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Protein
Submitted name:

Bcl-2-like protein 1

Gene

Bcl2l1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Bcl-2-like protein 1Imported
Submitted name:
Bcl-xbetaImported
Submitted name:
RCG37257Imported
Gene namesi
Name:Bcl2l1Imported
Synonyms:Bcl-xImported
ORF Names:rCG_37257Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2200. Bcl2l1.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043542.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 2420BH4_2InterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
HOVERGENiHBG004472.
TreeFamiTF315834.

Family and domain databases

InterProiIPR013279. Apop_reg_BclX.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TS62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEPERETPSA
60 70 80 90 100
INGNPSWHLA DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR
110 120 130 140 150
YRRAFSDLTS QLHITPGTAY QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL
160 170 180 190 200
CVESVDKEMQ VLVSRIASWM ATYLNDHLEP WIQENGGWVR TTPLVCPPLV
210 220 230 240 250
CLSSVEIPNC PFWSPGMVVE DIDYSGDIPG FTLIPGVNFG NIDDPVFKEP
260 270 280
VFFILATLVA PQFHSFVPIS RQRKTACVFT WLKT
Length:284
Mass (Da):31,776
Last modified:October 1, 2003 - v1
Checksum:iB8F35F641D4E029E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07054330 Genomic DNA. No translation available.
AABR07054331 Genomic DNA. No translation available.
AABR07054332 Genomic DNA. No translation available.
AABR07054333 Genomic DNA. No translation available.
AY141038 mRNA. Translation: AAN17784.1.
CH474050 Genomic DNA. Translation: EDL86043.1.
RefSeqiNP_001028844.1. NM_001033672.1.
NP_113723.2. NM_031535.2.
XP_006235326.1. XM_006235264.2.
UniGeneiRn.10323.

Genome annotation databases

EnsembliENSRNOT00000047416; ENSRNOP00000043542; ENSRNOG00000007946.
ENSRNOT00000091419; ENSRNOP00000069758; ENSRNOG00000007946.
GeneIDi24888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07054330 Genomic DNA. No translation available.
AABR07054331 Genomic DNA. No translation available.
AABR07054332 Genomic DNA. No translation available.
AABR07054333 Genomic DNA. No translation available.
AY141038 mRNA. Translation: AAN17784.1.
CH474050 Genomic DNA. Translation: EDL86043.1.
RefSeqiNP_001028844.1. NM_001033672.1.
NP_113723.2. NM_031535.2.
XP_006235326.1. XM_006235264.2.
UniGeneiRn.10323.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043542.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000047416; ENSRNOP00000043542; ENSRNOG00000007946.
ENSRNOT00000091419; ENSRNOP00000069758; ENSRNOG00000007946.
GeneIDi24888.

Organism-specific databases

CTDi598.
RGDi2200. Bcl2l1.

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00530000062935.
HOGENOMiHOG000056452.
HOVERGENiHBG004472.
TreeFamiTF315834.

Miscellaneous databases

NextBioi604742.

Family and domain databases

InterProiIPR013279. Apop_reg_BclX.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR003093. Bcl2_BH4.
IPR020731. Bcl2_BH4_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF12. PTHR11256:SF12. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]
PRINTSiPR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.
SMARTiSM00265. BH4. 1 hit.
[Graphical view]
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bcl-2-related protein family gene expression during oligodendroglial differentiation."
    Itoh T., Itoh A., Pleasure D.
    J. Neurochem. 85:1500-1512(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  6. Ensembl
    Submitted (JUN-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ7TS62_RAT
AccessioniPrimary (citable) accession number: Q7TS62
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: March 16, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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 one 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.