Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00512

- BCL9_HUMAN

UniProt

O00512 - BCL9_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

B-cell CLL/lymphoma 9 protein

Gene

BCL9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity).By similarity

GO - Biological processi

  1. canonical Wnt signaling pathway Source: Ensembl
  2. myotube differentiation involved in skeletal muscle regeneration Source: Ensembl
  3. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  4. skeletal muscle cell differentiation Source: Ensembl
  5. somatic stem cell maintenance Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
SignaLinkiO00512.

Names & Taxonomyi

Protein namesi
Recommended name:
B-cell CLL/lymphoma 9 protein
Short name:
B-cell lymphoma 9 protein
Short name:
Bcl-9
Alternative name(s):
Protein legless homolog
Gene namesi
Name:BCL9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1008. BCL9.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cis-Golgi network Source: MGI
  2. Golgi apparatus Source: Ensembl
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving BCL9 is found in a patient with precusor B-cell acute lymphoblastic leukemia (ALL). Translocation t(1;14)(q21;q32). This translocation leaves the coding region intact, but may have pathogenic effects due to alterations in the expression level of BCL9. Several cases of translocations within the 3'-UTR of BCL9 have been found in B-cell malignancies.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi358 – 3581H → A: Abolishes interaction with CTNNB1. 1 Publication
Mutagenesisi359 – 3591R → A: Abolishes interaction with CTNNB1. 1 Publication
Mutagenesisi366 – 3661L → A: Abolishes interaction with CTNNB1; when associated with A-369. 1 Publication
Mutagenesisi369 – 3691I → A: Abolishes interaction with CTNNB1; when associated with A-366. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA25318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14261426B-cell CLL/lymphoma 9 proteinPRO_0000064885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei172 – 1721Phosphothreonine1 Publication
Modified residuei315 – 3151Phosphothreonine1 Publication
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei352 – 3521PhosphoserineBy similarity
Modified residuei687 – 6871PhosphoserineBy similarity
Modified residuei844 – 8441N6-acetyllysineBy similarity
Modified residuei907 – 9071Phosphoserine1 Publication
Modified residuei917 – 9171Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00512.
PaxDbiO00512.
PRIDEiO00512.

PTM databases

PhosphoSiteiO00512.

Expressioni

Tissue specificityi

Detected at low levels in thymus, prostate, testis, ovary and small intestine, and at lower levels in spleen, colon and blood.

Gene expression databases

BgeeiO00512.
CleanExiHS_BCL9.
GenevestigatoriO00512.

Organism-specific databases

HPAiHPA020274.

Interactioni

Subunit structurei

Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
armP188243EBI-533127,EBI-216128From a different organism.
CDC73Q6P1J92EBI-533127,EBI-930143
CTNNB1P352222EBI-533127,EBI-491549
pygoQ9V9W83EBI-533127,EBI-152653From a different organism.
PYGO1Q9Y3Y47EBI-533127,EBI-3397474
PYGO2Q9BRQ02EBI-533127,EBI-932471

Protein-protein interaction databases

BioGridi107079. 5 interactions.
IntActiO00512. 8 interactions.
MINTiMINT-4773273.
STRINGi9606.ENSP00000234739.

Structurei

Secondary structure

1
1426
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi178 – 1803Combined sources
Helixi182 – 19312Combined sources
Beta strandi196 – 1994Combined sources
Helixi353 – 37321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GL7X-ray2.60C/F347-392[»]
2VP7X-ray1.65B174-205[»]
2VPBX-ray1.59B174-205[»]
2VPDX-ray2.77B/D174-205[»]
2VPEX-ray1.70B/D177-205[»]
2VPGX-ray1.60B/D177-205[»]
3SL9X-ray2.20C/D/F/H344-396[»]
ProteinModelPortaliO00512.
SMRiO00512. Positions 174-205, 348-374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00512.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 20529Interacts with PYGO1Add
BLAST
Regioni358 – 37417Interacts with CTNNB1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi231 – 13781148Pro-richAdd
BLAST
Compositional biasi331 – 3355Poly-Pro
Compositional biasi514 – 5174Poly-Pro
Compositional biasi900 – 9034Poly-Ala
Compositional biasi970 – 9734Poly-Pro

Sequence similaritiesi

Belongs to the BCL9 family.Curated

Phylogenomic databases

eggNOGiNOG74241.
GeneTreeiENSGT00730000110915.
HOGENOMiHOG000060118.
HOVERGENiHBG031116.
InParanoidiO00512.
OMAiPGGSDML.
OrthoDBiEOG7327N1.
PhylomeDBiO00512.
TreeFamiTF331144.

Family and domain databases

InterProiIPR015668. Bcl-9.
IPR024670. BCL9_beta-catenin-bd_dom.
[Graphical view]
PANTHERiPTHR15185. PTHR15185. 1 hit.
PfamiPF11502. BCL9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00512-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHSSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG
60 70 80 90 100
KQGGSASQSQ PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE
110 120 130 140 150
RSISADSFDQ RDPGTPNDDS DIKECNSADH IKSQDSQHTP HSMTPSNATA
160 170 180 190 200
PRSSTPSHGQ TTATEPTPAQ KTPAKVVYVF STEMANKAAE AVLKGQVETI
210 220 230 240 250
VSFHIQNISN NKTERSTAPL NTQISALRND PKPLPQQPPA PANQDQNSSQ
260 270 280 290 300
NTRLQPTPPI PAPAPKPAAP PRPLDRESPG VENKLIPSVG SPASSTPLPP
310 320 330 340 350
DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSSGE PPTLGENPDG
360 370 380 390 400
LSQEQLEHRE RSLQTLRDIQ RMLFPDEKEF TGAQSGGPQQ NPGVLDGPQK
410 420 430 440 450
KPEGPIQAMM AQSQSLGKGP GPRTDVGAPF GPQGHRDVPF SPDEMVPPSM
460 470 480 490 500
NSQSGTIGPD HLDHMTPEQI AWLKLQQEFY EEKRRKQEQV VVQQCSLQDM
510 520 530 540 550
MVHQHGPRGV VRGPPPPYQM TPSEGWAPGG TEPFSDGINM PHSLPPRGMA
560 570 580 590 600
PHPNMPGSQM RLPGFAGMIN SEMEGPNVPN PASRPGLSGV SWPDDVPKIP
610 620 630 640 650
DGRNFPPGQG IFSGPGRGER FPNPQGLSEE MFQQQLAEKQ LGLPPGMAME
660 670 680 690 700
GIRPSMEMNR MIPGSQRHME PGNNPIFPRI PVEGPLSPSR GDFPKGIPPQ
710 720 730 740 750
MGPGRELEFG MVPSGMKGDV NLNVNMGSNS QMIPQKMREA GAGPEEMLKL
760 770 780 790 800
RPGGSDMLPA QQKMVPLPFG EHPQQEYGMG PRPFLPMSQG PGSNSGLRNL
810 820 830 840 850
REPIGPDQRT NSRLSHMPPL PLNPSSNPTS LNTAPPVQRG LGRKPLDISV
860 870 880 890 900
AGSQVHSPGI NPLKSPTMHQ VQSPMLGSPS GNLKSPQTPS QLAGMLAGPA
910 920 930 940 950
AAASIKSPPV LGSAAASPVH LKSPSLPAPS PGWTSSPKPP LQSPGIPPNH
960 970 980 990 1000
KAPLTMASPA MLGNVESGGP PPPTASQPAS VNIPGSLPSS TPYTMPPEPT
1010 1020 1030 1040 1050
LSQNPLSIMM SRMSKFAMPS STPLYHDAIK TVASSDDDSP PARSPNLPSM
1060 1070 1080 1090 1100
NNMPGMGINT QNPRISGPNP VVPMPTLSPM GMTQPLSHSN QMPSPNAVGP
1110 1120 1130 1140 1150
NIPPHGVPMG PGLMSHNPIM GHGSQEPPMV PQGRMGFPQG FPPVQSPPQQ
1160 1170 1180 1190 1200
VPFPHNGPSG GQGSFPGGMG FPGEGPLGRP SNLPQSSADA ALCKPGGPGG
1210 1220 1230 1240 1250
PDSFTVLGNS MPSVFTDPDL QEVIRPGATG IPEFDLSRII PSEKPSQTLQ
1260 1270 1280 1290 1300
YFPRGEVPGR KQPQGPGPGF SHMQGMMGEQ APRMGLALPG MGGPGPVGTP
1310 1320 1330 1340 1350
DIPLGTAPSM PGHNPMRPPA FLQQGMMGPH HRMMSPAQST MPGQPTLMSN
1360 1370 1380 1390 1400
PAAAVGMIPG KDRGPAGLYT HPGPVGSPGM MMSMQGMMGP QQNIMIPPQM
1410 1420
RPRGMAADVG MGGFSQGPGN PGNMMF
Length:1,426
Mass (Da):149,290
Last modified:September 23, 2008 - v4
Checksum:i51EF3D0DCA2103CB
GO

Sequence cautioni

The sequence CAA73942.1 differs from that shown. Reason: Frameshift at position 1391. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401A → V in CAA73942. (PubMed:9490669)Curated
Sequence conflicti487 – 4871Q → P in CAA73942. (PubMed:9490669)Curated
Sequence conflicti609 – 6091Q → R in CAA73942. (PubMed:9490669)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti671 – 6711P → S.
Corresponds to variant rs3820129 [ dbSNP | Ensembl ].
VAR_046545
Natural varianti782 – 7821R → K.
Corresponds to variant rs34002844 [ dbSNP | Ensembl ].
VAR_046546

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13620 mRNA. Translation: CAA73942.1. Frameshift.
AL359207 Genomic DNA. Translation: CAI15198.1.
CH471223 Genomic DNA. Translation: EAW50932.1.
CCDSiCCDS30833.1.
RefSeqiNP_004317.2. NM_004326.3.
XP_005273028.1. XM_005272971.2.
XP_006711546.1. XM_006711483.1.
UniGeneiHs.415209.

Genome annotation databases

EnsembliENST00000234739; ENSP00000234739; ENSG00000116128.
GeneIDi607.
KEGGihsa:607.
UCSCiuc001epq.3. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13620 mRNA. Translation: CAA73942.1 . Frameshift.
AL359207 Genomic DNA. Translation: CAI15198.1 .
CH471223 Genomic DNA. Translation: EAW50932.1 .
CCDSi CCDS30833.1.
RefSeqi NP_004317.2. NM_004326.3.
XP_005273028.1. XM_005272971.2.
XP_006711546.1. XM_006711483.1.
UniGenei Hs.415209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GL7 X-ray 2.60 C/F 347-392 [» ]
2VP7 X-ray 1.65 B 174-205 [» ]
2VPB X-ray 1.59 B 174-205 [» ]
2VPD X-ray 2.77 B/D 174-205 [» ]
2VPE X-ray 1.70 B/D 177-205 [» ]
2VPG X-ray 1.60 B/D 177-205 [» ]
3SL9 X-ray 2.20 C/D/F/H 344-396 [» ]
ProteinModelPortali O00512.
SMRi O00512. Positions 174-205, 348-374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107079. 5 interactions.
IntActi O00512. 8 interactions.
MINTi MINT-4773273.
STRINGi 9606.ENSP00000234739.

PTM databases

PhosphoSitei O00512.

Proteomic databases

MaxQBi O00512.
PaxDbi O00512.
PRIDEi O00512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234739 ; ENSP00000234739 ; ENSG00000116128 .
GeneIDi 607.
KEGGi hsa:607.
UCSCi uc001epq.3. human.

Organism-specific databases

CTDi 607.
GeneCardsi GC01P147013.
H-InvDB HIX0028826.
HGNCi HGNC:1008. BCL9.
HPAi HPA020274.
MIMi 602597. gene.
neXtProti NX_O00512.
PharmGKBi PA25318.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG74241.
GeneTreei ENSGT00730000110915.
HOGENOMi HOG000060118.
HOVERGENi HBG031116.
InParanoidi O00512.
OMAi PGGSDML.
OrthoDBi EOG7327N1.
PhylomeDBi O00512.
TreeFami TF331144.

Enzyme and pathway databases

Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
SignaLinki O00512.

Miscellaneous databases

EvolutionaryTracei O00512.
GeneWikii BCL9.
GenomeRNAii 607.
NextBioi 2469.
PROi O00512.
SOURCEi Search...

Gene expression databases

Bgeei O00512.
CleanExi HS_BCL9.
Genevestigatori O00512.

Family and domain databases

InterProi IPR015668. Bcl-9.
IPR024670. BCL9_beta-catenin-bd_dom.
[Graphical view ]
PANTHERi PTHR15185. PTHR15185. 1 hit.
Pfami PF11502. BCL9. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of translocation t(1;14)(q21;q32) defines a novel gene (BCL9) at chromosome 1q21."
    Willis T.G., Zalcberg I.R., Coignet L.J.A., Wlodarska I., Stul M., Jadayel D.M., Bastard C., Treleaven J.G., Catovsky D., Silva M.L.M., Dyer M.J.S.
    Blood 91:1873-1881(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of pygopus to the nuclear beta-catenin-TCF complex."
    Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S., Murone M., Zuellig S., Basler K.
    Cell 109:47-60(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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].
  8. "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 THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-907 AND SER-917, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of a beta-catenin/BCL9/Tcf4 complex."
    Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.
    Mol. Cell 24:293-300(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 347-392 IN COMPLEX WITH CTNNB1 AND TCF7L2, INTERACTION WITH CTNNB1, MUTAGENESIS OF HIS-358; ARG-359; LEU-366 AND ILE-369.
  12. "Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex."
    Fiedler M., Sanchez-Barrena M.J., Nekrasov M., Mieszczanek J., Rybin V., Muller J., Evans P., Bienz M.
    Mol. Cell 30:507-518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 174-205 IN COMPLEX WITH PYGO1 AND HISTONE H3K4ME2.

Entry informationi

Entry nameiBCL9_HUMAN
AccessioniPrimary (citable) accession number: O00512
Secondary accession number(s): Q5T489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 23, 2008
Last modified: October 29, 2014
This is version 130 of the entry and version 4 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

Caution

It is uncertain whether Met-1 or Met-27 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3