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Protein

Bcl-2-associated transcription factor 1

Gene

Bclaf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1917580. Bclaf1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Nucleus speckle By similarity
  • Nucleusnucleoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 919919Bcl-2-associated transcription factor 1PRO_0000064889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei152 – 1521N6-acetyllysineBy similarity
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineBy similarity
Modified residuei196 – 1961PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei218 – 2181PhosphotyrosineBy similarity
Modified residuei221 – 2211PhosphoserineCombined sources
Modified residuei258 – 2581PhosphoserineBy similarity
Modified residuei263 – 2631PhosphoserineBy similarity
Modified residuei267 – 2671PhosphoserineBy similarity
Modified residuei283 – 2831PhosphotyrosineBy similarity
Modified residuei284 – 2841PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei305 – 3051PhosphothreonineCombined sources
Modified residuei330 – 3301N6-acetyllysine; alternateCombined sources
Cross-linki330 – 330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei339 – 3391PhosphothreonineBy similarity
Modified residuei383 – 3831PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei395 – 3951PhosphoserineCombined sources
Modified residuei400 – 4001PhosphothreonineCombined sources
Cross-linki411 – 411Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei419 – 4191N6-acetyllysine; alternateCombined sources
Cross-linki419 – 419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei435 – 4351N6-acetyllysine; alternateCombined sources
Cross-linki435 – 435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki455 – 455Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki460 – 460Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei470 – 4701PhosphoserineBy similarity
Modified residuei473 – 4731N6-acetyllysineCombined sources
Cross-linki489 – 489Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei494 – 4941PhosphoserineCombined sources
Cross-linki499 – 499Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei500 – 5001PhosphoserineBy similarity
Modified residuei510 – 5101PhosphoserineCombined sources
Modified residuei529 – 5291PhosphoserineCombined sources
Cross-linki534 – 534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki546 – 546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki548 – 548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei564 – 5641PhosphothreonineBy similarity
Modified residuei576 – 5761PhosphoserineBy similarity
Cross-linki578 – 578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei646 – 6461PhosphoserineBy similarity
Modified residuei656 – 6561PhosphoserineCombined sources
Modified residuei658 – 6581PhosphoserineBy similarity
Cross-linki674 – 674Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei688 – 6881PhosphoserineBy similarity
Modified residuei759 – 7591PhosphoserineBy similarity
Cross-linki777 – 777Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei802 – 8021Citrulline1 Publication
Cross-linki830 – 830Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8K019.
MaxQBiQ8K019.
PaxDbiQ8K019.
PRIDEiQ8K019.

PTM databases

iPTMnetiQ8K019.
PhosphoSiteiQ8K019.

Expressioni

Gene expression databases

BgeeiQ8K019.
CleanExiMM_BCLAF1.
ExpressionAtlasiQ8K019. baseline and differential.
GenevisibleiQ8K019. MM.

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 (By similarity). Component of the WTAP complex composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi215443. 6 interactions.
IntActiQ8K019. 4 interactions.
MINTiMINT-4089177.
STRINGi10090.ENSMUSP00000043583.

Structurei

3D structure databases

ProteinModelPortaliQ8K019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi141 – 1488Poly-Ser
Compositional biasi748 – 76215Poly-SerAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IJCD. Eukaryota.
ENOG4110X68. LUCA.
GeneTreeiENSGT00530000063211.
HOGENOMiHOG000054209.
HOVERGENiHBG050681.
InParanoidiQ8K019.
KOiK13087.
OMAiDDSKHKS.
PhylomeDBiQ8K019.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K019-1) [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
RIYSRDYRRD 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
EFNKSATSGD IWPGLSAYDN SPRSPHSPSP IATPPSQSSS CSDAPMLSTV
260 270 280 290 300
HSAKNTPSQH SHSIQHSPER SGSGSVGNGS SRYSPSQNSP IHHIPSRRSP
310 320 330 340 350
AKTITPQNAP REESRGRSSF YPEGDQETAK TGKFLKRFTD EESRVFLLDR
360 370 380 390 400
GNIRDKEAPK EKGSEKGRAD GDWDDQEVLD YFSDKESAKQ KFHDSEGDDT
410 420 430 440 450
EETEDYRQFR KSVLADQGKS FATSSHRNTE EEGPKYKSKV SLKGNRESDG
460 470 480 490 500
FREEKNYKLK ETAYIVERPS TAKDKHKEED KGSDRITVKK EVQSPEQVKS
510 520 530 540 550
EKLKELFDYS PPLHKSLDAR EKSIFREESP LRIKMIASDS HRPEVKLKMA
560 570 580 590 600
PVPLDDSNRP ASLTKDRLLA STLVHSVKKE QEFRSIFDHI KLPQANKSTS
610 620 630 640 650
ESFIQHIVSL VHHVKEQYFK SPAVTLNERF TSYQKATEEH STRQKSPEIH
660 670 680 690 700
RRIDISPSAL RKHTRLAGEE RGFKEEIQKG DKKLRCDSAD LRHDIDRRRK
710 720 730 740 750
ERSKERGDSK GSRESSGSRK QEKTPKDYKE YKPYKDDSKH KGRERDHSRS
760 770 780 790 800
SSSSASPSSP SSREEKESKK EREEEFKTHH EMKDYSGFAG VSRPRGTFFR
810 820 830 840 850
IRGRGRARGV FAGTNTGPNN SNTTFQKRPK EEEWDPEYTP KSKKYFLHDD
860 870 880 890 900
RDDGVDYWAK RGRGRGTFQR GRGRFNFKKS GSSPKWTHDK YQGDGIVEDD
910
EETMENNEEK KDRRKEEKE
Length:919
Mass (Da):106,002
Last modified:May 24, 2004 - v2
Checksum:iF57E6327B29B8920
GO
Isoform 2 (identifier: Q8K019-2) [UniParc]FASTAAdd to basket

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

Show »
Length:917
Mass (Da):105,828
Checksum:i15B92D9FC8086C26
GO
Isoform 3 (identifier: Q8K019-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-36: Missing.
     740-750: HKGRERDHSRS → NVFVFYTAYGG
     751-919: Missing.

Show »
Length:748
Mass (Da):86,036
Checksum:iA4DFB462DE1069B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161E → K in BAC37542 (PubMed:16141072).Curated
Sequence conflicti667 – 6671A → T in BAC37542 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 362Missing in isoform 2 and isoform 3. 2 PublicationsVSP_010372
Alternative sequencei740 – 75011HKGRERDHSRS → NVFVFYTAYGG in isoform 3. 1 PublicationVSP_010373Add
BLAST
Alternative sequencei751 – 919169Missing in isoform 3. 1 PublicationVSP_010374Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011802 mRNA. Translation: BAB27851.1.
AK079110 mRNA. Translation: BAC37542.1.
AK088741 mRNA. Translation: BAC40542.1.
BC034300 mRNA. Translation: AAH34300.1.
AK129071 mRNA. Translation: BAC97881.1.
CCDSiCCDS35858.1. [Q8K019-1]
CCDS78798.1. [Q8K019-2]
RefSeqiNP_001020563.1. NM_001025392.1. [Q8K019-1]
NP_722482.1. NM_153787.2. [Q8K019-2]
UniGeneiMm.294783.

Genome annotation databases

EnsembliENSMUST00000043881; ENSMUSP00000043583; ENSMUSG00000037608. [Q8K019-1]
ENSMUST00000185800; ENSMUSP00000140623; ENSMUSG00000037608. [Q8K019-2]
ENSMUST00000190156; ENSMUSP00000140428; ENSMUSG00000037608. [Q8K019-3]
GeneIDi72567.
KEGGimmu:72567.
UCSCiuc007ent.1. mouse. [Q8K019-2]
uc007enu.1. mouse. [Q8K019-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011802 mRNA. Translation: BAB27851.1.
AK079110 mRNA. Translation: BAC37542.1.
AK088741 mRNA. Translation: BAC40542.1.
BC034300 mRNA. Translation: AAH34300.1.
AK129071 mRNA. Translation: BAC97881.1.
CCDSiCCDS35858.1. [Q8K019-1]
CCDS78798.1. [Q8K019-2]
RefSeqiNP_001020563.1. NM_001025392.1. [Q8K019-1]
NP_722482.1. NM_153787.2. [Q8K019-2]
UniGeneiMm.294783.

3D structure databases

ProteinModelPortaliQ8K019.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215443. 6 interactions.
IntActiQ8K019. 4 interactions.
MINTiMINT-4089177.
STRINGi10090.ENSMUSP00000043583.

PTM databases

iPTMnetiQ8K019.
PhosphoSiteiQ8K019.

Proteomic databases

EPDiQ8K019.
MaxQBiQ8K019.
PaxDbiQ8K019.
PRIDEiQ8K019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043881; ENSMUSP00000043583; ENSMUSG00000037608. [Q8K019-1]
ENSMUST00000185800; ENSMUSP00000140623; ENSMUSG00000037608. [Q8K019-2]
ENSMUST00000190156; ENSMUSP00000140428; ENSMUSG00000037608. [Q8K019-3]
GeneIDi72567.
KEGGimmu:72567.
UCSCiuc007ent.1. mouse. [Q8K019-2]
uc007enu.1. mouse. [Q8K019-1]

Organism-specific databases

CTDi9774.
MGIiMGI:1917580. Bclaf1.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IJCD. Eukaryota.
ENOG4110X68. LUCA.
GeneTreeiENSGT00530000063211.
HOGENOMiHOG000054209.
HOVERGENiHBG050681.
InParanoidiQ8K019.
KOiK13087.
OMAiDDSKHKS.
PhylomeDBiQ8K019.
TreeFamiTF335939.

Miscellaneous databases

ChiTaRSiBclaf1. mouse.
NextBioi336507.
PROiQ8K019.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K019.
CleanExiMM_BCLAF1.
ExpressionAtlasiQ8K019. baseline and differential.
GenevisibleiQ8K019. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-164 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-917 (ISOFORM 2).
    Strain: C57BL/6J and NOD.
    Tissue: Embryo and Thymus.
  2. "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 2).
    Tissue: Retina.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-917 (ISOFORMS 1/2).
    Tissue: Brain.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-289; SER-383; SER-395; THR-400 AND SER-510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-383; SER-395 AND SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-529 AND SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-196; SER-198; SER-221; SER-284; SER-289; SER-299; THR-305; SER-383; SER-387; SER-395; THR-400; SER-494 AND SER-510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-330; LYS-419; LYS-435 AND LYS-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. Cited for: CITRULLINATION AT ARG-802.

Entry informationi

Entry nameiBCLF1_MOUSE
AccessioniPrimary (citable) accession number: Q8K019
Secondary accession number(s): Q8BNZ0, Q8C2E9, Q9CSW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: March 16, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.