Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cyclic AMP-responsive element-binding protein 3-like protein 1 (cAMP-responsive element-binding protein 3-like protein 1) (Old astrocyte specifically-induced substance) (OASIS) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 1]

 CR3L1_HUMAN             Reviewed;         519 AA.
Q96BA8; Q8N2D5; Q96CP0;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 142.
RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 1;
Short=cAMP-responsive element-binding protein 3-like protein 1;
AltName: Full=Old astrocyte specifically-induced substance;
Short=OASIS;
Contains:
RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 1;
Name=CREB3L1; Synonyms=OASIS; ORFNames=PSEC0238;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, ALTERNATIVE
SPLICING (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12054625; DOI=10.1016/S0006-291X(02)00253-X;
Omori Y., Imai J., Suzuki Y., Watanabe S., Tanigami A., Sugano S.;
"OASIS is a transcriptional activator of CREB/ATF family with a
transmembrane domain.";
Biochem. Biophys. Res. Commun. 293:470-477(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-519.
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-392; ARG-423 AND LEU-426, AND
PROTEOLYTIC PROCESSING.
PubMed=16417584; DOI=10.1111/j.1471-4159.2005.03596.x;
Murakami T., Kondo S., Ogata M., Kanemoto S., Saito A., Wanaka A.,
Imaizumi K.;
"Cleavage of the membrane-bound transcription factor OASIS in response
to endoplasmic reticulum stress.";
J. Neurochem. 96:1090-1100(2006).
[5]
FUNCTION IN VIRAL INFECTIONS, IDENTIFICATION OF TARGET GENES,
SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
PRO-392; PRO-395 AND ARG-423.
PubMed=21767813; DOI=10.1016/j.chom.2011.06.006;
Denard B., Seemann J., Chen Q., Gay A., Huang H., Chen Y., Ye J.;
"The membrane-bound transcription factor CREB3L1 is activated in
response to virus infection to inhibit proliferation of virus-infected
cells.";
Cell Host Microbe 10:65-74(2011).
[6]
UBIQUITINATION.
PubMed=22705851; DOI=10.1038/cdd.2012.77;
Kondo S., Hino S.I., Saito A., Kanemoto S., Kawasaki N., Asada R.,
Izumi S., Iwamoto H., Oki M., Miyagi H., Kaneko M., Nomura Y.,
Urano F., Imaizumi K.;
"Activation of OASIS family, ER stress transducers, is dependent on
its stabilization.";
Cell Death Differ. 19:1939-1949(2012).
[7]
FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
INTERACTION WITH SMAD4.
PubMed=25310401; DOI=10.1371/journal.pone.0108528;
Chen Q., Lee C.E., Denard B., Ye J.;
"Sustained induction of collagen synthesis by TGF-beta requires
regulated intramembrane proteolysis of CREB3L1.";
PLoS ONE 9:E108528-E108528(2014).
[8]
PROTEOLYTIC PROCESSING.
PubMed=27499293; DOI=10.1016/j.molcel.2016.06.032;
Chen Q., Denard B., Lee C.E., Han S., Ye J.S., Ye J.;
"Inverting the topology of a transmembrane protein by regulating the
translocation of the first transmembrane helix.";
Mol. Cell 63:567-578(2016).
[9]
POSSIBLE INVOLVEMENT IN OI16, AND SUBCELLULAR LOCATION.
PubMed=24079343; DOI=10.1186/1750-1172-8-154;
Symoens S., Malfait F., D'hondt S., Callewaert B., Dheedene A.,
Steyaert W., Baechinger H.P., De Paepe A., Kayserili H., Coucke P.J.;
"Deficiency for the ER-stress transducer OASIS causes severe recessive
osteogenesis imperfecta in humans.";
Orphanet J. Rare Dis. 8:154-154(2013).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-184, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcription factor involved in unfolded protein
response (UPR). Binds the DNA consensus sequence 5'-GTGXGCXGC-3'
(PubMed:21767813). In the absence of endoplasmic reticulum (ER)
stress, inserted into ER membranes, with N-terminal DNA-binding
and transcription activation domains oriented toward the cytosolic
face of the membrane. In response to ER stress, transported to the
Golgi, where it is cleaved in a site-specific manner by resident
proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal
cytosolic domain is translocated to the nucleus to effect
transcription of specific target genes. Plays a critical role in
bone formation through the transcription of COL1A1, and possibly
COL1A2, and the secretion of bone matrix proteins. Directly binds
to the UPR element (UPRE)-like sequence in an osteoblast-specific
COL1A1 promoter region and induces its transcription. Does not
regulate COL1A1 in other tissues, such as skin (By similarity).
Required to protect astrocytes from ER stress-induced cell death.
In astrocytes, binds to the cAMP response element (CRE) of the
BiP/HSPA5 promoter and participate in its transcriptional
activation (By similarity). Required for TGFB1 to activate genes
involved in the assembly of collagen extracellular matrix
(PubMed:25310401). {ECO:0000250|UniProtKB:Q9Z125,
ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:21767813,
ECO:0000269|PubMed:25310401}.
-!- FUNCTION: (Microbial infection) May play a role in limiting virus
spread by inhibiting proliferation of virus-infected cells. Upon
infection with diverse DNA and RNA viruses, inhibits cell-cycle
progression by binding to promoters and activating transcription
of genes encoding cell-cycle inhibitors, such as p21/CDKN1A
(PubMed:21767813). {ECO:0000269|PubMed:21767813}.
-!- SUBUNIT: Interacts with SMAD4, the interaction takes place upon
TGFB1 induction and SMAD4 acts as CREB3L1 coactivator to induce
the expression of genes involved in assembly of collagen
extracellular matrix. {ECO:0000269|PubMed:25310401}.
-!- INTERACTION:
P01031:C5; NbExp=3; IntAct=EBI-6942903, EBI-8558308;
Q9BXR6:CFHR5; NbExp=5; IntAct=EBI-6942903, EBI-11579371;
Q15125:EBP; NbExp=4; IntAct=EBI-6942903, EBI-3915253;
Q92520:FAM3C; NbExp=3; IntAct=EBI-6942903, EBI-2876774;
Q9UGM5:FETUB; NbExp=4; IntAct=EBI-6942903, EBI-13049494;
Q9H0Q3:FXYD6; NbExp=5; IntAct=EBI-6942903, EBI-713304;
O00155:GPR25; NbExp=5; IntAct=EBI-6942903, EBI-10178951;
Q8N5M9:JAGN1; NbExp=3; IntAct=EBI-6942903, EBI-10266796;
Q6N075:MFSD5; NbExp=3; IntAct=EBI-6942903, EBI-3920969;
Q99735:MGST2; NbExp=4; IntAct=EBI-6942903, EBI-11324706;
Q8IXM6:NRM; NbExp=3; IntAct=EBI-6942903, EBI-10262547;
Q6IB11:PGRMC1; NbExp=3; IntAct=EBI-6942903, EBI-10249941;
P26678:PLN; NbExp=3; IntAct=EBI-6942903, EBI-692836;
P60201-2:PLP1; NbExp=5; IntAct=EBI-6942903, EBI-12188331;
O43741:PRKAB2; NbExp=3; IntAct=EBI-6942903, EBI-1053424;
Q06455-4:RUNX1T1; NbExp=3; IntAct=EBI-6942903, EBI-10224192;
Q8IWU4:SLC30A8; NbExp=6; IntAct=EBI-6942903, EBI-10262251;
Q969S0:SLC35B4; NbExp=5; IntAct=EBI-6942903, EBI-10281213;
Q9NP94:SLC39A2; NbExp=4; IntAct=EBI-6942903, EBI-12898013;
P02786:TFRC; NbExp=4; IntAct=EBI-6942903, EBI-355727;
P17152:TMEM11; NbExp=3; IntAct=EBI-6942903, EBI-723946;
Q9BVK8:TMEM147; NbExp=5; IntAct=EBI-6942903, EBI-348587;
A2RU14:TMEM218; NbExp=5; IntAct=EBI-6942903, EBI-10173151;
Q8WY98:TMEM234; NbExp=3; IntAct=EBI-6942903, EBI-8642211;
P30536:TSPO; NbExp=5; IntAct=EBI-6942903, EBI-6623146;
O95159:ZFPL1; NbExp=4; IntAct=EBI-6942903, EBI-718439;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:16417584,
ECO:0000269|PubMed:25310401}; Single-pass type II membrane
protein. Note=ER membrane resident protein. Upon ER stress,
translocated to the Golgi apparatus where it is cleaved. The
cytosolic N-terminal fragment (processed cyclic AMP-responsive
element-binding protein 3-like protein 1) is transported into the
nucleus. {ECO:0000269|PubMed:12054625,
ECO:0000269|PubMed:16417584, ECO:0000269|PubMed:21767813,
ECO:0000269|PubMed:25310401}.
-!- SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-
binding protein 3-like protein 1: Nucleus
{ECO:0000269|PubMed:24079343, ECO:0000269|PubMed:25310401}.
Note=Upon ER stress, transported into the nucleus.
{ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:21767813,
ECO:0000269|PubMed:24079343, ECO:0000269|PubMed:25310401}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96BA8-1; Sequence=Displayed;
Name=2; Synonyms=OASISv1;
IsoId=Q96BA8-2; Sequence=VSP_025632;
-!- TISSUE SPECIFICITY: Expressed in several tissues, with highest
levels in pancreas and prostate. Expressed at relatively lower
levels in brain. {ECO:0000269|PubMed:12054625}.
-!- PTM: Upon ER stress, translocated to the Golgi apparatus, where it
is processed by regulated intramembrane proteolysis (RIP) to
release the cytosol-facing N-terminal transcription factor domain.
The cleavage is performed sequentially by site-1 and site-2
proteases (S1P/MBTPS1 and S2P/MBTPS2). RIP is induced by TGFB1 and
ceramide (PubMed:25310401, PubMed:27499293).
{ECO:0000269|PubMed:16417584, ECO:0000269|PubMed:21767813,
ECO:0000269|PubMed:25310401, ECO:0000269|PubMed:27499293}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9Z125}.
-!- PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked
ubiquitination, followed by rapid proteasomal degradation under
normal conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein
ligase dissociates from its substrate, ubiquitination does not
occur and CREB3L1 is stabilized. {ECO:0000269|PubMed:22705851}.
-!- DISEASE: Osteogenesis imperfecta 16 (OI16) [MIM:616229]: An
autosomal recessive form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae. OI16 is a severe form.
{ECO:0000269|PubMed:24079343}. Note=The disease may be caused by
mutations affecting the gene represented in this entry. OI16
affected patients show a genomic deletion encompassing CREB3L1 and
the first exon of DGKZ. The absence of this exon does not affect
all DGKZ isoforms, some are still produced at normal level. It
cannot be ruled out that DGKZ could contribute to the phenotype,
but in view of its role in bone formation, CREB3L1 is a strong
OI16-causing candidate (PubMed:24079343). This hypothesis is
corroborated by the observation of CREB3L1 knockout mice which
exhibit features reminiscent of severe human osteogenesis
imperfecta. {ECO:0000269|PubMed:24079343}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC11681.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB063321; BAC01278.1; -; mRNA.
EMBL; BC014097; AAH14097.1; -; mRNA.
EMBL; BC015781; AAH15781.1; -; mRNA.
EMBL; AK075538; BAC11681.1; ALT_INIT; mRNA.
CCDS; CCDS53620.1; -. [Q96BA8-1]
RefSeq; NP_443086.1; NM_052854.3. [Q96BA8-1]
UniGene; Hs.405961; -.
ProteinModelPortal; Q96BA8; -.
SMR; Q96BA8; -.
BioGrid; 124786; 31.
IntAct; Q96BA8; 150.
MINT; MINT-268046; -.
STRING; 9606.ENSP00000434939; -.
iPTMnet; Q96BA8; -.
PhosphoSitePlus; Q96BA8; -.
DMDM; 74751763; -.
MaxQB; Q96BA8; -.
PaxDb; Q96BA8; -.
PeptideAtlas; Q96BA8; -.
PRIDE; Q96BA8; -.
DNASU; 90993; -.
Ensembl; ENST00000621158; ENSP00000481956; ENSG00000157613. [Q96BA8-1]
GeneID; 90993; -.
KEGG; hsa:90993; -.
UCSC; uc021qik.3; human. [Q96BA8-1]
CTD; 90993; -.
DisGeNET; 90993; -.
EuPathDB; HostDB:ENSG00000157613.10; -.
GeneCards; CREB3L1; -.
HGNC; HGNC:18856; CREB3L1.
HPA; CAB026151; -.
HPA; HPA024069; -.
MalaCards; CREB3L1; -.
MIM; 616215; gene.
MIM; 616229; phenotype.
neXtProt; NX_Q96BA8; -.
OpenTargets; ENSG00000157613; -.
Orphanet; 79105; Myxofibrosarcoma.
Orphanet; 216812; Osteogenesis imperfecta type 3.
PharmGKB; PA134960108; -.
eggNOG; KOG0709; Eukaryota.
eggNOG; ENOG410ZZQM; LUCA.
GeneTree; ENSGT00520000055538; -.
HOGENOM; HOG000060150; -.
HOVERGEN; HBG057480; -.
InParanoid; Q96BA8; -.
KO; K09048; -.
OMA; EPPDGWE; -.
OrthoDB; EOG091G081Z; -.
PhylomeDB; Q96BA8; -.
TreeFam; TF316079; -.
Reactome; R-HSA-8874211; CREB3 factors activate genes.
SIGNOR; Q96BA8; -.
ChiTaRS; CREB3L1; human.
GenomeRNAi; 90993; -.
PRO; PR:Q96BA8; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000157613; -.
CleanEx; HS_CREB3L1; -.
ExpressionAtlas; Q96BA8; baseline and differential.
Genevisible; Q96BA8; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:ParkinsonsUK-UCL.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:ParkinsonsUK-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:ParkinsonsUK-UCL.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
GO; GO:0070278; P:extracellular matrix constituent secretion; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISS:ParkinsonsUK-UCL.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR004827; bZIP.
InterPro; IPR001630; Leuzip_CREB.
InterPro; IPR029805; OASIS.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR22952:SF24; PTHR22952:SF24; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00041; LEUZIPPRCREB.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Developmental protein; DNA-binding; Endoplasmic reticulum;
Glycoprotein; Isopeptide bond; Membrane; Nucleus;
Osteogenesis imperfecta; Polymorphism; Reference proteome;
Signal-anchor; Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Ubl conjugation; Unfolded protein response.
CHAIN 1 519 Cyclic AMP-responsive element-binding
protein 3-like protein 1.
/FTId=PRO_0000288064.
CHAIN 1 ? Processed cyclic AMP-responsive element-
binding protein 3-like protein 1.
/FTId=PRO_0000296206.
TOPO_DOM 1 374 Cytoplasmic. {ECO:0000255}.
TRANSMEM 375 395 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 396 519 Lumenal. {ECO:0000255}.
DOMAIN 290 353 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 60 Required for transcriptional activation.
REGION 292 321 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 332 353 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 392 395 S2P recognition.
{ECO:0000303|PubMed:21767813}.
MOTIF 423 426 S1P recognition.
{ECO:0000303|PubMed:21767813}.
COMPBIAS 146 154 Poly-Ala.
SITE 426 427 Cleavage; by S1P. {ECO:0000250}.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 184 184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 111 198 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_025632.
VARIANT 411 411 A -> T (in dbSNP:rs35652107).
/FTId=VAR_032392.
MUTAGEN 392 392 P->A: Abolishes proteolytic cleavage by
S2P; when associated with A-395.
{ECO:0000269|PubMed:21767813}.
MUTAGEN 392 392 P->L: Abolishes proteolytic cleavage by
S2P. {ECO:0000269|PubMed:16417584}.
MUTAGEN 395 395 P->A: Abolishes proteolytic cleavage by
S2P; when associated with A-392.
{ECO:0000269|PubMed:21767813}.
MUTAGEN 423 423 R->A: Abolishes proteolytic cleavage by
S1P. {ECO:0000269|PubMed:16417584,
ECO:0000269|PubMed:21767813}.
MUTAGEN 426 426 L->V: Abolishes proteolytic cleavage by
S1P. {ECO:0000269|PubMed:16417584}.
CONFLICT 249 249 A -> P (in Ref. 2; AAH14097).
{ECO:0000305}.
SEQUENCE 519 AA; 57005 MW; D08133CD8B02A3AC CRC64;
MDAVLEPFPA DRLFPGSSFL DLGDLNESDF LNNAHFPEHL DHFTENMEDF SNDLFSSFFD
DPVLDEKSPL LDMELDSPTP GIQAEHSYSL SGDSAPQSPL VPIKMEDTTQ DAEHGAWALG
HKLCSIMVKQ EQSPELPVDP LAAPSAMAAA AAMATTPLLG LSPLSRLPIP HQAPGEMTQL
PVIKAEPLEV NQFLKVTPED LVQMPPTPPS SHGSDSDGSQ SPRSLPPSSP VRPMARSSTA
ISTSPLLTAP HKLQGTSGPL LLTEEEKRTL IAEGYPIPTK LPLTKAEEKA LKRVRRKIKN
KISAQESRRK KKEYVECLEK KVETFTSENN ELWKKVETLE NANRTLLQQL QKLQTLVTNK
ISRPYKMAAT QTGTCLMVAA LCFVLVLGSL VPCLPEFSSG SQTVKEDPLA ADGVYTASQM
PSRSLLFYDD GAGLWEDGRS TLLPMEPPDG WEINPGGPAE QRPRDHLQHD HLDSTHETTK
YLSEAWPKDG GNGTSPDFSH SKEWFHDRDL GPNTTIKLS


Related products :

Catalog number Product name Quantity
EIAAB09237 cAMP-responsive element-binding protein 3-like protein 1,Creb3l1,Cyclic AMP-responsive element-binding protein 3-like protein 1,OASIS,Oasis,Old astrocyte specifically-induced substance,Rat,Rattus norv
EIAAB09238 cAMP-responsive element-binding protein 3-like protein 1,CREB3L1,Cyclic AMP-responsive element-binding protein 3-like protein 1,Homo sapiens,Human,OASIS,OASIS,Old astrocyte specifically-induced substa
EIAAB09236 cAMP-responsive element-binding protein 3-like protein 1,Creb3l1,Cyclic AMP-responsive element-binding protein 3-like protein 1,Mouse,Mus musculus,OASIS,Oasis,Old astrocyte specifically-induced substa
EIAAB09247 AIbZIP,Aibzip,Androgen-induced basic leucine zipper protein,cAMP-responsive element-binding protein 3-like protein 4,Creb3l4,Cyclic AMP-responsive element-binding protein 3-like protein 4,Rat,Rattus n
U1318b CLIA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA kit Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
EIAAB09243 cAMP-responsive element-binding protein 3-like protein 3,CREB3L3,CREBH,Cyclic AMP-responsive element-binding protein 3-like protein 3,Homo sapiens,Human,HYST1481,Transcription factor CREB-H
EIAAB09244 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Crebh,Cyclic AMP-responsive element-binding protein 3-like protein 3,Mouse,Mus musculus,Transcription factor CREB-H
EIAAB09242 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Cyclic AMP-responsive element-binding protein 3-like protein 3,Rat,Rattus norvegicus,Transcription factor CREB-H
EIAAB09240 Bbf2h7,cAMP-responsive element-binding protein 3-like protein 2,Creb3l2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Mouse,Mus musculus
E1318h ELISA kit cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
U1318h CLIA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
E1318h ELISA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
EIAAB09321 cAMP-responsive element-binding protein 5,CREB5,CREB-5,CREBPA,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Homo sapiens,Human
EIAAB09318 Bos taurus,Bovine,cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Luman
EIAAB09239 BBF2 human homolog on chromosome 7,BBF2H7,cAMP-responsive element-binding protein 3-like protein 2,CREB3L2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Homo sapiens,Human
EIAAB09245 Bos taurus,Bovine,cAMP-responsive element-binding protein 3-like protein 3,CREB3L3,Cyclic AMP-responsive element-binding protein 3-like protein 3
EIAAB09322 cAMP-responsive element-binding protein 5,Creb5,CREB-5,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Mouse,Mus musculus
EIAAB09246 Acre1,ATCE1,Atce1,Attaching to CRE-like 1,cAMP-responsive element-binding protein 3-like protein 4,Creb3l4,Cyclic AMP-responsive element-binding protein 3-like protein 4,Jal,mJAL,Mouse,Mus musculus,Ti
EIAAB09241 cAMP-responsive element-binding protein 3-like protein 2,Creb3l2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Ra69,Rat,Rattus norvegicus,SCI-related protein Ra69
EIAAB09320 cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Homo sapiens,Human,Luman,LZIP,Transcription factor LZIP-alpha
EIAAB09319 cAMP-responsive element-binding protein 3,Creb3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Lzip,Mouse,Mus musculus,Transcription factor LZIP
E1318r ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
E1318m ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur