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Q9NYF8

- BCLF1_HUMAN

UniProt

Q9NYF8 - BCLF1_HUMAN

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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

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

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
Complete GO annotation...

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-KW
  2. nucleolus Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

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

BgeeiQ9NYF8.
CleanExiHS_BCLAF1.
ExpressionAtlasiQ9NYF8. baseline and differential.
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. 52 interactions.
IntActiQ9NYF8. 35 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.
GeneTreeiENSGT00530000063211.
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

        10         20         30         40         50
MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD
60 70 80 90 100
RMYSRDYRRD YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR
110 120 130 140 150
HSRSPRRGRS RSRSPKRRSV SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY
160 170 180 190 200
SKSPVSKRRG SQEKQTKKAE GEPQEESPLK SKSQEEPKDT FEHDPSESID
210 220 230 240 250
EFNKSSATSG DIWPGLSAYD NSPRSPHSPS PIATPPSQSS SCSDAPMLST
260 270 280 290 300
VHSAKNTPSQ HSHSIQHSPE RSGSGSVGNG SSRYSPSQNS PIHHIPSRRS
310 320 330 340 350
PAKTIAPQNA PRDESRGRSS FYPDGGDQET AKTGKFLKRF TDEESRVFLL
360 370 380 390 400
DRGNTRDKEA SKEKGSEKGR AEGEWEDQEA LDYFSDKESG KQKFNDSEGD
410 420 430 440 450
DTEETEDYRQ FRKSVLADQG KSFATASHRN TEEEGLKYKS KVSLKGNRES
460 470 480 490 500
DGFREEKNYK LKETGYVVER PSTTKDKHKE EDKNSERITV KKETQSPEQV
510 520 530 540 550
KSEKLKDLFD YSPPLHKNLD AREKSTFREE SPLRIKMIAS DSHRPEVKLK
560 570 580 590 600
MAPVPLDDSN RPASLTKDRL LASTLVHSVK KEQEFRSIFD HIKLPQASKS
610 620 630 640 650
TSESFIQHIV SLVHHVKEQY FKSAAMTLNE RFTSYQKATE EHSTRQKSPE
660 670 680 690 700
IHRRIDISPS TLRKHTRLAG EERVFKEENQ KGDKKLRCDS ADLRHDIDRR
710 720 730 740 750
RKERSKERGD SKGSRESSGS RKQEKTPKDY KEYKSYKDDS KHKREQDHSR
760 770 780 790 800
SSSSSASPSS PSSREEKESK KEREEEFKTH HEMKEYSGFA GVSRPRGTFF
810 820 830 840 850
RIRGRGRARG VFAGTNTGPN NSNTTFQKRP KEEEWDPEYT PKSKKYFLHD
860 870 880 890 900
DRDDGVDYWA KRGRGRGTFQ RGRGRFNFKK SGSSPKWTHD KYQGDGIVED
910 920
EEETMENNEE KKDRRKEEKE
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]
CCDS75525.1. [Q9NYF8-2]
RefSeqiNP_001070908.1. NM_001077440.1. [Q9NYF8-3]
NP_001070909.1. NM_001077441.1. [Q9NYF8-4]
NP_055554.1. NM_014739.2. [Q9NYF8-1]
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 ]
CCDS75525.1. [Q9NYF8-2 ]
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 ]
UniGenei Hs.486542.

3D structure databases

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

Protein-protein interaction databases

BioGridi 115118. 52 interactions.
IntActi Q9NYF8. 35 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 GC06M136578.
HGNCi HGNC:16863. BCLAF1.
HPAi HPA006669.
HPA027770.
MIMi 612588. gene.
neXtProti NX_Q9NYF8.
PharmGKBi PA134868035.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG88012.
GeneTreei ENSGT00530000063211.
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

Bgeei Q9NYF8.
CleanExi HS_BCLAF1.
ExpressionAtlasi Q9NYF8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 129 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