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Protein

cAMP-responsive element-binding protein-like 2

Gene

CREBL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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. Identification in a chromosomal region frequently deleted in various cancers suggests that it might act as a tumor suppressor.1 Publication

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. positive regulation of fat cell differentiation Source: UniProtKB
  4. positive regulation of glucose import Source: UniProtKB
  5. positive regulation of lipid biosynthetic process Source: UniProtKB
  6. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. protein stabilization Source: UniProtKB
  9. signal transduction Source: ProtInc
  10. transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2350. CREBL2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA26868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 120120cAMP-responsive element-binding protein-like 2PRO_0000318192Add
BLAST

Post-translational modificationi

Phosphorylated by AMPK.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO60519.
PRIDEiO60519.

Expressioni

Gene expression databases

BgeeiO60519.
CleanExiHS_CREBL2.
GenevestigatoriO60519.

Organism-specific databases

HPAiHPA043738.

Interactioni

Subunit structurei

Interacts with CREB1; regulates CREB1 phosphorylation, stability and transcriptional activity.By similarity

Protein-protein interaction databases

BioGridi107779. 1 interaction.
IntActiO60519. 1 interaction.
STRINGi9606.ENSP00000228865.

Structurei

3D structure databases

ProteinModelPortaliO60519.
SMRiO60519. Positions 28-74.
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

eggNOGiNOG85470.
GeneTreeiENSGT00390000005388.
HOGENOMiHOG000111966.
HOVERGENiHBG107761.
InParanoidiO60519.
OMAiEANNNSW.
OrthoDBiEOG7TQV3F.
PhylomeDBiO60519.
TreeFamiTF323305.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O60519-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDSKVVGGK VKKPGKRGRK PAKIDLKAKL ERSRQSAREC RARKKLRYQY
60 70 80 90 100
LEELVSSRER AICALREELE MYKQWCMAMD QGKIPSEIKA LLTGEEQNKS
110 120
QQNSSRHTKA GKTDANSNSW
Length:120
Mass (Da):13,784
Last modified:July 31, 1998 - v1
Checksum:iE191B2D239EDA17B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039081 mRNA. Translation: AAC32314.1.
AB451461 mRNA. Translation: BAG70275.1.
CR542250 mRNA. Translation: CAG47046.1.
CH471094 Genomic DNA. Translation: EAW96269.1.
BC104873 mRNA. Translation: AAI04874.1.
BC106052 mRNA. Translation: AAI06053.1.
BC112157 mRNA. Translation: AAI12158.1.
CCDSiCCDS8651.1.
RefSeqiNP_001301.1. NM_001310.3.
UniGeneiHs.591156.

Genome annotation databases

EnsembliENST00000228865; ENSP00000228865; ENSG00000111269.
GeneIDi1389.
KEGGihsa:1389.
UCSCiuc001rap.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039081 mRNA. Translation: AAC32314.1.
AB451461 mRNA. Translation: BAG70275.1.
CR542250 mRNA. Translation: CAG47046.1.
CH471094 Genomic DNA. Translation: EAW96269.1.
BC104873 mRNA. Translation: AAI04874.1.
BC106052 mRNA. Translation: AAI06053.1.
BC112157 mRNA. Translation: AAI12158.1.
CCDSiCCDS8651.1.
RefSeqiNP_001301.1. NM_001310.3.
UniGeneiHs.591156.

3D structure databases

ProteinModelPortaliO60519.
SMRiO60519. Positions 28-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107779. 1 interaction.
IntActiO60519. 1 interaction.
STRINGi9606.ENSP00000228865.

Proteomic databases

PaxDbiO60519.
PRIDEiO60519.

Protocols and materials databases

DNASUi1389.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228865; ENSP00000228865; ENSG00000111269.
GeneIDi1389.
KEGGihsa:1389.
UCSCiuc001rap.1. human.

Organism-specific databases

CTDi1389.
GeneCardsiGC12P012764.
HGNCiHGNC:2350. CREBL2.
HPAiHPA043738.
MIMi603476. gene.
neXtProtiNX_O60519.
PharmGKBiPA26868.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG85470.
GeneTreeiENSGT00390000005388.
HOGENOMiHOG000111966.
HOVERGENiHBG107761.
InParanoidiO60519.
OMAiEANNNSW.
OrthoDBiEOG7TQV3F.
PhylomeDBiO60519.
TreeFamiTF323305.

Miscellaneous databases

ChiTaRSiCREBL2. human.
GenomeRNAii1389.
NextBioi5645.
PROiO60519.
SOURCEiSearch...

Gene expression databases

BgeeiO60519.
CleanExiHS_CREBL2.
GenevestigatoriO60519.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "CREBL2, a novel transcript from the chromosome 12 region flanked by ETV6 and CDKN1B."
    Hoornaert I., Marynen P., Baens M.
    Genomics 51:154-157(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Bone marrow.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Skin.
  7. "AMP-activated protein kinase phosphorylates transcription factors of the CREB family."
    Thomson D.M., Herway S.T., Fillmore N., Kim H., Brown J.D., Barrow J.R., Winder W.W.
    J. Appl. Physiol. 104:429-438(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY AMPK.

Entry informationi

Entry nameiCRBL2_HUMAN
AccessioniPrimary (citable) accession number: O60519
Secondary accession number(s): B5BUM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 4, 2008
Last sequence update: July 31, 1998
Last modified: January 6, 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.