Sequence length:
    940
    Sequence:
    50:
    MARKRAAGGE | PRGRELRSQK | SKAKSKARRE | EEEEDAFEDE | KPPKKSLLSK | 
    100:
    VSQGKRKRGC | SHPGGSADGP | AKKKVAKVTV | KSENLKVIKD | EALSDGDDLR | 
    150:
    DFPSDLKKAH | HLKRGATMNE | DSNEEEEESE | NDWEEVEELS | EPVLGDVRES | 
    200:
    TAFSRSLLPV | KPVEIEIETP | EQAKTRERSE | KIKLEFETYL | RRAMKRFNKG | 
    250:
    VHEDTHKVHL | LCLLANGFYR | NNICSQPDLH | AIGLSIIPAR | FTRVLPRDVD | 
    300:
    TYYLSNLVKW | FIGTFTVNAE | LSASEQDNLQ | TTLERRFAIY | SARDDEELVH | 
    350:
    IFLLILRALQ | LLTRLVLSLQ | PIPLKSATAK | GKKPSKERLT | ADPGGSSETS | 
    400:
    SQVLENHTKP | KTSKGTKQEE | TFAKGTCRPS | AKGKRNKGGR | KKRSKPSSSE | 
    450:
    EDEGPGDKQE | KATQRRPHGR | ERRVASRVSY | KEESGSDEAG | SGSDFELSSG | 
    500:
    EASDPSDEDS | EPGPPKQRKA | PAPQRTKAGS | KSASRTHRGS | HRKDPSLPAA | 
    550:
    SSSSSSSKRG | KKMCSDGEKA | EKRSIAGIDQ | WLEVFCEQEE | KWVCVDCVHG | 
    600:
    VVGQPLTCYK | YATKPMTYVV | GIDSDGWVRD | VTQRYDPVWM | TVTRKCRVDA | 
    650:
    EWWAETLRPY | QSPFMDREKK | EDLEFQAKHM | DQPLPTAIGL | YKNHPLYALK | 
    700:
    RHLLKYEAIY | PETAAILGYC | RGEAVYSRDC | VHTLHSRDTW | LKKARVVRLG | 
    750:
    EVPYKMVKGF | SNRARKARLA | EPQLREENDL | GLFGYWQTEE | YQPPVAVDGK | 
    800:
    VPRNEFGNVY | LFLPSMMPIG | CVQLNLPNLH | RVARKLDIDC | VQAITGFDFH | 
    850:
    GGYSHPVTDG | YIVCEEFKDV | LLTAWENEQA | VIERKEKEKK | EKRALGNWKL | 
    900:
    LAKGLLIRER | LKRRYGPKSE | AAAPHTDAGG | GLSSDEEEGT | SSQAEAARIL | 
    940:
    AASWPQNRED | EEKQKLKGGP | KKTKREKKAA | ASHLFPFEQL | 
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
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    Related Databases
    Pfam:
    UniGene:
    SMR:
    KEGG:
    MIM:
    String:
    Uniprot:
     
    FOR
    ELISA Kit for Human DNA repair protein complementing XP-C cells
    ELISA Kit for Human DNA repair protein complementing XP-C cells
    CLIA Kit for Human DNA repair protein complementing XP-C cells
    CLIA Kit for Human DNA repair protein complementing XP-C cells
    Polyclonal Antibody for Human DNA repair protein complementing XP-C cells
    Polyclonal Antibody for Human DNA repair protein complementing XP-C cells
    Monoclonal Antibody for Human DNA repair protein complementing XP-C cells
    Monoclonal Antibody for Human DNA repair protein complementing XP-C cells
    Protein for Human DNA repair protein complementing XP-C cells
    Protein for Human DNA repair protein complementing XP-C cells

    R&D Technical Data
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    Precision
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    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
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    Recovery
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    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
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    Linearity
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    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
    For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.
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    References
    1. 1.
      "Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23."
      Masutani C. , Sugasawa K. , Yanagisawa J. , Sonoyama T. , Ui M. , Enomoto T. , Takio K. , Tanaka K. , van der Spek P.J. , Bootsma D. , Hoeijmakers J.H.J. , Hanaoka F.
      EMBO J.13:1831-1843(1994) [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] (ISOFORM 1);PROTEIN SEQUENCE OF 2-55;VARIANTS VAL-499 AND LYS-939
    2. 2.
      "The human XPC DNA repair gene: arrangement, splice site information content and influence of a single nucleotide polymorphism in a splice acceptor site on alternative splicing and function."
      Khan S.G. , Muniz-Medina V. , Shahlavi T. , Baker C.C. , Inui H. , Ueda T. , Emmert S. , Schneider T.D. , Kraemer K.H.
      Nucleic Acids Res.30:3624-3631(2002) [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 [GENOMIC DNA];VARIANTS VAL-499 AND LYS-939;ALTERNATIVE SPLICING
    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 [MRNA] (ISOFORM 3)
      tissue: Fetal brain.
    4. 4.
      NIEHS SNPs program
      Submitted (2002-07) to the EMBL/GenBank/DDBJ databases
      [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 [GENOMIC DNA];VARIANTS VAL-16; PHE-48; ARG-86; GLN-314; HIS-492; VAL-499; ILE-513; GLU-632; HIS-671; MET-689; GLN-928 AND LYS-939
    5. 5.
      "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] (ISOFORM 2)
      tissue: Hippocampus.
    6. 6.
      "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M. , Scherer S.E. , Kaul R. , Wang J. , Yu J. , Sudbrak R. , Buhay C.J. , Chen R. , Cree A. , Ding Y. , Dugan-Rocha S. , Gill R. , Gunaratne P. , Harris R.A. , Hawes A.C. , Hernandez J. , Hodgson A.V. , Hume J. , more...
      Nature440:1194-1198(2006) [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]
    7. 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]
      [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: Testis.
    8. 8.
      Suzuki Y. , Sugano S. , Totoki Y. , Toyoda A. , Takeda T. , Sakaki Y. , Tanaka A. , Yokoyama S.
      Submitted (2005-04) to the EMBL/GenBank/DDBJ databases
      [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 69-940 (ISOFORM 1)
      tissue: Liver.
    9. 9.
      "Expression cloning of a human DNA repair gene involved in Xeroderma pigmentosum group C."
      Legerski R.J. , Peterson C.A.
      Nature359:70-73(1992) [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 119-940 (ISOFORM 1)
    10. 10.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ERRATUM
    11. 11.
      "XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes."
      van der Spek P.J. , Eker A. , Rademakers S. , Visser C. , Sugasawa K. , Masutani C. , Hanaoka F. , Bootsma D. , Hoeijmakers J.H.
      Nucleic Acids Res.24:2551-2559(1996) [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: SUBUNIT;SUBCELLULAR LOCATION
    12. 12.
      "Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity."
      Sugasawa K. , Ng J.M. , Masutani C. , Maekawa T. , Uchida A. , van der Spek P.J. , Eker A.P. , Rademakers S. , Visser C. , Aboussekhra A. , Wood R.D. , Hanaoka F. , Bootsma D. , Hoeijmakers J.H.
      Mol. Cell. Biol.17:6924-6931(1997) [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 RAD23A
    13. 13.
      "Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair."
      Sugasawa K. , Ng J.M. , Masutani C. , Iwai S. , van der Spek P.J. , Eker A.P. , Hanaoka F. , Bootsma D. , Hoeijmakers J.H.
      Mol. Cell2:223-232(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: FUNCTION OF THE XPC COMPLEX
    14. 14.
      "The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA."
      Yokoi M. , Masutani C. , Maekawa T. , Sugasawa K. , Ohkuma Y. , Hanaoka F.
      J. Biol. Chem.275:9870-9875(2000) [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;SUBUNIT;INTERACTION WITH CCNH; GTF2H1 AND ERCC3
    15. 15.
      "Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites."
      Batty D. , Rapic'-Otrin V. , Levine A.S. , Wood R.D.
      J. Mol. Biol.300:275-290(2000) [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 OF THE XPC COMPLEX
    16. 16.
      "Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair."
      Araki M. , Masutani C. , Takemura M. , Uchida A. , Sugasawa K. , Kondoh J. , Ohkuma Y. , Hanaoka F.
      J. Biol. Chem.276:18665-18672(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: INTERACTION WITH CETN2 AND RAD23B;SUBCELLULAR LOCATION;CHARACTERIZATION OF THE XPC COMPLEX
    17. 17.
      "A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex."
      Sugasawa K. , Shimizu Y. , Iwai S. , Hanaoka F.
      DNA Repair1:95-107(2002) [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 OF THE XPC COMPLEX
    18. 18.
      "The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH."
      Uchida A. , Sugasawa K. , Masutani C. , Dohmae N. , Araki M. , Yokoi M. , Ohkuma Y. , Hanaoka F.
      DNA Repair1:449-461(2002) [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: DNA-BINDING;INTERACTION WITH RAD23B; ERCC2 AND GTF2H1
    19. 19.
      "DNA bending by the human damage recognition complex XPC-HR23B."
      Janicijevic A. , Sugasawa K. , Shimizu Y. , Hanaoka F. , Wijgers N. , Djurica M. , Hoeijmakers J.H. , Wyman C.
      DNA Repair2:325-336(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: FUNCTION OF THE XPC COMPLEX
    20. 20.
      "Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase."
      Shimizu Y. , Iwai S. , Hanaoka F. , Sugasawa K.
      EMBO J.22:164-173(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: INTERACTION WITH TDG
    21. 21.
      "UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex."
      Sugasawa K. , Okuda Y. , Saijo M. , Nishi R. , Matsuda N. , Chu G. , Mori T. , Iwai S. , Tanaka K. , Tanaka K. , Hanaoka F.
      Cell121:387-400(2005) [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: UBIQUITINATION;INTERACTION WITH DDB2
    22. 22.
      "Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein."
      Nishi R. , Okuda Y. , Watanabe E. , Mori T. , Iwai S. , Masutani C. , Sugasawa K. , Hanaoka F.
      Mol. Cell. Biol.25:5664-5674(2005) [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 CETN2 AND RAD23B;MUTAGENESIS OF TRP-848; LEU-851 AND LEU-855
    23. 23.
      "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V. , Blagoev B. , Gnad F. , Macek B. , Kumar C. , Mortensen P. , Mann M.
      Cell127:635-648(2006) [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-129;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Cervix carcinoma.
    24. 24.
      "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F. , Zhao Y. , Desiderio D.M. , Beranova-Giorgianni S.
      Electrophoresis28:2027-2034(2007) [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Prostate cancer.
    25. 25.
      "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
      Matsuoka S. , Ballif B.A. , Smogorzewska A. , McDonald E.R. III , Hurov K.E. , Luo J. , Bakalarski C.E. , Zhao Z. , Solimini N. , Lerenthal Y. , Shiloh Y. , Gygi S.P. , Elledge S.J.
      Science316:1160-1166(2007) [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Embryonic kidney.
    26. 26.
      "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T. , Yi W. , Lu B. , Park S.K. , Xu T. , Lee J.-D. , Yates J.R. III
      J. Proteome Res.7:1346-1351(2008) [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Cervix carcinoma.
    27. 27.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-169; SER-883; SER-884 AND SER-891;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Cervix carcinoma.
    28. 28.
      "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G. , Ye M. , Zhou H. , Jiang X. , Feng S. , Jiang X. , Tian R. , Wan D. , Zou H. , Gu J.
      Proteomics8:1346-1361(2008) [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Liver.
    29. 29.
      "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V. , Lundgren D.H. , Hwang S.-I. , Rezaul K. , Wu L. , Eng J.K. , Rodionov V. , Han D.K.
      Sci. Signal.2:RA46-RA46(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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Leukemic T-cell.
    30. 30.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-129; SER-883 AND SER-884;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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