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Q92843

- B2CL2_HUMAN

UniProt

Q92843 - B2CL2_HUMAN

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Protein

Bcl-2-like protein 2

Gene
BCL2L2, BCLW, KIAA0271
Organism
Homo sapiens (Human)
Status
Reviewed - 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 binding Source: IntAct
  2. protein heterodimerization activity Source: RefGenome
  3. protein homodimerization activity Source: RefGenome

GO - Biological processi

  1. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
  2. intrinsic apoptotic signaling pathway in response to DNA damage Source: RefGenome
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of intrinsic apoptotic signaling pathway Source: RefGenome
  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; Peripheral membrane protein
Note: Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane.2 Publications

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial outer membrane Source: RefGenome
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

ArrayExpressiQ92843.
BgeeiQ92843.
CleanExiHS_BCL2L2.
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. 13 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 – 2415
Beta strandi30 – 323
Helixi33 – 353
Helixi41 – 7030
Helixi72 – 743
Helixi75 – 8814
Helixi92 – 11221
Helixi117 – 13115
Turni132 – 1343
Helixi135 – 1406
Helixi143 – 1519
Helixi156 – 16813
Turni171 – 1766

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MK3NMR-A2-171[»]
1O0LNMR-A1-183[»]
1ZY3NMR-A2-171[»]
2Y6WX-ray2.00A/B1-164[»]
ProteinModelPortaliQ92843.
SMRiQ92843. Positions 1-183.

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.

Phylogenomic databases

eggNOGiNOG300479.
HOGENOMiHOG000056452.
InParanoidiQ92843.
KOiK02163.
OMAiCAVSIRI.
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. Align

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

MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG    50
DEFETRFRRT FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF 100
VFGAALCAES VNKEMEPLVG QVQEWMVAYL ETQLADWIHS SGGWAEFTAL 150
YGDGALEEAR RLREGNWASV RTVLTGAVAL GALVTVGAFF ASK 193
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.

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.

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. VSP_042064Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_001186768.1. NM_001199839.1.
NP_004041.1. NM_004050.4.
UniGenei Hs.410026.
Hs.735863.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MK3 NMR - A 2-171 [» ]
1O0L NMR - A 1-183 [» ]
1ZY3 NMR - A 2-171 [» ]
2Y6W X-ray 2.00 A/B 1-164 [» ]
ProteinModelPortali Q92843.
SMRi Q92843. Positions 1-183.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107071. 13 interactions.
DIPi DIP-33700N.
IntActi Q92843. 13 interactions.
MINTi MINT-206525.
STRINGi 9606.ENSP00000250405.

Chemistry

ChEMBLi CHEMBL4677.

Protein family/group databases

TCDBi 1.A.21.1.5. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSitei Q92843.

Polymorphism databases

DMDMi 296434404.

Proteomic databases

MaxQBi Q92843.
PaxDbi Q92843.
PRIDEi Q92843.

Protocols and materials databases

DNASUi 599.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000250405 ; ENSP00000250405 ; ENSG00000129473 . [Q92843-1 ]
ENST00000553781 ; ENSP00000451320 ; ENSG00000258643 . [Q92843-2 ]
ENST00000557008 ; ENSP00000452479 ; ENSG00000258643 . [Q92843-2 ]
GeneIDi 599.
KEGGi hsa:599.
UCSCi uc001wjg.4. human. [Q92843-1 ]
uc001wjh.4. human. [Q92843-2 ]

Organism-specific databases

CTDi 599.
GeneCardsi GC14P023776.
GC14P023777.
HGNCi HGNC:995. BCL2L2.
HGNC:42959. BCL2L2-PABPN1.
HPAi CAB040539.
HPA000637.
MIMi 601931. gene.
neXtProti NX_Q92843.
PharmGKBi PA25307.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300479.
HOGENOMi HOG000056452.
InParanoidi Q92843.
KOi K02163.
OMAi CAVSIRI.
PhylomeDBi Q92843.
TreeFami TF105907.
TF315834.

Miscellaneous databases

ChiTaRSi BCL2L2. human.
EvolutionaryTracei Q92843.
GeneWikii BCL2L2.
GenomeRNAii 599.
NextBioi 2439.
PROi Q92843.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92843.
Bgeei Q92843.
CleanExi HS_BCL2L2.
Genevestigatori Q92843.

Family and domain databases

InterProi IPR013280. 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 ]
PANTHERi PTHR11256. PTHR11256. 1 hit.
PTHR11256:SF13. PTHR11256:SF13. 1 hit.
Pfami PF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view ]
PRINTSi PR01865. APOPREGBCLW.
PR01862. BCL2FAMILY.
SMARTi SM00265. BH4. 1 hit.
[Graphical view ]
PROSITEi PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  17. "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: September 3, 2014
This is version 143 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

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