O00512 (BCL9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

BCL9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1426 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity By similarity. Ref.4
Subunit structure	Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2.
Subcellular location	Nucleus By similarity.
Tissue specificity	Detected at low levels in thymus, prostate, testis, ovary and small intestine, and at lower levels in spleen, colon and blood.
Involvement in disease	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.
Sequence similarities	Belongs to the BCL9 family.
Caution	It is uncertain whether Met-1 or Met-27 is the initiator.
Sequence caution	The sequence CAA73942.1 differs from that shown. Reason: Frameshift at position 1391.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara myotube differentiation involved in skeletal muscle regeneration Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara somatic stem cell maintenance Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
arm	P18824	3	EBI-533127,EBI-216128	From a different organism.
CDC73	Q6P1J9	2	EBI-533127,EBI-930143
CTNNB1	P35222	2	EBI-533127,EBI-491549
pygo	Q9V9W8	3	EBI-533127,EBI-152653	From a different organism.
PYGO1	Q9Y3Y4	7	EBI-533127,EBI-3397474

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1426

1426

B-cell CLL/lymphoma 9 protein

PRO_0000064885

Regions

Region

347 – 377

31

CTNNB1-binding

Compositional bias

231 – 1378

1148

Pro-rich

Compositional bias

331 – 335

5

Poly-Pro

Compositional bias

514 – 517

4

Poly-Pro

Compositional bias

900 – 903

4

Poly-Ala

Compositional bias

970 – 973

4

Poly-Pro

Amino acid modifications

Modified residue

172

1

Phosphothreonine Ref.6

Modified residue

315

1

Phosphothreonine Ref.7

Modified residue

318

1

Phosphoserine Ref.5

Modified residue

352

1

Phosphoserine By similarity

Modified residue

907

1

Phosphoserine Ref.9

Modified residue

917

1

Phosphoserine Ref.9

Natural variations

Natural variant

671

1

P → S.
Corresponds to variant rs3820129 [ dbSNP | Ensembl ].

VAR_046545

Natural variant

782

1

R → K.
Corresponds to variant rs34002844 [ dbSNP | Ensembl ].

VAR_046546

Experimental info

Sequence conflict

240

1

A → V in CAA73942. Ref.1

Sequence conflict

487

1

Q → P in CAA73942. Ref.1

Sequence conflict

609

1

Q → R in CAA73942. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

1426

Helix Strand Turn

Details...

Beta strand

178 – 180

3

Helix

182 – 193

12

Beta strand

196 – 199

4

Helix

353 – 373

21

Sequences

	Sequence		Length	Mass (Da)
	O00512 [UniParc]. Last modified September 23, 2008. Version 4. Checksum: 51EF3D0DCA2103CB	FASTA	1,426	149,290
	10 20 30 40 50 60 MHSSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG KQGGSASQSQ 70 80 90 100 110 120 PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE RSISADSFDQ RDPGTPNDDS 130 140 150 160 170 180 DIKECNSADH IKSQDSQHTP HSMTPSNATA PRSSTPSHGQ TTATEPTPAQ KTPAKVVYVF 190 200 210 220 230 240 STEMANKAAE AVLKGQVETI VSFHIQNISN NKTERSTAPL NTQISALRND PKPLPQQPPA 250 260 270 280 290 300 PANQDQNSSQ NTRLQPTPPI PAPAPKPAAP PRPLDRESPG VENKLIPSVG SPASSTPLPP 310 320 330 340 350 360 DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSSGE PPTLGENPDG LSQEQLEHRE 370 380 390 400 410 420 RSLQTLRDIQ RMLFPDEKEF TGAQSGGPQQ NPGVLDGPQK KPEGPIQAMM AQSQSLGKGP 430 440 450 460 470 480 GPRTDVGAPF GPQGHRDVPF SPDEMVPPSM NSQSGTIGPD HLDHMTPEQI AWLKLQQEFY 490 500 510 520 530 540 EEKRRKQEQV VVQQCSLQDM MVHQHGPRGV VRGPPPPYQM TPSEGWAPGG TEPFSDGINM 550 560 570 580 590 600 PHSLPPRGMA PHPNMPGSQM RLPGFAGMIN SEMEGPNVPN PASRPGLSGV SWPDDVPKIP 610 620 630 640 650 660 DGRNFPPGQG IFSGPGRGER FPNPQGLSEE MFQQQLAEKQ LGLPPGMAME GIRPSMEMNR 670 680 690 700 710 720 MIPGSQRHME PGNNPIFPRI PVEGPLSPSR GDFPKGIPPQ MGPGRELEFG MVPSGMKGDV 730 740 750 760 770 780 NLNVNMGSNS QMIPQKMREA GAGPEEMLKL RPGGSDMLPA QQKMVPLPFG EHPQQEYGMG 790 800 810 820 830 840 PRPFLPMSQG PGSNSGLRNL REPIGPDQRT NSRLSHMPPL PLNPSSNPTS LNTAPPVQRG 850 860 870 880 890 900 LGRKPLDISV AGSQVHSPGI NPLKSPTMHQ VQSPMLGSPS GNLKSPQTPS QLAGMLAGPA 910 920 930 940 950 960 AAASIKSPPV LGSAAASPVH LKSPSLPAPS PGWTSSPKPP LQSPGIPPNH KAPLTMASPA 970 980 990 1000 1010 1020 MLGNVESGGP PPPTASQPAS VNIPGSLPSS TPYTMPPEPT LSQNPLSIMM SRMSKFAMPS 1030 1040 1050 1060 1070 1080 STPLYHDAIK TVASSDDDSP PARSPNLPSM NNMPGMGINT QNPRISGPNP VVPMPTLSPM 1090 1100 1110 1120 1130 1140 GMTQPLSHSN QMPSPNAVGP NIPPHGVPMG PGLMSHNPIM GHGSQEPPMV PQGRMGFPQG 1150 1160 1170 1180 1190 1200 FPPVQSPPQQ VPFPHNGPSG GQGSFPGGMG FPGEGPLGRP SNLPQSSADA ALCKPGGPGG 1210 1220 1230 1240 1250 1260 PDSFTVLGNS MPSVFTDPDL QEVIRPGATG IPEFDLSRII PSEKPSQTLQ YFPRGEVPGR 1270 1280 1290 1300 1310 1320 KQPQGPGPGF SHMQGMMGEQ APRMGLALPG MGGPGPVGTP DIPLGTAPSM PGHNPMRPPA 1330 1340 1350 1360 1370 1380 FLQQGMMGPH HRMMSPAQST MPGQPTLMSN PAAAVGMIPG KDRGPAGLYT HPGPVGSPGM 1390 1400 1410 1420 MMSMQGMMGP QQNIMIPPQM RPRGMAADVG MGGFSQGPGN PGNMMF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"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.
[9]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y13620 mRNA. Translation: CAA73942.1. Frameshift.
AL359207 Genomic DNA. Translation: CAI15198.1.
CH471223 Genomic DNA. Translation: EAW50932.1.

IPI

IPI00160290.

RefSeq

NP_004317.2. NM_004326.2.
XP_003960280.1. XM_003960231.1.

UniGene

Hs.415209.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O00512.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00512. 8 interactions.

STRING

9606.ENSP00000234739.

PTM databases

PhosphoSite

O00512.

Proteomic databases

PaxDb

O00512.

PRIDE

O00512.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000234739; ENSP00000234739; ENSG00000116128.
ENST00000585295; ENSP00000464022; ENSG00000266095.

GeneID

101060700.
607.

KEGG

hsa:101060700.
hsa:607.

UCSC

uc001epq.3. human.

Organism-specific databases

CTD

607.

GeneCards

GC01P147013.

H-InvDB

HIX0028826.

HGNC

HGNC:1008. BCL9.

HPA

HPA020274.

MIM

602597. gene.

neXtProt

NX_O00512.

PharmGKB

PA25318.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG74241.

HOGENOM

HOG000060118.

HOVERGEN

HBG031116.

InParanoid

O00512.

OMA

PGGSDML.

OrthoDB

EOG405S0G.

PhylomeDB

O00512.

Gene expression databases

Bgee

O00512.

CleanEx

HS_BCL9.

Genevestigator

O00512.

GermOnline

ENSG00000116128. Homo sapiens.

Family and domain databases

InterPro

IPR015668. Bcl-9.
IPR024670. BCL9_beta-catenin-bd_dom.
[Graphical view]

PANTHER

PTHR15185. PTHR15185. 1 hit.

Pfam

PF11502. BCL9. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O00512.

NextBio

2469.

SOURCE

Search...

Entry information

Entry name

BCL9_HUMAN

Accession

Primary (citable) accession number: O00512
Secondary accession number(s): Q5T489

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 114 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.