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O00273

- DFFA_HUMAN

UniProt

O00273 - DFFA_HUMAN

Protein

DNA fragmentation factor subunit alpha

Gene

DFFA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Inhibitor of the caspase-activated DNase (DFF40).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei117 – 1182Cleavage; by caspase-3
    Sitei224 – 2252Cleavage; by caspase-3

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic DNA fragmentation Source: Reactome
    2. apoptotic process Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. negative regulation of apoptotic DNA fragmentation Source: MGI
    5. negative regulation of execution phase of apoptosis Source: BHF-UCL
    6. positive regulation of apoptotic process Source: Ensembl
    7. thymocyte apoptotic process Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_13462. Activation of DNA fragmentation factor.
    SignaLinkiO00273.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA fragmentation factor subunit alpha
    Alternative name(s):
    DNA fragmentation factor 45 kDa subunit
    Short name:
    DFF-45
    Inhibitor of CAD
    Short name:
    ICAD
    Gene namesi
    Name:DFFA
    Synonyms:DFF1, DFF45
    ORF Names:H13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2772. DFFA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. nuclear chromatin Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 331331DNA fragmentation factor subunit alphaPRO_0000144716Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei315 – 3151Phosphoserine4 Publications

    Post-translational modificationi

    Caspase-3 cleaves DFF45 at 2 sites to generate an active factor.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00273.
    PaxDbiO00273.
    PeptideAtlasiO00273.
    PRIDEiO00273.

    PTM databases

    PhosphoSiteiO00273.

    Miscellaneous databases

    PMAP-CutDBQ5T6G5.

    Expressioni

    Gene expression databases

    ArrayExpressiO00273.
    BgeeiO00273.
    CleanExiHS_DFFA.
    GenevestigatoriO00273.

    Organism-specific databases

    HPAiCAB002679.
    HPA018859.
    HPA019938.
    HPA025230.

    Interactioni

    Subunit structurei

    Heterodimer of DFFA and DFFB.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DffbO547888EBI-727171,EBI-7365197From a different organism.

    Protein-protein interaction databases

    BioGridi108040. 37 interactions.
    IntActiO00273. 9 interactions.
    MINTiMINT-365527.
    STRINGi9606.ENSP00000366237.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi39 – 5012
    Beta strandi60 – 634
    Turni64 – 663
    Helixi73 – 786
    Beta strandi84 – 885
    Helixi239 – 2468
    Turni251 – 2544
    Helixi257 – 2648
    Helixi268 – 2747
    Helixi279 – 29719
    Helixi298 – 3003

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IBXNMR-B11-100[»]
    1IYRNMR-A225-331[»]
    1KOYNMR-A239-300[»]
    DisProtiDP00173.
    ProteinModelPortaliO00273.
    SMRiO00273. Positions 12-100, 225-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00273.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9680CIDE-NPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CIDE-N domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG40170.
    HOGENOMiHOG000112204.
    HOVERGENiHBG000683.
    InParanoidiO00273.
    KOiK02310.
    OMAiNEKWAYN.
    OrthoDBiEOG7JQBP8.
    PhylomeDBiO00273.
    TreeFamiTF102021.

    Family and domain databases

    Gene3Di1.10.1490.10. 1 hit.
    InterProiIPR003508. CIDE-N_dom.
    IPR027296. DFF-C_dom.
    IPR017299. DNA_fragmentation_factor_asu.
    IPR015121. DNA_fragmentation_mid_dom.
    [Graphical view]
    PfamiPF02017. CIDE-N. 1 hit.
    PF09033. DFF-C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037865. DFF_alpha. 1 hit.
    ProDomiPD316494. DNA_fragmentation_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00266. CAD. 1 hit.
    [Graphical view]
    SUPFAMiSSF81783. SSF81783. 1 hit.
    PROSITEiPS51135. CIDE_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform DFF45 (identifier: O00273-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL    50
    AIDKSLTPVT LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD 100
    GGTAWISQES FDVDETDSGA GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV 150
    DAPCSDLAQE LRQSCATVQR LQHTLQQVLD QREEVRQSKQ LLQLYLQALE 200
    KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH ILTALREKQA 250
    PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE RELALRLQQT 300
    QSLHSLRSIS ASKASPPGDL QNPKRARQDP T 331
    Length:331
    Mass (Da):36,522
    Last modified:July 1, 1997 - v1
    Checksum:i8656FE45DB003DF3
    GO
    Isoform DFF35 (identifier: O00273-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-268: LVTKEDP → VGGNQGH
         269-331: Missing.

    Show »
    Length:268
    Mass (Da):29,411
    Checksum:iEA130F9D27145474
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911R → W in AAH07721. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei262 – 2687LVTKEDP → VGGNQGH in isoform DFF35. 2 PublicationsVSP_001085
    Alternative sequencei269 – 33163Missing in isoform DFF35. 2 PublicationsVSP_001086Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91985 mRNA. Translation: AAC51249.1.
    AF087573 mRNA. Translation: AAD32953.1.
    AF103799 mRNA. Translation: AAF02419.1.
    BT006980 mRNA. Translation: AAP35626.1.
    AK313317 mRNA. Translation: BAG36122.1.
    AL354956 Genomic DNA. Translation: CAI19196.1.
    AL354956 Genomic DNA. Translation: CAI19197.1.
    CH471130 Genomic DNA. Translation: EAW71656.1.
    CH471130 Genomic DNA. Translation: EAW71657.1.
    BC000037 mRNA. Translation: AAH00037.1.
    BC007112 mRNA. Translation: AAH07112.1.
    BC007721 mRNA. Translation: AAH07721.1.
    CCDSiCCDS118.1. [O00273-1]
    CCDS119.1. [O00273-2]
    RefSeqiNP_004392.1. NM_004401.2. [O00273-1]
    NP_998731.1. NM_213566.1. [O00273-2]
    UniGeneiHs.484782.

    Genome annotation databases

    EnsembliENST00000377036; ENSP00000366235; ENSG00000160049. [O00273-2]
    ENST00000377038; ENSP00000366237; ENSG00000160049. [O00273-1]
    GeneIDi1676.
    KEGGihsa:1676.
    UCSCiuc001arj.3. human. [O00273-1]
    uc001ark.3. human. [O00273-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91985 mRNA. Translation: AAC51249.1 .
    AF087573 mRNA. Translation: AAD32953.1 .
    AF103799 mRNA. Translation: AAF02419.1 .
    BT006980 mRNA. Translation: AAP35626.1 .
    AK313317 mRNA. Translation: BAG36122.1 .
    AL354956 Genomic DNA. Translation: CAI19196.1 .
    AL354956 Genomic DNA. Translation: CAI19197.1 .
    CH471130 Genomic DNA. Translation: EAW71656.1 .
    CH471130 Genomic DNA. Translation: EAW71657.1 .
    BC000037 mRNA. Translation: AAH00037.1 .
    BC007112 mRNA. Translation: AAH07112.1 .
    BC007721 mRNA. Translation: AAH07721.1 .
    CCDSi CCDS118.1. [O00273-1 ]
    CCDS119.1. [O00273-2 ]
    RefSeqi NP_004392.1. NM_004401.2. [O00273-1 ]
    NP_998731.1. NM_213566.1. [O00273-2 ]
    UniGenei Hs.484782.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IBX NMR - B 11-100 [» ]
    1IYR NMR - A 225-331 [» ]
    1KOY NMR - A 239-300 [» ]
    DisProti DP00173.
    ProteinModelPortali O00273.
    SMRi O00273. Positions 12-100, 225-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108040. 37 interactions.
    IntActi O00273. 9 interactions.
    MINTi MINT-365527.
    STRINGi 9606.ENSP00000366237.

    PTM databases

    PhosphoSitei O00273.

    Proteomic databases

    MaxQBi O00273.
    PaxDbi O00273.
    PeptideAtlasi O00273.
    PRIDEi O00273.

    Protocols and materials databases

    DNASUi 1676.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377036 ; ENSP00000366235 ; ENSG00000160049 . [O00273-2 ]
    ENST00000377038 ; ENSP00000366237 ; ENSG00000160049 . [O00273-1 ]
    GeneIDi 1676.
    KEGGi hsa:1676.
    UCSCi uc001arj.3. human. [O00273-1 ]
    uc001ark.3. human. [O00273-2 ]

    Organism-specific databases

    CTDi 1676.
    GeneCardsi GC01M010516.
    HGNCi HGNC:2772. DFFA.
    HPAi CAB002679.
    HPA018859.
    HPA019938.
    HPA025230.
    MIMi 601882. gene.
    neXtProti NX_O00273.
    PharmGKBi PA27254.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40170.
    HOGENOMi HOG000112204.
    HOVERGENi HBG000683.
    InParanoidi O00273.
    KOi K02310.
    OMAi NEKWAYN.
    OrthoDBi EOG7JQBP8.
    PhylomeDBi O00273.
    TreeFami TF102021.

    Enzyme and pathway databases

    Reactomei REACT_13462. Activation of DNA fragmentation factor.
    SignaLinki O00273.

    Miscellaneous databases

    ChiTaRSi DFFA. human.
    EvolutionaryTracei O00273.
    GeneWikii DFFA.
    GenomeRNAii 1676.
    NextBioi 6896.
    PMAP-CutDB Q5T6G5.
    PROi O00273.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00273.
    Bgeei O00273.
    CleanExi HS_DFFA.
    Genevestigatori O00273.

    Family and domain databases

    Gene3Di 1.10.1490.10. 1 hit.
    InterProi IPR003508. CIDE-N_dom.
    IPR027296. DFF-C_dom.
    IPR017299. DNA_fragmentation_factor_asu.
    IPR015121. DNA_fragmentation_mid_dom.
    [Graphical view ]
    Pfami PF02017. CIDE-N. 1 hit.
    PF09033. DFF-C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037865. DFF_alpha. 1 hit.
    ProDomi PD316494. DNA_fragmentation_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00266. CAD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81783. SSF81783. 1 hit.
    PROSITEi PS51135. CIDE_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis."
      Liu X., Zou H., Slaughter C., Wang X.
      Cell 89:175-184(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF45), PROTEIN SEQUENCE OF 171-181; 190-201; 214-218 AND 230-242.
    2. "Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40."
      Gu J.J., Dong R.P., Zhang C., McLaughlin D.F., Wu M.X., Schlossman S.F.
      J. Biol. Chem. 274:20759-20762(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF35).
    3. "Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells."
      Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.
      Nucleic Acids Res. 27:4008-4017(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DFF35).
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DFF45).
    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.
      , 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] (ISOFORM DFF45).
      Tissue: Mammary gland.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM DFF45).
      Tissue: Eye, Kidney and Skeletal muscle.
    9. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-16; 171-182; 190-201; 214-246; 249-269 AND 297-307, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45."
      Zhou P., Lugovskoy A.A., McCarty J.S., Li P., Wagner G.
      Proc. Natl. Acad. Sci. U.S.A. 98:6051-6055(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 11-100.

    Entry informationi

    Entry nameiDFFA_HUMAN
    AccessioniPrimary (citable) accession number: O00273
    Secondary accession number(s): Q5T6G5
    , Q5T6G6, Q96I97, Q9Y6C6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 153 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3