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P47811 - MK14_MOUSE

UniProt

P47811 - MK14_MOUSE

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Protein

Mitogen-activated protein kinase 14

Gene

Mapk14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Phosphorylates S100A9 at 'Thr-113' (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+

Enzyme regulationi

Activated by cell stresses such as DNA damage, heat shock, osmotic shock, anisomycin and sodium arsenite, as well as pro-inflammatory stimuli such as bacterial lipopolysaccharide (LPS) and interleukin-1. Activation occurs through dual phosphorylation of Thr-180 and Tyr-182 by either of two dual specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and potentially also MAP2K4/MKK4, as well as by TAB1-mediated autophosphorylation. MAPK14 phosphorylated on both Thr-180 and Tyr-182 is 10-20-fold more active than MAPK14 phosphorylated only on Thr-180, whereas MAPK14 phosphorylated on Tyr-182 alone is inactive. whereas Thr-180 is necessary for catalysis, Tyr-182 may be required for auto-activation and substrate recognition. Phosphorylated at Tyr-323 by ZAP70 in an alternative activation pathway in response to TCR signaling in T-cells. This alternative pathway is inhibited by GADD45A. Inhibited by dual specificity phosphatases, such as DUSP1, DUSP10, and DUSP16. Specifically inhibited by the binding of pyridinyl-imidazole compounds, which are cytokine-suppressive anti-inflammatory drugs (CSAID). SB203580 is an inhibitor of MAPK14.3 Publications

Kineticsi

  1. KM=212 µM for ATP (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
  2. KM=1669 µM for ATP (when only Thr-180 is phosphorylated)1 Publication
  3. KM=656 µM for EGFR peptide as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
  4. KM=2800 µM for EGFR peptide as a substrate (when only Thr-180 is phosphorylated)1 Publication
  5. KM=2.03 µM for ATF2 as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
  6. KM=20.1 µM for ATF2 as a substrate (when only Thr-180 is phosphorylated)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321Inhibitor2 Publications
Binding sitei35 – 351Inhibitor2 Publications
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Binding sitei53 – 531Inhibitor2 Publications
Binding sitei71 – 711Inhibitor2 Publications
Binding sitei109 – 1091Inhibitor; via amide nitrogen and carbonyl oxygen2 Publications
Binding sitei111 – 1111Inhibitor; via amide nitrogen2 Publications
Active sitei168 – 1681Proton acceptorPROSITE-ProRule annotation
Binding sitei168 – 1681Inhibitor2 Publications
Binding sitei169 – 1691Inhibitor; via carbonyl oxygen2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: MGI
  3. MAP kinase activity Source: UniProtKB
  4. NFAT protein binding Source: BHF-UCL
  5. protein kinase activity Source: MGI
  6. protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  1. angiogenesis Source: MGI
  2. apoptotic process Source: UniProtKB-KW
  3. cartilage condensation Source: AgBase
  4. cell morphogenesis Source: MGI
  5. cellular response to DNA damage stimulus Source: MGI
  6. cellular response to ionizing radiation Source: MGI
  7. cellular response to lipopolysaccharide Source: MGI
  8. cellular response to vascular endothelial growth factor stimulus Source: MGI
  9. chondrocyte differentiation Source: AgBase
  10. DNA damage checkpoint Source: MGI
  11. fatty acid oxidation Source: MGI
  12. glucose metabolic process Source: MGI
  13. intracellular signal transduction Source: UniProtKB
  14. lipopolysaccharide-mediated signaling pathway Source: MGI
  15. myoblast differentiation involved in skeletal muscle regeneration Source: MGI
  16. negative regulation of canonical Wnt signaling pathway Source: AgBase
  17. osteoclast differentiation Source: BHF-UCL
  18. p38MAPK cascade Source: UniProtKB
  19. peptidyl-serine phosphorylation Source: BHF-UCL
  20. positive regulation of brown fat cell differentiation Source: MGI
  21. positive regulation of erythrocyte differentiation Source: MGI
  22. positive regulation of myoblast differentiation Source: UniProtKB
  23. positive regulation of myoblast fusion Source: UniProtKB
  24. positive regulation of myotube differentiation Source: UniProtKB
  25. positive regulation of protein import into nucleus Source: MGI
  26. positive regulation of reactive oxygen species metabolic process Source: MGI
  27. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  28. protein phosphorylation Source: MGI
  29. regulation of transcription, DNA-templated Source: MGI
  30. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  31. response to lipopolysaccharide Source: MGI
  32. response to muramyl dipeptide Source: MGI
  33. signal transduction in response to DNA damage Source: MGI
  34. skeletal muscle tissue development Source: MGI
  35. stress-induced premature senescence Source: MGI
  36. striated muscle cell differentiation Source: MGI
  37. transcription, DNA-templated Source: UniProtKB-KW
  38. transmembrane receptor protein serine/threonine kinase signaling pathway Source: MGI
  39. vascular endothelial growth factor receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 3474.
ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
REACT_198696. KSRP destabilizes mRNA.
REACT_204811. Activation of the AP-1 family of transcription factors.
REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_207601. p38MAPK events.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_215063. ERK/MAPK targets.
REACT_237946. activated TAK1 mediates p38 MAPK activation.
REACT_243212. DSCAM interactions.
REACT_250548. Platelet sensitization by LDL.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_258600. CDO in myogenesis.
REACT_259068. ADP signalling through P2Y purinoceptor 1.
SABIO-RKP47811.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 14 (EC:2.7.11.24)
Short name:
MAP kinase 14
Short name:
MAPK 14
Alternative name(s):
CRK1
Mitogen-activated protein kinase p38 alpha
Short name:
MAP kinase p38 alpha
Gene namesi
Name:Mapk14
Synonyms:Crk1, Csbp1, Csbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1346865. Mapk14.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cell Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. extracellular vesicular exosome Source: MGI
  5. mitochondrion Source: MGI
  6. nucleus Source: UniProtKB
  7. spindle pole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801T → A: Phosphorylation blocked. 1 Publication
Mutagenesisi182 – 1821Y → F: Phosphorylation blocked. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 360359Mitogen-activated protein kinase 14PRO_0000186292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei16 – 161PhosphothreonineBy similarity
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei152 – 1521N6-acetyllysineBy similarity
Modified residuei180 – 1801Phosphothreonine; alternate4 Publications
Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis; alternateBy similarity
Modified residuei182 – 1821Phosphotyrosine; alternate4 Publications
Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis; alternateBy similarity
Modified residuei323 – 3231Phosphotyrosine; by ZAP70By similarity

Post-translational modificationi

Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory cytokines, environmental stress or growth factors, which activates the enzyme. Dual phosphorylation can also be mediated by TAB1-mediated autophosphorylation. TCR engagement in T-cells also leads to Tyr-323 phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16.5 Publications
Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 (By similarity).By similarity
Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP47811.
PaxDbiP47811.
PRIDEiP47811.

PTM databases

PhosphoSiteiP47811.

Expressioni

Tissue specificityi

Macrophages, monocytes, T- and B-lymphocytes. Isoform 2 is specifically expressed in kidney and liver.

Gene expression databases

BgeeiP47811.
CleanExiMM_MAPK14.
ExpressionAtlasiP47811. baseline and differential.
GenevestigatoriP47811.

Interactioni

Subunit structurei

Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR. This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation. Interacts with SPAG9, SUPT20H and GADD45A. Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60 and TAB1 (By similarity). Interacts with casein kinase II subunits CSNK2A1 and CSNK2B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DUSP9Q999562EBI-298727,EBI-3906678From a different organism.
Lcp1Q612335EBI-298727,EBI-309345
Mapk11Q9WUI110EBI-298727,EBI-645081
Mapkapk2P491382EBI-298727,EBI-298776
Slc12a2P550122EBI-298727,EBI-621078
Stk39Q9Z1W92EBI-298727,EBI-444764

Protein-protein interaction databases

BioGridi204969. 20 interactions.
DIPiDIP-31073N.
IntActiP47811. 26 interactions.
MINTiMINT-1204448.
STRINGi10090.ENSMUSP00000004990.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Beta strandi16 – 216Combined sources
Beta strandi24 – 329Combined sources
Beta strandi34 – 4310Combined sources
Turni44 – 474Combined sources
Beta strandi48 – 5710Combined sources
Helixi62 – 7716Combined sources
Beta strandi87 – 904Combined sources
Helixi96 – 983Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 1196Combined sources
Helixi124 – 14320Combined sources
Helixi153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi176 – 1827Combined sources
Helixi185 – 1884Combined sources
Helixi191 – 1933Combined sources
Beta strandi197 – 1993Combined sources
Helixi204 – 21815Combined sources
Helixi228 – 23912Combined sources
Helixi244 – 2474Combined sources
Helixi253 – 2608Combined sources
Helixi270 – 2734Combined sources
Turni274 – 2763Combined sources
Helixi279 – 28810Combined sources
Turni293 – 2953Combined sources
Helixi299 – 3035Combined sources
Helixi306 – 3083Combined sources
Turni309 – 3113Combined sources
Helixi314 – 3163Combined sources
Helixi326 – 3294Combined sources
Helixi334 – 34613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LEWX-ray2.30A13-360[»]
1LEZX-ray2.30A1-360[»]
1P38X-ray2.10A1-360[»]
1YW2X-ray2.01A1-360[»]
1YWRX-ray1.95A1-360[»]
2EWAX-ray2.10A1-360[»]
2GHLX-ray2.10A5-352[»]
2GHMX-ray2.35A5-352[»]
2GTMX-ray1.90A5-352[»]
2GTNX-ray1.80A5-352[»]
2OZAX-ray2.70B2-360[»]
2PUUX-ray2.50A5-352[»]
3P4KX-ray2.30A1-360[»]
3P5KX-ray2.09A2-360[»]
3P78X-ray2.30A2-360[»]
3P79X-ray2.10A2-360[»]
3P7AX-ray2.31A2-360[»]
3P7BX-ray1.90A2-360[»]
3P7CX-ray2.30A2-360[»]
3PY3X-ray2.10A1-360[»]
3TG1X-ray2.71A1-360[»]
4KA3X-ray2.71A1-360[»]
4LOOX-ray1.95A1-360[»]
4LOPX-ray2.05A/B/C/D1-360[»]
4LOQX-ray2.32A/B/C/D1-360[»]
ProteinModelPortaliP47811.
SMRiP47811. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 308285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1116Inhibitor-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1823TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOVERGENiHBG014652.
InParanoidiP47811.
KOiK04441.
OMAiAVNERCE.
PhylomeDBiP47811.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P47811-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSQERPTFYR QELNKTIWEV PERYQNLSPV GSGAYGSVCA AFDTKTGHRV 
        60         70         80         90        100
AVKKLSRPFQ SIIHAKRTYR ELRLLKHMKH ENVIGLLDVF TPARSLEEFN 
       110        120        130        140        150
DVYLVTHLMG ADLNNIVKCQ KLTDDHVQFL IYQILRGLKY IHSADIIHRD 
       160        170        180        190        200
LKPSNLAVNE DCELKILDFG LARHTDDEMT GYVATRWYRA PEIMLNWMHY 
       210        220        230        240        250
NQTVDIWSVG CIMAELLTGR TLFPGTDHID QLKLILRLVG TPGAELLKKI 
       260        270        280        290        300
SSESARNYIQ SLAQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA 
       310        320        330        340        350
QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP 
       360
PPLDQEEMES
Length:360
Mass (Da):41,287
Last modified:January 23, 2007 - v3
Checksum:iDFB03EBCE97BB51A
GO
Isoform 2 (identifier: P47811-2) [UniParc]FASTAAdd to Basket

Also known as: Piccolo

The sequence of this isoform differs from the canonical sequence as follows:
     255-278: ARNYIQSLAQMPKMNFANVFIGAN → DAK
     279-360: Missing.

Show »
Length:257
Mass (Da):29,540
Checksum:iABDF65DC32AF0387
GO
Isoform 3 (identifier: P47811-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-254: DQLKLILRLVGTPGAELLKKISSES → NQLQQIMRLTGTPPAYLINRMPSHE

Show »
Length:360
Mass (Da):41,487
Checksum:iF1F20352F76590BD
GO
Isoform 4 (identifier: P47811-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.

Show »
Length:283
Mass (Da):32,327
Checksum:i895D71CB69550519
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981E → G in AAF06348. 1 PublicationCurated
Sequence conflicti107 – 1082HL → LS in AAF06348. 1 PublicationCurated
Sequence conflicti115 – 1151N → R in AAF06348. 1 PublicationCurated
Sequence conflicti124 – 1241D → G in AAF06348. 1 PublicationCurated
Sequence conflicti159 – 1624NEDC → TQVI in AAF06348. 1 PublicationCurated
Sequence conflicti166 – 1661I → L in AAF06348. 1 PublicationCurated
Sequence conflicti202 – 2021Q → R in AAF06348. 1 PublicationCurated
Sequence conflicti211 – 2122CI → GF in AAF06348. 1 PublicationCurated
Sequence conflicti224 – 2241P → L in AAF06348. 1 PublicationCurated
Sequence conflicti271 – 2711A → P in AAF06348. 1 PublicationCurated
Sequence conflicti299 – 2991A → V in AAF06348. 1 PublicationCurated
Sequence conflicti315 – 3151D → Y in AAF06348. 1 PublicationCurated
Isoform 3 (identifier: P47811-3)
Sequence conflicti238 – 2381L → M in BAA19741. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7777Missing in isoform 4. 1 PublicationVSP_022359Add
BLAST
Alternative sequencei230 – 25425DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform 3. 3 PublicationsVSP_007544Add
BLAST
Alternative sequencei255 – 27824ARNYI…FIGAN → DAK in isoform 2. 1 PublicationVSP_004846Add
BLAST
Alternative sequencei279 – 36082Missing in isoform 2. 1 PublicationVSP_007545Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10871 mRNA. Translation: AAA20888.1.
D83073 mRNA. Translation: BAA19741.1.
AF128892 mRNA. Translation: AAF34818.1.
AK151348 mRNA. Translation: BAE30324.1.
AK153025 mRNA. Translation: BAE31659.1.
AK089059 mRNA. Translation: BAC40726.1.
AK133684 mRNA. Translation: BAE21782.1.
CT009661 Genomic DNA. Translation: CAQ52036.1.
CT009661 Genomic DNA. Translation: CAQ52037.1.
BC012235 mRNA. Translation: AAH12235.1.
AF195850 mRNA. Translation: AAF06348.1.
X65067 mRNA. Translation: CAA46200.1.
CCDSiCCDS28583.1. [P47811-1]
CCDS50048.1. [P47811-3]
PIRiI49066.
RefSeqiNP_001161980.1. NM_001168508.1. [P47811-3]
NP_001161985.1. NM_001168513.1. [P47811-4]
NP_001161986.1. NM_001168514.1. [P47811-4]
NP_036081.1. NM_011951.3. [P47811-1]
UniGeneiMm.311337.

Genome annotation databases

EnsembliENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436. [P47811-3]
ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436. [P47811-1]
ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436. [P47811-4]
ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436. [P47811-4]
GeneIDi26416.
KEGGimmu:26416.
UCSCiuc008brl.2. mouse. [P47811-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10871 mRNA. Translation: AAA20888.1.
D83073 mRNA. Translation: BAA19741.1.
AF128892 mRNA. Translation: AAF34818.1.
AK151348 mRNA. Translation: BAE30324.1.
AK153025 mRNA. Translation: BAE31659.1.
AK089059 mRNA. Translation: BAC40726.1.
AK133684 mRNA. Translation: BAE21782.1.
CT009661 Genomic DNA. Translation: CAQ52036.1.
CT009661 Genomic DNA. Translation: CAQ52037.1.
BC012235 mRNA. Translation: AAH12235.1.
AF195850 mRNA. Translation: AAF06348.1.
X65067 mRNA. Translation: CAA46200.1.
CCDSiCCDS28583.1. [P47811-1]
CCDS50048.1. [P47811-3]
PIRiI49066.
RefSeqiNP_001161980.1. NM_001168508.1. [P47811-3]
NP_001161985.1. NM_001168513.1. [P47811-4]
NP_001161986.1. NM_001168514.1. [P47811-4]
NP_036081.1. NM_011951.3. [P47811-1]
UniGeneiMm.311337.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LEWX-ray2.30A13-360[»]
1LEZX-ray2.30A1-360[»]
1P38X-ray2.10A1-360[»]
1YW2X-ray2.01A1-360[»]
1YWRX-ray1.95A1-360[»]
2EWAX-ray2.10A1-360[»]
2GHLX-ray2.10A5-352[»]
2GHMX-ray2.35A5-352[»]
2GTMX-ray1.90A5-352[»]
2GTNX-ray1.80A5-352[»]
2OZAX-ray2.70B2-360[»]
2PUUX-ray2.50A5-352[»]
3P4KX-ray2.30A1-360[»]
3P5KX-ray2.09A2-360[»]
3P78X-ray2.30A2-360[»]
3P79X-ray2.10A2-360[»]
3P7AX-ray2.31A2-360[»]
3P7BX-ray1.90A2-360[»]
3P7CX-ray2.30A2-360[»]
3PY3X-ray2.10A1-360[»]
3TG1X-ray2.71A1-360[»]
4KA3X-ray2.71A1-360[»]
4LOOX-ray1.95A1-360[»]
4LOPX-ray2.05A/B/C/D1-360[»]
4LOQX-ray2.32A/B/C/D1-360[»]
ProteinModelPortaliP47811.
SMRiP47811. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204969. 20 interactions.
DIPiDIP-31073N.
IntActiP47811. 26 interactions.
MINTiMINT-1204448.
STRINGi10090.ENSMUSP00000004990.

Chemistry

BindingDBiP47811.
ChEMBLiCHEMBL2336.

PTM databases

PhosphoSiteiP47811.

Proteomic databases

MaxQBiP47811.
PaxDbiP47811.
PRIDEiP47811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436. [P47811-3]
ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436. [P47811-1]
ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436. [P47811-4]
ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436. [P47811-4]
GeneIDi26416.
KEGGimmu:26416.
UCSCiuc008brl.2. mouse. [P47811-1]

Organism-specific databases

CTDi1432.
MGIiMGI:1346865. Mapk14.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOVERGENiHBG014652.
InParanoidiP47811.
KOiK04441.
OMAiAVNERCE.
PhylomeDBiP47811.
TreeFamiTF105100.

Enzyme and pathway databases

BRENDAi2.7.11.24. 3474.
ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
REACT_198696. KSRP destabilizes mRNA.
REACT_204811. Activation of the AP-1 family of transcription factors.
REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_207601. p38MAPK events.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_215063. ERK/MAPK targets.
REACT_237946. activated TAK1 mediates p38 MAPK activation.
REACT_243212. DSCAM interactions.
REACT_250548. Platelet sensitization by LDL.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_258600. CDO in myogenesis.
REACT_259068. ADP signalling through P2Y purinoceptor 1.
SABIO-RKP47811.

Miscellaneous databases

ChiTaRSiMapk14. mouse.
EvolutionaryTraceiP47811.
NextBioi304425.
PROiP47811.
SOURCEiSearch...

Gene expression databases

BgeeiP47811.
CleanExiMM_MAPK14.
ExpressionAtlasiP47811. baseline and differential.
GenevestigatoriP47811.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells."
    Han J., Lee J.-D., Bibbs L., Ulevitch R.J.
    Science 265:808-811(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. Higashitsuji H., Fujita J.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Piccolo, a new alternative spliced form of p38/CSBP1/Mxi2 that is specifically expressed in kidney and liver."
    Faccio L., Fusco C., Zervos S.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Kidney.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Pituitary and Thymus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  7. Yin Z., Li J., Sha J., Zhou Z., Lin M., Wang L.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-318 (ISOFORM 3).
    Tissue: Testis.
  8. "Novel CDC2-related protein kinases produced in murine hematopoietic stem cells."
    Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.
    Gene 124:305-306(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-186.
    Strain: CBA.
    Tissue: Bone marrow.
  9. "Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms."
    Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J., Ulevitch R.J., Davis R.J.
    Science 267:682-685(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  10. "A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase."
    Blanco-Aparicio C., Torres J., Pulido R.
    J. Cell Biol. 147:1129-1136(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPRR, SUBCELLULAR LOCATION.
  11. "Deficiency of the stress kinase p38alpha results in embryonic lethality: characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells."
    Allen M., Svensson L., Roach M., Hambor J., McNeish J., Gabel C.A.
    J. Exp. Med. 191:859-870(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
    Tissue: Embryonic stem cell.
  12. "Requirement for p38alpha in erythropoietin expression: a role for stress kinases in erythropoiesis."
    Tamura K., Sudo T., Senftleben U., Dadak A.M., Johnson R., Karin M.
    Cell 102:221-231(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
    Strain: C57BL/6J.
  13. "MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts."
    Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S.
    Mol. Cell. Biol. 22:2871-2881(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF RPS6KA5/MSK1 AND RPS6KA4/MSK2.
  14. "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors."
    Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.
    Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPAG9.
  15. "The autoimmune suppressor Gadd45alpha inhibits the T cell alternative p38 activation pathway."
    Salvador J.M., Mittelstadt P.R., Belova G.I., Fornace A.J. Jr., Ashwell J.D.
    Nat. Immunol. 6:396-402(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GADD45A, PHOSPHORYLATION AT TYR-323, AUTOPHOSPHORYLATION, ENZYME REGULATION, FUNCTION.
  16. "p38 and a p38-interacting protein are critical for downregulation of E-cadherin during mouse gastrulation."
    Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.
    Cell 125:957-969(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT20H.
  17. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states."
    Zhang Y.Y., Mei Z.Q., Wu J.W., Wang Z.X.
    J. Biol. Chem. 283:26591-26601(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-180 AND TYR-182, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  20. "In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance."
    Shi Y., Gaestel M.
    Biol. Chem. 383:1519-1536(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  21. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  22. "Mechanisms and functions of p38 MAPK signalling."
    Cuadrado A., Nebreda A.R.
    Biochem. J. 429:403-417(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  23. "The structure of mitogen-activated protein kinase p38 at 2.1-A resolution."
    Wang Z., Harkins P.C., Ulevitch R.J., Han J., Cobb M.H., Goldsmith E.J.
    Proc. Natl. Acad. Sci. U.S.A. 94:2327-2332(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  24. "Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b."
    Chang C.I., Xu B.E., Akella R., Cobb M.H., Goldsmith E.J.
    Mol. Cell 9:1241-1249(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MEF2A AND MAP2K3.
  25. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  26. Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  27. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-360 IN COMPLEX WITH MAPKAPK2.
  28. "A distinct interaction mode revealed by the crystal structure of the kinase p38alpha with the MAPK binding domain of the phosphatase MKP5."
    Zhang Y.Y., Wu J.W., Wang Z.X.
    Sci. Signal. 4:RA88-RA88(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH DUSP10, CATALYTIC ACTIVITY, DEPHOSPHORYLATION BY DUSP10, INTERACTION WITH DUSP10.
+Additional computationally mapped references.

Entry informationi

Entry nameiMK14_MOUSE
AccessioniPrimary (citable) accession number: P47811
Secondary accession number(s): B2KF37
, B2KF38, O08666, Q3U6R5, Q3UZS3, Q8C289, Q9JLV8, Q9QZ80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.