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Protein

Protein BEX2

Gene

BEX2

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

Functioni

Regulator of mitochondrial apoptosis and G1 cell cycle in breast cancer. Protects the breast cancer cells against mitochondrial apoptosis and this effect is mediated through the modulation of BCL2 protein family, which involves the positive regulation of anti-apoptotic member BCL2 and the negative regulation of pro-apoptotic members BAD, BAK1 and PUMA. Required for the normal cell cycle progression during G1 in breast cancer cells through the regulation of CCND1 and CDKN1A. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity.1 Publication

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. regulation of apoptotic process Source: UniProtKB
  4. regulation of cell cycle Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BEX2
Alternative name(s):
Brain-expressed X-linked protein 2
Short name:
hBex2
Gene namesi
Name:BEX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:30933. BEX2.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134977614.

Polymorphism and mutation databases

BioMutaiBEX2.
DMDMi74752443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128128Protein BEX2PRO_0000229777Add
BLAST

Proteomic databases

PaxDbiQ9BXY8.
PRIDEiQ9BXY8.

PTM databases

PhosphoSiteiQ9BXY8.

Expressioni

Tissue specificityi

Expressed in central nervous system, with high level in pituitary, cerebellum and temporal lobe. Widely expressed in breast cancer cell lines.2 Publications

Gene expression databases

BgeeiQ9BXY8.
CleanExiHS_BEX2.
ExpressionAtlasiQ9BXY8. baseline and differential.
GenevestigatoriQ9BXY8.

Organism-specific databases

HPAiHPA042224.
HPA045384.

Interactioni

Subunit structurei

Interacts with OMP (By similarity). Interacts with LMO2, possibly leading to regulate the transcriptional activity of a DNA-binding complex containing LMO2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BLZF1Q9H2G93EBI-745073,EBI-2548012
CALCOCO2Q131373EBI-745073,EBI-739580
CEP70Q8NHQ13EBI-745073,EBI-739624
FSD2A1L4K13EBI-745073,EBI-5661036
KRT15P190123EBI-745073,EBI-739566
KRT31Q153233EBI-745073,EBI-948001
KRT38O760153EBI-745073,EBI-1047263
KRT40Q6A1623EBI-745073,EBI-10171697
KRTAP10-8P604103EBI-745073,EBI-10171774
KRTAP5-9P263713EBI-745073,EBI-3958099
LZTS2Q9BRK43EBI-745073,EBI-741037
MAGEA11P43364-23EBI-745073,EBI-10178634
MAGEA4Q1RN333EBI-745073,EBI-10194128
MIPOL1Q8TD103EBI-745073,EBI-2548751
MKRN3Q130643EBI-745073,EBI-2340269
NECAB2H3BTW23EBI-745073,EBI-10172876
PNMA1Q8ND903EBI-745073,EBI-302345
PRDM14Q9GZV83EBI-745073,EBI-3957793
SSX2IPQ9Y2D83EBI-745073,EBI-2212028
TRAF1Q130773EBI-745073,EBI-359224
TRAF2Q129333EBI-745073,EBI-355744
TRIM27P143733EBI-745073,EBI-719493
TRIM42A1L4B63EBI-745073,EBI-10172216

Protein-protein interaction databases

BioGridi124218. 27 interactions.
IntActiQ9BXY8. 33 interactions.
STRINGi9606.ENSP00000361759.

Structurei

3D structure databases

ProteinModelPortaliQ9BXY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the BEX family.Curated

Phylogenomic databases

eggNOGiNOG244262.
GeneTreeiENSGT00740000115473.
HOGENOMiHOG000236300.
HOVERGENiHBG080240.
InParanoidiQ9BXY8.
OMAiRWDIMHR.
OrthoDBiEOG7XPZ7S.
PhylomeDBiQ9BXY8.
TreeFamiTF337909.

Family and domain databases

InterProiIPR007623. BEX.
IPR021156. TF_A-like/BEX-like.
[Graphical view]
PfamiPF04538. BEX. 1 hit.
[Graphical view]
PIRSFiPIRSF008633. BEX. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BXY8-1) [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
MESKEERALN NLIVENVNQE NDEKDEKEQV ANKGEPLALP LNVSEYCVPR
60 70 80 90 100
GNRRRFRVRQ PILQYRWDIM HRLGEPQARM REENMERIGE EVRQLMEKLR
110 120
EKQLSHSLRA VSTDPPHHDH HDEFCLMP
Length:128
Mass (Da):15,321
Last modified:June 1, 2001 - v1
Checksum:iF6302EC28F71D2A8
GO
Isoform 2 (identifier: Q9BXY8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQKMVVCGAKCCGDAPHVENREEETARIGPGVM

Note: Gene prediction based on EST data.

Show »
Length:160
Mass (Da):18,719
Checksum:i0C3D806EE0A4A527
GO

Sequence cautioni

The sequence CAI43072.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MQKMVVCGAKCCGDAPHVEN REEETARIGPGVM in isoform 2. CuratedVSP_046808

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY833560 mRNA. Translation: AAX40678.1.
AF251053 mRNA. Translation: AAK34943.1.
AK312085 mRNA. Translation: BAG35021.1.
AL133348 Genomic DNA. Translation: CAI43071.1.
AL133348 Genomic DNA. Translation: CAI43072.1. Sequence problems.
Z70233 Genomic DNA. Translation: CAD24039.1.
CH471190 Genomic DNA. Translation: EAW54715.1.
CH471190 Genomic DNA. Translation: EAW54716.1.
BC015522 mRNA. Translation: AAH15522.1.
CCDSiCCDS14505.1. [Q9BXY8-1]
CCDS55467.1. [Q9BXY8-2]
RefSeqiNP_001161871.1. NM_001168399.1. [Q9BXY8-2]
NP_001161872.1. NM_001168400.1.
NP_001161873.1. NM_001168401.1. [Q9BXY8-1]
NP_116010.1. NM_032621.3. [Q9BXY8-1]
UniGeneiHs.398989.

Genome annotation databases

EnsembliENST00000372674; ENSP00000361759; ENSG00000133134. [Q9BXY8-1]
ENST00000372677; ENSP00000361762; ENSG00000133134. [Q9BXY8-1]
ENST00000536889; ENSP00000442521; ENSG00000133134. [Q9BXY8-2]
GeneIDi84707.
KEGGihsa:84707.
UCSCiuc004ekb.3. human. [Q9BXY8-1]

Polymorphism and mutation databases

BioMutaiBEX2.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY833560 mRNA. Translation: AAX40678.1.
AF251053 mRNA. Translation: AAK34943.1.
AK312085 mRNA. Translation: BAG35021.1.
AL133348 Genomic DNA. Translation: CAI43071.1.
AL133348 Genomic DNA. Translation: CAI43072.1. Sequence problems.
Z70233 Genomic DNA. Translation: CAD24039.1.
CH471190 Genomic DNA. Translation: EAW54715.1.
CH471190 Genomic DNA. Translation: EAW54716.1.
BC015522 mRNA. Translation: AAH15522.1.
CCDSiCCDS14505.1. [Q9BXY8-1]
CCDS55467.1. [Q9BXY8-2]
RefSeqiNP_001161871.1. NM_001168399.1. [Q9BXY8-2]
NP_001161872.1. NM_001168400.1.
NP_001161873.1. NM_001168401.1. [Q9BXY8-1]
NP_116010.1. NM_032621.3. [Q9BXY8-1]
UniGeneiHs.398989.

3D structure databases

ProteinModelPortaliQ9BXY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124218. 27 interactions.
IntActiQ9BXY8. 33 interactions.
STRINGi9606.ENSP00000361759.

PTM databases

PhosphoSiteiQ9BXY8.

Polymorphism and mutation databases

BioMutaiBEX2.
DMDMi74752443.

Proteomic databases

PaxDbiQ9BXY8.
PRIDEiQ9BXY8.

Protocols and materials databases

DNASUi84707.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372674; ENSP00000361759; ENSG00000133134. [Q9BXY8-1]
ENST00000372677; ENSP00000361762; ENSG00000133134. [Q9BXY8-1]
ENST00000536889; ENSP00000442521; ENSG00000133134. [Q9BXY8-2]
GeneIDi84707.
KEGGihsa:84707.
UCSCiuc004ekb.3. human. [Q9BXY8-1]

Organism-specific databases

CTDi84707.
GeneCardsiGC0XM102564.
HGNCiHGNC:30933. BEX2.
HPAiHPA042224.
HPA045384.
MIMi300691. gene.
neXtProtiNX_Q9BXY8.
PharmGKBiPA134977614.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244262.
GeneTreeiENSGT00740000115473.
HOGENOMiHOG000236300.
HOVERGENiHBG080240.
InParanoidiQ9BXY8.
OMAiRWDIMHR.
OrthoDBiEOG7XPZ7S.
PhylomeDBiQ9BXY8.
TreeFamiTF337909.

Miscellaneous databases

ChiTaRSiBEX2. human.
GeneWikiiBEX2.
GenomeRNAii84707.
NextBioi74802.
PROiQ9BXY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BXY8.
CleanExiHS_BEX2.
ExpressionAtlasiQ9BXY8. baseline and differential.
GenevestigatoriQ9BXY8.

Family and domain databases

InterProiIPR007623. BEX.
IPR021156. TF_A-like/BEX-like.
[Graphical view]
PfamiPF04538. BEX. 1 hit.
[Graphical view]
PIRSFiPIRSF008633. BEX. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the Bex gene family in humans, mice, and rats."
    Alvarez E., Zhou W., Witta S.E., Freed C.R.
    Gene 357:18-28(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S., Tang R., Chen X., Wu C.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Uterus.
  7. "Human Bex2 interacts with LMO2 and regulates the transcriptional activity of a novel DNA-binding complex."
    Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J., Qiang B., Liu Y.-J., Peng X.
    Nucleic Acids Res. 33:6555-6565(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LMO2.
  8. "BEX2 regulates mitochondrial apoptosis and G1 cell cycle in breast cancer."
    Naderi A., Liu J., Bennett I.C.
    Int. J. Cancer 126:1596-1610(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiBEX2_HUMAN
AccessioniPrimary (citable) accession number: Q9BXY8
Secondary accession number(s): B2R574
, D3DXA2, F5H7H5, Q5JVV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 104 of the entry and version 1 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

Was named BEX1 by some authors.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.