ID ZFN2B_MOUSE Reviewed; 257 AA.
AC Q91X58; Q9D0W4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=AN1-type zinc finger protein 2B {ECO:0000305};
DE AltName: Full=Arsenite-inducible RNA-associated protein-like protein {ECO:0000303|PubMed:18467495};
DE Short=AIRAP-like protein {ECO:0000303|PubMed:18467495};
DE Flags: Precursor;
GN Name=Zfand2b {ECO:0000312|MGI:MGI:1916068};
GN Synonyms=Airapl {ECO:0000303|PubMed:18467495};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP FUNCTION, UBIQUITIN-BINDING, INTERACTION WITH PROTEASOME, SUBCELLULAR
RP LOCATION, TOPOLOGY, MUTAGENESIS OF SER-163; SER-173; SER-187; ALA-201;
RP ALA-229; ALA-231 AND CYS-254, PHOSPHORYLATION AT SER-163; SER-173 AND
RP SER-187 BY MAPK14, ISOPRENYLATION AT CYS-254, METHYLATION AT CYS-254, AND
RP DOMAIN.
RX PubMed=18467495; DOI=10.1073/pnas.0707025105;
RA Yun C., Stanhill A., Yang Y., Zhang Y., Haynes C.M., Xu C.F., Neubert T.A.,
RA Mor A., Philips M.R., Ron D.;
RT "Proteasomal adaptation to environmental stress links resistance to
RT proteotoxicity with longevity in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7094-7099(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, UBIQUITIN-BINDING, INTERACTION WITH BAG6, DERL1, FAF2, NPLOC4;
RP UFD1 AND VCP, AND REGION.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
RN [7]
RP FUNCTION, INTERACTION WITH BAG6 AND VCP, DOMAIN, AND MUTAGENESIS OF
RP ALA-201; ALA-229 AND ALA-231.
RX PubMed=26337389; DOI=10.1091/mbc.e15-02-0085;
RA Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.;
RT "Proteasomal degradation of preemptive quality control (pQC) substrates is
RT mediated by an AIRAPL-p97 complex.";
RL Mol. Biol. Cell 26:3719-3727(2015).
RN [8]
RP FUNCTION, INTERACTION WITH IGF1R, AND DISRUPTION PHENOTYPE.
RX PubMed=26692333; DOI=10.1038/nm.4013;
RA Osorio F.G., Soria-Valles C., Santiago-Fernandez O., Bernal T.,
RA Mittelbrunn M., Colado E., Rodriguez F., Bonzon-Kulichenko E., Vazquez J.,
RA Porta-de-la-Riva M., Ceron J., Fueyo A., Li J., Green A.R., Freije J.M.,
RA Lopez-Otin C.;
RT "Loss of the proteostasis factor AIRAPL causes myeloid transformation by
RT deregulating IGF-1 signaling.";
RL Nat. Med. 22:91-96(2016).
RN [9] {ECO:0007744|PDB:4XKH}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 187-240 IN COMPLEX WITH
RP LYS-48-LINKED TRI-UBIQUITIN CHAIN, INTERACTION WITH BAG6 AND PROTEASOME,
RP DOMAIN, AND MUTAGENESIS OF LEU-202; ALA-205; LEU-206; 213-ALA--SER-220;
RP LYS-214; PRO-215; LEU-218; LEU-226; ALA-227; LEU-228; ALA-229; GLN-230;
RP ALA-231 AND SER-233.
RX PubMed=26876100; DOI=10.1016/j.str.2015.12.017;
RA Rahighi S., Braunstein I., Ternette N., Kessler B., Kawasaki M., Kato R.,
RA Matsui T., Weiss T.M., Stanhill A., Wakatsuki S.;
RT "Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin
RT Chains.";
RL Structure 24:412-422(2016).
CC -!- FUNCTION: Plays a role in protein homeostasis by regulating both the
CC translocation and the ubiquitin-mediated proteasomal degradation of
CC nascent proteins at the endoplasmic reticulum (PubMed:24160817,
CC PubMed:26337389, PubMed:26692333). It is involved in the regulation of
CC signal-mediated translocation of proteins into the endoplasmic
CC reticulum (PubMed:24160817). It also plays a role in the ubiquitin-
CC mediated proteasomal degradation of proteins for which signal-mediated
CC translocation to the endoplasmic reticulum has failed (PubMed:18467495,
CC PubMed:26337389). May therefore function in the endoplasmic reticulum
CC stress-induced pre-emptive quality control, a mechanism that
CC selectively attenuates the translocation of newly synthesized proteins
CC into the endoplasmic reticulum and reroutes them to the cytosol for
CC proteasomal degradation (PubMed:24160817, PubMed:26337389). By
CC controlling the steady-state expression of the IGF1R receptor,
CC indirectly regulates the insulin-like growth factor receptor signaling
CC pathway (PubMed:26692333). {ECO:0000269|PubMed:18467495,
CC ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389,
CC ECO:0000269|PubMed:26692333}.
CC -!- SUBUNIT: Binds 'Lys-48'-linked polyubiquitin chains of ubiquitinated
CC proteins (PubMed:18467495, PubMed:24160817, PubMed:26876100).
CC Associates with the proteasome complex; upon exposure to arsenite
CC (PubMed:18467495, PubMed:26876100). Interacts (via VIM motif) with VCP;
CC the interaction is direct (PubMed:24160817, PubMed:26337389). Interacts
CC with BAG6 (PubMed:24160817, PubMed:26337389, PubMed:26876100).
CC Interacts with IGF1R (nascent precursor form) (PubMed:26692333).
CC Interacts with DERL1, FAF2, NPLOC4 and UFD1; probably through VCP
CC (PubMed:24160817). {ECO:0000269|PubMed:18467495,
CC ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389,
CC ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:26876100}.
CC -!- INTERACTION:
CC Q91X58; Q9R1P4: Psma1; NbExp=2; IntAct=EBI-15701753, EBI-991653;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18467495}; Lipid-anchor
CC {ECO:0000305|PubMed:18467495}.
CC -!- DOMAIN: The UIM domains specifically bind 'Lys-48'-linked ubiquitin
CC polymers (PubMed:18467495, PubMed:26876100). The UIM domains mediate
CC interaction with polyubiquitinated proteins (PubMed:18467495,
CC PubMed:26337389). {ECO:0000269|PubMed:18467495,
CC ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26876100}.
CC -!- PTM: Phosphorylated by MAPK14 (Probable). Phosphorylation has no effect
CC on association with the proteasome complex (Probable).
CC {ECO:0000305|PubMed:18467495}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice undergo premature death due to the
CC occurrence of myelo-proliferative neoplasms. The absence of Zfand2b
CC plays a driver role in the development of these neoplasms by
CC hyperactivating the insulin-like growth factor receptor signaling
CC pathway. This is due to increased expression, in particular at the cell
CC surface, of the IGF1R receptor. {ECO:0000269|PubMed:26692333}.
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DR EMBL; AK004332; BAB23266.1; -; mRNA.
DR EMBL; AK151430; BAE30394.1; -; mRNA.
DR EMBL; BC011495; AAH11495.1; -; mRNA.
DR CCDS; CCDS15064.1; -.
DR RefSeq; NP_001153377.1; NM_001159905.1.
DR RefSeq; NP_001153378.1; NM_001159906.1.
DR RefSeq; NP_081122.2; NM_026846.3.
DR PDB; 4XKH; X-ray; 3.00 A; C/E/H=187-240.
DR PDBsum; 4XKH; -.
DR AlphaFoldDB; Q91X58; -.
DR SMR; Q91X58; -.
DR BioGRID; 213068; 26.
DR DIP; DIP-46091N; -.
DR IntAct; Q91X58; 2.
DR STRING; 10090.ENSMUSP00000027394; -.
DR GlyGen; Q91X58; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q91X58; -.
DR PhosphoSitePlus; Q91X58; -.
DR SwissPalm; Q91X58; -.
DR EPD; Q91X58; -.
DR jPOST; Q91X58; -.
DR MaxQB; Q91X58; -.
DR PaxDb; 10090-ENSMUSP00000027394; -.
DR ProteomicsDB; 302127; -.
DR Pumba; Q91X58; -.
DR Antibodypedia; 51845; 253 antibodies from 15 providers.
DR DNASU; 68818; -.
DR Ensembl; ENSMUST00000027394.12; ENSMUSP00000027394.6; ENSMUSG00000026197.13.
DR Ensembl; ENSMUST00000160439.8; ENSMUSP00000125086.2; ENSMUSG00000026197.13.
DR GeneID; 68818; -.
DR KEGG; mmu:68818; -.
DR UCSC; uc007bnw.2; mouse.
DR AGR; MGI:1916068; -.
DR CTD; 130617; -.
DR MGI; MGI:1916068; Zfand2b.
DR VEuPathDB; HostDB:ENSMUSG00000026197; -.
DR eggNOG; KOG3183; Eukaryota.
DR GeneTree; ENSGT00940000159648; -.
DR InParanoid; Q91X58; -.
DR OMA; IICPLCT; -.
DR OrthoDB; 103213at2759; -.
DR PhylomeDB; Q91X58; -.
DR TreeFam; TF314219; -.
DR BioGRID-ORCS; 68818; 1 hit in 76 CRISPR screens.
DR PRO; PR:Q91X58; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91X58; Protein.
DR Bgee; ENSMUSG00000026197; Expressed in granulocyte and 258 other cell types or tissues.
DR ExpressionAtlas; Q91X58; baseline and differential.
DR Genevisible; Q91X58; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:Ensembl.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0045047; P:protein targeting to ER; IMP:UniProtKB.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; ISO:MGI.
DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 2.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR000058; Znf_AN1.
DR PANTHER; PTHR14677:SF13; AN1-TYPE ZINC FINGER PROTEIN 2B; 1.
DR PANTHER; PTHR14677; ARSENITE INDUCUBLE RNA ASSOCIATED PROTEIN AIP-1-RELATED; 1.
DR Pfam; PF01428; zf-AN1; 2.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00154; ZnF_AN1; 2.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 2.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS51039; ZF_AN1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..254
FT /note="AN1-type zinc finger protein 2B"
FT /id="PRO_0000232877"
FT PROPEP 255..257
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:18467495"
FT /id="PRO_0000444336"
FT DOMAIN 197..216
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 221..240
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 4..52
FT /note="AN1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT ZN_FING 94..142
FT /note="AN1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 141..151
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000305|PubMed:24160817"
FT REGION 152..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 254..257
FT /note="CAAX motif"
FT /evidence="ECO:0000305|PubMed:18467495"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 163
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000305|PubMed:18467495"
FT MOD_RES 173
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000305|PubMed:18467495"
FT MOD_RES 187
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000305|PubMed:18467495"
FT MOD_RES 254
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305|PubMed:18467495"
FT LIPID 254
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:18467495"
FT MUTAGEN 163
FT /note="S->A: No effect on association with the proteasome
FT complex; when associated with A-173 and A-187."
FT /evidence="ECO:0000269|PubMed:18467495"
FT MUTAGEN 163
FT /note="S->D: No effect on association with the proteasome
FT complex; when associated with D-173 and D-187."
FT /evidence="ECO:0000269|PubMed:18467495"
FT MUTAGEN 173
FT /note="S->A: No effect on association with the proteasome
FT complex; when associated with A-163 and A-187."
FT /evidence="ECO:0000269|PubMed:18467495"
FT MUTAGEN 173
FT /note="S->D: No effect on association with the proteasome
FT complex; when associated with D-163 and D-187."
FT /evidence="ECO:0000269|PubMed:18467495"
FT MUTAGEN 187
FT /note="S->A: No effect on association with the proteasome
FT complex; when associated with A-163 and A-173."
FT /evidence="ECO:0000269|PubMed:18467495"
FT MUTAGEN 187
FT /note="S->D: No effect on association with the proteasome
FT complex; when associated with D-163 and D-173."
FT /evidence="ECO:0000269|PubMed:18467495"
FT MUTAGEN 201
FT /note="A->Q: Loss of interaction with ubiquitin polymers
FT and ubiquitinated proteins, loss of interaction with BAG6
FT and no effect on association with the proteasome complex;
FT when associated with Q-229 and Q-231."
FT /evidence="ECO:0000269|PubMed:18467495,
FT ECO:0000269|PubMed:26337389"
FT MUTAGEN 202
FT /note="L->A: Decreased 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 205
FT /note="A->Q: Decreased 'Lys-48'-linked polyubiquitin
FT binding. Loss of 'Lys-48'-linked polyubiquitin binding,
FT loss of interaction with BAG6 and loss of association with
FT the proteasome complex; when associated with Q-229 and Q-
FT 231."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 206
FT /note="L->A: Decreased 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 213..220
FT /note="AKPQVLSS->QQQQQQQQ: No effect on 'Lys-48'-linked
FT polyubiquitin binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 214
FT /note="K->A,G: No effect on 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 215
FT /note="P->A,G: No effect on 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 215
FT /note="Missing: No effect on 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 218
FT /note="L->A: No effect on 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 226
FT /note="L->A: No effect on 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 227
FT /note="A->Q: Decreased 'Lys-48'-linked polyubiquitin
FT binding; when associated with A-230."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 228
FT /note="L->A: Decreased 'Lys-48'-linked polyubiquitin
FT binding. Loss of interaction with BAG6. Decreased
FT association with the proteasome complex."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 229
FT /note="A->Q: Decreased 'Lys-48'-linked polyubiquitin
FT binding. Loss of interaction with ubiquitin polymers and
FT ubiquitinated proteins, loss of interaction with BAG6 and
FT no effect on association with the proteasome complex; when
FT associated with Q-201 and Q-231. Loss of 'Lys-48'-linked
FT polyubiquitin binding, loss of interaction with BAG6 and
FT loss of association with the proteasome complex; when
FT associated with Q-205 and Q-231."
FT /evidence="ECO:0000269|PubMed:18467495,
FT ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26876100"
FT MUTAGEN 230
FT /note="Q->A: Decreased 'Lys-48'-linked polyubiquitin
FT binding; when associated with Q-227."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 231
FT /note="A->Q: Decreased 'Lys-48'-linked polyubiquitin
FT binding. Loss of interaction with ubiquitin polymers and
FT ubiquitinated proteins, loss of interaction with BAG6 and
FT no effect on association with the proteasome complex; when
FT associated with Q-201 and Q-229. Loss of 'Lys-48'-linked
FT polyubiquitin binding, loss of interaction with BAG6 and
FT loss of association with the proteasome complex; when
FT associated with Q-205 and Q-229."
FT /evidence="ECO:0000269|PubMed:18467495,
FT ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26876100"
FT MUTAGEN 233
FT /note="S->G: Decreased 'Lys-48'-linked polyubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:26876100"
FT MUTAGEN 254
FT /note="C->S: Loss of localization to the endoplasmic
FT reticulum membrane. Loss of interaction with BAG6. No
FT effect on association with the proteasome complex."
FT /evidence="ECO:0000269|PubMed:18467495"
FT CONFLICT 174
FT /note="P -> S (in Ref. 1; BAB23266)"
FT /evidence="ECO:0000305"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:4XKH"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:4XKH"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:4XKH"
SQ SEQUENCE 257 AA; 27895 MW; D9B35C96BB3876E2 CRC64;
MEFPDLGAHC SEPSCQRLDF LPLKCDACSG IFCADHVAYA QHHCGSAYQK DIQVPVCPLC
NVPVPVARGE PPDRAVGEHI DRDCRSDPAQ QKRKIFTNKC ERSGCRQREM MKLTCDRCGR
NFCIKHRHPL DHECSGEGHQ TSRAGLAAIS RAQGLASTST APSPSRTLPS SSSPSRATPQ
LPTRTASPVI ALQNGLSEDE ALQRALELSL AEAKPQVLSS QEEDDLALAQ ALSASEAEYQ
QQQAQSRSLK PSNCSLC
//
