Mapk14

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.By similarity

Cofactorⁱ

Mg²⁺By similarity

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 (By similarity).By similarity

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	53	ATPPROSITE-ProRule annotation		1
Active siteⁱ	150	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	30 – 38	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

apoptotic process Source: UniProtKB-KW
intracellular signal transduction
Source: UniProtKB
Inferred from sequence or structural similarityⁱ
- 7914033
p38MAPK cascade Source: UniProtKB
positive regulation of myoblast differentiation Source: UniProtKB
positive regulation of myoblast fusion Source: UniProtKB
positive regulation of myotube differentiation Source: UniProtKB
positive regulation of transcription by RNA polymerase II
Source: RGD
Inferred from mutant phenotypeⁱ
- 23589286
protein autophosphorylation
Source: RGD
Inferred from direct assayⁱ
- 16407200
protein phosphorylation
Source: RGD
Inferred from direct assayⁱ
regulation of transcription by RNA polymerase II Source: UniProtKB
response to glucose
Source: RGD
Inferred from expression patternⁱ
- 18579738
stress-activated MAPK cascade
Source: RGD
Inferred from direct assayⁱ
- 16407200
transcription, DNA-templated Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Serine/threonine-protein kinase, Transferase
Biological process	Apoptosis, Stress response, Transcription, Transcription regulation
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.11.24 5301

BRENDAⁱ

2.7.11.24 5301

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:Csbp1, Csbp2
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	70496 Mapk14

RGDⁱ

70496 Mapk14

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL4825

ChEMBLⁱ

CHEMBL4825

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity
ChainⁱPRO_0000186294	2 – 360	Mitogen-activated protein kinase 14Add BLAST		359

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineBy similarity	1
Modified residueⁱ	2	PhosphoserineCombined sources	1
Modified residueⁱ	16	PhosphothreonineBy similarity	1
Modified residueⁱ	53	N6-acetyllysineBy similarity	1
Modified residueⁱ	152	N6-acetyllysineBy similarity	1
Modified residueⁱ	180	PhosphothreonineCombined sources	1
Modified residueⁱ	182	PhosphotyrosineCombined sources	1
Modified residueⁱ	323	Phosphotyrosine; by ZAP70By similarity	1

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 (By similarity). PPM1D also mediates dephosphorylation and inactivation of MAPK14 (By similarity).By similarity

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

PaxDbⁱ	P70618
PRIDEⁱ	P70618

PTM databases

iPTMnetⁱ	P70618
PhosphoSitePlusⁱ	P70618

Interactionⁱ

Subunit structureⁱ

Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity). Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR (By similarity). This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation (By similarity). Interacts with SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may regulate its dephosphorylation (By similarity).By similarity

GO - Molecular functionⁱ

protein C-terminus binding
Source: RGD
Inferred from physical interactionⁱ
- 16407200

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-29878N
IntActⁱ	P70618, 2 interactors
Molecular INTeraction database More...MINTⁱ	P70618
STRINGⁱ	10116.ENSRNOP00000000617

Chemistry databases

BindingDBⁱ

P70618

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P70618
SMRⁱ	P70618
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	24 – 308	Protein kinasePROSITE-ProRule annotationAdd BLAST		285

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	180 – 182	TXY		3

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

Phylogenomic databases

eggNOGⁱ	KOG0660 Eukaryota ENOG410XNY0 LUCA
HOGENOMⁱ	HOG000233024
HOVERGENⁱ	HBG014652
InParanoidⁱ	P70618
PhylomeDBⁱ	P70618

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd07877 STKc_p38alpha, 1 hit
InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR003527 MAP_kinase_CS IPR008352 MAPK_p38-like IPR038784 p38alpha IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
PRINTSⁱ	PR01773 P38MAPKINASE
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS01351 MAPK, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: P70618-1) [UniParc]FASTA Add 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 QELNKTVWEV 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 EPYDQSFESR DFLIDEWKSL TYDEVISFVP 
       360
PPLDQEEMES

Length:360

Mass (Da):41,321

Last modified:January 23, 2007 - v3

Checksum:ⁱ59FBF1FC3398C5CA

GO

Isoform 2 (identifier: P70618-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MSQERPTFYR QELNKTVWEV 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 TLFPGTDHIN QLQQIMRLTG TPPAYLINRM 
       260        270        280        290        300
PSHEARNYIQ SLAQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA 
       310        320        330        340        350
QALAHAYFAQ YHDPDDEPVA EPYDQSFESR DFLIDEWKSL TYDEVISFVP 
       360
PPLDQEEMES

Show »

Length:360

Mass (Da):41,521

Checksum:ⁱ77B9CC122D86E06D

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	59	F → V in AAB51285 (Ref. 2) Curated	1
Sequence conflictⁱ	61	S → P in AAB51285 (Ref. 2) Curated	1
Sequence conflictⁱ	68	T → S in AAB51285 (Ref. 2) Curated	1
Sequence conflictⁱ	321	E → D in AAB51285 (Ref. 2) Curated	1
Sequence conflictⁱ	321	E → D in AAK15541 (Ref. 3) Curated	1
Sequence conflictⁱ	332	F → L in AAB51285 (Ref. 2) Curated	1
Sequence conflictⁱ	332	F → L in AAK15541 (Ref. 3) Curated	1
Sequence conflictⁱ	359	E → D in AAB51285 (Ref. 2) Curated	1
Sequence conflictⁱ	359	E → D in AAK15541 (Ref. 3) Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_004847	230 – 254	DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform 2. 1 PublicationAdd BLAST		25

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U73142 mRNA Translation: AAC71059.1 U91847 mRNA Translation: AAB51285.1 AF346293 mRNA Translation: AAK15541.1
UniGeneⁱ	Rn.88085

Genome annotation databases

UCSC genome browser More...UCSCⁱ	RGD:70496 rat [P70618-1]

UCSCⁱ

RGD:70496 rat [P70618-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P70618	Mitogen-activated protein kinase 14	)	HUMAN		360
Mitogen-activated protein kinase		CALJA		360
Mitogen-activated protein kinase		PANTR		360
Mitogen-activated protein kinase		SHEEP		360
Mitogen-activated protein kinase		SAIBB		360
+239
P70618-2	UPI000268A614		HUMAN		383
UPI00093C9263		great roundleaf bat		362
Mitogen-activated protein kinase		DANRE		361
UPI00033330EB		JACJA		360
UPI00032AF3F9		OCHPR		360
+22

Protein	Similar proteins		Species	Score	Length
P70618	Mitogen-activated protein kinase 14	)	HUMAN		360
Mitogen-activated protein kinase		CALJA		360
Mitogen-activated protein kinase		PANTR		360
Mitogen-activated protein kinase		SHEEP		360
Mitogen-activated protein kinase		SAIBB		360
+246
P70618-2	UPI0003EDD7F1		LEPWE		365
UPI00045E0B73		CHLSB		302
UPI000CEAB8BD		PHYCD		345
UPI000268A614		HUMAN		383
UPI00093C9263		great roundleaf bat		362
+68

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U73142 mRNA Translation: AAC71059.1 U91847 mRNA Translation: AAB51285.1 AF346293 mRNA Translation: AAK15541.1
UniGeneⁱ	Rn.88085

3D structure databases

ProteinModelPortalⁱ	P70618
SMRⁱ	P70618
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-29878N
IntActⁱ	P70618, 2 interactors
Molecular INTeraction database More...MINTⁱ	P70618
STRINGⁱ	10116.ENSRNOP00000000617

Chemistry databases

BindingDBⁱ	P70618
ChEMBLⁱ	CHEMBL4825

PTM databases

iPTMnetⁱ	P70618
PhosphoSitePlusⁱ	P70618

Proteomic databases

PaxDbⁱ	P70618
PRIDEⁱ	P70618

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

UCSC genome browser More...UCSCⁱ	RGD:70496 rat [P70618-1]

UCSCⁱ

RGD:70496 rat [P70618-1]

Organism-specific databases

Rat genome database More...RGDⁱ	70496 Mapk14

RGDⁱ

70496 Mapk14

Phylogenomic databases

eggNOGⁱ	KOG0660 Eukaryota ENOG410XNY0 LUCA
HOGENOMⁱ	HOG000233024
HOVERGENⁱ	HBG014652
InParanoidⁱ	P70618
PhylomeDBⁱ	P70618

Enzyme and pathway databases

BRENDAⁱ	2.7.11.24 5301

BRENDAⁱ

2.7.11.24 5301

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P70618

PROⁱ

PR:P70618

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd07877 STKc_p38alpha, 1 hit
InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR003527 MAP_kinase_CS IPR008352 MAPK_p38-like IPR038784 p38alpha IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit
PRINTSⁱ	PR01773 P38MAPKINASE
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS01351 MAPK, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MK14_RAT
Accessionⁱ	P70618Primary (citable) accession number: P70618 Secondary accession number(s): O08594, Q99MG4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	January 23, 2007
	Last modified:	June 20, 2018
	This is version 161 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

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Proteomes

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Supporting data

UniProtKB - P70618 (MK14_RAT)

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Mitogen-activated protein kinase 14

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Nucleus

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ