DCTN4_HUMAN
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 03-AUG-2022, entry version 162.
DE RecName: Full=Dynactin subunit 4;
DE Short=Dyn4;
DE AltName: Full=Dynactin subunit p62;
GN Name=DCTN4;
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: Could have a dual role in dynein targeting and in ACTR1A/Arp1
CC subunit of dynactin pointed-end capping. Could be involved in ACTR1A
CC pointed-end binding and in additional roles in linking dynein and
CC dynactin to the cortical cytoskeleton.
CC -!- SUBUNIT: Member of the pointed-end complex of the dynactin shoulder
CC complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10 (By
CC similarity). Binds directly to the ACTR1A subunit of dynactin.
CC Interacts with ATP7B, but not ATP7A, in a copper-dependent manner.
CC Interacts with ANK2; this interaction is required for localization at
CC costameres (By similarity). {ECO:0000250}.
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}.
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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; 117.
DR IntAct; Q9UJW0; 41.
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; Q9UJW0; -.
DR PeptideAtlas; Q9UJW0; -.
DR PRIDE; Q9UJW0; -.
DR ProteomicsDB; 84667; -. [Q9UJW0-1]
DR ProteomicsDB; 84668; -. [Q9UJW0-2]
DR ProteomicsDB; 84669; -. [Q9UJW0-3]
DR Antibodypedia; 4309; 231 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 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; EPKFIVW; -.
DR OrthoDB; 853728at2759; -.
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; 386 hits in 1086 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 200 other tissues.
DR ExpressionAtlas; Q9UJW0; baseline and differential.
DR Genevisible; Q9UJW0; HS.
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:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR InterPro; IPR008603; DCTN4.
DR PANTHER; PTHR13034; PTHR13034; 1.
DR Pfam; PF05502; Dynactin_p62; 2.
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 S-
FT 33; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 33
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 51
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 54
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-70, S-73; S-76; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 70
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-73; S-76; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 73
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-76; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 76
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-73; S-79; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 79
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-73; S-76; S-111; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 111
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-114; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 114
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-277
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 277
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-114
FT and S-280."
FT /evidence="ECO:0000269|PubMed:16554302"
FT MUTAGEN 280
FT /note="C->S: Loss of ATP7B-binding; when associated with S-
FT 30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-114
FT 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
