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Protein

Bcl-2-like protein 2

Gene

BCL2L2

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

Functioni

Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.1 Publication

GO - Molecular functioni

  1. protein heterodimerization activity Source: GO_Central
  2. protein homodimerization activity Source: GO_Central

GO - Biological processi

  1. extrinsic apoptotic signaling pathway in absence of ligand Source: GO_Central
  2. intrinsic apoptotic signaling pathway in response to DNA damage Source: GO_Central
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of intrinsic apoptotic signaling pathway Source: GO_Central
  5. Sertoli cell proliferation Source: Ensembl
  6. spermatogenesis Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Protein family/group databases

TCDBi1.A.21.1.5. the bcl-2 (bcl-2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl-2-like protein 2
Short name:
Bcl2-L-2
Alternative name(s):
Apoptosis regulator Bcl-W
Gene namesi
Name:BCL2L2
Synonyms:BCLW, KIAA0271
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:995. BCL2L2.
HGNC:42959. BCL2L2-PABPN1.

Subcellular locationi

Mitochondrion membrane 2 Publications; Peripheral membrane protein 2 Publications
Note: Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane.

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrial outer membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25307.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 193192Bcl-2-like protein 2PRO_0000143066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92843.
PaxDbiQ92843.
PRIDEiQ92843.

PTM databases

PhosphoSiteiQ92843.

Expressioni

Tissue specificityi

Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines.1 Publication

Gene expression databases

BgeeiQ92843.
CleanExiHS_BCL2L2.
ExpressionAtlasiQ92843. baseline and differential.
GenevestigatoriQ92843.

Organism-specific databases

HPAiCAB040539.
HPA000637.

Interactioni

Subunit structurei

Interacts with BOP.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BAXQ078123EBI-707714,EBI-516580
BBC3Q9BXH12EBI-707714,EBI-519884
BCL2L11O435214EBI-707714,EBI-526406
BIDP559575EBI-707714,EBI-519672
BIKQ133232EBI-707714,EBI-700794
BmfQ91ZE92EBI-707714,EBI-708032From a different organism.
TP53BP2Q136252EBI-707714,EBI-77642

Protein-protein interaction databases

BioGridi107071. 19 interactions.
DIPiDIP-33700N.
IntActiQ92843. 13 interactions.
MINTiMINT-206525.
STRINGi9606.ENSP00000250405.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2415Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 373Combined sources
Helixi41 – 6020Combined sources
Helixi65 – 673Combined sources
Turni68 – 703Combined sources
Turni72 – 743Combined sources
Helixi75 – 8612Combined sources
Turni87 – 893Combined sources
Helixi93 – 11220Combined sources
Helixi117 – 13317Combined sources
Helixi135 – 1406Combined sources
Helixi144 – 1518Combined sources
Helixi156 – 16813Combined sources
Turni171 – 1766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MK3NMR-A2-171[»]
1O0LNMR-A1-183[»]
1ZY3NMR-A2-171[»]
2Y6WX-ray2.00A/B1-164[»]
4CIMX-ray1.50A/B1-163[»]
P/Q38-58[»]
ProteinModelPortaliQ92843.
SMRiQ92843. Positions 1-183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92843.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 2921BH4Add
BLAST
Motifi85 – 10420BH1Add
BLAST
Motifi136 – 15116BH2Add
BLAST

Domaini

The BH4 motif seems to be involved in the anti-apoptotic function.
The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2.

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Phylogenomic databases

eggNOGiNOG300479.
GeneTreeiENSGT00390000001517.
ENSGT00530000062935.
HOGENOMiHOG000056452.
InParanoidiQ92843.
KOiK02163.
OMAiLANWIHR.
PhylomeDBiQ92843.
TreeFamiTF105907.
TF315834.

Family and domain databases

InterProiIPR013280. Apop_reg_BclW.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF13. PTHR11256:SF13. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01865. APOPREGBCLW.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q92843-1) [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
MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG
60 70 80 90 100
DEFETRFRRT FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF
110 120 130 140 150
VFGAALCAES VNKEMEPLVG QVQEWMVAYL ETQLADWIHS SGGWAEFTAL
160 170 180 190
YGDGALEEAR RLREGNWASV RTVLTGAVAL GALVTVGAFF ASK
Length:193
Mass (Da):20,746
Last modified:May 18, 2010 - v2
Checksum:i3542243A532B1762
GO
Isoform 3 (identifier: Q92843-2) [UniParc]FASTAAdd to basket

Also known as: BCL2L2-PABPN1

The sequence of this isoform differs from the canonical sequence as follows:
     145-193: AEFTALYGDG...VTVGAFFASK → ELEAIKARVR...ARATSWYSPY

Note: Based on a readthrough transcript which may produce a BCL2L2-PABPN1 fusion protein. No experimental confirmation available. Contains a phosphoserine at position 177. Contains a phosphoserine at position 262.5 Publications

Show »
Length:333
Mass (Da):37,171
Checksum:iF2C9A67BF3D38122
GO

Sequence cautioni

The sequence BAA19666.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331Q → R.6 Publications
Corresponds to variant rs910332 [ dbSNP | Ensembl ].
VAR_048418

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei145 – 19349AEFTA…FFASK → ELEAIKARVREMEEEAEKLK ELQNEVEKQMNMSPPPGNAG PVIMSIEEKMEADARSIYVG NVDYGATAEELEAHFHGCGS VNRVTILCDKFSGHPKGFAY IEFSDKESVRTSLALDESLF RGRQIKVIPKRTNRPGISTT DRGFPRARYRARTTNYNSSR SRFYSGFNSRPRGRVYRGRA RATSWYSPY in isoform 3. 1 PublicationVSP_042064Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59747 mRNA. Translation: AAB09055.1.
D87461 mRNA. Translation: BAA19666.2. Different initiation.
BT019549 mRNA. Translation: AAV38356.1.
AK289519 mRNA. Translation: BAF82208.1.
AL049829 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66169.1.
BC011637 mRNA. No translation available.
BC021198 mRNA. Translation: AAH21198.1.
BC104789 mRNA. Translation: AAI04790.1.
BC113522 mRNA. Translation: AAI13523.1.
RefSeqiNP_001186768.1. NM_001199839.1.
NP_004041.1. NM_004050.4.
UniGeneiHs.410026.
Hs.735863.

Genome annotation databases

EnsembliENST00000250405; ENSP00000250405; ENSG00000129473. [Q92843-1]
ENST00000553781; ENSP00000451320; ENSG00000258643. [Q92843-2]
ENST00000557008; ENSP00000452479; ENSG00000258643. [Q92843-2]
GeneIDi599.
KEGGihsa:599.
UCSCiuc001wjg.4. human. [Q92843-1]
uc001wjh.4. human. [Q92843-2]

Polymorphism databases

DMDMi296434404.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59747 mRNA. Translation: AAB09055.1.
D87461 mRNA. Translation: BAA19666.2. Different initiation.
BT019549 mRNA. Translation: AAV38356.1.
AK289519 mRNA. Translation: BAF82208.1.
AL049829 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66169.1.
BC011637 mRNA. No translation available.
BC021198 mRNA. Translation: AAH21198.1.
BC104789 mRNA. Translation: AAI04790.1.
BC113522 mRNA. Translation: AAI13523.1.
RefSeqiNP_001186768.1. NM_001199839.1.
NP_004041.1. NM_004050.4.
UniGeneiHs.410026.
Hs.735863.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MK3NMR-A2-171[»]
1O0LNMR-A1-183[»]
1ZY3NMR-A2-171[»]
2Y6WX-ray2.00A/B1-164[»]
4CIMX-ray1.50A/B1-163[»]
P/Q38-58[»]
ProteinModelPortaliQ92843.
SMRiQ92843. Positions 1-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107071. 19 interactions.
DIPiDIP-33700N.
IntActiQ92843. 13 interactions.
MINTiMINT-206525.
STRINGi9606.ENSP00000250405.

Chemistry

BindingDBiQ92843.
ChEMBLiCHEMBL4677.

Protein family/group databases

TCDBi1.A.21.1.5. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSiteiQ92843.

Polymorphism databases

DMDMi296434404.

Proteomic databases

MaxQBiQ92843.
PaxDbiQ92843.
PRIDEiQ92843.

Protocols and materials databases

DNASUi599.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250405; ENSP00000250405; ENSG00000129473. [Q92843-1]
ENST00000553781; ENSP00000451320; ENSG00000258643. [Q92843-2]
ENST00000557008; ENSP00000452479; ENSG00000258643. [Q92843-2]
GeneIDi599.
KEGGihsa:599.
UCSCiuc001wjg.4. human. [Q92843-1]
uc001wjh.4. human. [Q92843-2]

Organism-specific databases

CTDi599.
GeneCardsiGC14P023791.
GC14P023792.
HGNCiHGNC:995. BCL2L2.
HGNC:42959. BCL2L2-PABPN1.
HPAiCAB040539.
HPA000637.
MIMi601931. gene.
neXtProtiNX_Q92843.
PharmGKBiPA25307.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300479.
GeneTreeiENSGT00390000001517.
ENSGT00530000062935.
HOGENOMiHOG000056452.
InParanoidiQ92843.
KOiK02163.
OMAiLANWIHR.
PhylomeDBiQ92843.
TreeFamiTF105907.
TF315834.

Miscellaneous databases

ChiTaRSiBCL2L2. human.
EvolutionaryTraceiQ92843.
GeneWikiiBCL2L2.
GenomeRNAii599.
NextBioi2439.
PROiQ92843.
SOURCEiSearch...

Gene expression databases

BgeeiQ92843.
CleanExiHS_BCL2L2.
ExpressionAtlasiQ92843. baseline and differential.
GenevestigatoriQ92843.

Family and domain databases

InterProiIPR013280. Apop_reg_BclW.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF13. PTHR11256:SF13. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01865. APOPREGBCLW.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bcl-w, a novel member of the Bcl-2 family, promotes cell survival."
    Gibson L., Holmgreen S.P., Huang D.C., Bernard O., Copeland N.G., Jenkins N.A., Sutherland G.R., Baker E., Adams J.M., Cory S.
    Oncogene 13:665-675(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT ARG-133.
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-133.
    Tissue: Brain.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-133.
  4. "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] (ISOFORM 1), VARIANT ARG-133.
    Tissue: Cerebellum.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-133.
  7. "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] (ISOFORMS 1 AND 3), VARIANT ARG-133.
    Tissue: Brain, Lung and Rhabdomyosarcoma.
  8. "Tissue expression and subcellular localization of the pro-survival molecule Bcl-w."
    O'Reilly L.A., Print C., Hausmann G., Moriishi K., Cory S., Huang D.C.S., Strasser A.
    Cell Death Differ. 8:486-494(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity."
    Wilson-Annan J., O'Reilly L.A., Crawford S.A., Hausmann G., Beaumont J.G., Parma L.P., Chen L., Lackmann M., Lithgow T., Hinds M.G., Day C.L., Adams J.M., Huang D.C.S.
    J. Cell Biol. 162:877-887(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "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 SER-177 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-177 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity."
    Hinds M.G., Lackmann M., Skea G.L., Harrison P.J., Huang D.C.S., Day C.L.
    EMBO J. 22:1497-1507(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-183.
  18. "Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix."
    Denisov A.Y., Madiraju M.S.R., Chen G., Khadir A., Beauparlant P., Attardo G., Shore G.C., Gehring K.
    J. Biol. Chem. 278:21124-21128(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-171.

Entry informationi

Entry nameiB2CL2_HUMAN
AccessioniPrimary (citable) accession number: Q92843
Secondary accession number(s): A8K0F4, Q2M3U0, Q5U0H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: March 4, 2015
This is version 149 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

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.