ID DCTN4_HUMAN Reviewed; 460 AA. AC Q9UJW0; B3KWW0; D3DQH0; E5RGT5; Q8TAN8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 171. DE RecName: Full=Dynactin subunit 4; DE Short=Dyn4; DE AltName: Full=Dynactin subunit p62; GN Name=DCTN4 {ECO:0000312|HGNC:HGNC:15518}; 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), SUBUNIT, AND SUBCELLULAR LOCATION. RC TISSUE=Neuron; RX PubMed=10671518; DOI=10.1074/jbc.275.7.4834; RA Karki S., Tokito M.K., Holzbaur E.L.F.; RT "A dynactin subunit with a highly conserved cysteine-rich motif interacts RT directly with Arp1."; RL J. Biol. Chem. 275:4834-4839(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-342. RC TISSUE=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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-95. RC TISSUE=Brain; 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 [6] RP INTERACTION WITH ATP7B, AND MUTAGENESIS OF CYS-30; CYS-33; CYS-51; CYS-54; RP CYS-70; CYS-73; CYS-76; CYS-79; CYS-111; CYS-114; CYS-277 AND CYS-280. RX PubMed=16554302; DOI=10.1074/jbc.m512745200; RA Lim C.M., Cater M.A., Mercer J.F., La Fontaine S.; RT "Copper-dependent interaction of dynactin subunit p62 with the N terminus RT of ATP7B but not ATP7A."; RL J. Biol. Chem. 281:14006-14014(2006). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, 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: Part of the dynactin complex that activates the molecular CC motor dynein for ultra-processive transport along microtubules. CC {ECO:0000250|UniProtKB:A0A4X1TB62}. CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex part of a CC tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or CC HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and CC consists of an actin-related filament composed of a shoulder domain, a CC pointed end and a barbed end. Its length is defined by its flexible CC shoulder domain. The soulder is composed of 2 DCTN1 subunits, 4 DCTN2 CC and 2 DCTN3. The 4 DCNT2 (via N-terminus) bind the ACTR1A filament and CC act as molecular rulers to determine the length. The pointed end is CC important for binding dynein-dynactin cargo adapters. Consists of 4 CC subunits: ACTR10, DCNT4, DCTN5 and DCTN6. The barbed end is composed of CC a CAPZA1:CAPZB heterodimers, which binds ACTR1A/ACTB filament and CC dynactin and stabilizes dynactin (By similarity). Interacts with ATP7B, CC but not ATP7A, in a copper-dependent manner (PubMed:16554302). CC Interacts with ANK2; this interaction is required for localization at CC costameres (By similarity). {ECO:0000250|UniProtKB:A0A4X1TB62, CC ECO:0000250|UniProtKB:Q8CBY8, ECO:0000269|PubMed:16554302}. CC -!- INTERACTION: CC Q9UJW0; Q9NZ32: ACTR10; NbExp=3; IntAct=EBI-2134033, EBI-2559426; CC Q9UJW0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2134033, EBI-739580; CC Q9UJW0; Q08379: GOLGA2; NbExp=7; IntAct=EBI-2134033, EBI-618309; CC Q9UJW0; P42858: HTT; NbExp=3; IntAct=EBI-2134033, EBI-466029; CC Q9UJW0; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-2134033, EBI-742948; CC Q9UJW0; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-2134033, EBI-302345; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10671518}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:10671518}. Cytoplasm, CC cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm, CC cell cortex {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm, myofibril, CC sarcomere {ECO:0000250|UniProtKB:Q8CBY8}. Note=Has a punctate CC cytoplasmic distribution as well as centrosomal distribution typical of CC dynactin (PubMed:10671518). Overexpression in cultured mammalian cells CC revealed colocalization with cortical actin, stress fibers, and focal CC adhesion sites, sites of potential interaction between microtubules and CC the cell cortex (By similarity). In skeletal muscles, costamere CC localization requires the presence of ANK2 (By similarity). CC {ECO:0000250|UniProtKB:Q8CBY8, ECO:0000250|UniProtKB:Q9QUR2, CC ECO:0000269|PubMed:10671518}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UJW0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJW0-2; Sequence=VSP_041306; CC Name=3; CC IsoId=Q9UJW0-3; Sequence=VSP_041307; CC -!- SIMILARITY: Belongs to the dynactin subunit 4 family. {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; AF195120; AAF03896.1; -; mRNA. DR EMBL; AK125973; BAG54272.1; -; mRNA. DR EMBL; AK000299; BAA91066.1; -; mRNA. DR EMBL; AC008450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008453; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61706.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61707.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61709.1; -; Genomic_DNA. DR EMBL; BC026323; AAH26323.1; -; mRNA. DR CCDS; CCDS4310.1; -. [Q9UJW0-1] DR CCDS; CCDS47310.1; -. [Q9UJW0-3] DR CCDS; CCDS47311.1; -. [Q9UJW0-2] DR RefSeq; NP_001129115.1; NM_001135643.1. [Q9UJW0-3] DR RefSeq; NP_001129116.1; NM_001135644.1. [Q9UJW0-2] DR RefSeq; NP_057305.1; NM_016221.3. [Q9UJW0-1] DR RefSeq; XP_011535946.1; XM_011537644.1. [Q9UJW0-2] DR RefSeq; XP_011535947.1; XM_011537645.1. [Q9UJW0-2] DR AlphaFoldDB; Q9UJW0; -. DR SMR; Q9UJW0; -. DR BioGRID; 119345; 158. DR IntAct; Q9UJW0; 43. DR MINT; Q9UJW0; -. DR STRING; 9606.ENSP00000414906; -. DR GlyGen; Q9UJW0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UJW0; -. DR PhosphoSitePlus; Q9UJW0; -. DR BioMuta; DCTN4; -. DR DMDM; 62900106; -. DR EPD; Q9UJW0; -. DR jPOST; Q9UJW0; -. DR MassIVE; Q9UJW0; -. DR MaxQB; Q9UJW0; -. DR PaxDb; 9606-ENSP00000414906; -. DR PeptideAtlas; Q9UJW0; -. DR ProteomicsDB; 84667; -. [Q9UJW0-1] DR ProteomicsDB; 84668; -. [Q9UJW0-2] DR ProteomicsDB; 84669; -. [Q9UJW0-3] DR Pumba; Q9UJW0; -. DR Antibodypedia; 4309; 245 antibodies from 28 providers. DR DNASU; 51164; -. DR Ensembl; ENST00000424236.5; ENSP00000411251.1; ENSG00000132912.13. [Q9UJW0-2] DR Ensembl; ENST00000446090.6; ENSP00000414906.2; ENSG00000132912.13. [Q9UJW0-3] DR Ensembl; ENST00000447998.7; ENSP00000416968.2; ENSG00000132912.13. [Q9UJW0-1] DR GeneID; 51164; -. DR KEGG; hsa:51164; -. DR MANE-Select; ENST00000447998.7; ENSP00000416968.2; NM_016221.4; NP_057305.1. DR UCSC; uc003lsu.4; human. [Q9UJW0-1] DR AGR; HGNC:15518; -. DR CTD; 51164; -. DR DisGeNET; 51164; -. DR GeneCards; DCTN4; -. DR HGNC; HGNC:15518; DCTN4. DR HPA; ENSG00000132912; Low tissue specificity. DR MalaCards; DCTN4; -. DR MIM; 614758; gene. DR neXtProt; NX_Q9UJW0; -. DR OpenTargets; ENSG00000132912; -. DR Orphanet; 586; Cystic fibrosis. DR PharmGKB; PA27183; -. DR VEuPathDB; HostDB:ENSG00000132912; -. DR eggNOG; KOG3896; Eukaryota. DR GeneTree; ENSGT00390000006954; -. DR HOGENOM; CLU_030384_0_0_1; -. DR InParanoid; Q9UJW0; -. DR OMA; IYFCRHC; -. DR OrthoDB; 5483333at2759; -. DR PhylomeDB; Q9UJW0; -. DR TreeFam; TF105249; -. DR PathwayCommons; Q9UJW0; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR SignaLink; Q9UJW0; -. DR SIGNOR; Q9UJW0; -. DR BioGRID-ORCS; 51164; 398 hits in 1164 CRISPR screens. DR ChiTaRS; DCTN4; human. DR GenomeRNAi; 51164; -. DR Pharos; Q9UJW0; Tbio. DR PRO; PR:Q9UJW0; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9UJW0; Protein. DR Bgee; ENSG00000132912; Expressed in biceps brachii and 202 other cell types or tissues. DR ExpressionAtlas; Q9UJW0; baseline and differential. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell. DR GO; GO:0000922; C:spindle pole; IEA:Ensembl. DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell. DR InterPro; IPR008603; DCTN4. DR PANTHER; PTHR13034; DYNACTIN P62 SUBUNIT; 1. DR PANTHER; PTHR13034:SF2; DYNACTIN SUBUNIT 4; 1. DR Pfam; PF05502; Dynactin_p62; 2. DR Genevisible; Q9UJW0; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..460 FT /note="Dynactin subunit 4" FT /id="PRO_0000079823" FT COILED 152..172 FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 407 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9QUR2" FT CROSSLNK 215 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..57 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041306" FT VAR_SEQ 179 FT /note="S -> SQHTIHVV (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_041307" FT VARIANT 95 FT /note="P -> T (in dbSNP:rs11550931)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_054037" FT VARIANT 263 FT /note="Y -> C (in dbSNP:rs35772018)" FT /id="VAR_033847" FT VARIANT 342 FT /note="F -> L (in dbSNP:rs11954652)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_024336" FT VARIANT 438 FT /note="S -> N (in dbSNP:rs3733923)" FT /id="VAR_024337" FT MUTAGEN 30 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-33; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 33 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 51 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-54; S-70, S-73; S-76; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 54 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-70, S-73; S-76; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 70 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-73; S-76; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 73 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-76; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 76 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-73; S-79; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 79 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-111; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 111 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-114; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 114 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; FT S-277 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 277 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; FT S-114 and S-280." FT /evidence="ECO:0000269|PubMed:16554302" FT MUTAGEN 280 FT /note="C->S: Loss of ATP7B-binding; when associated with FT S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; FT S-114 and S-277." FT /evidence="ECO:0000269|PubMed:16554302" SQ SEQUENCE 460 AA; 52337 MW; 2105D6C0A713B11D CRC64; MASLLQSDRV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATSI STQLPDDPAK TTMKKAYYLA CGFCRWTSRD VGMADKSVAS GGWQEPENPH TQRMNKLIEY YQQLAQKEKV ERDRKKLARR RNYMPLAFSD KYGLGTRLQR PRAGASISTL AGLSLKEGED QKEIKIEPAQ AVDEVEPLPE DYYTRPVNLT EVTTLQQRLL QPDFQPVCAS QLYPRHKHLL IKRSLRCRKC EHNLSKPEFN PTSIKFKIQL VAVNYIPEVR IMSIPNLRYM KESQVLLTLT NPVENLTHVT LFECEEGDPD DINSTAKVVV PPKELVLAGK DAAAEYDELA EPQDFQDDPD IIAFRKANKV GIFIKVTPQR EEGEVTVCFK MKHDFKNLAA PIRPIEESDQ GTEVIWLTQH VELSLGPLLP //