Protein: TERA2_CAEEL
Sequence: MASVPTQRDEKEKKNDELATAILKDKKRPNRLIIDQSDNDDNSMVMLSQAKMDELGLFRGDSVILKGKKRRETVSIVLNADNCPNDKIKMNKVVRNNLRSRLGDVVSISSAQLEYGKRVHVLPIDDTIEGLTGNLFDVFLRPYFTDAYRPVHKGDIFTVQAAMRTVEFKVVETDPAPACIVAPDTVIHYEGDPIKREEEEEALNEVGYDDLGGVRKQLAQIKEMVELPLRHPQLFKAIGVKPPRGILLFGPPGTGKTLIARAVANETGAFFFLINGPEIMSKMSGESESNLRKAFAECEKNSPAILFIDEIDAIAPKREKAHGEVEKRIVSQLLTLMDGLKTRAHVVVIAATNRPNSIDGALRRFGRFDREIDIGIPDAVGRLEILRIHTKNMKLGEDVDLEQVANECHGFVGADLASLCSEAAIQQIREKMELIDLEDDTIDAEVLNSLAVTMENFRFAMGKSSPSALREAVVETPNTTWSDIGGLQNVKRELQELVQYPVEHPEKYLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVRDVFDKARAAAPCVLFFDELDSIAKARGGSVGDAGGAADRVINQVLTEMDGMNAKKNVFIIGATNRPDIIDPAVLRPGRLDQLIYIPLPDEASRLQIFKASLRKTPLSADLDLNFLAKNTVGFSGADLTEICQRACKLAIRESIEREIRQEKERQDRSARGEELMEDELADPVPEITRAHFEEAMKFARRSVTDNDIRKYEMFAQTLQQSRGFGNNFKFPGEAPSAGQPVGGNGGSGGNDDDDLYN
What is the function of this protein?
ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:18782221, PubMed:22768338).  However, able to prevent aggregation of unfolded proteins also in an ATP-independent manner (PubMed:18782221).  Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains (PubMed:19545544).  Involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260).  This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260).  Together with udf-2 and chn-1, regulates myosin assembly in body wall muscles by targeting myosin chaperone unc-45 for proteasomal degradation (PubMed:17369820).  During oocyte meiosis and together with cdc-48. 1, required for chromosome condensation at the diakinesis phase in prophase I and for progression of metaphase I (PubMed:17512499).  During the first embryonic cell division, regulates DNA replication and thus chromosome segregation and decondensation, and nuclear envelope re-assembly (PubMed:18097415, PubMed:18728180, PubMed:21981920, PubMed:26842564).  In S phase and in association with ufd-1, npl-4. 1 and/or npl-4. 2 and ubxn-3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:21981920, PubMed:26842564).  Regulates ubxn-3 nuclear localization during S phase (PubMed:26842564).  During the first embryonic cell divisions and together with cdc-48. 1, regulates the re-assembly of the nuclear envelope after mitosis possibly by inactivating kinase air-2, a component of the chromosomal passenger complex (CPC) (PubMed:18097415).
What are the official names of this protein?
Transitional endoplasmic reticulum ATPase homolog 2, Cell division cycle-related protein 48.2, p97/CDC48 homolog 2.
What is the protein family that this protein belongs to?
Belongs to the AAA ATPase family. CDC48 subfamily.
What are the subcellular locations of this protein?
Cytoplasm.