CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011216
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Copper-transporting ATPase 1 
Protein Synonyms/Alias
 Copper pump 1; Menkes disease-associated protein 
Gene Name
 ATP7A 
Gene Synonyms/Alias
 MC1; MNK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
333VTPESLRKAIEAVSPubiquitination[1]
855IKVVPGGKFPVDGRVubiquitination[2, 3]
1471INSLLSDKRSLNSVVubiquitination[2]
Reference
 [1] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells. 
Sequence Annotation
 DOMAIN 9 75 HMA 1.
 DOMAIN 172 238 HMA 2.
 DOMAIN 278 344 HMA 3.
 DOMAIN 378 444 HMA 4.
 DOMAIN 489 555 HMA 5.
 DOMAIN 565 631 HMA 6.
 REGION 1486 1500 PDZD11-binding.
 MOTIF 1487 1488 Endocytosis signal.
 ACT_SITE 1044 1044 4-aspartylphosphate intermediate (By
 METAL 1301 1301 Magnesium (By similarity).
 METAL 1305 1305 Magnesium (By similarity).
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 1212 1212 Phosphothreonine (By similarity).
 CARBOHYD 686 686 N-linked (GlcNAc...) (Potential).
 CARBOHYD 975 975 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Copper; Copper transport; Cytoplasm; Disease mutation; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1500 AA 
Protein Sequence
MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK 60
TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP 120
QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM 180
TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK 240
QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS 300
ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS 360
SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE 420
YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD 480
KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP 540
MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA 600
TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF 660
CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC 720
VPVQFFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITF 780
FDTPPMLFVF IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE 840
LVQRGDIIKV VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL 900
LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI ATLLVWIVIG 960
FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA 1020
QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLTESNRISH HKILAIVGTA 1080
ESNSEHPLGT AITKYCKQEL DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN 1140
NIKNASLVQI DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN 1200
DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV VLMTGDNSKT 1260
ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT 1320
GTDVAIEAAD VVLIRNDLLD VVASIDLSRE TVKRIRINFV FALIYNLVGI PIAAGVFMPI 1380
GLVLQPWMGS AAMAASSVSV VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI 1440
DDTSRNSPKL GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL 1500 
Gene Ontology
 GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
 GO:0031526; C:brush border membrane; IEA:Compara.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005770; C:late endosome; IDA:UniProtKB.
 GO:0043005; C:neuron projection; ISS:UniProtKB.
 GO:0043025; C:neuronal cell body; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0030141; C:secretory granule; IEA:Compara.
 GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO:0030140; C:trans-Golgi network transport vesicle; IMP:HGNC.
 GO:0005524; F:ATP binding; TAS:HGNC.
 GO:0004008; F:copper-exporting ATPase activity; ISS:UniProtKB.
 GO:0016532; F:superoxide dismutase copper chaperone activity; ISS:UniProtKB.
 GO:0001568; P:blood vessel development; ISS:UniProtKB.
 GO:0001974; P:blood vessel remodeling; ISS:UniProtKB.
 GO:0051216; P:cartilage development; ISS:UniProtKB.
 GO:0006878; P:cellular copper ion homeostasis; IMP:UniProtKB.
 GO:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
 GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
 GO:0015677; P:copper ion import; ISS:UniProtKB.
 GO:0048813; P:dendrite morphogenesis; IEA:Compara.
 GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
 GO:0042417; P:dopamine metabolic process; ISS:UniProtKB.
 GO:0048251; P:elastic fiber assembly; ISS:UniProtKB.
 GO:0051542; P:elastin biosynthetic process; ISS:UniProtKB.
 GO:0042414; P:epinephrine metabolic process; ISS:UniProtKB.
 GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0007626; P:locomotory behavior; ISS:UniProtKB.
 GO:0048286; P:lung alveolus development; ISS:UniProtKB.
 GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
 GO:0048553; P:negative regulation of metalloenzyme activity; ISS:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
 GO:0042421; P:norepinephrine biosynthetic process; IEA:Compara.
 GO:0042415; P:norepinephrine metabolic process; ISS:UniProtKB.
 GO:0018205; P:peptidyl-lysine modification; ISS:UniProtKB.
 GO:0043473; P:pigmentation; ISS:UniProtKB.
 GO:0048554; P:positive regulation of metalloenzyme activity; ISS:UniProtKB.
 GO:0051353; P:positive regulation of oxidoreductase activity; IDA:UniProtKB.
 GO:0021860; P:pyramidal neuron development; ISS:UniProtKB.
 GO:0010468; P:regulation of gene expression; IEA:Compara.
 GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProtKB.
 GO:0001836; P:release of cytochrome c from mitochondria; IEA:Compara.
 GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
 GO:0010041; P:response to iron(III) ion; IEA:Compara.
 GO:0010043; P:response to zinc ion; IEA:Compara.
 GO:0042428; P:serotonin metabolic process; ISS:UniProtKB.
 GO:0043588; P:skin development; ISS:UniProtKB.
 GO:0042093; P:T-helper cell differentiation; ISS:UniProtKB.
 GO:0006568; P:tryptophan metabolic process; ISS:UniProtKB.
 GO:0006570; P:tyrosine metabolic process; IEA:Compara. 
Interpro
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR027256; Cation_transp_P-typ_ATPase_IB.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom.
 IPR017969; Heavy-metal-associated_CS.
 IPR006121; HeavyMe-assoc_HMA.
 IPR006122; HMA_Cu_ion-bd. 
Pfam
 PF00122; E1-E2_ATPase
 PF00403; HMA
 PF00702; Hydrolase 
SMART
  
PROSITE
 PS00154; ATPASE_E1_E2
 PS01047; HMA_1
 PS50846; HMA_2 
PRINTS
 PR00119; CATATPASE.