ID CR3L1_HUMAN Reviewed; 519 AA.
AC Q96BA8; Q8N2D5; Q96CP0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 1;
DE Short=cAMP-responsive element-binding protein 3-like protein 1;
DE AltName: Full=Old astrocyte specifically-induced substance;
DE Short=OASIS {ECO:0000303|PubMed:16417584};
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 1;
GN Name=CREB3L1 {ECO:0000312|HGNC:HGNC:18856};
GN Synonyms=OASIS {ECO:0000303|PubMed:16417584}; ORFNames=PSEC0238;
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), DNA-BINDING, ALTERNATIVE SPLICING
RP (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12054625; DOI=10.1016/s0006-291x(02)00253-x;
RA Omori Y., Imai J., Suzuki Y., Watanabe S., Tanigami A., Sugano S.;
RT "OASIS is a transcriptional activator of CREB/ATF family with a
RT transmembrane domain.";
RL Biochem. Biophys. Res. Commun. 293:470-477(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-519.
RC TISSUE=Embryo;
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 [4]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-392; ARG-423 AND LEU-426, AND
RP PROTEOLYTIC PROCESSING.
RX PubMed=16417584; DOI=10.1111/j.1471-4159.2005.03596.x;
RA Murakami T., Kondo S., Ogata M., Kanemoto S., Saito A., Wanaka A.,
RA Imaizumi K.;
RT "Cleavage of the membrane-bound transcription factor OASIS in response to
RT endoplasmic reticulum stress.";
RL J. Neurochem. 96:1090-1100(2006).
RN [5]
RP FUNCTION IN VIRAL INFECTIONS, IDENTIFICATION OF TARGET GENES, SUBCELLULAR
RP LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF PRO-392; PRO-395 AND
RP ARG-423.
RX PubMed=21767813; DOI=10.1016/j.chom.2011.06.006;
RA Denard B., Seemann J., Chen Q., Gay A., Huang H., Chen Y., Ye J.;
RT "The membrane-bound transcription factor CREB3L1 is activated in response
RT to virus infection to inhibit proliferation of virus-infected cells.";
RL Cell Host Microbe 10:65-74(2011).
RN [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND INTERACTION
RP WITH SMAD4.
RX PubMed=25310401; DOI=10.1371/journal.pone.0108528;
RA Chen Q., Lee C.E., Denard B., Ye J.;
RT "Sustained induction of collagen synthesis by TGF-beta requires regulated
RT intramembrane proteolysis of CREB3L1.";
RL PLoS ONE 9:E108528-E108528(2014).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=27499293; DOI=10.1016/j.molcel.2016.06.032;
RA Chen Q., Denard B., Lee C.E., Han S., Ye J.S., Ye J.;
RT "Inverting the topology of a transmembrane protein by regulating the
RT translocation of the first transmembrane helix.";
RL Mol. Cell 63:567-578(2016).
RN [9]
RP POSSIBLE INVOLVEMENT IN OI16, AND SUBCELLULAR LOCATION.
RX PubMed=24079343; DOI=10.1186/1750-1172-8-154;
RA Symoens S., Malfait F., D'hondt S., Callewaert B., Dheedene A.,
RA Steyaert W., Baechinger H.P., De Paepe A., Kayserili H., Coucke P.J.;
RT "Deficiency for the ER-stress transducer OASIS causes severe recessive
RT osteogenesis imperfecta in humans.";
RL Orphanet J. Rare Dis. 8:154-154(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-184, 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: [Cyclic AMP-responsive element-binding protein 3-like protein
CC 1]: Precursor of the transcription factor form (Processed cyclic AMP-
CC responsive element-binding protein 3-like protein 1), which is embedded
CC in the endoplasmic reticulum membrane with N-terminal DNA-binding and
CC transcription activation domains oriented toward the cytosolic face of
CC the membrane (PubMed:12054625, PubMed:16417584, PubMed:25310401). In
CC response to ER stress or DNA damage, transported to the Golgi, where it
CC is cleaved in a site-specific manner by resident proteases S1P/MBTPS1
CC and S2P/MBTPS2. The released N-terminal cytosolic domain is
CC translocated to the nucleus where it activates transcription of
CC specific target genes involved in the cell-cycle progression inhibition
CC (PubMed:12054625, PubMed:21767813, PubMed:25310401).
CC {ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:16417584,
CC ECO:0000269|PubMed:21767813, ECO:0000269|PubMed:25310401}.
CC -!- FUNCTION: [Processed cyclic AMP-responsive element-binding protein 3-
CC like protein 1]: Transcription factor involved in cell type specific
CC DNA damage and unfolded protein response (UPR). Binds the DNA consensus
CC sequence 5'-GTGXGCXGC-3' (PubMed:21767813). Plays a critical role in
CC bone formation through the transcription of COL1A1, and possibly
CC COL1A2, and the secretion of bone matrix proteins. Directly binds to
CC the UPR element (UPRE)-like sequence in an osteoblast-specific COL1A1
CC promoter region and induces its transcription. Does not regulate COL1A1
CC in other tissues, such as skin (By similarity). Required to protect
CC astrocytes from ER stress-induced cell death. In astrocytes, binds to
CC the cAMP response element (CRE) of the BiP/HSPA5 promoter and
CC participate in its transcriptional activation (By similarity). In
CC astrocytes and osteoblasts, upon DNA damage, inhibits cell-cycle
CC progression after G2/M phase by binding to promoters and activating
CC transcription of genes encoding cell-cycle inhibitors, such as
CC p21/CDKN1A (By similarity). Required for TGFB1 to activate genes
CC involved in the assembly of collagen extracellular matrix
CC (PubMed:25310401). {ECO:0000250|UniProtKB:Q9Z125,
CC ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:21767813,
CC ECO:0000269|PubMed:25310401}.
CC -!- FUNCTION: (Microbial infection) May play a role in limiting virus
CC spread by inhibiting proliferation of virus-infected cells. Upon
CC infection with diverse DNA and RNA viruses, inhibits cell-cycle
CC progression by binding to promoters and activating transcription of
CC genes encoding cell-cycle inhibitors, such as p21/CDKN1A
CC (PubMed:21767813). {ECO:0000269|PubMed:21767813}.
CC -!- SUBUNIT: Interacts with SMAD4, the interaction takes place upon TGFB1
CC induction and SMAD4 acts as a CREB3L1 coactivator to induce the
CC expression of genes involved in assembly of collagen extracellular
CC matrix. {ECO:0000269|PubMed:25310401}.
CC -!- INTERACTION:
CC Q96BA8; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-6942903, EBI-10225815;
CC Q96BA8; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-6942903, EBI-11277970;
CC Q96BA8; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-6942903, EBI-10827839;
CC Q96BA8; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-6942903, EBI-2803601;
CC Q96BA8; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-6942903, EBI-1754287;
CC Q96BA8; Q9NUQ2: AGPAT5; NbExp=3; IntAct=EBI-6942903, EBI-6916385;
CC Q96BA8; Q9BVK2: ALG8; NbExp=3; IntAct=EBI-6942903, EBI-3921603;
CC Q96BA8; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-6942903, EBI-12109402;
CC Q96BA8; Q16853: AOC3; NbExp=3; IntAct=EBI-6942903, EBI-3921628;
CC Q96BA8; P05090: APOD; NbExp=3; IntAct=EBI-6942903, EBI-715495;
CC Q96BA8; Q96PS8: AQP10; NbExp=3; IntAct=EBI-6942903, EBI-12820279;
CC Q96BA8; P41181: AQP2; NbExp=3; IntAct=EBI-6942903, EBI-12701138;
CC Q96BA8; Q9H2C2: ARV1; NbExp=3; IntAct=EBI-6942903, EBI-11724186;
CC Q96BA8; P07306: ASGR1; NbExp=3; IntAct=EBI-6942903, EBI-1172335;
CC Q96BA8; O15155: BET1; NbExp=3; IntAct=EBI-6942903, EBI-749204;
CC Q96BA8; O95393: BMP10; NbExp=3; IntAct=EBI-6942903, EBI-3922513;
CC Q96BA8; Q12983: BNIP3; NbExp=3; IntAct=EBI-6942903, EBI-749464;
CC Q96BA8; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-6942903, EBI-12244618;
CC Q96BA8; Q96F05: C11orf24; NbExp=3; IntAct=EBI-6942903, EBI-2836238;
CC Q96BA8; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-6942903, EBI-12003442;
CC Q96BA8; P01031: C5; NbExp=3; IntAct=EBI-6942903, EBI-8558308;
CC Q96BA8; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-6942903, EBI-10271156;
CC Q96BA8; P19397: CD53; NbExp=5; IntAct=EBI-6942903, EBI-6657396;
CC Q96BA8; P21854: CD72; NbExp=5; IntAct=EBI-6942903, EBI-307924;
CC Q96BA8; A0A0S2Z5R8: CD99L2; NbExp=3; IntAct=EBI-6942903, EBI-16434925;
CC Q96BA8; Q9BXR6: CFHR5; NbExp=6; IntAct=EBI-6942903, EBI-11579371;
CC Q96BA8; P13569: CFTR; NbExp=3; IntAct=EBI-6942903, EBI-349854;
CC Q96BA8; Q9H5X1: CIAO2A; NbExp=5; IntAct=EBI-6942903, EBI-752069;
CC Q96BA8; Q9NWW5: CLN6; NbExp=5; IntAct=EBI-6942903, EBI-6165897;
CC Q96BA8; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-6942903, EBI-7247651;
CC Q96BA8; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-6942903, EBI-2807956;
CC Q96BA8; Q6PI25: CNIH2; NbExp=3; IntAct=EBI-6942903, EBI-12815321;
CC Q96BA8; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-6942903, EBI-10241815;
CC Q96BA8; P21964: COMT; NbExp=3; IntAct=EBI-6942903, EBI-372265;
CC Q96BA8; Q5RI15: COX20; NbExp=3; IntAct=EBI-6942903, EBI-2834035;
CC Q96BA8; Q68CJ9: CREB3L3; NbExp=2; IntAct=EBI-6942903, EBI-852194;
CC Q96BA8; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-6942903, EBI-10267100;
CC Q96BA8; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-6942903, EBI-12019274;
CC Q96BA8; O14569: CYB561D2; NbExp=3; IntAct=EBI-6942903, EBI-717654;
CC Q96BA8; P78329: CYP4F2; NbExp=3; IntAct=EBI-6942903, EBI-1752413;
CC Q96BA8; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-6942903, EBI-8645574;
CC Q96BA8; Q15125: EBP; NbExp=5; IntAct=EBI-6942903, EBI-3915253;
CC Q96BA8; P54852: EMP3; NbExp=3; IntAct=EBI-6942903, EBI-3907816;
CC Q96BA8; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-6942903, EBI-12279764;
CC Q96BA8; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-6942903, EBI-711490;
CC Q96BA8; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-6942903, EBI-10976398;
CC Q96BA8; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-6942903, EBI-11337888;
CC Q96BA8; Q92520: FAM3C; NbExp=4; IntAct=EBI-6942903, EBI-2876774;
CC Q96BA8; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-6942903, EBI-12142299;
CC Q96BA8; Q9UGM5: FETUB; NbExp=3; IntAct=EBI-6942903, EBI-13049494;
CC Q96BA8; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-6942903, EBI-12175685;
CC Q96BA8; Q9H0Q3: FXYD6; NbExp=6; IntAct=EBI-6942903, EBI-713304;
CC Q96BA8; P01350: GAST; NbExp=5; IntAct=EBI-6942903, EBI-3436637;
CC Q96BA8; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-6942903, EBI-11991950;
CC Q96BA8; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-6942903, EBI-6166686;
CC Q96BA8; Q9Y3E0: GOLT1B; NbExp=3; IntAct=EBI-6942903, EBI-4402607;
CC Q96BA8; O14653: GOSR2; NbExp=5; IntAct=EBI-6942903, EBI-4401517;
CC Q96BA8; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-6942903, EBI-11955647;
CC Q96BA8; O00155: GPR25; NbExp=7; IntAct=EBI-6942903, EBI-10178951;
CC Q96BA8; O60883: GPR37L1; NbExp=3; IntAct=EBI-6942903, EBI-2927498;
CC Q96BA8; Q6Y1H2: HACD2; NbExp=3; IntAct=EBI-6942903, EBI-530257;
CC Q96BA8; Q01638-2: IL1RL1; NbExp=3; IntAct=EBI-6942903, EBI-12838366;
CC Q96BA8; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-6942903, EBI-8503746;
CC Q96BA8; P11215: ITGAM; NbExp=3; IntAct=EBI-6942903, EBI-2568251;
CC Q96BA8; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-6942903, EBI-10266796;
CC Q96BA8; O00180: KCNK1; NbExp=5; IntAct=EBI-6942903, EBI-3914675;
CC Q96BA8; O95214: LEPROTL1; NbExp=3; IntAct=EBI-6942903, EBI-750776;
CC Q96BA8; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-6942903, EBI-2820517;
CC Q96BA8; Q9UBY5: LPAR3; NbExp=5; IntAct=EBI-6942903, EBI-12033434;
CC Q96BA8; Q16873: LTC4S; NbExp=5; IntAct=EBI-6942903, EBI-12241118;
CC Q96BA8; P21145: MAL; NbExp=3; IntAct=EBI-6942903, EBI-3932027;
CC Q96BA8; Q969L2: MAL2; NbExp=3; IntAct=EBI-6942903, EBI-944295;
CC Q96BA8; Q13021: MALL; NbExp=3; IntAct=EBI-6942903, EBI-750078;
CC Q96BA8; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-6942903, EBI-12243024;
CC Q96BA8; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-6942903, EBI-10317612;
CC Q96BA8; Q6N075: MFSD5; NbExp=6; IntAct=EBI-6942903, EBI-3920969;
CC Q96BA8; O43451: MGAM; NbExp=3; IntAct=EBI-6942903, EBI-2829774;
CC Q96BA8; Q99735: MGST2; NbExp=3; IntAct=EBI-6942903, EBI-11324706;
CC Q96BA8; O14880: MGST3; NbExp=3; IntAct=EBI-6942903, EBI-724754;
CC Q96BA8; Q8IY49-2: MMD2; NbExp=3; IntAct=EBI-6942903, EBI-13349813;
CC Q96BA8; P11836: MS4A1; NbExp=3; IntAct=EBI-6942903, EBI-2808234;
CC Q96BA8; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-6942903, EBI-12070086;
CC Q96BA8; Q9H115: NAPB; NbExp=3; IntAct=EBI-6942903, EBI-3921185;
CC Q96BA8; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-6942903, EBI-2863634;
CC Q96BA8; Q99519: NEU1; NbExp=5; IntAct=EBI-6942903, EBI-721517;
CC Q96BA8; Q92982: NINJ1; NbExp=3; IntAct=EBI-6942903, EBI-2802124;
CC Q96BA8; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-6942903, EBI-10317425;
CC Q96BA8; Q8IXM6: NRM; NbExp=3; IntAct=EBI-6942903, EBI-10262547;
CC Q96BA8; P42857: NSG1; NbExp=3; IntAct=EBI-6942903, EBI-6380741;
CC Q96BA8; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-6942903, EBI-2804156;
CC Q96BA8; Q8NH19: OR10AG1; NbExp=3; IntAct=EBI-6942903, EBI-13339917;
CC Q96BA8; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-6942903, EBI-1054848;
CC Q96BA8; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-6942903, EBI-11075081;
CC Q96BA8; Q6TCH4: PAQR6; NbExp=3; IntAct=EBI-6942903, EBI-17265310;
CC Q96BA8; I3L0A0: PEDS1-UBE2V1; NbExp=3; IntAct=EBI-6942903, EBI-12213001;
CC Q96BA8; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-6942903, EBI-981985;
CC Q96BA8; E9PRZ2: PGAP2; NbExp=3; IntAct=EBI-6942903, EBI-16438210;
CC Q96BA8; Q9UHJ9: PGAP2; NbExp=3; IntAct=EBI-6942903, EBI-10321427;
CC Q96BA8; Q9UHJ9-5: PGAP2; NbExp=6; IntAct=EBI-6942903, EBI-12092917;
CC Q96BA8; Q6IB11: PGRMC1; NbExp=3; IntAct=EBI-6942903, EBI-10249941;
CC Q96BA8; P26678: PLN; NbExp=3; IntAct=EBI-6942903, EBI-692836;
CC Q96BA8; P60201: PLP1; NbExp=3; IntAct=EBI-6942903, EBI-8653150;
CC Q96BA8; P60201-2: PLP1; NbExp=16; IntAct=EBI-6942903, EBI-12188331;
CC Q96BA8; Q04941: PLP2; NbExp=3; IntAct=EBI-6942903, EBI-608347;
CC Q96BA8; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-6942903, EBI-10485931;
CC Q96BA8; Q8IY26: PLPP6; NbExp=5; IntAct=EBI-6942903, EBI-11721828;
CC Q96BA8; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-6942903, EBI-12955265;
CC Q96BA8; Q01453: PMP22; NbExp=3; IntAct=EBI-6942903, EBI-2845982;
CC Q96BA8; Q59EV6: PPGB; NbExp=3; IntAct=EBI-6942903, EBI-14210385;
CC Q96BA8; O43741: PRKAB2; NbExp=4; IntAct=EBI-6942903, EBI-1053424;
CC Q96BA8; P43378: PTPN9; NbExp=3; IntAct=EBI-6942903, EBI-742898;
CC Q96BA8; Q96AA3: RFT1; NbExp=3; IntAct=EBI-6942903, EBI-6269616;
CC Q96BA8; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-6942903, EBI-9916444;
CC Q96BA8; Q02161-2: RHD; NbExp=3; IntAct=EBI-6942903, EBI-17249212;
CC Q96BA8; Q5GAN6: RNASE10; NbExp=3; IntAct=EBI-6942903, EBI-12423312;
CC Q96BA8; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-6942903, EBI-10224192;
CC Q96BA8; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-6942903, EBI-8636004;
CC Q96BA8; Q9NTJ5: SACM1L; NbExp=6; IntAct=EBI-6942903, EBI-3917235;
CC Q96BA8; Q14162: SCARF1; NbExp=3; IntAct=EBI-6942903, EBI-12056025;
CC Q96BA8; O00767: SCD; NbExp=3; IntAct=EBI-6942903, EBI-2684237;
CC Q96BA8; O95968: SCGB1D1; NbExp=3; IntAct=EBI-6942903, EBI-12825395;
CC Q96BA8; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-6942903, EBI-8652744;
CC Q96BA8; O75396: SEC22B; NbExp=3; IntAct=EBI-6942903, EBI-1058865;
CC Q96BA8; P60059: SEC61G; NbExp=5; IntAct=EBI-6942903, EBI-4402709;
CC Q96BA8; Q9NTN9-2: SEMA4G; NbExp=5; IntAct=EBI-6942903, EBI-12913124;
CC Q96BA8; Q8TD22: SFXN5; NbExp=3; IntAct=EBI-6942903, EBI-17274136;
CC Q96BA8; Q13183: SLC13A2; NbExp=3; IntAct=EBI-6942903, EBI-17460043;
CC Q96BA8; Q8WWT9: SLC13A3; NbExp=3; IntAct=EBI-6942903, EBI-12938720;
CC Q96BA8; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-6942903, EBI-12243266;
CC Q96BA8; P11169: SLC2A3; NbExp=3; IntAct=EBI-6942903, EBI-725116;
CC Q96BA8; Q8IWU4: SLC30A8; NbExp=9; IntAct=EBI-6942903, EBI-10262251;
CC Q96BA8; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-6942903, EBI-12363689;
CC Q96BA8; P78383: SLC35B1; NbExp=3; IntAct=EBI-6942903, EBI-12147661;
CC Q96BA8; Q8TB61: SLC35B2; NbExp=5; IntAct=EBI-6942903, EBI-1054782;
CC Q96BA8; Q969S0: SLC35B4; NbExp=8; IntAct=EBI-6942903, EBI-10281213;
CC Q96BA8; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-6942903, EBI-17295964;
CC Q96BA8; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-6942903, EBI-12898013;
CC Q96BA8; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-6942903, EBI-2823239;
CC Q96BA8; Q9NWF4: SLC52A1; NbExp=3; IntAct=EBI-6942903, EBI-12904614;
CC Q96BA8; P30825: SLC7A1; NbExp=5; IntAct=EBI-6942903, EBI-4289564;
CC Q96BA8; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-6942903, EBI-8640191;
CC Q96BA8; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-6942903, EBI-12188413;
CC Q96BA8; Q08629: SPOCK1; NbExp=3; IntAct=EBI-6942903, EBI-2682560;
CC Q96BA8; Q14534: SQLE; NbExp=3; IntAct=EBI-6942903, EBI-3905171;
CC Q96BA8; Q13277: STX3; NbExp=3; IntAct=EBI-6942903, EBI-1394295;
CC Q96BA8; O15400: STX7; NbExp=5; IntAct=EBI-6942903, EBI-3221827;
CC Q96BA8; Q9UNK0: STX8; NbExp=5; IntAct=EBI-6942903, EBI-727240;
CC Q96BA8; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-6942903, EBI-12187159;
CC Q96BA8; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-6942903, EBI-1049004;
CC Q96BA8; Q9NZ01: TECR; NbExp=3; IntAct=EBI-6942903, EBI-2877718;
CC Q96BA8; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-6942903, EBI-10329860;
CC Q96BA8; P02786: TFRC; NbExp=3; IntAct=EBI-6942903, EBI-355727;
CC Q96BA8; O14925: TIMM23; NbExp=3; IntAct=EBI-6942903, EBI-1047996;
CC Q96BA8; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-6942903, EBI-6268651;
CC Q96BA8; Q96CP7: TLCD1; NbExp=3; IntAct=EBI-6942903, EBI-11337932;
CC Q96BA8; P55061: TMBIM6; NbExp=3; IntAct=EBI-6942903, EBI-1045825;
CC Q96BA8; P17152: TMEM11; NbExp=6; IntAct=EBI-6942903, EBI-723946;
CC Q96BA8; A0PK00: TMEM120B; NbExp=5; IntAct=EBI-6942903, EBI-10171534;
CC Q96BA8; Q9BVK8: TMEM147; NbExp=9; IntAct=EBI-6942903, EBI-348587;
CC Q96BA8; Q9Y6G1: TMEM14A; NbExp=5; IntAct=EBI-6942903, EBI-2800360;
CC Q96BA8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-6942903, EBI-8638294;
CC Q96BA8; Q9P0S9: TMEM14C; NbExp=5; IntAct=EBI-6942903, EBI-2339195;
CC Q96BA8; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-6942903, EBI-741829;
CC Q96BA8; Q969S6: TMEM203; NbExp=3; IntAct=EBI-6942903, EBI-12274070;
CC Q96BA8; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-6942903, EBI-12876824;
CC Q96BA8; A2RU14: TMEM218; NbExp=7; IntAct=EBI-6942903, EBI-10173151;
CC Q96BA8; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-6942903, EBI-347385;
CC Q96BA8; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-6942903, EBI-12195227;
CC Q96BA8; Q8WY98: TMEM234; NbExp=3; IntAct=EBI-6942903, EBI-8642211;
CC Q96BA8; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-6942903, EBI-11528917;
CC Q96BA8; P56557: TMEM50B; NbExp=3; IntAct=EBI-6942903, EBI-12366453;
CC Q96BA8; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-6942903, EBI-12015604;
CC Q96BA8; P01375: TNF; NbExp=3; IntAct=EBI-6942903, EBI-359977;
CC Q96BA8; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-6942903, EBI-717441;
CC Q96BA8; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-6942903, EBI-12003398;
CC Q96BA8; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-6942903, EBI-11996766;
CC Q96BA8; O60636: TSPAN2; NbExp=3; IntAct=EBI-6942903, EBI-3914288;
CC Q96BA8; P30536: TSPO; NbExp=7; IntAct=EBI-6942903, EBI-6623146;
CC Q96BA8; Q5TGU0: TSPO2; NbExp=5; IntAct=EBI-6942903, EBI-12195249;
CC Q96BA8; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-6942903, EBI-2819725;
CC Q96BA8; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-6942903, EBI-4401271;
CC Q96BA8; P23763-3: VAMP1; NbExp=3; IntAct=EBI-6942903, EBI-12097582;
CC Q96BA8; P63027: VAMP2; NbExp=3; IntAct=EBI-6942903, EBI-520113;
CC Q96BA8; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-6942903, EBI-6256462;
CC Q96BA8; Q14508: WFDC2; NbExp=3; IntAct=EBI-6942903, EBI-723529;
CC Q96BA8; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-6942903, EBI-751210;
CC Q96BA8; Q96MV8: ZDHHC15; NbExp=5; IntAct=EBI-6942903, EBI-12837904;
CC Q96BA8; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-6942903, EBI-10268111;
CC Q96BA8; O95159: ZFPL1; NbExp=5; IntAct=EBI-6942903, EBI-718439;
CC -!- SUBCELLULAR LOCATION: [Cyclic AMP-responsive element-binding protein 3-
CC like protein 1]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12054625, ECO:0000269|PubMed:16417584,
CC ECO:0000269|PubMed:25310401}; 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:0000269|PubMed:12054625,
CC ECO:0000269|PubMed:16417584, ECO:0000269|PubMed:21767813,
CC ECO:0000269|PubMed:25310401}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 1]: Nucleus {ECO:0000269|PubMed:24079343,
CC ECO:0000269|PubMed:25310401}. Note=Upon ER stress or DNA damage,
CC transported into the nucleus. {ECO:0000269|PubMed:12054625,
CC ECO:0000269|PubMed:21767813, ECO:0000269|PubMed:24079343,
CC ECO:0000269|PubMed:25310401}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96BA8-1; Sequence=Displayed;
CC Name=2; Synonyms=OASISv1;
CC IsoId=Q96BA8-2; Sequence=VSP_025632;
CC -!- TISSUE SPECIFICITY: Expressed in several tissues, with highest levels
CC in pancreas and prostate. Expressed at relatively lower levels in
CC brain. {ECO:0000269|PubMed:12054625}.
CC -!- PTM: Upon ER stress or DNA damage, translocated to the Golgi apparatus,
CC where it is processed by regulated intramembrane proteolysis (RIP) to
CC release the cytosol-facing N-terminal transcription factor domain. The
CC cleavage is performed sequentially by site-1 and site-2 proteases
CC (S1P/MBTPS1 and S2P/MBTPS2) (PubMed:16417584, PubMed:21767813,
CC PubMed:25310401, PubMed:27499293). RIP is induced by TGFB1 and ceramide
CC (PubMed:25310401, PubMed:27499293). {ECO:0000269|PubMed:16417584,
CC ECO:0000269|PubMed:21767813, ECO:0000269|PubMed:25310401,
CC ECO:0000269|PubMed:27499293}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9Z125}.
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 CREB3L1 is stabilized. {ECO:0000269|PubMed:22705851}.
CC -!- DISEASE: Osteogenesis imperfecta 16 (OI16) [MIM:616229]: An autosomal
CC recessive form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI16 is a severe form. {ECO:0000269|PubMed:24079343}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry. OI16 affected patients show a genomic deletion encompassing
CC CREB3L1 and the first exon of DGKZ. The absence of this exon does not
CC affect all DGKZ isoforms, some are still produced at normal level. It
CC cannot be ruled out that DGKZ could contribute to the phenotype, but in
CC view of its role in bone formation, CREB3L1 is a strong OI16-causing
CC candidate (PubMed:24079343). This hypothesis is corroborated by the
CC observation of CREB3L1 knockout mice which exhibit features reminiscent
CC of severe human osteogenesis imperfecta. {ECO:0000269|PubMed:24079343}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11681.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB063321; BAC01278.1; -; mRNA.
DR EMBL; BC014097; AAH14097.1; -; mRNA.
DR EMBL; BC015781; AAH15781.1; -; mRNA.
DR EMBL; AK075538; BAC11681.1; ALT_INIT; mRNA.
DR CCDS; CCDS53620.1; -. [Q96BA8-1]
DR RefSeq; NP_443086.1; NM_052854.3. [Q96BA8-1]
DR AlphaFoldDB; Q96BA8; -.
DR SMR; Q96BA8; -.
DR BioGRID; 124786; 251.
DR IntAct; Q96BA8; 200.
DR MINT; Q96BA8; -.
DR STRING; 9606.ENSP00000481956; -.
DR GlyCosmos; Q96BA8; 2 sites, No reported glycans.
DR GlyGen; Q96BA8; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96BA8; -.
DR PhosphoSitePlus; Q96BA8; -.
DR BioMuta; CREB3L1; -.
DR DMDM; 74751763; -.
DR jPOST; Q96BA8; -.
DR MassIVE; Q96BA8; -.
DR MaxQB; Q96BA8; -.
DR PaxDb; 9606-ENSP00000481956; -.
DR PeptideAtlas; Q96BA8; -.
DR ProteomicsDB; 76059; -. [Q96BA8-1]
DR ProteomicsDB; 76060; -. [Q96BA8-2]
DR Antibodypedia; 6395; 296 antibodies from 37 providers.
DR DNASU; 90993; -.
DR Ensembl; ENST00000621158.5; ENSP00000481956.1; ENSG00000157613.11. [Q96BA8-1]
DR GeneID; 90993; -.
DR KEGG; hsa:90993; -.
DR MANE-Select; ENST00000621158.5; ENSP00000481956.1; NM_052854.4; NP_443086.1.
DR UCSC; uc021qik.3; human. [Q96BA8-1]
DR AGR; HGNC:18856; -.
DR CTD; 90993; -.
DR DisGeNET; 90993; -.
DR GeneCards; CREB3L1; -.
DR HGNC; HGNC:18856; CREB3L1.
DR HPA; ENSG00000157613; Tissue enhanced (pancreas, salivary gland).
DR MalaCards; CREB3L1; -.
DR MIM; 616215; gene.
DR MIM; 616229; phenotype.
DR neXtProt; NX_Q96BA8; -.
DR OpenTargets; ENSG00000157613; -.
DR Orphanet; 79105; Myxofibrosarcoma.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR PharmGKB; PA134960108; -.
DR VEuPathDB; HostDB:ENSG00000157613; -.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000159848; -.
DR HOGENOM; CLU_037638_1_0_1; -.
DR InParanoid; Q96BA8; -.
DR OMA; SNQTTGP; -.
DR OrthoDB; 3679507at2759; -.
DR PhylomeDB; Q96BA8; -.
DR TreeFam; TF316079; -.
DR PathwayCommons; Q96BA8; -.
DR Reactome; R-HSA-8874211; CREB3 factors activate genes.
DR SignaLink; Q96BA8; -.
DR SIGNOR; Q96BA8; -.
DR BioGRID-ORCS; 90993; 12 hits in 1174 CRISPR screens.
DR ChiTaRS; CREB3L1; human.
DR GenomeRNAi; 90993; -.
DR Pharos; Q96BA8; Tbio.
DR PRO; PR:Q96BA8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96BA8; Protein.
DR Bgee; ENSG00000157613; Expressed in nasal cavity epithelium and 162 other cell types or tissues.
DR ExpressionAtlas; Q96BA8; baseline and differential.
DR Genevisible; Q96BA8; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035497; F:cAMP response element binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:ParkinsonsUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0070278; P:extracellular matrix constituent secretion; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
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; ISS:ParkinsonsUK-UCL.
DR CDD; cd14689; bZIP_CREB3; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46004; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN A; 1.
DR PANTHER; PTHR46004:SF1; CYCLIC AMP-RESPONSIVE ELEMENT-BINDING PROTEIN 3-LIKE PROTEIN 1; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00041; LEUZIPPRCREB.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; DNA-binding;
KW Endoplasmic reticulum; Glycoprotein; Host-virus interaction;
KW Isopeptide bond; Membrane; Nucleus; Osteogenesis imperfecta;
KW Reference proteome; Signal-anchor; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Unfolded protein response.
FT CHAIN 1..519
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 1"
FT /id="PRO_0000288064"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 1"
FT /id="PRO_0000296206"
FT TOPO_DOM 1..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..519
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 290..353
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..60
FT /note="Required for transcriptional activation"
FT REGION 71..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..321
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 332..353
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 484..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 392..395
FT /note="MBTPS2 recognition"
FT /evidence="ECO:0000303|PubMed:21767813"
FT MOTIF 423..426
FT /note="MBTPS1 recognition"
FT /evidence="ECO:0000303|PubMed:21767813"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 426..427
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250|UniProtKB:P18850"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 111..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025632"
FT VARIANT 411
FT /note="A -> T (in dbSNP:rs35652107)"
FT /id="VAR_032392"
FT MUTAGEN 392
FT /note="P->A: Abolishes proteolytic cleavage by MBTPS2; when
FT associated with A-395."
FT /evidence="ECO:0000269|PubMed:21767813"
FT MUTAGEN 392
FT /note="P->L: Abolishes proteolytic cleavage by MBTPS2."
FT /evidence="ECO:0000269|PubMed:16417584"
FT MUTAGEN 395
FT /note="P->A: Abolishes proteolytic cleavage by MBTPS2; when
FT associated with A-392."
FT /evidence="ECO:0000269|PubMed:21767813"
FT MUTAGEN 423
FT /note="R->A: Abolishes proteolytic cleavage by MBTPS1."
FT /evidence="ECO:0000269|PubMed:16417584,
FT ECO:0000269|PubMed:21767813"
FT MUTAGEN 426
FT /note="L->V: Abolishes proteolytic cleavage by MBTPS1."
FT /evidence="ECO:0000269|PubMed:16417584"
FT CONFLICT 249
FT /note="A -> P (in Ref. 2; AAH14097)"
FT /evidence="ECO:0000305"
SQ 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
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