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

USC-OGP 2-DE database  Search by                Maps             Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal World-2DPAGE Repository Exclude local DBs has only effect if a remote interface is selected

Searching in 'USC-OGP 2-DE database' for entry matching: ACTN4_HUMAN USC-OGP 2-DE database:  ACTN4_HUMAN ACTN4_HUMAN General information about the entry View entry in simple text format Entry name ACTN4_HUMAN Primary accession number O43707 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=Alpha-actinin-4 {ECO:0000305}; AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000303|PubMed:10656685};. Gene name Name=ACTN4 {ECO:0000312|HGNC:HGNC:166} 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 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1102: pI=5.91; Mw=122096 SPOT OGP-1104: pI=5.37; Mw=117553 SPOT OGP-1105: pI=5.51; Mw=115893 SPOT OGP-1331: pI=5.13; Mw=16684 Cross-references UniProtKB/Swiss-Prot O43707; ACTN4_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 ACTN4_HUMAN Primary accession number O43707 Secondary accession number(s) A4K467 D6PXK4 O76048 Sequence was last modified on  February 21, 2001 (version 2) Annotations were last modified on  March 15, 2017 (version 200) Name and origin of the protein Description RecName: Full=Alpha-actinin-4 {ECO:0000305}; AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000303|PubMed:10656685}; Gene name Name=ACTN4 {ECO:0000312|HGNC:HGNC:166} Encoded on Name=ACTN4 {ECO:0000312|HGNC:HGNC:166 Keywords 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; Cell junction; Complete proteome; Cytoplasm; Disease mutation; Metal-binding; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL U48734; AAC17470.1; ALT_FRAME; mRNA EMBL GU987085; ADG03678.1; -; mRNA EMBL DQ431186; ABD96103.1; -; mRNA EMBL AC008649; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL AC022144; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL BC005033; AAH05033.1; -; mRNA EMBL AL047603; -; NOT_ANNOTATED_CDS; mRNA EMBL AU118403; -; NOT_ANNOTATED_CDS; mRNA EMBL D89980; BAA24447.1; ALT_INIT; mRNA CCDS CCDS12518.1; -. [O43707-1]; . RefSeq NP_004915.2; NM_004924.5. [O43707-1]; . UniGene Hs.270291; -; . PDB 1WLX; NMR; -; A=519-645 PDB 1YDI; X-ray; 1.80 A; B=734-757 PDB 2R0O; X-ray; 2.20 A; A/B=47-271 PDBsum 1WLX; -; . PDBsum 1YDI; -; . PDBsum 2R0O; -; . ProteinModelPortal O43707; -; . SMR O43707; -; . BioGrid 106596; 122; . DIP DIP-33179N; -; . IntAct O43707; 83; . MINT MINT-4998602; -; . STRING 9606.ENSP00000252699; -; . iPTMnet O43707; -; . PhosphoSitePlus O43707; -; . SwissPalm O43707; -; . BioMuta ACTN4; -; . REPRODUCTION-2DPAGE O43707; -; . EPD O43707; -; . MaxQB O43707; -; . PaxDb O43707; -; . PeptideAtlas O43707; -; . PRIDE O43707; -; . DNASU 81; -; . Ensembl ENST00000252699; ENSP00000252699; ENSG00000130402. [O43707-1]; . Ensembl ENST00000390009; ENSP00000439497; ENSG00000130402. [O43707-2]; . Ensembl ENST00000634692; ENSP00000488962; ENSG00000282844. [O43707-2]; . Ensembl ENST00000634960; ENSP00000489220; ENSG00000282844. [O43707-1]; . GeneID 81; -; . KEGG hsa:81; -; . UCSC uc002oja.3; human. [O43707-1]; . CTD 81; -; . DisGeNET 81; -; . GeneCards ACTN4; -; . HGNC HGNC:166; ACTN4; . HPA HPA001873; -; . HPA HPA006035; -; . MalaCards ACTN4; -; . MIM 603278; phenotype; . MIM 604638; gene; . neXtProt NX_O43707; -; . OpenTargets ENSG00000130402; -; . Orphanet 93213; Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis; . PharmGKB PA23; -; . eggNOG KOG0035; Eukaryota; . eggNOG COG5069; LUCA; . GeneTree ENSGT00760000118813; -; . HOGENOM HOG000263418; -; . HOVERGEN HBG050453; -; . InParanoid O43707; -; . KO K05699; -; . OMA KQRDYET; -; . OrthoDB EOG091G020R; -; . PhylomeDB O43707; -; . TreeFam TF352676; -; . Reactome R-HSA-114608; Platelet degranulation; . Reactome R-HSA-373753; Nephrin interactions; . SIGNOR O43707; -; . ChiTaRS ACTN4; human; . EvolutionaryTrace O43707; -; . GeneWiki Actinin_alpha_4; -; . GenomeRNAi 81; -; . PMAP-CutDB O43707; -; . PRO PR:O43707; -; . Proteomes UP000005640; Chromosome 19; . Bgee ENSG00000130402; -; . CleanEx HS_ACTN4; -; . ExpressionAtlas O43707; baseline and differential; . Genevisible O43707; HS; . GO GO:0005903; C:brush border; IEA:Ensembl; . GO GO:0005911; C:cell-cell junction; IEA:Ensembl; . GO GO:0030863; C:cortical cytoskeleton; IEA:Ensembl; . GO GO:0005737; C:cytoplasm; IDA:UniProtKB; . GO GO:0005829; C:cytosol; IDA:HPA; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0005615; C:extracellular space; IDA:UniProtKB; . GO GO:0005925; C:focal adhesion; IDA:UniProtKB; . GO GO:0005622; C:intracellular; IDA:UniProtKB; . GO GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB; . GO GO:0043005; C:neuron projection; IEA:Ensembl; . GO GO:0016604; C:nuclear body; IDA:HPA; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB; . GO GO:0031093; C:platelet alpha granule lumen; TAS:Reactome; . GO GO:0043234; C:protein complex; IDA:UniProtKB; . GO GO:0031143; C:pseudopodium; TAS:UniProtKB; . GO GO:0001725; C:stress fiber; IEA:Ensembl; . GO GO:0030018; C:Z disc; IEA:Ensembl; . GO GO:0003779; F:actin binding; TAS:UniProtKB; . GO GO:0051015; F:actin filament binding; IDA:UniProtKB; . GO GO:0005509; F:calcium ion binding; IEA:InterPro; . GO GO:0031490; F:chromatin DNA binding; IDA:UniProtKB; . GO GO:0005178; F:integrin binding; TAS:UniProtKB; . GO GO:0044325; F:ion channel binding; IPI:UniProtKB; . GO GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IMP:UniProtKB; . GO GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB; . GO GO:0001882; F:nucleoside binding; IDA:UniProtKB; . GO GO:0042803; F:protein homodimerization activity; IPI:UniProtKB; . GO GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB; . GO GO:0003723; F:RNA binding; IDA:UniProtKB; . GO GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB; . GO GO:0051017; P:actin filament bundle assembly; IEA:Ensembl; . GO GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl; . GO GO:0051271; P:negative regulation of cellular component movement; IEA:Ensembl; . GO GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB; . GO GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB; . GO GO:0002576; P:platelet degranulation; TAS:Reactome; . GO GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB; . GO GO:0051272; P:positive regulation of cellular component movement; IDA:UniProtKB; . GO GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:UniProtKB; . GO GO:0048549; P:positive regulation of pinocytosis; IEA:Ensembl; . GO GO:0032417; P:positive regulation of sodium:proton antiporter activity; NAS:UniProtKB; . GO GO:1902396; P:protein localization to bicellular tight junction; IEA:Ensembl; . GO GO:0015031; P:protein transport; IEA:UniProtKB-KW; . GO GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB; . GO GO:1903506; P:regulation of nucleic acid-templated transcription; IMP:UniProtKB; . GO GO:0001666; P:response to hypoxia; IEA:Ensembl; . GO GO:0048384; P:retinoic acid receptor signaling pathway; IDA:UniProtKB; . GO GO:0030050; P:vesicle transport along actin filament; IMP:UniProtKB; . CDD cd00014; CH; 2; . CDD cd00051; EFh; 1; . Gene3D 1.10.238.10; -; 2; . Gene3D 1.10.418.10; -; 2; . InterPro IPR001589; Actinin_actin-bd_CS; . InterPro IPR001715; CH-domain; . InterPro IPR011992; EF-hand-dom_pair; . InterPro IPR014837; EF-hand_Ca_insen; . InterPro IPR018247; EF_Hand_1_Ca_BS; . InterPro IPR002048; EF_hand_dom; . InterPro IPR018159; Spectrin/alpha-actinin; . InterPro IPR002017; Spectrin_repeat; . Pfam PF00307; CH; 2; . Pfam PF08726; EFhand_Ca_insen; 1; . Pfam PF00435; Spectrin; 4; . SMART SM00033; CH; 2; . SMART SM00054; EFh; 2; . SMART SM00150; SPEC; 4; . SUPFAM SSF47473; SSF47473; 1; . SUPFAM SSF47576; SSF47576; 1; . PROSITE PS00019; ACTININ_1; 1; . PROSITE PS00020; ACTININ_2; 1; . PROSITE PS50021; CH; 2; . PROSITE PS00018; EF_HAND_1; 1; . PROSITE PS50222; EF_HAND_2; 2; .

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• SWISS-2DPAGE - The Geneva Two-dimensional polyacrylamide gel electrophoresis database.
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