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O00273

- DFFA_HUMAN

UniProt

O00273 - DFFA_HUMAN

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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

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 - 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiO00273.
CleanExiHS_DFFA.
ExpressionAtlasiO00273. baseline and differential.
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. 39 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 – 5012Combined sources
Beta strandi60 – 634Combined sources
Turni64 – 663Combined sources
Helixi73 – 786Combined sources
Beta strandi84 – 885Combined sources
Helixi239 – 2468Combined sources
Turni251 – 2544Combined sources
Helixi257 – 2648Combined sources
Helixi268 – 2747Combined sources
Helixi279 – 29719Combined sources
Helixi298 – 3003Combined sources

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.
GeneTreeiENSGT00510000048128.
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

        10         20         30         40         50
MEVTGDAGVP ESGEIRTLKP CLLRRNYSRE QHGVAASCLE DLRSKACDIL
60 70 80 90 100
AIDKSLTPVT LVLAEDGTIV DDDDYFLCLP SNTKFVALAS NEKWAYNNSD
110 120 130 140 150
GGTAWISQES FDVDETDSGA GLKWKNVARQ LKEDLSSIIL LSEEDLQMLV
160 170 180 190 200
DAPCSDLAQE LRQSCATVQR LQHTLQQVLD QREEVRQSKQ LLQLYLQALE
210 220 230 240 250
KEGSLLSKQE ESKAAFGEEV DAVDTGISRE TSSDVALASH ILTALREKQA
260 270 280 290 300
PELSLSSQDL ELVTKEDPKA LAVALNWDIK KTETVQEACE RELALRLQQT
310 320 330
QSLHSLRSIS ASKASPPGDL QNPKRARQDP T
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. 39 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.
GeneTreei ENSGT00510000048128.
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

Bgeei O00273.
CleanExi HS_DFFA.
ExpressionAtlasi O00273. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 154 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