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Q9NYF8

- BCLF1_HUMAN

UniProt

Q9NYF8 - BCLF1_HUMAN

Protein

Bcl-2-associated transcription factor 1

Gene

BCLAF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (24 May 2004)
      Previous versions | rss
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    Functioni

    Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. positive regulation of apoptotic process Source: MGI
    4. positive regulation of DNA-templated transcription, initiation Source: UniProtKB
    5. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    6. positive regulation of response to DNA damage stimulus Source: UniProtKB
    7. regulation of DNA-templated transcription in response to stress Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bcl-2-associated transcription factor 1
    Short name:
    Btf
    Gene namesi
    Name:BCLAF1
    Synonyms:BTF, KIAA0164
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:16863. BCLAF1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134868035.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 920920Bcl-2-associated transcription factor 1PRO_0000064888Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021Phosphoserine1 Publication
    Modified residuei104 – 1041Phosphoserine1 Publication
    Modified residuei152 – 1521N6-acetyllysine1 Publication
    Modified residuei177 – 1771Phosphoserine6 Publications
    Modified residuei181 – 1811Phosphoserine1 Publication
    Modified residuei196 – 1961Phosphoserine2 Publications
    Modified residuei198 – 1981Phosphoserine2 Publications
    Modified residuei222 – 2221Phosphoserine4 Publications
    Modified residuei264 – 2641Phosphoserine1 Publication
    Modified residuei268 – 2681Phosphoserine4 Publications
    Modified residuei284 – 2841Phosphotyrosine1 Publication
    Modified residuei285 – 2851Phosphoserine1 Publication
    Modified residuei290 – 2901Phosphoserine5 Publications
    Modified residuei297 – 2971Phosphoserine1 Publication
    Modified residuei332 – 3321N6-acetyllysineBy similarity
    Modified residuei341 – 3411Phosphothreonine1 Publication
    Modified residuei385 – 3851Phosphoserine4 Publications
    Modified residuei389 – 3891Phosphoserine2 Publications
    Modified residuei397 – 3971Phosphoserine8 Publications
    Modified residuei402 – 4021Phosphothreonine4 Publications
    Modified residuei421 – 4211N6-acetyllysineBy similarity
    Modified residuei437 – 4371N6-acetyllysine1 Publication
    Modified residuei472 – 4721Phosphoserine1 Publication
    Modified residuei475 – 4751N6-acetyllysineBy similarity
    Modified residuei494 – 4941Phosphothreonine1 Publication
    Modified residuei496 – 4961Phosphoserine2 Publications
    Modified residuei502 – 5021Phosphoserine1 Publication
    Modified residuei512 – 5121Phosphoserine5 Publications
    Modified residuei531 – 5311Phosphoserine5 Publications
    Modified residuei566 – 5661Phosphothreonine1 Publication
    Modified residuei578 – 5781Phosphoserine2 Publications
    Modified residuei648 – 6481Phosphoserine1 Publication
    Modified residuei658 – 6581Phosphoserine4 Publications
    Modified residuei660 – 6601Phosphoserine1 Publication
    Modified residuei690 – 6901Phosphoserine1 Publication
    Modified residuei760 – 7601Phosphoserine1 Publication
    Modified residuei803 – 8031CitrullineBy similarity

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYF8.
    PaxDbiQ9NYF8.
    PRIDEiQ9NYF8.

    PTM databases

    PhosphoSiteiQ9NYF8.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9NYF8.
    BgeeiQ9NYF8.
    CleanExiHS_BCLAF1.
    GenevestigatoriQ9NYF8.

    Organism-specific databases

    HPAiHPA006669.
    HPA027770.

    Interactioni

    Subunit structurei

    Interacts with Bcl-2 related proteins, EMD, with the adenovirus E1B 19 kDa protein and with DNA. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2P104152EBI-437804,EBI-77694
    EMDP504023EBI-437804,EBI-489887

    Protein-protein interaction databases

    BioGridi115118. 44 interactions.
    IntActiQ9NYF8. 34 interactions.
    MINTiMINT-92502.
    STRINGi9606.ENSP00000031135.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NYF8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi141 – 1488Poly-Ser
    Compositional biasi749 – 76315Poly-SerAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG88012.
    HOVERGENiHBG050681.
    InParanoidiQ9NYF8.
    KOiK13087.
    OMAiDSKHKSR.
    OrthoDBiEOG78SQHB.
    PhylomeDBiQ9NYF8.
    TreeFamiTF335939.

    Family and domain databases

    InterProiIPR026668. Bcl-2_assoc_TF1.
    IPR029199. THRAP3_BCLAF1.
    [Graphical view]
    PANTHERiPTHR15268:SF4. PTHR15268:SF4. 1 hit.
    PfamiPF15440. THRAP3_BCLAF1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NYF8-1) [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

    MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD    50
    RMYSRDYRRD YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR 100
    HSRSPRRGRS RSRSPKRRSV SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY 150
    SKSPVSKRRG SQEKQTKKAE GEPQEESPLK SKSQEEPKDT FEHDPSESID 200
    EFNKSSATSG DIWPGLSAYD NSPRSPHSPS PIATPPSQSS SCSDAPMLST 250
    VHSAKNTPSQ HSHSIQHSPE RSGSGSVGNG SSRYSPSQNS PIHHIPSRRS 300
    PAKTIAPQNA PRDESRGRSS FYPDGGDQET AKTGKFLKRF TDEESRVFLL 350
    DRGNTRDKEA SKEKGSEKGR AEGEWEDQEA LDYFSDKESG KQKFNDSEGD 400
    DTEETEDYRQ FRKSVLADQG KSFATASHRN TEEEGLKYKS KVSLKGNRES 450
    DGFREEKNYK LKETGYVVER PSTTKDKHKE EDKNSERITV KKETQSPEQV 500
    KSEKLKDLFD YSPPLHKNLD AREKSTFREE SPLRIKMIAS DSHRPEVKLK 550
    MAPVPLDDSN RPASLTKDRL LASTLVHSVK KEQEFRSIFD HIKLPQASKS 600
    TSESFIQHIV SLVHHVKEQY FKSAAMTLNE RFTSYQKATE EHSTRQKSPE 650
    IHRRIDISPS TLRKHTRLAG EERVFKEENQ KGDKKLRCDS ADLRHDIDRR 700
    RKERSKERGD SKGSRESSGS RKQEKTPKDY KEYKSYKDDS KHKREQDHSR 750
    SSSSSASPSS PSSREEKESK KEREEEFKTH HEMKEYSGFA GVSRPRGTFF 800
    RIRGRGRARG VFAGTNTGPN NSNTTFQKRP KEEEWDPEYT PKSKKYFLHD 850
    DRDDGVDYWA KRGRGRGTFQ RGRGRFNFKK SGSSPKWTHD KYQGDGIVED 900
    EEETMENNEE KKDRRKEEKE 920
    Length:920
    Mass (Da):106,122
    Last modified:May 24, 2004 - v2
    Checksum:i8892B98E54F52C20
    GO
    Isoform 2 (identifier: Q9NYF8-2) [UniParc]FASTAAdd to Basket

    Also known as: Btf-l

    The sequence of this isoform differs from the canonical sequence as follows:
         35-36: Missing.

    Show »
    Length:918
    Mass (Da):105,948
    Checksum:i8DD27EC0EC8FBFC5
    GO
    Isoform 3 (identifier: Q9NYF8-3) [UniParc]FASTAAdd to Basket

    Also known as: Btf-s, BP-1

    The sequence of this isoform differs from the canonical sequence as follows:
         35-36: Missing.
         800-848: Missing.

    Show »
    Length:869
    Mass (Da):100,232
    Checksum:i6A11356844C6EF40
    GO
    Isoform 4 (identifier: Q9NYF8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         339-511: Missing.

    Show »
    Length:747
    Mass (Da):85,937
    Checksum:i85CDAF9B406FAE0F
    GO

    Sequence cautioni

    The sequence AAH47687.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH47887.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH56894.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH63846.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAA11481.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41S → A in AAF64304. (PubMed:10330179)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661G → A.
    Corresponds to variant rs9942517 [ dbSNP | Ensembl ].
    VAR_059591
    Natural varianti209 – 2091S → C.
    Corresponds to variant rs6940018 [ dbSNP | Ensembl ].
    VAR_050692
    Natural varianti459 – 4591Y → D.
    Corresponds to variant rs1967446 [ dbSNP | Ensembl ].
    VAR_050693
    Natural varianti461 – 4611L → H.
    Corresponds to variant rs1967445 [ dbSNP | Ensembl ].
    VAR_050694
    Natural varianti629 – 6291N → S.
    Corresponds to variant rs7381749 [ dbSNP | Ensembl ].
    VAR_050695
    Natural varianti875 – 8751R → C.
    Corresponds to variant rs34541670 [ dbSNP | Ensembl ].
    VAR_050696

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 362Missing in isoform 2 and isoform 3. 2 PublicationsVSP_010369
    Alternative sequencei339 – 511173Missing in isoform 4. 1 PublicationVSP_010371Add
    BLAST
    Alternative sequencei800 – 84849Missing in isoform 3. 1 PublicationVSP_010370Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF249273 mRNA. Translation: AAF64304.1.
    D79986 mRNA. Translation: BAA11481.2. Different initiation.
    AL121713 Genomic DNA. Translation: CAB96722.1.
    CH471051 Genomic DNA. Translation: EAW47950.1.
    CH471051 Genomic DNA. Translation: EAW47951.1.
    BC047687 mRNA. Translation: AAH47687.1. Sequence problems.
    BC047887 mRNA. Translation: AAH47887.1. Sequence problems.
    BC056894 mRNA. Translation: AAH56894.1. Sequence problems.
    BC063846 mRNA. Translation: AAH63846.1. Sequence problems.
    BC132780 mRNA. Translation: AAI32781.1.
    BC144281 mRNA. Translation: AAI44282.1.
    CCDSiCCDS47485.1. [Q9NYF8-4]
    CCDS47486.1. [Q9NYF8-3]
    CCDS5177.1. [Q9NYF8-1]
    RefSeqiNP_001070908.1. NM_001077440.1. [Q9NYF8-3]
    NP_001070909.1. NM_001077441.1. [Q9NYF8-4]
    NP_055554.1. NM_014739.2. [Q9NYF8-1]
    XP_005267293.1. XM_005267236.2. [Q9NYF8-2]
    UniGeneiHs.486542.

    Genome annotation databases

    EnsembliENST00000353331; ENSP00000229446; ENSG00000029363. [Q9NYF8-3]
    ENST00000392348; ENSP00000376159; ENSG00000029363. [Q9NYF8-3]
    ENST00000527759; ENSP00000434826; ENSG00000029363. [Q9NYF8-2]
    ENST00000530767; ENSP00000436501; ENSG00000029363. [Q9NYF8-4]
    ENST00000531224; ENSP00000435210; ENSG00000029363. [Q9NYF8-1]
    GeneIDi9774.
    KEGGihsa:9774.
    UCSCiuc003qgw.1. human. [Q9NYF8-4]
    uc003qgx.1. human. [Q9NYF8-1]
    uc003qgy.1. human. [Q9NYF8-3]
    uc011ede.1. human. [Q9NYF8-2]

    Polymorphism databases

    DMDMi47605556.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF249273 mRNA. Translation: AAF64304.1 .
    D79986 mRNA. Translation: BAA11481.2 . Different initiation.
    AL121713 Genomic DNA. Translation: CAB96722.1 .
    CH471051 Genomic DNA. Translation: EAW47950.1 .
    CH471051 Genomic DNA. Translation: EAW47951.1 .
    BC047687 mRNA. Translation: AAH47687.1 . Sequence problems.
    BC047887 mRNA. Translation: AAH47887.1 . Sequence problems.
    BC056894 mRNA. Translation: AAH56894.1 . Sequence problems.
    BC063846 mRNA. Translation: AAH63846.1 . Sequence problems.
    BC132780 mRNA. Translation: AAI32781.1 .
    BC144281 mRNA. Translation: AAI44282.1 .
    CCDSi CCDS47485.1. [Q9NYF8-4 ]
    CCDS47486.1. [Q9NYF8-3 ]
    CCDS5177.1. [Q9NYF8-1 ]
    RefSeqi NP_001070908.1. NM_001077440.1. [Q9NYF8-3 ]
    NP_001070909.1. NM_001077441.1. [Q9NYF8-4 ]
    NP_055554.1. NM_014739.2. [Q9NYF8-1 ]
    XP_005267293.1. XM_005267236.2. [Q9NYF8-2 ]
    UniGenei Hs.486542.

    3D structure databases

    ProteinModelPortali Q9NYF8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115118. 44 interactions.
    IntActi Q9NYF8. 34 interactions.
    MINTi MINT-92502.
    STRINGi 9606.ENSP00000031135.

    PTM databases

    PhosphoSitei Q9NYF8.

    Polymorphism databases

    DMDMi 47605556.

    Proteomic databases

    MaxQBi Q9NYF8.
    PaxDbi Q9NYF8.
    PRIDEi Q9NYF8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353331 ; ENSP00000229446 ; ENSG00000029363 . [Q9NYF8-3 ]
    ENST00000392348 ; ENSP00000376159 ; ENSG00000029363 . [Q9NYF8-3 ]
    ENST00000527759 ; ENSP00000434826 ; ENSG00000029363 . [Q9NYF8-2 ]
    ENST00000530767 ; ENSP00000436501 ; ENSG00000029363 . [Q9NYF8-4 ]
    ENST00000531224 ; ENSP00000435210 ; ENSG00000029363 . [Q9NYF8-1 ]
    GeneIDi 9774.
    KEGGi hsa:9774.
    UCSCi uc003qgw.1. human. [Q9NYF8-4 ]
    uc003qgx.1. human. [Q9NYF8-1 ]
    uc003qgy.1. human. [Q9NYF8-3 ]
    uc011ede.1. human. [Q9NYF8-2 ]

    Organism-specific databases

    CTDi 9774.
    GeneCardsi GC06M136621.
    HGNCi HGNC:16863. BCLAF1.
    HPAi HPA006669.
    HPA027770.
    MIMi 612588. gene.
    neXtProti NX_Q9NYF8.
    PharmGKBi PA134868035.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG88012.
    HOVERGENi HBG050681.
    InParanoidi Q9NYF8.
    KOi K13087.
    OMAi DSKHKSR.
    OrthoDBi EOG78SQHB.
    PhylomeDBi Q9NYF8.
    TreeFami TF335939.

    Miscellaneous databases

    ChiTaRSi BCLAF1. human.
    GeneWikii BCLAF1.
    GenomeRNAii 9774.
    NextBioi 36794.
    PROi Q9NYF8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYF8.
    Bgeei Q9NYF8.
    CleanExi HS_BCLAF1.
    Genevestigatori Q9NYF8.

    Family and domain databases

    InterProi IPR026668. Bcl-2_assoc_TF1.
    IPR029199. THRAP3_BCLAF1.
    [Graphical view ]
    PANTHERi PTHR15268:SF4. PTHR15268:SF4. 1 hit.
    Pfami PF15440. THRAP3_BCLAF1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins."
      Kasof G.M., Goyal L., White E.
      Mol. Cell. Biol. 19:4390-4404(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    2. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-676 (ISOFORM 4).
      Tissue: Brain, Pancreas, Testis and Uterus.
    6. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
      Submitted (APR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 168-182; 189-204; 256-271; 284-298; 304-312; 319-332; 394-409; 422-439; 461-475; 505-517; 525-534; 537-548; 551-581; 587-593; 623-631; 654-664; 785-796; 832-842 AND 846-852, PHOSPHORYLATION AT SER-177; SER-268; SER-290; SER-512; SER-531 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    7. "Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy."
      Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N., Mori C., Wilson K.L., Hiraoka Y.
      Eur. J. Biochem. 271:1035-1045(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EMD.
    8. "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.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-389; SER-397; THR-402; SER-531 AND SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: FUNCTION, IDENTIFICATION IN THE SNARP COMPLEX.
    12. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-222; SER-264; SER-268; TYR-284; SER-290; THR-341; SER-385; SER-389; SER-397; THR-402; SER-512; SER-531; SER-578 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-222; SER-290; SER-385; SER-397; THR-402 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152 AND LYS-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-102; SER-104; SER-177; SER-196; SER-198; SER-222; SER-268; SER-290; SER-297; SER-385; SER-397; THR-402; SER-472; SER-496; SER-502; SER-512; SER-531; THR-566; SER-578; SER-658 AND SER-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-177; SER-196; SER-198; SER-222; SER-268; SER-285; SER-290; SER-385; SER-397; THR-494; SER-496; SER-512; SER-531; SER-658; SER-660 AND SER-760, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBCLF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYF8
    Secondary accession number(s): A2RU75
    , B7ZM58, E1P586, Q14673, Q86WU6, Q86WY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3