DJB12_HUMAN
ID DJB12_HUMAN Reviewed; 375 AA.
AC Q9NXW2; B7Z7I3; Q9H6H0;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 5.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=DnaJ homolog subfamily B member 12 {ECO:0000303|PubMed:21150129};
GN Name=DNAJB12 {ECO:0000303|PubMed:21150129, ECO:0000312|HGNC:HGNC:14891};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue, Kidney epithelium, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Pancreas;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH HSPA8, AND
RP MUTAGENESIS OF HIS-138.
RX PubMed=21150129; DOI=10.1247/csf.10023;
RA Yamamoto Y.H., Kimura T., Momohara S., Takeuchi M., Tani T., Kimata Y.,
RA Kadokura H., Kohno K.;
RT "A novel ER J-protein DNAJB12 accelerates ER-associated degradation of
RT membrane proteins including CFTR.";
RL Cell Struct. Funct. 35:107-116(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21673190; DOI=10.1128/mbio.00101-11;
RA Goodwin E.C., Lipovsky A., Inoue T., Magaldi T.G., Edwards A.P.,
RA Van Goor K.E., Paton A.W., Paton J.C., Atwood W.J., Tsai B., DiMaio D.;
RT "BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum
RT are required for efficient simian virus 40 infection.";
RL MBio 2:E00101-E00111(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH HSPA8, AND
RP MUTAGENESIS OF HIS-138.
RX PubMed=21148293; DOI=10.1091/mbc.e10-09-0760;
RA Grove D.E., Fan C.Y., Ren H.Y., Cyr D.M.;
RT "The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to
RT facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508.";
RL Mol. Biol. Cell 22:301-314(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF
RP HIS-138.
RX PubMed=24732912; DOI=10.1371/journal.pone.0094322;
RA Goodwin E.C., Motamedi N., Lipovsky A., Fernandez-Busnadiego R., DiMaio D.;
RT "Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus
RT by membranes associated with a novel nuclear pore structure.";
RL PLoS ONE 9:E94322-E94322(2014).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND IDENTIFICATION IN A COMPLEX WITH
RP DNAJB14.
RX PubMed=24675744; DOI=10.1371/journal.ppat.1004007;
RA Walczak C.P., Ravindran M.S., Inoue T., Tsai B.;
RT "A cytosolic chaperone complexes with dynamic membrane J-proteins and
RT mobilizes a nonenveloped virus out of the endoplasmic reticulum.";
RL PLoS Pathog. 10:E1004007-E1004007(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 184-GLY--PHE-212.
RX PubMed=27916661; DOI=10.1016/j.molcel.2016.10.027;
RA Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.;
RT "Tetrameric assembly of K(+) channels requires ER-located chaperone
RT proteins.";
RL Mol. Cell 65:52-65(2017).
RN [13]
RP METHYLATION AT HIS-185, AND MUTAGENESIS OF HIS-185.
RX PubMed=33563959; DOI=10.1038/s41467-020-20670-7;
RA Davydova E., Shimazu T., Schuhmacher M.K., Jakobsson M.E.,
RA Willemen H.L.D.M., Liu T., Moen A., Ho A.Y.Y., Malecki J., Schroer L.,
RA Pinto R., Suzuki T., Groensberg I.A., Sohtome Y., Akakabe M., Weirich S.,
RA Kikuchi M., Olsen J.V., Dohmae N., Umehara T., Sodeoka M., Siino V.,
RA McDonough M.A., Eijkelkamp N., Schofield C.J., Jeltsch A., Shinkai Y.,
RA Falnes P.O.;
RT "The methyltransferase METTL9 mediates pervasive 1-methylhistidine
RT modification in mammalian proteomes.";
RL Nat. Commun. 12:891-891(2021).
RN [14]
RP STRUCTURE BY NMR OF 110-174.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of J-domain from human DnaJ subfamily B member 12.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC protein folding and trafficking, prevent aggregation of client
CC proteins, and promote unfolded proteins to endoplasmic reticulum-
CC associated degradation (ERAD) pathway (PubMed:21150129,
CC PubMed:21148293). Acts by determining HSPA8/Hsc70's ATPase and
CC polypeptide-binding activities (PubMed:21148293). Can also act
CC independently of HSPA8/Hsc70: together with DNAJB14, acts as a
CC chaperone that promotes maturation of potassium channels KCND2 and
CC KCNH2 by stabilizing nascent channel subunits and assembling them into
CC tetramers (PubMed:27916661). While stabilization of nascent channel
CC proteins is dependent on HSPA8/Hsc70, the process of oligomerization of
CC channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When
CC overexpressed, forms membranous structures together with DNAJB14 and
CC HSPA8/Hsc70 within the nucleus; the role of these structures, named
CC DJANGOs, is still unclear (PubMed:24732912).
CC {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129,
CC ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.
CC -!- FUNCTION: (Microbial infection) In case of infection by polyomavirus,
CC involved in the virus endoplasmic reticulum membrane penetration and
CC infection (PubMed:21673190, PubMed:24675744).
CC {ECO:0000269|PubMed:21673190, ECO:0000269|PubMed:24675744}.
CC -!- SUBUNIT: Homodimer and homotetramer (PubMed:27916661). Interacts (via J
CC domain) with HSPA8/Hsc70 (PubMed:21150129, PubMed:21148293,
CC PubMed:24732912, PubMed:27916661). Forms a multiprotein complex, at
CC least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction
CC with DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744).
CC {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129,
CC ECO:0000269|PubMed:24675744, ECO:0000269|PubMed:24732912,
CC ECO:0000269|PubMed:27916661}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21148293, ECO:0000269|PubMed:21150129,
CC ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}; Single-pass
CC membrane protein {ECO:0000255}. Nucleus membrane
CC {ECO:0000269|PubMed:24732912}; Single-pass membrane protein
CC {ECO:0000305}. Note=Localizes to the endoplasmic reticulum membrane
CC (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661).
CC When overexpressed, forms membranous structures in the nucleus
CC (PubMed:24732912). {ECO:0000269|PubMed:21148293,
CC ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912,
CC ECO:0000269|PubMed:27916661}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXW2-2; Sequence=VSP_039040;
CC -!- PTM: Methylated at His-185 by METTL9. {ECO:0000305|PubMed:33563959}.
CC -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15289.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH13619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK000034; BAA90896.1; -; mRNA.
DR EMBL; AK025942; BAB15289.1; ALT_INIT; mRNA.
DR EMBL; AK302071; BAH13619.1; ALT_INIT; mRNA.
DR EMBL; AC091769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011812; AAH11812.2; -; mRNA.
DR EMBL; BC064920; AAH64920.1; -; mRNA.
DR CCDS; CCDS7316.2; -. [Q9NXW2-1]
DR RefSeq; NP_001002762.2; NM_001002762.2. [Q9NXW2-1]
DR RefSeq; NP_060096.3; NM_017626.4. [Q9NXW2-1]
DR PDB; 2CTP; NMR; -; A=110-174.
DR PDBsum; 2CTP; -.
DR AlphaFoldDB; Q9NXW2; -.
DR SMR; Q9NXW2; -.
DR BioGRID; 120150; 148.
DR IntAct; Q9NXW2; 25.
DR MINT; Q9NXW2; -.
DR STRING; 9606.ENSP00000345575; -.
DR TCDB; 1.P.1.1.1; the polyoma virus sv40 er penetration channel (vpec) family.
DR iPTMnet; Q9NXW2; -.
DR PhosphoSitePlus; Q9NXW2; -.
DR BioMuta; DNAJB12; -.
DR DMDM; 294862531; -.
DR EPD; Q9NXW2; -.
DR jPOST; Q9NXW2; -.
DR MassIVE; Q9NXW2; -.
DR PaxDb; Q9NXW2; -.
DR PeptideAtlas; Q9NXW2; -.
DR PRIDE; Q9NXW2; -.
DR ProteomicsDB; 83139; -. [Q9NXW2-1]
DR ProteomicsDB; 83140; -. [Q9NXW2-2]
DR Antibodypedia; 2545; 181 antibodies from 25 providers.
DR DNASU; 54788; -.
DR Ensembl; ENST00000444643.8; ENSP00000403313.2; ENSG00000148719.16. [Q9NXW2-1]
DR GeneID; 54788; -.
DR KEGG; hsa:54788; -.
DR MANE-Select; ENST00000444643.8; ENSP00000403313.2; NM_017626.7; NP_060096.4.
DR UCSC; uc057tyc.1; human. [Q9NXW2-1]
DR CTD; 54788; -.
DR DisGeNET; 54788; -.
DR GeneCards; DNAJB12; -.
DR HGNC; HGNC:14891; DNAJB12.
DR HPA; ENSG00000148719; Low tissue specificity.
DR MIM; 608376; gene.
DR neXtProt; NX_Q9NXW2; -.
DR OpenTargets; ENSG00000148719; -.
DR PharmGKB; PA27414; -.
DR VEuPathDB; HostDB:ENSG00000148719; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000155590; -.
DR InParanoid; Q9NXW2; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q9NXW2; -.
DR PathwayCommons; Q9NXW2; -.
DR SignaLink; Q9NXW2; -.
DR BioGRID-ORCS; 54788; 62 hits in 1076 CRISPR screens.
DR ChiTaRS; DNAJB12; human.
DR EvolutionaryTrace; Q9NXW2; -.
DR GenomeRNAi; 54788; -.
DR Pharos; Q9NXW2; Tbio.
DR PRO; PR:Q9NXW2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NXW2; protein.
DR Bgee; ENSG00000148719; Expressed in tongue squamous epithelium and 206 other tissues.
DR ExpressionAtlas; Q9NXW2; baseline and differential.
DR Genevisible; Q9NXW2; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; IDA:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR015399; DUF1977_DnaJ-like.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09320; DUF1977; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Endoplasmic reticulum; Host-virus interaction; Membrane; Methylation;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..375
FT /note="DnaJ homolog subfamily B member 12"
FT /id="PRO_0000071037"
FT TOPO_DOM 1..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21148293,
FT ECO:0000305|PubMed:21150129"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..375
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21148293,
FT ECO:0000305|PubMed:21150129"
FT DOMAIN 112..176
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 45..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 185
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000305|PubMed:33563959"
FT VAR_SEQ 369..375
FT /note="VQASLHG -> TMKSLENFW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039040"
FT VARIANT 304
FT /note="E -> K (in dbSNP:rs3750784)"
FT /id="VAR_017864"
FT MUTAGEN 138
FT /note="H->Q: Abolishes interaction with HSPA8/Hsc70."
FT /evidence="ECO:0000269|PubMed:21148293,
FT ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:24732912"
FT MUTAGEN 184..212
FT /note="Missing: In delta(G/F); impaired ability to form
FT tetramers and impaired ability to promote potassium channel
FT assembly into tetramers."
FT /evidence="ECO:0000269|PubMed:27916661"
FT MUTAGEN 185
FT /note="H->R: Abolished histidine methylation by METTL9."
FT /evidence="ECO:0000269|PubMed:33563959"
FT CONFLICT 70
FT /note="T -> S (in Ref. 1; BAA90896)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="F -> S (in Ref. 1; BAA90896)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> G (in Ref. 1; BAH13619)"
FT /evidence="ECO:0000305"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:2CTP"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:2CTP"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2CTP"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:2CTP"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:2CTP"
SQ SEQUENCE 375 AA; 41860 MW; A9F0C7F3E22EF76F CRC64;
MESNKDEAER CISIALKAIQ SNQPDRALRF LEKAQRLYPT PRVRALIESL NQKPQTAGDQ
PPPTDTTHAT HRKAGGTDAP SANGEAGGES TKGYTAEQVA AVKRVKQCKD YYEILGVSRG
ASDEDLKKAY RRLALKFHPD KNHAPGATEA FKAIGTAYAV LSNPEKRKQY DQFGDDKSQA
ARHGHGHGDF HRGFEADISP EDLFNMFFGG GFPSSNVHVY SNGRMRYTYQ QRQDRRDNQG
DGGLGVFVQL MPILILILVS ALSQLMVSSP PYSLSPRPSV GHIHRRVTDH LGVVYYVGDT
FSEEYTGSSL KTVERNVEDD YIANLRNNCW KEKQQKEGLL YRARYFGDTD MYHRAQKMGT
PSCSRLSEVQ ASLHG
