CRBL2_HUMAN
ID CRBL2_HUMAN Reviewed; 120 AA.
AC O60519; B5BUM5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=cAMP-responsive element-binding protein-like 2;
GN Name=CREBL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=9693048; DOI=10.1006/geno.1998.5366;
RA Hoornaert I., Marynen P., Baens M.;
RT "CREBL2, a novel transcript from the chromosome 12 region flanked by ETV6
RT and CDKN1B.";
RL Genomics 51:154-157(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=18063805; DOI=10.1152/japplphysiol.00900.2007;
RA Thomson D.M., Herway S.T., Fillmore N., Kim H., Brown J.D., Barrow J.R.,
RA Winder W.W.;
RT "AMP-activated protein kinase phosphorylates transcription factors of the
RT CREB family.";
RL J. Appl. Physiol. 104:429-438(2008).
CC -!- FUNCTION: Probable regulator of CREB1 transcriptional activity which is
CC involved in adipose cells differentiation. May also play a regulatory
CC role in the cell cycle. Identification in a chromosomal region
CC frequently deleted in various cancers suggests that it might act as a
CC tumor suppressor. {ECO:0000269|PubMed:9693048}.
CC -!- SUBUNIT: Interacts with CREB1; regulates CREB1 phosphorylation,
CC stability and transcriptional activity. {ECO:0000250}.
CC -!- INTERACTION:
CC O60519; Q8IUR6: CREBRF; NbExp=5; IntAct=EBI-2872455, EBI-1042699;
CC O60519; P35638: DDIT3; NbExp=3; IntAct=EBI-2872455, EBI-742651;
CC O60519; Q16236: NFE2L2; NbExp=5; IntAct=EBI-2872455, EBI-2007911;
CC O60519; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-2872455, EBI-2692890;
CC O60519; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2872455, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by AMPK. {ECO:0000269|PubMed:18063805}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; AF039081; AAC32314.1; -; mRNA.
DR EMBL; AB451461; BAG70275.1; -; mRNA.
DR EMBL; CR542250; CAG47046.1; -; mRNA.
DR EMBL; CH471094; EAW96269.1; -; Genomic_DNA.
DR EMBL; BC104873; AAI04874.1; -; mRNA.
DR EMBL; BC106052; AAI06053.1; -; mRNA.
DR EMBL; BC112157; AAI12158.1; -; mRNA.
DR CCDS; CCDS8651.1; -.
DR RefSeq; NP_001301.1; NM_001310.3.
DR AlphaFoldDB; O60519; -.
DR SMR; O60519; -.
DR BioGRID; 107779; 9.
DR IntAct; O60519; 7.
DR STRING; 9606.ENSP00000228865; -.
DR BioMuta; CREBL2; -.
DR MassIVE; O60519; -.
DR PaxDb; O60519; -.
DR PeptideAtlas; O60519; -.
DR PRIDE; O60519; -.
DR ProteomicsDB; 49456; -.
DR Antibodypedia; 23508; 69 antibodies from 18 providers.
DR DNASU; 1389; -.
DR Ensembl; ENST00000228865.3; ENSP00000228865.2; ENSG00000111269.3.
DR GeneID; 1389; -.
DR KEGG; hsa:1389; -.
DR MANE-Select; ENST00000228865.3; ENSP00000228865.2; NM_001310.4; NP_001301.1.
DR UCSC; uc001rap.3; human.
DR CTD; 1389; -.
DR DisGeNET; 1389; -.
DR GeneCards; CREBL2; -.
DR HGNC; HGNC:2350; CREBL2.
DR HPA; ENSG00000111269; Tissue enhanced (adrenal).
DR MIM; 603476; gene.
DR neXtProt; NX_O60519; -.
DR OpenTargets; ENSG00000111269; -.
DR PharmGKB; PA26868; -.
DR VEuPathDB; HostDB:ENSG00000111269; -.
DR eggNOG; KOG4515; Eukaryota.
DR GeneTree; ENSGT00390000005388; -.
DR HOGENOM; CLU_134161_0_0_1; -.
DR InParanoid; O60519; -.
DR OMA; DQGRMPE; -.
DR OrthoDB; 1551209at2759; -.
DR PhylomeDB; O60519; -.
DR TreeFam; TF323305; -.
DR PathwayCommons; O60519; -.
DR SignaLink; O60519; -.
DR SIGNOR; O60519; -.
DR BioGRID-ORCS; 1389; 12 hits in 1102 CRISPR screens.
DR ChiTaRS; CREBL2; human.
DR GenomeRNAi; 1389; -.
DR Pharos; O60519; Tdark.
DR PRO; PR:O60519; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O60519; protein.
DR Bgee; ENSG00000111269; Expressed in germinal epithelium of ovary and 212 other tissues.
DR Genevisible; O60519; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR039250; CREBL2/REPTOR-BP.
DR PANTHER; PTHR21051; PTHR21051; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Differentiation; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..120
FT /note="cAMP-responsive element-binding protein-like 2"
FT /id="PRO_0000318192"
FT DOMAIN 23..86
FT /note="bZIP"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..60
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT REGION 62..69
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT REGION 93..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 13784 MW; E191B2D239EDA17B CRC64;
MDDSKVVGGK VKKPGKRGRK PAKIDLKAKL ERSRQSAREC RARKKLRYQY LEELVSSRER
AICALREELE MYKQWCMAMD QGKIPSEIKA LLTGEEQNKS QQNSSRHTKA GKTDANSNSW
