CR3L2_HUMAN
ID CR3L2_HUMAN Reviewed; 520 AA.
AC Q70SY1; Q6P454; Q6ZMR6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 2;
DE Short=cAMP-responsive element-binding protein 3-like protein 2;
DE AltName: Full=BBF2 human homolog on chromosome 7;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 2;
GN Name=CREB3L2; Synonyms=BBF2H7;
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] (ISOFORM 1), VARIANTS THR-100 DEL AND ILE-130,
RP TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH FUS.
RC TISSUE=Lung, and Placenta;
RX PubMed=12915480; DOI=10.1093/hmg/ddg237;
RA Storlazzi C.T., Mertens F., Nascimento A., Isaksson M., Wejde J.,
RA Brosjoe O., Mandahl N., Panagopoulos I.;
RT "Fusion of the FUS and BBF2H7 genes in low grade fibromyxoid sarcoma.";
RL Hum. Mol. Genet. 12:2349-2358(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS THR-100 DEL AND
RP ILE-130.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP THR-100 DEL AND ILE-130.
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 [5]
RP CHROMOSOMAL TRANSLOCATION WITH FUS.
RX PubMed=15139001; DOI=10.1002/gcc.20037;
RA Panagopoulos I., Storlazzi C.T., Fletcher C.D., Fletcher J.A.,
RA Nascimento A., Domanski H.A., Wejde J., Brosjo O., Rydholm A., Isaksson M.,
RA Mandahl N., Mertens F.;
RT "The chimeric FUS/CREB3l2 gene is specific for low-grade fibromyxoid
RT sarcoma.";
RL Genes Chromosomes Cancer 40:218-228(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION, GLYCOSYLATION, AND INDUCTION BY ER STRESS.
RX PubMed=17178827; DOI=10.1128/mcb.01552-06;
RA Kondo S., Saito A., Hino S., Murakami T., Ogata M., Kanemoto S., Nara S.,
RA Yamashita A., Yoshinaga K., Hara H., Imaizumi K.;
RT "BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of
RT endoplasmic reticulum stress transducer.";
RL Mol. Cell. Biol. 27:1716-1729(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP UBIQUITINATION.
RX PubMed=22705851; DOI=10.1038/cdd.2012.77;
RA Kondo S., Hino S.I., Saito A., Kanemoto S., Kawasaki N., Asada R.,
RA Izumi S., Iwamoto H., Oki M., Miyagi H., Kaneko M., Nomura Y., Urano F.,
RA Imaizumi K.;
RT "Activation of OASIS family, ER stress transducers, is dependent on its
RT stabilization.";
RL Cell Death Differ. 19:1939-1949(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-191, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription factor involved in unfolded protein response
CC (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted
CC into ER membranes, with N-terminal DNA-binding and transcription
CC activation domains oriented toward the cytosolic face of the membrane.
CC In response to ER stress, transported to the Golgi, where it is cleaved
CC in a site-specific manner by resident proteases S1P/MBTPS1 and
CC S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to
CC the nucleus to effect transcription of specific target genes. Plays a
CC critical role in chondrogenesis by activating the transcription of
CC SEC23A, which promotes the transport and secretion of cartilage matrix
CC proteins, and possibly that of ER biogenesis-related genes (By
CC similarity). In a neuroblastoma cell line, protects cells from ER
CC stress-induced death (PubMed:17178827). In vitro activates
CC transcription of target genes via direct binding to the CRE site
CC (PubMed:17178827). {ECO:0000250|UniProtKB:Q8BH52,
CC ECO:0000269|PubMed:17178827}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8BH52}; Single-pass type II membrane protein.
CC Note=ER membrane resident protein. Upon ER stress, translocated to the
CC Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment
CC (processed cyclic AMP-responsive element-binding protein 3-like protein
CC 1) is transported into the nucleus. {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 2]: Nucleus. Note=Upon ER stress, translocated
CC into the nucleus. {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q70SY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70SY1-2; Sequence=VSP_025636;
CC Name=3;
CC IsoId=Q70SY1-3; Sequence=VSP_025634, VSP_025635;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in placenta,
CC lung, spleen and intestine, and lowest levels in heart, brain, skeletal
CC muscle, thymus, colon and leukocytes. In fetal tissues, the weakest
CC expression is detected in brain and heart.
CC {ECO:0000269|PubMed:12915480}.
CC -!- INDUCTION: Up-regulated by ER stress at the transcript and protein
CC levels, the increase at the protein level is much higher than at the
CC transcript level. This induction is accompanied by increased
CC proteolytic cleavage that releases the N-terminal transcription factor
CC domain. {ECO:0000269|PubMed:17178827}.
CC -!- PTM: Upon ER stress, translocated to the Golgi apparatus, where it is
CC processed by regulated intramembrane proteolysis (RIP) to release the
CC cytosol-facing N-terminal transcription factor domain. The cleavage is
CC performed sequentially by site-1 and site-2 proteases (S1P/MBTPS1 and
CC S2P/MBTPS2). {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17178827}.
CC -!- PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked
CC ubiquitination, followed by rapid proteasomal degradation under normal
CC conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein ligase
CC dissociates from its substrate, ubiquitination does not occur and
CC CREB3L2 is stabilized. {ECO:0000269|PubMed:22705851}.
CC -!- DISEASE: Note=A chromosomal aberration involving CREB3L2 is found in
CC low grade fibromyxoid sarcoma (LGFMS). Translocation t(7;16)(q33;p11)
CC with FUS.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/153/creb3l2-(camp-responsive-element-binding-protein-3-like-2)";
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DR EMBL; AJ549092; CAD79342.1; -; mRNA.
DR EMBL; AJ549387; CAD79347.1; -; mRNA.
DR EMBL; AK131517; BAD18659.1; -; mRNA.
DR EMBL; CH236950; EAL24050.1; -; Genomic_DNA.
DR EMBL; BC063666; AAH63666.1; -; mRNA.
DR EMBL; BC110813; AAI10814.1; -; mRNA.
DR CCDS; CCDS34760.1; -. [Q70SY1-1]
DR CCDS; CCDS59083.1; -. [Q70SY1-3]
DR RefSeq; NP_001240704.1; NM_001253775.1. [Q70SY1-3]
DR RefSeq; NP_919047.2; NM_194071.3. [Q70SY1-1]
DR AlphaFoldDB; Q70SY1; -.
DR SMR; Q70SY1; -.
DR BioGRID; 122277; 34.
DR IntAct; Q70SY1; 14.
DR STRING; 9606.ENSP00000329140; -.
DR GlyGen; Q70SY1; 3 sites.
DR iPTMnet; Q70SY1; -.
DR PhosphoSitePlus; Q70SY1; -.
DR BioMuta; CREB3L2; -.
DR DMDM; 296439387; -.
DR EPD; Q70SY1; -.
DR jPOST; Q70SY1; -.
DR MassIVE; Q70SY1; -.
DR MaxQB; Q70SY1; -.
DR PaxDb; Q70SY1; -.
DR PeptideAtlas; Q70SY1; -.
DR PRIDE; Q70SY1; -.
DR ProteomicsDB; 68563; -. [Q70SY1-1]
DR ProteomicsDB; 68564; -. [Q70SY1-2]
DR ProteomicsDB; 68565; -. [Q70SY1-3]
DR Antibodypedia; 18186; 255 antibodies from 32 providers.
DR DNASU; 64764; -.
DR Ensembl; ENST00000330387.11; ENSP00000329140.6; ENSG00000182158.16. [Q70SY1-1]
DR Ensembl; ENST00000452463.5; ENSP00000410314.1; ENSG00000182158.16. [Q70SY1-3]
DR Ensembl; ENST00000456390.5; ENSP00000403550.1; ENSG00000182158.16. [Q70SY1-2]
DR GeneID; 64764; -.
DR KEGG; hsa:64764; -.
DR MANE-Select; ENST00000330387.11; ENSP00000329140.6; NM_194071.4; NP_919047.2.
DR UCSC; uc003vtw.4; human. [Q70SY1-1]
DR CTD; 64764; -.
DR DisGeNET; 64764; -.
DR GeneCards; CREB3L2; -.
DR HGNC; HGNC:23720; CREB3L2.
DR HPA; ENSG00000182158; Low tissue specificity.
DR MalaCards; CREB3L2; -.
DR MIM; 608834; gene.
DR neXtProt; NX_Q70SY1; -.
DR OpenTargets; ENSG00000182158; -.
DR Orphanet; 79105; Myxofibrosarcoma.
DR PharmGKB; PA134914841; -.
DR VEuPathDB; HostDB:ENSG00000182158; -.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000157659; -.
DR HOGENOM; CLU_037638_0_0_1; -.
DR InParanoid; Q70SY1; -.
DR OMA; TDALMKP; -.
DR PhylomeDB; Q70SY1; -.
DR TreeFam; TF316079; -.
DR PathwayCommons; Q70SY1; -.
DR Reactome; R-HSA-8874211; CREB3 factors activate genes.
DR SignaLink; Q70SY1; -.
DR SIGNOR; Q70SY1; -.
DR BioGRID-ORCS; 64764; 13 hits in 1099 CRISPR screens.
DR ChiTaRS; CREB3L2; human.
DR GenomeRNAi; 64764; -.
DR Pharos; Q70SY1; Tbio.
DR PRO; PR:Q70SY1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q70SY1; protein.
DR Bgee; ENSG00000182158; Expressed in saphenous vein and 198 other tissues.
DR ExpressionAtlas; Q70SY1; baseline and differential.
DR Genevisible; Q70SY1; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0035497; F:cAMP response element binding; IMP:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR InterPro; IPR029804; BBF2H7.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46004:SF2; PTHR46004:SF2; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromosomal rearrangement;
KW Developmental protein; DNA-binding; Endoplasmic reticulum; Glycoprotein;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Signal-anchor; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Unfolded protein response.
FT CHAIN 1..520
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 2"
FT /id="PRO_0000288067"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 2"
FT /id="PRO_0000296209"
FT TOPO_DOM 1..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..520
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 294..357
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 195..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..325
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 336..357
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 427..430
FT /note="S1P recognition"
FT /evidence="ECO:0000303|PubMed:17178827"
FT COMPBIAS 207..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 195..248
FT /note="APVDHLHLPPTPPSSHGSDSEGSLSPNPRLHPFSLPQTHSPSRAAPRAPSAL
FT SS -> GLSALPVSLWVMDMVSGSTEREYGERAGMSLYHRCCSWLYEIALFLKNKNFAS
FT K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025634"
FT VAR_SEQ 249..520
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025635"
FT VAR_SEQ 424..520
FT /note="VRSRNLLIYEEHSPPEESSSPGSAGELGGWDRGSSLLRVSGLESRPDVDLPH
FT FIISNETSLEKSVLLELQQHLVSAKLEGNETLKVVELDRRVNTTF -> GKTACGKLGR
FT VLFYFPRAGFLSLPKGIFCESPMFKKW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025636"
FT VARIANT 100
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:12915480, ECO:0000269|PubMed:15489334"
FT /id="VAR_062385"
FT VARIANT 130
FT /note="V -> I (in dbSNP:rs273957)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:12915480, ECO:0000269|PubMed:15489334"
FT /id="VAR_062386"
SQ SEQUENCE 520 AA; 57415 MW; 64699072EEB454D3 CRC64;
MEVLESGEQG VLQWDRKLSE LSEPGDGEAL MYHTHFSELL DEFSQNVLGQ LLNDPFLSEK
SVSMEVEPSP TSPAPLIQAE HSYSLCEEPR AQSPFTHITT SDSFNDDEVE SEKWYLSTDF
PSTSIKTEPV TDEPPPGLVP SVTLTITAIS TPLEKEEPPL EMNTGVDSSC QTIIPKIKLE
PHEVDQFLNF SPKEAPVDHL HLPPTPPSSH GSDSEGSLSP NPRLHPFSLP QTHSPSRAAP
RAPSALSSSP LLTAPHKLQG SGPLVLTEEE KRTLIAEGYP IPTKLPLSKS EEKALKKIRR
KIKNKISAQE SRRKKKEYMD SLEKKVESCS TENLELRKKV EVLENTNRTL LQQLQKLQTL
VMGKVSRTCK LAGTQTGTCL MVVVLCFAVA FGSFFQGYGP YPSATKMALP SQHSLQEPYT
ASVVRSRNLL IYEEHSPPEE SSSPGSAGEL GGWDRGSSLL RVSGLESRPD VDLPHFIISN
ETSLEKSVLL ELQQHLVSAK LEGNETLKVV ELDRRVNTTF
