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: Q16539 USC-OGP 2-DE database:  Q16539 Q16539 General information about the entry View entry in simple text format Entry name MK14_HUMAN Primary accession number Q16539 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=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; EC=2.7.11.24 {ECO:0000269|PubMed:11010976, ECO:0000269|PubMed:15284239, ECO:0000269|PubMed:7493921}; AltName: Full=Cytokine suppressive anti-inflammatory drug-binding protein; Short=CSAID-binding protein; Short=CSBP; AltName: Full=MAP kinase MXI2; AltName: Full=MAX-interacting protein 2; AltName: Full=Mitogen-activated protein kinase p38 alpha; Short=MAP kinase p38 alpha; AltName: Full=Stress-activated protein kinase 2a; Short=SAPK2a;. Gene name Name=MAPK14 Synonyms=CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A 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_5-6 {PLATELET 5-6} Homo sapiens (Human)   map experimental info   PLATELET_5-6 MAP LOCATIONS: SPOT OGP-0716: pI=5.42; Mw=41024 Cross-references UniProtKB/Swiss-Prot Q16539; MK14_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 MK14_HUMAN Primary accession number Q16539 Secondary accession number(s) A6ZJ92 A8K6P4 B0LPH0 B5TY32 O60776 Q13083 Q14084 Q8TDX0 Sequence was last modified on  January 23, 2007 (version 3) Annotations were last modified on  March 15, 2017 (version 209) Name and origin of the protein Description RecName: Full=Mitogen-activated protein kinase 14; Short=MAP kinase 14; Short=MAPK 14; EC=2.7.11.24 {ECO:0000269|PubMed:11010976, ECO:0000269|PubMed:15284239, ECO:0000269|PubMed:7493921}; AltName: Full=Cytokine suppressive anti-inflammatory drug-binding protein; Short=CSAID-binding protein; Short=CSBP; AltName: Full=MAP kinase MXI2; AltName: Full=MAX-interacting protein 2; AltName: Full=Mitogen-activated protein kinase p38 alpha; Short=MAP kinase p38 alpha; AltName: Full=Stress-activated protein kinase 2a; Short=SAPK2a; Gene name Name=MAPK14 Synonyms=CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A Encoded on Name=MAPK14; Synonyms=CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A Keywords 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Stress response; Transcription; Transcription regulation; Transferase; Ubl conjugation. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL L35263; AAA57455.1; -; mRNA EMBL L35264; AAA57456.1; -; mRNA EMBL L35253; AAA74301.1; -; mRNA EMBL U19775; AAC50329.1; -; mRNA EMBL AF100544; AAF36770.1; -; mRNA EMBL AB074150; BAB85654.1; -; mRNA EMBL FJ032367; ACI00233.1; -; mRNA EMBL AK291709; BAF84398.1; -; mRNA EMBL BT006933; AAP35579.1; -; mRNA EMBL CR536505; CAG38743.1; -; mRNA EMBL EU332860; ABY87549.1; -; Genomic_DNA EMBL Z95152; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL CH471081; EAX03869.1; -; Genomic_DNA EMBL BC000092; AAH00092.1; -; mRNA EMBL BC031574; AAH31574.1; -; mRNA CCDS CCDS4815.1; -. [Q16539-2]; . CCDS CCDS4816.1; -. [Q16539-1]; . CCDS CCDS4817.1; -. [Q16539-4]; . PIR S53536; S53536; . RefSeq NP_001306.1; NM_001315.2. [Q16539-2]; . RefSeq NP_620581.1; NM_139012.2. [Q16539-1]; . RefSeq NP_620582.1; NM_139013.2. [Q16539-3]; . RefSeq NP_620583.1; NM_139014.2. [Q16539-4]; . UniGene Hs.485233; -; . PDB 1A9U; X-ray; 2.50 A; A=1-360 PDB 1BL6; X-ray; 2.50 A; A=1-360 PDB 1BL7; X-ray; 2.50 A; A=1-360 PDB 1BMK; X-ray; 2.40 A; A=1-360 PDB 1DI9; X-ray; 2.60 A; A=1-360 PDB 1IAN; X-ray; 2.00 A; A=2-360 PDB 1KV1; X-ray; 2.50 A; A=1-360 PDB 1KV2; X-ray; 2.80 A; A=1-360 PDB 1M7Q; X-ray; 2.40 A; A=1-360 PDB 1OUK; X-ray; 2.50 A; A=1-360 PDB 1OUY; X-ray; 2.50 A; A=1-360 PDB 1OVE; X-ray; 2.10 A; A=1-360 PDB 1OZ1; X-ray; 2.10 A; A=1-360 PDB 1R39; X-ray; 2.30 A; A=1-360 PDB 1R3C; X-ray; 2.00 A; A=1-360 PDB 1W7H; X-ray; 2.21 A; A=2-360 PDB 1W82; X-ray; 2.20 A; A=2-360 PDB 1W83; X-ray; 2.50 A; A=2-360 PDB 1W84; X-ray; 2.20 A; A=2-360 PDB 1WBN; X-ray; 2.40 A; A=2-360 PDB 1WBO; X-ray; 2.16 A; A=2-360 PDB 1WBS; X-ray; 1.80 A; A=2-360 PDB 1WBT; X-ray; 2.00 A; A=2-360 PDB 1WBV; X-ray; 2.00 A; A=2-360 PDB 1WBW; X-ray; 2.41 A; A=2-360 PDB 1WFC; X-ray; 2.30 A; A=1-360 PDB 1YQJ; X-ray; 2.00 A; A=2-360 PDB 1ZYJ; X-ray; 2.00 A; A=1-360 PDB 1ZZ2; X-ray; 2.00 A; A=1-360 PDB 1ZZL; X-ray; 2.00 A; A=4-354 PDB 2BAJ; X-ray; 2.25 A; A=2-360 PDB 2BAK; X-ray; 2.20 A; A=2-360 PDB 2BAL; X-ray; 2.10 A; A=2-360 PDB 2BAQ; X-ray; 2.80 A; A=2-360 PDB 2FSL; X-ray; 1.70 A; X=2-360 PDB 2FSM; X-ray; 1.86 A; X=2-360 PDB 2FSO; X-ray; 1.83 A; X=2-360 PDB 2FST; X-ray; 1.45 A; X=2-360 PDB 2GFS; X-ray; 1.75 A; A=2-360 PDB 2I0H; X-ray; 2.00 A; A=1-360 PDB 2LGC; NMR; -; A=2-354 PDB 2NPQ; X-ray; 1.80 A; A=2-360 PDB 2OKR; X-ray; 2.00 A; A/D=2-360 PDB 2ONL; X-ray; 4.00 A; A/B=2-360 PDB 2QD9; X-ray; 1.70 A; A=2-360 PDB 2RG5; X-ray; 2.40 A; A=2-360 PDB 2RG6; X-ray; 1.72 A; A=2-360 PDB 2Y8O; X-ray; 1.95 A; A=1-360 PDB 2YIS; X-ray; 2.00 A; A=2-360 PDB 2YIW; X-ray; 2.00 A; A=2-360 PDB 2YIX; X-ray; 2.30 A; A=4-354 PDB 2ZAZ; X-ray; 1.80 A; A=1-360 PDB 2ZB0; X-ray; 2.10 A; A=1-360 PDB 2ZB1; X-ray; 2.50 A; A=1-360 PDB 3BV2; X-ray; 2.40 A; A=2-360 PDB 3BV3; X-ray; 2.59 A; A=2-360 PDB 3BX5; X-ray; 2.40 A; A=2-360 PDB 3C5U; X-ray; 2.80 A; A=2-360 PDB 3CTQ; X-ray; 1.95 A; A=5-352 PDB 3D7Z; X-ray; 2.10 A; A=1-360 PDB 3D83; X-ray; 1.90 A; A=1-360 PDB 3DS6; X-ray; 2.90 A; A/B/C/D=1-360 PDB 3DT1; X-ray; 2.80 A; A=1-360 PDB 3E92; X-ray; 2.00 A; A=1-360 PDB 3E93; X-ray; 2.00 A; A=1-360 PDB 3FC1; X-ray; 2.40 A; X=1-360 PDB 3FI4; X-ray; 2.20 A; A=1-360 PDB 3FKL; X-ray; 2.00 A; A=1-360 PDB 3FKN; X-ray; 2.00 A; A=1-360 PDB 3FKO; X-ray; 2.00 A; A=1-360 PDB 3FL4; X-ray; 1.80 A; A=1-360 PDB 3FLN; X-ray; 1.90 A; C=1-360 PDB 3FLQ; X-ray; 1.90 A; A=1-360 PDB 3FLS; X-ray; 2.30 A; A=1-360 PDB 3FLW; X-ray; 2.10 A; A=1-360 PDB 3FLY; X-ray; 1.80 A; A=1-360 PDB 3FLZ; X-ray; 2.23 A; A=1-360 PDB 3FMH; X-ray; 1.90 A; A=1-360 PDB 3FMJ; X-ray; 2.00 A; A=1-360 PDB 3FMK; X-ray; 1.70 A; A=1-360 PDB 3FML; X-ray; 2.10 A; A=1-360 PDB 3FMM; X-ray; 2.00 A; A=1-360 PDB 3FMN; X-ray; 1.90 A; A=1-360 PDB 3FSF; X-ray; 2.10 A; A=1-360 PDB 3FSK; X-ray; 2.00 A; A=1-360 PDB 3GC7; X-ray; 1.80 A; A=1-360 PDB 3GCP; X-ray; 2.25 A; A=2-360 PDB 3GCQ; X-ray; 2.00 A; A=2-360 PDB 3GCS; X-ray; 2.10 A; A=2-360 PDB 3GCU; X-ray; 2.10 A; A/B=2-360 PDB 3GCV; X-ray; 2.30 A; A=2-360 PDB 3GFE; X-ray; 2.10 A; A=1-360 PDB 3GI3; X-ray; 2.40 A; A=1-360 PDB 3HA8; X-ray; 2.48 A; A=1-360 PDB 3HEC; X-ray; 2.50 A; A=5-352 PDB 3HEG; X-ray; 2.20 A; A=5-352 PDB 3HL7; X-ray; 1.88 A; A=1-360 PDB 3HLL; X-ray; 1.95 A; A=1-360 PDB 3HP2; X-ray; 2.15 A; A=1-360 PDB 3HP5; X-ray; 2.30 A; A=1-360 PDB 3HRB; X-ray; 2.20 A; A=2-360 PDB 3HUB; X-ray; 2.25 A; A=2-360 PDB 3HUC; X-ray; 1.80 A; A=2-360 PDB 3HV3; X-ray; 2.00 A; A=2-360 PDB 3HV4; X-ray; 2.60 A; A/B=2-360 PDB 3HV5; X-ray; 2.25 A; A/B=2-360 PDB 3HV6; X-ray; 1.95 A; A=2-360 PDB 3HV7; X-ray; 2.40 A; A=2-360 PDB 3HVC; X-ray; 2.10 A; A=1-360 PDB 3IPH; X-ray; 2.10 A; A=1-360 PDB 3ITZ; X-ray; 2.25 A; A=1-360 PDB 3IW5; X-ray; 2.50 A; A=2-360 PDB 3IW6; X-ray; 2.10 A; A=2-360 PDB 3IW7; X-ray; 2.40 A; A=2-360 PDB 3IW8; X-ray; 2.00 A; A=2-360 PDB 3K3I; X-ray; 1.70 A; A=5-352 PDB 3K3J; X-ray; 2.00 A; A=1-360 PDB 3KF7; X-ray; 2.00 A; A=1-360 PDB 3KQ7; X-ray; 1.80 A; A=1-360 PDB 3L8S; X-ray; 2.35 A; A=2-360 PDB 3L8X; X-ray; 2.15 A; A=2-360 PDB 3LFA; X-ray; 2.10 A; A=2-360 PDB 3LFB; X-ray; 2.60 A; A=2-360 PDB 3LFC; X-ray; 2.80 A; A=2-360 PDB 3LFD; X-ray; 3.40 A; A=2-360 PDB 3LFE; X-ray; 2.30 A; A=2-360 PDB 3LFF; X-ray; 1.50 A; A=2-360 PDB 3LHJ; X-ray; 3.31 A; A=1-360 PDB 3MGY; X-ray; 2.10 A; A=1-360 PDB 3MH0; X-ray; 2.00 A; A=1-360 PDB 3MH1; X-ray; 2.20 A; A=1-360 PDB 3MH2; X-ray; 2.30 A; A=1-360 PDB 3MH3; X-ray; 2.20 A; A=1-360 PDB 3MPA; X-ray; 2.10 A; A=1-360 PDB 3MPT; X-ray; 1.89 A; A=1-360 PDB 3MVL; X-ray; 2.80 A; A/B=2-360 PDB 3MVM; X-ray; 2.00 A; A/B=2-360 PDB 3MW1; X-ray; 2.80 A; A=2-360 PDB 3NEW; X-ray; 2.51 A; A=1-360 PDB 3NNU; X-ray; 2.40 A; A=1-354 PDB 3NNV; X-ray; 2.10 A; A=1-354 PDB 3NNW; X-ray; 1.89 A; A=1-354 PDB 3NNX; X-ray; 2.28 A; A=1-354 PDB 3NWW; X-ray; 2.09 A; A=2-360 PDB 3O8P; X-ray; 2.10 A; A=1-360 PDB 3O8T; X-ray; 2.00 A; A=1-360 PDB 3O8U; X-ray; 2.10 A; A=1-360 PDB 3OBG; X-ray; 2.80 A; A=1-360 PDB 3OBJ; X-ray; 2.40 A; A=1-360 PDB 3OC1; X-ray; 2.59 A; A=1-360 PDB 3OCG; X-ray; 2.21 A; A=2-360 PDB 3OD6; X-ray; 2.68 A; X=1-360 PDB 3ODY; X-ray; 2.20 A; X=1-360 PDB 3ODZ; X-ray; 2.30 A; X=1-360 PDB 3OEF; X-ray; 1.60 A; X=1-360 PDB 3PG3; X-ray; 2.00 A; A=2-360 PDB 3QUD; X-ray; 2.00 A; A=2-360 PDB 3QUE; X-ray; 2.70 A; A=2-360 PDB 3RIN; X-ray; 2.20 A; A=1-360 PDB 3ROC; X-ray; 1.70 A; A=1-360 PDB 3S3I; X-ray; 1.80 A; A=4-352 PDB 3S4Q; X-ray; 2.27 A; A=2-360 PDB 3U8W; X-ray; 2.15 A; A=1-360 PDB 3UVP; X-ray; 2.40 A; A=2-360 PDB 3UVQ; X-ray; 2.20 A; A=2-360 PDB 3UVR; X-ray; 2.10 A; A=2-360 PDB 3ZS5; X-ray; 1.60 A; A=2-360 PDB 3ZSG; X-ray; 1.89 A; A=2-360 PDB 3ZSH; X-ray; 2.05 A; A=2-360 PDB 3ZSI; X-ray; 2.40 A; A=2-360 PDB 3ZYA; X-ray; 1.90 A; A=1-360 PDB 4A9Y; X-ray; 2.20 A; A=2-360 PDB 4AA0; X-ray; 1.80 A; A=2-360 PDB 4AA4; X-ray; 2.30 A; A=2-360 PDB 4AA5; X-ray; 2.38 A; A=2-360 PDB 4AAC; X-ray; 2.50 A; A=2-360 PDB 4DLI; X-ray; 1.91 A; A=2-360 PDB 4DLJ; X-ray; 2.60 A; A=2-360 PDB 4E5A; X-ray; 1.87 A; X=1-360 PDB 4E5B; X-ray; 2.00 A; A=1-360 PDB 4E6A; X-ray; 2.09 A; A=1-360 PDB 4E6C; X-ray; 2.39 A; A=1-360 PDB 4E8A; X-ray; 2.70 A; A=1-360 PDB 4EH2; X-ray; 2.00 A; A=2-360 PDB 4EH3; X-ray; 2.40 A; A=2-360 PDB 4EH4; X-ray; 2.50 A; A=2-360 PDB 4EH5; X-ray; 2.00 A; A=2-360 PDB 4EH6; X-ray; 2.10 A; A=2-360 PDB 4EH7; X-ray; 2.10 A; A=2-360 PDB 4EH8; X-ray; 2.20 A; A=2-360 PDB 4EH9; X-ray; 2.10 A; A=2-360 PDB 4EHV; X-ray; 1.60 A; A=2-360 PDB 4EWQ; X-ray; 2.10 A; A=2-360 PDB 4F9W; X-ray; 2.00 A; A=2-360 PDB 4F9Y; X-ray; 1.85 A; A=2-360 PDB 4FA2; X-ray; 2.00 A; A=2-360 PDB 4GEO; X-ray; 1.66 A; A=2-360 PDB 4KIN; X-ray; 1.97 A; A/B/C/D=2-360 PDB 4KIP; X-ray; 2.27 A; A/B=2-360 PDB 4KIQ; X-ray; 2.50 A; A/B/C/D=2-360 PDB 4L8M; X-ray; 2.10 A; A=2-360 PDB 4R3C; X-ray; 2.06 A; A=2-360 PDB 4ZTH; X-ray; 2.15 A; A=2-360 PDB 5ETA; X-ray; 2.80 A; A/B=1-360 PDB 5ETC; X-ray; 2.42 A; A=1-360 PDB 5ETF; X-ray; 2.40 A; A=1-360 PDB 5ETI; X-ray; 2.80 A; A=1-360 PDBsum 1A9U; -; . PDBsum 1BL6; -; . PDBsum 1BL7; -; . PDBsum 1BMK; -; . PDBsum 1DI9; -; . PDBsum 1IAN; -; . PDBsum 1KV1; -; . PDBsum 1KV2; -; . PDBsum 1M7Q; -; . PDBsum 1OUK; -; . PDBsum 1OUY; -; . PDBsum 1OVE; -; . PDBsum 1OZ1; -; . PDBsum 1R39; -; . PDBsum 1R3C; -; . PDBsum 1W7H; -; . PDBsum 1W82; -; . PDBsum 1W83; -; . PDBsum 1W84; -; . PDBsum 1WBN; -; . PDBsum 1WBO; -; . PDBsum 1WBS; -; . PDBsum 1WBT; -; . PDBsum 1WBV; -; . PDBsum 1WBW; -; . PDBsum 1WFC; -; . PDBsum 1YQJ; -; . PDBsum 1ZYJ; -; . PDBsum 1ZZ2; -; . PDBsum 1ZZL; -; . PDBsum 2BAJ; -; . PDBsum 2BAK; -; . PDBsum 2BAL; -; . PDBsum 2BAQ; -; . PDBsum 2FSL; -; . PDBsum 2FSM; -; . PDBsum 2FSO; -; . PDBsum 2FST; -; . PDBsum 2GFS; -; . PDBsum 2I0H; -; . PDBsum 2LGC; -; . PDBsum 2NPQ; -; . PDBsum 2OKR; -; . PDBsum 2ONL; -; . PDBsum 2QD9; -; . PDBsum 2RG5; -; . PDBsum 2RG6; -; . PDBsum 2Y8O; -; . PDBsum 2YIS; -; . PDBsum 2YIW; -; . PDBsum 2YIX; -; . PDBsum 2ZAZ; -; . PDBsum 2ZB0; -; . PDBsum 2ZB1; -; . PDBsum 3BV2; -; . PDBsum 3BV3; -; . PDBsum 3BX5; -; . PDBsum 3C5U; -; . PDBsum 3CTQ; -; . PDBsum 3D7Z; -; . PDBsum 3D83; -; . PDBsum 3DS6; -; . PDBsum 3DT1; -; . PDBsum 3E92; -; . PDBsum 3E93; -; . PDBsum 3FC1; -; . PDBsum 3FI4; -; . PDBsum 3FKL; -; . PDBsum 3FKN; -; . PDBsum 3FKO; -; . PDBsum 3FL4; -; . PDBsum 3FLN; -; . PDBsum 3FLQ; -; . PDBsum 3FLS; -; . PDBsum 3FLW; -; . PDBsum 3FLY; -; . PDBsum 3FLZ; -; . PDBsum 3FMH; -; . PDBsum 3FMJ; -; . PDBsum 3FMK; -; . PDBsum 3FML; -; . PDBsum 3FMM; -; . PDBsum 3FMN; -; . PDBsum 3FSF; -; . PDBsum 3FSK; -; . PDBsum 3GC7; -; . PDBsum 3GCP; -; . PDBsum 3GCQ; -; . PDBsum 3GCS; -; . PDBsum 3GCU; -; . PDBsum 3GCV; -; . PDBsum 3GFE; -; . PDBsum 3GI3; -; . PDBsum 3HA8; -; . PDBsum 3HEC; -; . PDBsum 3HEG; -; . PDBsum 3HL7; -; . PDBsum 3HLL; -; . PDBsum 3HP2; -; . PDBsum 3HP5; -; . PDBsum 3HRB; -; . PDBsum 3HUB; -; . PDBsum 3HUC; -; . PDBsum 3HV3; -; . PDBsum 3HV4; -; . PDBsum 3HV5; -; . PDBsum 3HV6; -; . PDBsum 3HV7; -; . PDBsum 3HVC; -; . PDBsum 3IPH; -; . PDBsum 3ITZ; -; . PDBsum 3IW5; -; . PDBsum 3IW6; -; . PDBsum 3IW7; -; . PDBsum 3IW8; -; . PDBsum 3K3I; -; . PDBsum 3K3J; -; . PDBsum 3KF7; -; . PDBsum 3KQ7; -; . PDBsum 3L8S; -; . PDBsum 3L8X; -; . PDBsum 3LFA; -; . PDBsum 3LFB; -; . PDBsum 3LFC; -; . PDBsum 3LFD; -; . PDBsum 3LFE; -; . PDBsum 3LFF; -; . PDBsum 3LHJ; -; . PDBsum 3MGY; -; . PDBsum 3MH0; -; . PDBsum 3MH1; -; . PDBsum 3MH2; -; . PDBsum 3MH3; -; . PDBsum 3MPA; -; . PDBsum 3MPT; -; . PDBsum 3MVL; -; . PDBsum 3MVM; -; . PDBsum 3MW1; -; . PDBsum 3NEW; -; . PDBsum 3NNU; -; . PDBsum 3NNV; -; . PDBsum 3NNW; -; . PDBsum 3NNX; -; . PDBsum 3NWW; -; . PDBsum 3O8P; -; . PDBsum 3O8T; -; . PDBsum 3O8U; -; . PDBsum 3OBG; -; . PDBsum 3OBJ; -; . PDBsum 3OC1; -; . PDBsum 3OCG; -; . PDBsum 3OD6; -; . PDBsum 3ODY; -; . PDBsum 3ODZ; -; . PDBsum 3OEF; -; . PDBsum 3PG3; -; . PDBsum 3QUD; -; . PDBsum 3QUE; -; . PDBsum 3RIN; -; . PDBsum 3ROC; -; . PDBsum 3S3I; -; . PDBsum 3S4Q; -; . PDBsum 3U8W; -; . PDBsum 3UVP; -; . PDBsum 3UVQ; -; . PDBsum 3UVR; -; . PDBsum 3ZS5; -; . PDBsum 3ZSG; -; . PDBsum 3ZSH; -; . PDBsum 3ZSI; -; . PDBsum 3ZYA; -; . PDBsum 4A9Y; -; . PDBsum 4AA0; -; . PDBsum 4AA4; -; . PDBsum 4AA5; -; . PDBsum 4AAC; -; . PDBsum 4DLI; -; . PDBsum 4DLJ; -; . PDBsum 4E5A; -; . PDBsum 4E5B; -; . PDBsum 4E6A; -; . PDBsum 4E6C; -; . PDBsum 4E8A; -; . PDBsum 4EH2; -; . PDBsum 4EH3; -; . PDBsum 4EH4; -; . PDBsum 4EH5; -; . PDBsum 4EH6; -; . PDBsum 4EH7; -; . PDBsum 4EH8; -; . PDBsum 4EH9; -; . PDBsum 4EHV; -; . PDBsum 4EWQ; -; . PDBsum 4F9W; -; . PDBsum 4F9Y; -; . PDBsum 4FA2; -; . PDBsum 4GEO; -; . PDBsum 4KIN; -; . PDBsum 4KIP; -; . PDBsum 4KIQ; -; . PDBsum 4L8M; -; . PDBsum 4R3C; -; . PDBsum 4ZTH; -; . PDBsum 5ETA; -; . PDBsum 5ETC; -; . PDBsum 5ETF; -; . PDBsum 5ETI; -; . ProteinModelPortal Q16539; -; . SMR Q16539; -; . BioGrid 107819; 198; . DIP DIP-30987N; -; . IntAct Q16539; 100; . MINT MINT-126546; -; . STRING 9606.ENSP00000229794; -; . BindingDB Q16539; -; . ChEMBL CHEMBL260; -; . DrugBank DB02277; 1-(5-Tert-Butyl-2-Methyl-2h-Pyrazol-3-Yl)-3-(4-Chloro-Phenyl)-Urea; . DrugBank DB03044; 1-(5-Tert-Butyl-2-P-Tolyl-2h-Pyrazol-3-Yl)-3-[4-(2-Morpholin-4-Yl-Ethoxy)-Naphthalen-1-Yl]-Urea; . DrugBank DB06882; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea; . DrugBank DB08395; 2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE; . DrugBank DB03110; 2-Chlorophenol; . DrugBank DB07942; 2-fluoro-4-[4-(4-fluorophenyl)-1H-pyrazol-3-yl]pyridine; . DrugBank DB07943; 2-{4-[5-(4-chlorophenyl)-4-pyrimidin-4-yl-1H-pyrazol-3-yl]piperidin-1-yl}-2-oxoethanol; . DrugBank DB08093; 3-(1-NAPHTHYLMETHOXY)PYRIDIN-2-AMINE; . DrugBank DB02352; 3-(Benzyloxy)Pyridin-2-Amine; . DrugBank DB08730; 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-6-YL]BENZAMIDE; . DrugBank DB08091; 3-FLUORO-5-MORPHOLIN-4-YL-N-[3-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-5-YL]BENZAMIDE; . DrugBank DB08092; 3-fluoro-N-1H-indol-5-yl-5-morpholin-4-ylbenzamide; . DrugBank DB04632; 4-(2-HYDROXYBENZYLAMINO)-N-(3-(4-FLUOROPHENOXY)PHENYL)PIPERIDINE-1-SULFONAMIDE; . DrugBank DB08522; 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE; . DrugBank DB03980; 4-(Fluorophenyl)-1-Cyclopropylmethyl-5-(2-Amino-4-Pyrimidinyl)Imidazole; . DrugBank DB07829; 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE; . DrugBank DB07607; 4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE; . DrugBank DB08521; 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE; . DrugBank DB01761; 4-[5-[2-(1-Phenyl-Ethylamino)-Pyrimidin-4-Yl]-1-Methyl-4-(3-Trifluoromethylphenyl)-1h-Imidazol-2-Yl]-Piperidine; . DrugBank DB07459; 4-PHENOXY-N-(PYRIDIN-2-YLMETHYL)BENZAMIDE; . DrugBank DB01988; 6((S)-3-Benzylpiperazin-1-Yl)-3-(Naphthalen-2-Yl)-4-(Pyridin-4-Yl)Pyrazine; . DrugBank DB08423; [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL][3-(PIPERIDIN-4-YLOXY)PHENYL]METHANONE; . DrugBank DB01953; Inhibitor of P38 Kinase; . DrugBank DB05157; KC706; . DrugBank DB08064; N-(3-TERT-BUTYL-1H-PYRAZOL-5-YL)-N'-{4-CHLORO-3-[(PYRIDIN-3-YLOXY)METHYL]PHENYL}UREA; . DrugBank DB08068; N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]-3-FLUORO-; . DrugBank DB07307; N-cyclopropyl-4-methyl-3-[1-(2-methylphenyl)phthalazin-6-yl]benzamide; . DrugBank DB08351; N-cyclopropyl-4-methyl-3-{2-[(2-morpholin-4-ylethyl)amino]quinazolin-6-yl}benzamide; . DrugBank DB04338; SB220025; . DrugBank DB05412; SCIO-469; . DrugBank DB04797; Triazolopyridine; . DrugBank DB05470; VX-702; . GuidetoPHARMACOLOGY 1499; -; . iPTMnet Q16539; -; . PhosphoSitePlus Q16539; -; . BioMuta MAPK14; -; . OGP Q16539; -; . EPD Q16539; -; . MaxQB Q16539; -; . PaxDb Q16539; -; . PeptideAtlas Q16539; -; . PRIDE Q16539; -; . DNASU 1432; -; . Ensembl ENST00000229794; ENSP00000229794; ENSG00000112062. [Q16539-1]; . Ensembl ENST00000229795; ENSP00000229795; ENSG00000112062. [Q16539-2]; . Ensembl ENST00000310795; ENSP00000308669; ENSG00000112062. [Q16539-4]; . GeneID 1432; -; . KEGG hsa:1432; -; . UCSC uc003olp.4; human. [Q16539-1]; . CTD 1432; -; . DisGeNET 1432; -; . GeneCards MAPK14; -; . HGNC HGNC:6876; MAPK14; . HPA CAB010285; -; . HPA CAB040578; -; . HPA HPA051825; -; . MIM 600289; gene; . neXtProt NX_Q16539; -; . OpenTargets ENSG00000112062; -; . PharmGKB PA30621; -; . eggNOG KOG0660; Eukaryota; . eggNOG ENOG410XNY0; LUCA; . GeneTree ENSGT00550000074271; -; . HOGENOM HOG000233024; -; . HOVERGEN HBG014652; -; . InParanoid Q16539; -; . KO K04441; -; . OMA IQSLAQM; -; . OrthoDB EOG091G08QL; -; . PhylomeDB Q16539; -; . TreeFam TF105100; -; . BioCyc MetaCyc:HS03507-MONOMER; -; . BRENDA 2.7.11.24; 2681; . Reactome R-HSA-168638; NOD1/2 Signaling Pathway; . Reactome R-HSA-171007; p38MAPK events; . Reactome R-HSA-198753; ERK/MAPK targets; . Reactome R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation; . Reactome R-HSA-2559580; Oxidative Stress Induced Senescence; . Reactome R-HSA-375170; CDO in myogenesis; . Reactome R-HSA-376172; DSCAM interactions; . Reactome R-HSA-418592; ADP signalling through P2Y purinoceptor 1; . Reactome R-HSA-432142; Platelet sensitization by LDL; . Reactome R-HSA-4420097; VEGFA-VEGFR2 Pathway; . Reactome R-HSA-450302; activated TAK1 mediates p38 MAPK activation; . Reactome R-HSA-450341; Activation of the AP-1 family of transcription factors; . Reactome R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA; . Reactome R-HSA-6798695; Neutrophil degranulation; . Reactome R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation; . SignaLink Q16539; -; . SIGNOR Q16539; -; . ChiTaRS MAPK14; human; . EvolutionaryTrace Q16539; -; . GeneWiki MAPK14; -; . GenomeRNAi 1432; -; . PRO PR:Q16539; -; . Proteomes UP000005640; Chromosome 6; . Bgee ENSG00000112062; -; . CleanEx HS_MAPK14; -; . ExpressionAtlas Q16539; baseline and differential; . Genevisible Q16539; HS; . GO GO:0005737; C:cytoplasm; ISS:UniProtKB; . GO GO:0005829; C:cytosol; TAS:Reactome; . 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:0005739; C:mitochondrion; IEA:Ensembl; . GO GO:0016607; C:nuclear speck; IDA:HPA; . GO GO:0005654; C:nucleoplasm; TAS:Reactome; . GO GO:0005634; C:nucleus; ISS:UniProtKB; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0000922; C:spindle pole; IEA:Ensembl; . GO GO:0005524; F:ATP binding; IEA:UniProtKB-KW; . GO GO:0019899; F:enzyme binding; IPI:BHF-UCL; . GO GO:0004707; F:MAP kinase activity; IDA:UniProtKB; . GO GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc; . GO GO:0051525; F:NFAT protein binding; ISS:BHF-UCL; . GO GO:0019903; F:protein phosphatase binding; IPI:UniProtKB; . GO GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome; . GO GO:0070935; P:3'-UTR-mediated mRNA stabilization; TAS:UniProtKB; . GO GO:0000187; P:activation of MAPK activity; TAS:Reactome; . GO GO:0001525; P:angiogenesis; IEA:Ensembl; . GO GO:0006915; P:apoptotic process; IEA:UniProtKB-KW; . GO GO:0001502; P:cartilage condensation; IEA:Ensembl; . GO GO:0000902; P:cell morphogenesis; IEA:Ensembl; . GO GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc; . GO GO:0071479; P:cellular response to ionizing radiation; IMP:BHF-UCL; . GO GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI; . GO GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL; . GO GO:0098586; P:cellular response to virus; IMP:UniProtKB; . GO GO:0006935; P:chemotaxis; TAS:ProtInc; . GO GO:0002062; P:chondrocyte differentiation; IEA:Ensembl; . GO GO:0000077; P:DNA damage checkpoint; IEA:Ensembl; . GO GO:0019395; P:fatty acid oxidation; IEA:Ensembl; . GO GO:0006006; P:glucose metabolic process; IEA:Ensembl; . GO GO:0035556; P:intracellular signal transduction; IDA:UniProtKB; . GO GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl; . GO GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc; . GO GO:0014835; P:myoblast differentiation involved in skeletal muscle regeneration; IEA:Ensembl; . GO GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0030316; P:osteoclast differentiation; ISS:BHF-UCL; . GO GO:0038066; P:p38MAPK cascade; ISS:UniProtKB; . GO GO:0018105; P:peptidyl-serine phosphorylation; ISS:BHF-UCL; . GO GO:0001890; P:placenta development; IEA:Ensembl; . GO GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl; . GO GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl; . GO GO:0031281; P:positive regulation of cyclase activity; IMP:CACAO; . GO GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:BHF-UCL; . GO GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB; . GO GO:0046326; P:positive regulation of glucose import; IEA:Ensembl; . GO GO:2001184; P:positive regulation of interleukin-12 secretion; IMP:UniProtKB; . GO GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome; . GO GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB; . GO GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB; . GO GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB; . GO GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl; . GO GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL; . GO GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl; . GO GO:0007265; P:Ras protein signal transduction; TAS:Reactome; . GO GO:1900015; P:regulation of cytokine production involved in inflammatory response; IDA:CACAO; . GO GO:0030278; P:regulation of ossification; IEA:Ensembl; . GO GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome; . GO GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome; . GO GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB; . GO GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl; . GO GO:0035994; P:response to muscle stretch; IEA:Ensembl; . GO GO:0007165; P:signal transduction; TAS:ProtInc; . GO GO:0042770; P:signal transduction in response to DNA damage; IMP:BHF-UCL; . GO GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl; . GO GO:0090400; P:stress-induced premature senescence; IMP:BHF-UCL; . GO GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl; . GO GO:0006351; P:transcription; DNA-templated; IEA:UniProtKB-KW GO GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IEA:Ensembl; . GO GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL; . InterPro IPR011009; Kinase-like_dom; . InterPro IPR003527; MAP_kinase_CS; . InterPro IPR008352; MAPK_p38; . InterPro IPR000719; Prot_kinase_dom; . InterPro IPR017441; Protein_kinase_ATP_BS; . Pfam PF00069; Pkinase; 1; . PRINTS PR01773; P38MAPKINASE; . SMART SM00220; S_TKc; 1; . SUPFAM SSF56112; SSF56112; 1; . PROSITE PS01351; MAPK; 1; . PROSITE PS00107; PROTEIN_KINASE_ATP; 1; . PROSITE PS50011; PROTEIN_KINASE_DOM; 1; .

Gateways to other related servers

• The World-2DPAGE Constellation - Entry point to the world-wide 2-DPAGE resources.
• World-2DPAGE Repository - A public repository for gel-based proteomics data linked to protein identification published in the literature.
• World-2DPAGE Portal - A dynamic portal to query simultaneously world-wide gel-based proteomics databases.
• SWISS-2DPAGE - The Geneva Two-dimensional polyacrylamide gel electrophoresis database.
• ExPASy - The resources web server of the Swiss Institute of Bioinformatics

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