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O00512

- BCL9_HUMAN

UniProt

O00512 - BCL9_HUMAN

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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.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct

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. Golgi apparatus Source: Ensembl
  2. cis-Golgi network Source: MGI
  3. nucleus Source: UniProtKB-SubCell
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 protein
PRO_0000064885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041Phosphoserine By similarity
Modified residuei172 – 1721Phosphothreonine1 Publication
Modified residuei315 – 3151Phosphothreonine1 Publication
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine By similarity
Modified residuei687 – 6871Phosphoserine By similarity
Modified residuei844 – 8441N6-acetyllysine By 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'.1 Publication

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiO00512.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 20529Interacts with PYGO1
Add
BLAST
Regioni358 – 37417Interacts with CTNNB1
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the BCL9 family.

Phylogenomic databases

eggNOGiNOG74241.
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

MHSSNPKVRS SPSGNTQSSP KSKQEVMVRP PTVMSPSGNP QLDSKFSNQG     50
KQGGSASQSQ PSPCDSKSGG HTPKALPGPG GSMGLKNGAG NGAKGKGKRE 100
RSISADSFDQ RDPGTPNDDS DIKECNSADH IKSQDSQHTP HSMTPSNATA 150
PRSSTPSHGQ TTATEPTPAQ KTPAKVVYVF STEMANKAAE AVLKGQVETI 200
VSFHIQNISN NKTERSTAPL NTQISALRND PKPLPQQPPA PANQDQNSSQ 250
NTRLQPTPPI PAPAPKPAAP PRPLDRESPG VENKLIPSVG SPASSTPLPP 300
DGTGPNSTPN NRAVTPVSQG SNSSSADPKA PPPPPVSSGE PPTLGENPDG 350
LSQEQLEHRE RSLQTLRDIQ RMLFPDEKEF TGAQSGGPQQ NPGVLDGPQK 400
KPEGPIQAMM AQSQSLGKGP GPRTDVGAPF GPQGHRDVPF SPDEMVPPSM 450
NSQSGTIGPD HLDHMTPEQI AWLKLQQEFY EEKRRKQEQV VVQQCSLQDM 500
MVHQHGPRGV VRGPPPPYQM TPSEGWAPGG TEPFSDGINM PHSLPPRGMA 550
PHPNMPGSQM RLPGFAGMIN SEMEGPNVPN PASRPGLSGV SWPDDVPKIP 600
DGRNFPPGQG IFSGPGRGER FPNPQGLSEE MFQQQLAEKQ LGLPPGMAME 650
GIRPSMEMNR MIPGSQRHME PGNNPIFPRI PVEGPLSPSR GDFPKGIPPQ 700
MGPGRELEFG MVPSGMKGDV NLNVNMGSNS QMIPQKMREA GAGPEEMLKL 750
RPGGSDMLPA QQKMVPLPFG EHPQQEYGMG PRPFLPMSQG PGSNSGLRNL 800
REPIGPDQRT NSRLSHMPPL PLNPSSNPTS LNTAPPVQRG LGRKPLDISV 850
AGSQVHSPGI NPLKSPTMHQ VQSPMLGSPS GNLKSPQTPS QLAGMLAGPA 900
AAASIKSPPV LGSAAASPVH LKSPSLPAPS PGWTSSPKPP LQSPGIPPNH 950
KAPLTMASPA MLGNVESGGP PPPTASQPAS VNIPGSLPSS TPYTMPPEPT 1000
LSQNPLSIMM SRMSKFAMPS STPLYHDAIK TVASSDDDSP PARSPNLPSM 1050
NNMPGMGINT QNPRISGPNP VVPMPTLSPM GMTQPLSHSN QMPSPNAVGP 1100
NIPPHGVPMG PGLMSHNPIM GHGSQEPPMV PQGRMGFPQG FPPVQSPPQQ 1150
VPFPHNGPSG GQGSFPGGMG FPGEGPLGRP SNLPQSSADA ALCKPGGPGG 1200
PDSFTVLGNS MPSVFTDPDL QEVIRPGATG IPEFDLSRII PSEKPSQTLQ 1250
YFPRGEVPGR KQPQGPGPGF SHMQGMMGEQ APRMGLALPG MGGPGPVGTP 1300
DIPLGTAPSM PGHNPMRPPA FLQQGMMGPH HRMMSPAQST MPGQPTLMSN 1350
PAAAVGMIPG KDRGPAGLYT HPGPVGSPGM MMSMQGMMGP QQNIMIPPQM 1400
RPRGMAADVG MGGFSQGPGN PGNMMF 1426
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti240 – 2401A → V in CAA73942. 1 Publication
Sequence conflicti487 – 4871Q → P in CAA73942. 1 Publication
Sequence conflicti609 – 6091Q → R in CAA73942. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000585295; ENSP00000464022; ENSG00000266095.
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 .
ENST00000585295 ; ENSP00000464022 ; ENSG00000266095 .
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.
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: September 3, 2014
This is version 128 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.

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

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