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Reviewed, UniProtKB/Swiss-Prot Q9NYF8 (BCLF1_HUMAN)

Last modified February 9, 2010. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bcl-2-associated transcription factor 1
      Short name=Btf
Gene names
Name: BCLAF1
Synonyms: BTF, KIAA0164
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length920 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Death-promoting transcriptional repressor.

Subunit structure

Interacts with Bcl-2 related proteins, EMD, with the adenovirus E1B 19 kDa protein and with DNA. Ref.7

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Ubiquitous.

Sequence caution

The sequence AAH47687.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

The sequence AAH47887.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

The sequence AAH56894.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

The sequence AAH63846.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

EMDP504022EBI-437804,EBI-489887

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYF8-1)

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.
Isoform 2 (identifier: Q9NYF8-2)

Also known as: Btf-l;

The sequence of this isoform differs from the canonical sequence as follows:
     35-36: Missing.
Isoform 3 (identifier: Q9NYF8-3)

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.
Isoform 4 (identifier: Q9NYF8-4)

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 920920Bcl-2-associated transcription factor 1
PRO_0000064888

Regions

Compositional bias141 – 1488Poly-Ser
Compositional bias749 – 76315Poly-Ser

Amino acid modifications

Modified residue1021Phosphoserine Ref.10
Modified residue1041Phosphoserine Ref.10
Modified residue1191Phosphoserine Ref.8
Modified residue1221Phosphoserine By similarity
Modified residue1251Phosphoserine By similarity
Modified residue1481Phosphoserine Ref.8
Modified residue1511Phosphoserine Ref.8
Modified residue1521N6-acetyllysine Ref.26
Modified residue1531Phosphoserine Ref.8
Modified residue1611Phosphoserine Ref.10
Modified residue1771Phosphoserine Ref.10 Ref.8 Ref.6 Ref.14 Ref.15 Ref.16 Ref.20 Ref.21 Ref.23 Ref.25
Modified residue1811Phosphoserine Ref.20
Modified residue1831Phosphoserine Ref.15
Modified residue1981Phosphoserine Ref.15
Modified residue2171Phosphoserine Ref.8
Modified residue2221Phosphoserine Ref.8 Ref.20 Ref.23 Ref.25 Ref.12
Modified residue2641Phosphoserine Ref.15 Ref.20
Modified residue2681Phosphoserine Ref.6 Ref.15 Ref.20
Modified residue2761Phosphoserine Ref.15
Modified residue2811Phosphoserine Ref.8
Modified residue2841Phosphotyrosine Ref.15 Ref.20
Modified residue2851Phosphoserine Ref.15 Ref.12
Modified residue2871Phosphoserine Ref.15 Ref.23
Modified residue2901Phosphoserine Ref.6 Ref.15 Ref.20 Ref.23 Ref.25 Ref.12
Modified residue2971Phosphoserine Ref.15
Modified residue3151Phosphoserine Ref.15
Modified residue3191Phosphoserine Ref.15
Modified residue3201Phosphoserine Ref.15
Modified residue3351N6-acetyllysine Ref.26
Modified residue3411Phosphothreonine Ref.20
Modified residue3851Phosphoserine Ref.10 Ref.15 Ref.20 Ref.23 Ref.25 Ref.12
Modified residue3891Phosphoserine Ref.20
Modified residue3971Phosphoserine Ref.10 Ref.8 Ref.15 Ref.16 Ref.20 Ref.21 Ref.23 Ref.25 Ref.13 Ref.19
Modified residue4021Phosphothreonine Ref.10 Ref.15 Ref.20 Ref.23 Ref.25
Modified residue4051Phosphothreonine Ref.15
Modified residue4081Phosphotyrosine Ref.15
Modified residue4211N6-acetyllysine Ref.26
Modified residue4371N6-acetyllysine Ref.26
Modified residue4431Phosphoserine Ref.15
Modified residue4501Phosphoserine Ref.10 Ref.15
Modified residue4891Phosphothreonine Ref.15
Modified residue4941Phosphothreonine Ref.15
Modified residue4961Phosphoserine Ref.10 Ref.15 Ref.16 Ref.12
Modified residue5021Phosphoserine Ref.15
Modified residue5111Phosphotyrosine Ref.15
Modified residue5121Phosphoserine Ref.10 Ref.6 Ref.14 Ref.15 Ref.16 Ref.20 Ref.23 Ref.25 Ref.12 Ref.17
Modified residue5251Phosphoserine Ref.15 Ref.23
Modified residue5261Phosphothreonine Ref.15
Modified residue5311Phosphoserine Ref.10 Ref.6 Ref.14 Ref.15 Ref.16 Ref.20 Ref.17 Ref.9
Modified residue5781Phosphoserine Ref.14 Ref.20
Modified residue6371N6-acetyllysine Ref.26
Modified residue6481Phosphoserine Ref.10 Ref.15
Modified residue6581Phosphoserine Ref.10 Ref.8 Ref.6 Ref.14 Ref.15 Ref.16 Ref.20 Ref.23 Ref.12 Ref.9 Ref.11 Ref.18
Modified residue6601Phosphoserine Ref.16
Modified residue6611Phosphothreonine Ref.14 Ref.15 Ref.16
Modified residue6901Phosphoserine Ref.10
Modified residue7111Phosphoserine Ref.15
Modified residue7201Phosphoserine Ref.15
Modified residue7571Phosphoserine Ref.23
Modified residue7601Phosphoserine Ref.8
Modified residue8401Phosphothreonine Ref.20 Ref.25 Ref.12

Natural variations

Alternative sequence35 – 362Missing in isoform 2 and isoform 3.
VSP_010369
Alternative sequence339 – 511173Missing in isoform 4.
VSP_010371
Alternative sequence800 – 84849Missing in isoform 3.
VSP_010370
Natural variant661G → A: dbSNP rs9942517.
VAR_059591
Natural variant2091S → C: dbSNP rs6940018.
VAR_050692
Natural variant4591Y → D: dbSNP rs1967446.
VAR_050693
Natural variant4611L → H: dbSNP rs1967445.
VAR_050694
Natural variant6291N → S: dbSNP rs7381749.
VAR_050695
Natural variant8751R → C: dbSNP rs34541670.
VAR_050696

Experimental info

Sequence conflict41S → A in AAF64304. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: 8892B98E54F52C20

FASTA920106,122
        10         20         30         40         50         60 
MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD RMYSRDYRRD 

        70         80         90        100        110        120 
YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR HSRSPRRGRS RSRSPKRRSV 

       130        140        150        160        170        180 
SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY SKSPVSKRRG SQEKQTKKAE GEPQEESPLK 

       190        200        210        220        230        240 
SKSQEEPKDT FEHDPSESID EFNKSSATSG DIWPGLSAYD NSPRSPHSPS PIATPPSQSS 

       250        260        270        280        290        300 
SCSDAPMLST VHSAKNTPSQ HSHSIQHSPE RSGSGSVGNG SSRYSPSQNS PIHHIPSRRS 

       310        320        330        340        350        360 
PAKTIAPQNA PRDESRGRSS FYPDGGDQET AKTGKFLKRF TDEESRVFLL DRGNTRDKEA 

       370        380        390        400        410        420 
SKEKGSEKGR AEGEWEDQEA LDYFSDKESG KQKFNDSEGD DTEETEDYRQ FRKSVLADQG 

       430        440        450        460        470        480 
KSFATASHRN TEEEGLKYKS KVSLKGNRES DGFREEKNYK LKETGYVVER PSTTKDKHKE 

       490        500        510        520        530        540 
EDKNSERITV KKETQSPEQV KSEKLKDLFD YSPPLHKNLD AREKSTFREE SPLRIKMIAS 

       550        560        570        580        590        600 
DSHRPEVKLK MAPVPLDDSN RPASLTKDRL LASTLVHSVK KEQEFRSIFD HIKLPQASKS 

       610        620        630        640        650        660 
TSESFIQHIV SLVHHVKEQY FKSAAMTLNE RFTSYQKATE EHSTRQKSPE IHRRIDISPS 

       670        680        690        700        710        720 
TLRKHTRLAG EERVFKEENQ KGDKKLRCDS ADLRHDIDRR RKERSKERGD SKGSRESSGS 

       730        740        750        760        770        780 
RKQEKTPKDY KEYKSYKDDS KHKREQDHSR SSSSSASPSS PSSREEKESK KEREEEFKTH 

       790        800        810        820        830        840 
HEMKEYSGFA GVSRPRGTFF RIRGRGRARG VFAGTNTGPN NSNTTFQKRP KEEEWDPEYT 

       850        860        870        880        890        900 
PKSKKYFLHD DRDDGVDYWA KRGRGRGTFQ RGRGRFNFKK SGSSPKWTHD KYQGDGIVED 

       910        920 
EEETMENNEE KKDRRKEEKE

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Isoform 2 (Btf-l).

Checksum: 8DD27EC0EC8FBFC5
Show »

FASTA918105,948
Isoform 3 (Btf-s) (BP-1).

Checksum: 6A11356844C6EF40
Show »

FASTA869100,232
Isoform 4.

Checksum: 85CDAF9B406FAE0F
Show »

FASTA74785,937

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References

« Hide 'large scale' references
[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: 10330179] [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: 8724849] [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. expand/collapse author list , 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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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, 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: 15009215] [Abstract]
Cited for: INTERACTION WITH EMD.
[8]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-148; SER-151; SER-153; SER-177; SER-217; SER-222; SER-281; SER-397; SER-658 AND SER-760, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531 AND SER-658, MASS SPECTROMETRY.
[10]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-104; SER-161; SER-177; SER-385; SER-397; THR-402; SER-450; SER-496; SER-512; SER-531; SER-648; SER-658 AND SER-690, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-285; SER-290; SER-385; SER-496; SER-512; SER-658 AND THR-840, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"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: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, MASS SPECTROMETRY.
[14]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-512; SER-531; SER-578; SER-658 AND THR-661, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-183; SER-198; SER-264; SER-268; SER-276; TYR-284; SER-285; SER-287; SER-290; SER-297; SER-315; SER-319; SER-320; SER-385; SER-397; THR-402; THR-405; TYR-408; SER-443; SER-450; THR-489; THR-494; SER-496; SER-502; TYR-511; SER-512; SER-525; THR-526; SER-531; SER-648; SER-658; THR-661; SER-711 AND SER-720, MASS SPECTROMETRY.
[16]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-397; SER-496; SER-512; SER-531; SER-658; SER-660 AND THR-661, MASS SPECTROMETRY.
[17]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND SER-531, MASS SPECTROMETRY.
[18]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, MASS SPECTROMETRY.
[19]"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: 19367720] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, MASS SPECTROMETRY.
Tissue: T-cell.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; 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; SER-658 AND THR-840, MASS SPECTROMETRY.
[21]"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: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-397, MASS SPECTROMETRY.
Tissue: Liver.
[22]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-222; SER-287; SER-290; SER-385; SER-397; THR-402; SER-512; SER-525; SER-658 AND SER-757, MASS SPECTROMETRY.
[24]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, MASS SPECTROMETRY.
[25]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-222; SER-290; SER-385; SER-397; THR-402; SER-512 AND THR-840, MASS SPECTROMETRY.
Tissue: T-cell.
[26]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152; LYS-335; LYS-421; LYS-437 AND LYS-637, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF249273 mRNA. Translation: AAF64304.1.
D79986 mRNA. Translation: BAA11481.2. Different initiation.
AL121713 Genomic DNA. Translation: CAB96722.1.
CH471051 Genomic DNA. Translation: EAW47950.1.
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.
IPIIPI00006079.
IPI00413671.
IPI00413672.
IPI00413673.
RefSeqNP_001070908.1.
NP_001070909.1.
NP_055554.1.
UniGeneHs.486542

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NYF8. 6 interactions.
STRINGQ9NYF8.

PTM databases

PhosphoSiteQ9NYF8.

Proteomic databases

PRIDEQ9NYF8.

Genome annotation databases

EnsemblENST00000031135; ENSP00000031135; ENSG00000029363; Homo sapiens. [Genome view]
ENST00000392348; ENSP00000376159; ENSG00000029363; Homo sapiens. [Genome view]
GeneID9774.
KEGGhsa:9774.
UCSCuc003qgw.1. human.
uc003qgx.1. human.
uc003qgy.1. human.

Organism-specific databases

CTD9774.
GeneCardsGC06M136621.
GC06M136622.
H-InvDBHIX0006243.
HGNCHGNC:16863. BCLAF1.
HPAHPA006669.
HPA027770.
MIM612588. gene.
PharmGKBPA134868035.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG282098.
HOVERGENQ9NYF8.
InParanoidQ9NYF8.
OMAFFRIRGR.
OrthoDBEOG9BZQN9.
PhylomeDBQ9NYF8.

Gene expression databases

ArrayExpressQ9NYF8.
BgeeQ9NYF8.
CleanExHS_BCLAF1.
GenevestigatorQ9NYF8.
GermOnlineENSG00000029363. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio36794.
SOURCESearch...

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Entry information

Entry nameBCLF1_HUMAN
AccessionPrimary (citable) accession number: Q9NYF8
Secondary accession number(s): A2RU75 expand/collapse secondary AC list , B7ZM58, Q14673, Q86WU6, Q86WY0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: February 9, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents