Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

cAMP-responsive element-binding protein-like 2

Gene

Crebl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • positive regulation of fat cell differentiation Source: UniProtKB
  • positive regulation of glucose import Source: UniProtKB
  • positive regulation of lipid biosynthetic process Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-responsive element-binding protein-like 2
Gene namesi
Name:Crebl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1889385. Crebl2.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123cAMP-responsive element-binding protein-like 2PRO_0000318193Add
BLAST

Post-translational modificationi

Phosphorylated by AMPK.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ32M00.
PaxDbiQ32M00.
PRIDEiQ32M00.

Expressioni

Tissue specificityi

Widely expressed with higher expression in adipose tissue, skeletal muscle, and liver (at protein level).1 Publication

Inductioni

Up-regulated during preadipocyte differentiation (at protein level).1 Publication

Gene expression databases

BgeeiQ32M00.
CleanExiMM_CREBL2.

Interactioni

Subunit structurei

Interacts with CREB1; regulates CREB1 phosphorylation, stability and transcriptional activity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Creb1Q011474EBI-5314489,EBI-2291098

Protein-protein interaction databases

IntActiQ32M00. 1 interaction.
STRINGi10090.ENSMUSP00000035304.

Structurei

3D structure databases

ProteinModelPortaliQ32M00.
SMRiQ32M00. Positions 29-74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8664bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 6032Basic motifBy similarityAdd
BLAST
Regioni62 – 698Leucine-zipperBy similarity

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated

Phylogenomic databases

eggNOGiENOG410J0Q3. Eukaryota.
ENOG4111T4Y. LUCA.
HOGENOMiHOG000111966.
HOVERGENiHBG107761.
InParanoidiQ32M00.
OrthoDBiEOG7TQV3F.
PhylomeDBiQ32M00.
TreeFamiTF323305.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q32M00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDSKVVGGK VKKPGKRGRK PAKIDLKAKL ERSRQSAREC RARKKLRYQY
60 70 80 90 100
LEELVSSRER AICALREELE MYKQWCMAMD QGKIPSEIRA LLTGEEQSKP
110 120
QQNSSRHPKA GKTDANTNSL VGN
Length:123
Mass (Da):14,002
Last modified:December 6, 2005 - v1
Checksum:iA1B85B8AA582D62E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031N → S in BAC32383 (PubMed:16141072).Curated
Sequence conflicti116 – 1161N → D in BAC32383 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK045467 mRNA. Translation: BAC32383.1.
BC109358 mRNA. Translation: AAI09359.1.
BC109359 mRNA. Translation: AAI09360.1.
CCDSiCCDS20640.1.
RefSeqiNP_808355.1. NM_177687.3.
UniGeneiMm.267010.

Genome annotation databases

GeneIDi232430.
KEGGimmu:232430.
UCSCiuc009ekt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK045467 mRNA. Translation: BAC32383.1.
BC109358 mRNA. Translation: AAI09359.1.
BC109359 mRNA. Translation: AAI09360.1.
CCDSiCCDS20640.1.
RefSeqiNP_808355.1. NM_177687.3.
UniGeneiMm.267010.

3D structure databases

ProteinModelPortaliQ32M00.
SMRiQ32M00. Positions 29-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ32M00. 1 interaction.
STRINGi10090.ENSMUSP00000035304.

Proteomic databases

EPDiQ32M00.
PaxDbiQ32M00.
PRIDEiQ32M00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi232430.
KEGGimmu:232430.
UCSCiuc009ekt.1. mouse.

Organism-specific databases

CTDi1389.
MGIiMGI:1889385. Crebl2.

Phylogenomic databases

eggNOGiENOG410J0Q3. Eukaryota.
ENOG4111T4Y. LUCA.
HOGENOMiHOG000111966.
HOVERGENiHBG107761.
InParanoidiQ32M00.
OrthoDBiEOG7TQV3F.
PhylomeDBiQ32M00.
TreeFamiTF323305.

Miscellaneous databases

NextBioi381111.
PROiQ32M00.
SOURCEiSearch...

Gene expression databases

BgeeiQ32M00.
CleanExiMM_CREBL2.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  2. "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].
  3. "CREBL2, interacting with CREB, induces adipogenesis in 3T3-L1 adipocytes."
    Ma X., Zhang H., Yuan L., Jing H., Thacker P., Li D.
    Biochem. J. 439:27-38(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION, INTERACTION WITH CREB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiCRBL2_MOUSE
AccessioniPrimary (citable) accession number: Q32M00
Secondary accession number(s): Q8BR67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 6, 2005
Last modified: March 16, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.