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Abnova
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Sequence of this protein is as follows: MMLIPMASVM AVTEPKWVSV WSRFLWVTLL SMVLGSLLAL LLPLGAVEEQ CLAVLKGLYL LRSKPDRAQH AATKCTSPST ELSITSRGAT LLVAKTKASP AGKLEARAAL NQALEMKRQG KREKAQKLFM HALKMDPDFV DALTEFGIFS EEDKDIIQAD YLYTRALTIS PYHEKALVNR DRTLPLVEEI DQRYFSIIDS KVKKVMSIPK GNSALRRVME ETYYHHIYHT VAIEGNTLTL SEIRHILETR YAVPGKSLEE QNEVIGMHAA MKYINTTLVS RIGSVTISDV LEIHRRVLGY VDPVEAGRFR TTQVLVGHHI PPHPQDVEKQ MQEFVQWLNS EEAMNLHPVE FAALAHYKLV YIHPFIDGNG RTSRLLMNLI LMQAGYPPIT IRKEQRSDYY HVLEAANEGD VRPFIRFIAK CTETTLDTLL FATTEYSVAL PEAQPNHSGF KETLPVKP
Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context. The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place. Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:25601083). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity. Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (PubMed:19362538, PubMed:25601083). [UniProt]
仅用于科研。不用于诊断过程。未经明确授权不得转售。