USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

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Searching in 'USC-OGP 2-DE database' for entry matching: TERA_HUMAN USC-OGP 2-DE database:  TERA_HUMAN TERA_HUMAN General information about the entry View entry in simple text format Entry name TERA_HUMAN Primary accession number P55072 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: Full=Transitional endoplasmic reticulum ATPase; Short=TER ATPase; EC=3.6.4.6 {ECO:0000269|PubMed:26471729}; AltName: Full=15S Mg(2+)-ATPase p97 subunit; AltName: Full=Valosin-containing protein; Short=VCP;. Gene name Name=VCP Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein PLATELET_4-7 {PLATELET 4-7} Homo sapiens (Human)   map experimental info   PLATELET_4-7 MAP LOCATIONS: SPOT OGP-0274: pI=5.21; Mw=120018 SPOT OGP-0285: pI=5.10; Mw=107696 SPOT OGP-0286: pI=5.13; Mw=107696 PLATELET_5-6 {PLATELET 5-6} Homo sapiens (Human)   map experimental info   PLATELET_5-6 MAP LOCATIONS: SPOT OGP-0615: pI=5.11; Mw=103755 SPOT OGP-0616: pI=5.13; Mw=102264 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1110: pI=5.27; Mw=108968 SPOT OGP-1223: pI=6.07; Mw=35353 Cross-references UniProtKB/Swiss-Prot P55072; TERA_HUMAN. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 0.0 Entry name TERA_HUMAN Primary accession number P55072 Secondary accession number(s) B2R5T8 Q0V924 Q2TAI5 Q969G7 Q9UCD5 Sequence was last modified on  January 23, 2007 (version 4) Annotations were last modified on  March 15, 2017 (version 188) Name and origin of the protein Description RecName: Full=Transitional endoplasmic reticulum ATPase; Short=TER ATPase; EC=3.6.4.6 {ECO:0000269|PubMed:26471729}; AltName: Full=15S Mg(2+)-ATPase p97 subunit; AltName: Full=Valosin-containing protein; Short=VCP; Gene name Name=VCP Encoded on Name=VCP Keywords 3D-structure; Acetylation; Amyotrophic lateral sclerosis; ATP-binding; Autophagy; Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; Endoplasmic reticulum; Hydrolase; Lipid-binding; Methylation; Neurodegeneration; Neuropathy; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transport; Ubl conjugation; Ubl conjugation pathway. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL AC004472; AAC07984.1; -; Genomic_DNA EMBL AF100752; AAD43016.1; -; mRNA EMBL AK312310; BAG35235.1; -; mRNA EMBL AL353795; CAH70993.1; -; Genomic_DNA EMBL CH471071; EAW58404.1; -; Genomic_DNA EMBL BC110913; AAI10914.1; -; mRNA EMBL BC121794; AAI21795.1; -; mRNA EMBL Z70768; CAA94809.1; -; mRNA CCDS CCDS6573.1; -; . PIR T02243; T02243; . RefSeq NP_009057.1; NM_007126.3; . UniGene Hs.529782; -; . PDB 3EBB; X-ray; 1.90 A; E/F/G/H=797-806 PDB 3HU1; X-ray; 2.81 A; A/B/C/D/E/F=1-481 PDB 3HU2; X-ray; 2.85 A; A/B/C/D/E/F=1-481 PDB 3HU3; X-ray; 2.20 A; A/B=1-481 PDB 3QC8; X-ray; 2.20 A; A=21-196 PDB 3QQ7; X-ray; 2.65 A; A=2-187 PDB 3QQ8; X-ray; 2.00 A; A=2-187 PDB 3QWZ; X-ray; 2.00 A; A=1-208 PDB 3TIW; X-ray; 1.80 A; A/B=1-187 PDB 4KDI; X-ray; 1.86 A; A/B=21-196 PDB 4KDL; X-ray; 1.81 A; A=21-196 PDB 4KLN; X-ray; 2.62 A; A/B/C/D/E/F=1-481 PDB 4KO8; X-ray; 1.98 A; A/B=1-481 PDB 4KOD; X-ray; 2.96 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481 PDB 4P0A; X-ray; 2.30 A; B/D=797-806 PDB 5B6C; X-ray; 1.55 A; A=21-191 PDB 5C18; X-ray; 3.30 A; A/B/C/D/E/F=2-806 PDB 5C19; X-ray; 4.20 A; A/B/C/D/E/F=2-806 PDB 5C1A; X-ray; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-806 PDB 5C1B; X-ray; 3.08 A; A/B/C/D/E/F=2-806 PDB 5DYG; X-ray; 2.20 A; A=1-460 PDB 5DYI; X-ray; 3.71 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481 PDB 5EPP; X-ray; 1.88 A; A=21-199 PDB 5FTJ; EM; 2.30 A; A/B/C/D/E/F=1-806 PDB 5FTK; EM; 2.40 A; A/B/C/D/E/F=1-806 PDB 5FTL; EM; 3.30 A; A/B/C/D/E/F=1-806 PDB 5FTM; EM; 3.20 A; A/B/C/D/E/F=1-806 PDB 5FTN; EM; 3.30 A; A/B/C/D/E/F=1-806 PDB 5GLF; X-ray; 2.25 A; A/C/E/G=21-199 PDB 5IFS; X-ray; 2.46 A; B/D=1-481 PDB 5IFW; X-ray; 3.40 A; B=2-806 PDBsum 3EBB; -; . PDBsum 3HU1; -; . PDBsum 3HU2; -; . PDBsum 3HU3; -; . PDBsum 3QC8; -; . PDBsum 3QQ7; -; . PDBsum 3QQ8; -; . PDBsum 3QWZ; -; . PDBsum 3TIW; -; . PDBsum 4KDI; -; . PDBsum 4KDL; -; . PDBsum 4KLN; -; . PDBsum 4KO8; -; . PDBsum 4KOD; -; . PDBsum 4P0A; -; . PDBsum 5B6C; -; . PDBsum 5C18; -; . PDBsum 5C19; -; . PDBsum 5C1A; -; . PDBsum 5C1B; -; . PDBsum 5DYG; -; . PDBsum 5DYI; -; . PDBsum 5EPP; -; . PDBsum 5FTJ; -; . PDBsum 5FTK; -; . PDBsum 5FTL; -; . PDBsum 5FTM; -; . PDBsum 5FTN; -; . PDBsum 5GLF; -; . PDBsum 5IFS; -; . PDBsum 5IFW; -; . ProteinModelPortal P55072; -; . SMR P55072; -; . BioGrid 113258; 604; . DIP DIP-33543N; -; . IntAct P55072; 95; . MINT MINT-272884; -; . STRING 9606.ENSP00000351777; -; . BindingDB P55072; -; . ChEMBL CHEMBL1075145; -; . DrugBank DB04395; Phosphoaminophosphonic Acid-Adenylate Ester; . TCDB 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family; . iPTMnet P55072; -; . PhosphoSitePlus P55072; -; . SwissPalm P55072; -; . BioMuta VCP; -; . DMDM 6094447; -; . DOSAC-COBS-2DPAGE P55072; -; . OGP P55072; -; . REPRODUCTION-2DPAGE IPI00022774; -; . REPRODUCTION-2DPAGE P55072; -; . EPD P55072; -; . PaxDb P55072; -; . PeptideAtlas P55072; -; . PRIDE P55072; -; . TopDownProteomics P55072; -; . Ensembl ENST00000358901; ENSP00000351777; ENSG00000165280; . GeneID 7415; -; . KEGG hsa:7415; -; . CTD 7415; -; . DisGeNET 7415; -; . GeneCards VCP; -; . GeneReviews VCP; -; . HGNC HGNC:12666; VCP; . HPA CAB005593; -; . HPA HPA012728; -; . HPA HPA012814; -; . MalaCards VCP; -; . MIM 167320; phenotype; . MIM 601023; gene; . MIM 613954; phenotype; . MIM 616687; phenotype; . neXtProt NX_P55072; -; . OpenTargets ENSG00000165280; -; . Orphanet 329478; Adult-onset distal myopathy due to VCP mutation; . Orphanet 803; Amyotrophic lateral sclerosis; . Orphanet 275864; Behavioral variant of frontotemporal dementia; . Orphanet 275872; Frontotemporal dementia with motor neuron disease; . Orphanet 52430; Inclusion body myopathy with Paget disease of bone and frontotemporal dementia; . Orphanet 100070; Progressive non-fluent aphasia; . Orphanet 100069; Semantic dementia; . Orphanet 329475; Spastic paraplegia - Paget disease of bone; . PharmGKB PA37289; -; . eggNOG KOG0730; Eukaryota; . eggNOG COG0464; LUCA; . GeneTree ENSGT00860000133780; -; . HOGENOM HOG000223224; -; . HOVERGEN HBG001226; -; . InParanoid P55072; -; . KO K13525; -; . OMA MADSKGD; -; . OrthoDB EOG091G024K; -; . PhylomeDB P55072; -; . TreeFam TF300542; -; . Reactome R-HSA-110320; Translesion Synthesis by POLH; . Reactome R-HSA-3371511; HSF1 activation; . Reactome R-HSA-382556; ABC-family proteins mediated transport; . Reactome R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle; . Reactome R-HSA-5358346; Hedgehog ligand biogenesis; . Reactome R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD; . Reactome R-HSA-5678895; Defective CFTR causes cystic fibrosis; . Reactome R-HSA-5689877; Josephin domain DUBs; . Reactome R-HSA-5689896; Ovarian tumor domain proteases; . Reactome R-HSA-6798695; Neutrophil degranulation; . Reactome R-HSA-8876725; Protein methylation; . SignaLink P55072; -; . SIGNOR P55072; -; . ChiTaRS VCP; human; . EvolutionaryTrace P55072; -; . GeneWiki Valosin-containing_protein; -; . GenomeRNAi 7415; -; . PRO PR:P55072; -; . Proteomes UP000005640; Chromosome 9; . Bgee ENSG00000165280; -; . CleanEx HS_VCP; -; . ExpressionAtlas P55072; baseline and differential; . Genevisible P55072; HS; . GO GO:0035578; C:azurophil granule lumen; TAS:Reactome; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:UniProtKB; . GO GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB; . GO GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB; . GO GO:0005811; C:lipid particle; IDA:MGI; . GO GO:0043209; C:myelin sheath; IEA:Ensembl; . GO GO:0005654; C:nucleoplasm; IDA:HPA; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL; . GO GO:0000502; C:proteasome complex; IDA:BHF-UCL; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0035861; C:site of double-strand break; IDA:UniProtKB; . GO GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISS:ParkinsonsUK-UCL; . GO GO:1990730; C:VCP-NSFL1C complex; ISS:ParkinsonsUK-UCL; . GO GO:0043531; F:ADP binding; IEA:Ensembl; . GO GO:0005524; F:ATP binding; IEA:UniProtKB-KW; . GO GO:0016887; F:ATPase activity; IMP:UniProtKB; . GO GO:1904288; F:BAT3 complex binding; IPI:ParkinsonsUK-UCL; . GO GO:0035800; F:deubiquitinase activator activity; IDA:ParkinsonsUK-UCL; . GO GO:0042802; F:identical protein binding; IPI:IntAct; . GO GO:0008289; F:lipid binding; IEA:UniProtKB-KW; . GO GO:0031593; F:polyubiquitin binding; IDA:BHF-UCL; . GO GO:0019904; F:protein domain specific binding; IPI:UniProtKB; . GO GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL; . GO GO:0003723; F:RNA binding; IDA:UniProtKB; . GO GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL; . GO GO:0044389; F:ubiquitin-like protein ligase binding; IPI:ParkinsonsUK-UCL; . GO GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL; . GO GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB; . GO GO:0070842; P:aggresome assembly; IEA:Ensembl; . GO GO:0046034; P:ATP metabolic process; IEA:Ensembl; . GO GO:0097352; P:autophagosome maturation; IMP:UniProtKB; . GO GO:0006914; P:autophagy; IMP:UniProtKB; . GO GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB; . GO GO:0006281; P:DNA repair; NAS:UniProtKB; . GO GO:0006302; P:double-strand break repair; IDA:UniProtKB; . GO GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:UniProtKB; . GO GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl; . GO GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:ParkinsonsUK-UCL; . GO GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB; . GO GO:0036503; P:ERAD pathway; IMP:UniProtKB; . GO GO:0070987; P:error-free translesion synthesis; TAS:Reactome; . GO GO:0045184; P:establishment of protein localization; TAS:UniProtKB; . GO GO:0072389; P:flavin adenine dinucleotide catabolic process; IMP:ParkinsonsUK-UCL; . GO GO:0006734; P:NADH metabolic process; IMP:ParkinsonsUK-UCL; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:ParkinsonsUK-UCL; . GO GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; IDA:ParkinsonsUK-UCL; . GO GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL; . GO GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:ParkinsonsUK-UCL; . GO GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL; . GO GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL; . GO GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL; . GO GO:1903006; P:positive regulation of protein K63-linked deubiquitination; IDA:ParkinsonsUK-UCL; . GO GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB; . GO GO:0016579; P:protein deubiquitination; TAS:Reactome; . GO GO:0006457; P:protein folding; TAS:Reactome; . GO GO:0034214; P:protein hexamerization; IEA:Ensembl; . GO GO:0051260; P:protein homooligomerization; IEA:Ensembl; . GO GO:0006479; P:protein methylation; TAS:Reactome; . GO GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB; . GO GO:0016567; P:protein ubiquitination; IDA:UniProtKB; . GO GO:1903715; P:regulation of aerobic respiration; IMP:ParkinsonsUK-UCL; . GO GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB; . GO GO:0030970; P:retrograde protein transport; ER to cytosol; IDA:UniProtKB GO GO:0019985; P:translesion synthesis; IMP:UniProtKB; . GO GO:0055085; P:transmembrane transport; TAS:Reactome; . GO GO:0019079; P:viral genome replication; IMP:CACAO; . Gene3D 3.10.330.10; -; 1; . Gene3D 3.40.50.300; -; 2; . InterPro IPR003593; AAA+_ATPase; . InterPro IPR005938; AAA_ATPase_CDC48; . InterPro IPR009010; Asp_de-COase-like_dom; . InterPro IPR003959; ATPase_AAA_core; . InterPro IPR003960; ATPase_AAA_CS; . InterPro IPR004201; Cdc48_dom2; . InterPro IPR029067; CDC48_domain_2-like; . InterPro IPR003338; CDC4_N-term_subdom; . InterPro IPR027417; P-loop_NTPase; . InterPro IPR015415; Vps4_C; . Pfam PF00004; AAA; 2; . Pfam PF02933; CDC48_2; 1; . Pfam PF02359; CDC48_N; 1; . Pfam PF09336; Vps4_C; 1; . SMART SM00382; AAA; 2; . SMART SM01072; CDC48_2; 1; . SMART SM01073; CDC48_N; 1; . SUPFAM SSF50692; SSF50692; 1; . SUPFAM SSF52540; SSF52540; 2; . SUPFAM SSF54585; SSF54585; 1; . TIGRFAMs TIGR01243; CDC48; 1; . PROSITE PS00674; AAA; 2; .

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