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Protein

Mitogen-activated protein kinase 1

Gene

MAPK1

Organism
Homo sapiens (Human)
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. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.
Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-185 and Tyr-187 in response to external stimuli like insulin or NGF. Both phosphorylations are required for activity. This phosphorylation causes dramatic conformational changes, which enable full activation and interaction of MAPK1/ERK2 with its substrates. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54ATPPROSITE-ProRule annotation1
Binding sitei54Inhibitor6 Publications1
Binding sitei108Inhibitor; via amide nitrogen and carbonyl oxygen6 Publications1
Binding sitei114Inhibitor6 Publications1
Active sitei149Proton acceptorPROSITE-ProRule annotation1
Binding sitei154Inhibitor6 Publications1
Binding sitei166Inhibitor6 Publications1
Binding sitei167Inhibitor6 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 39ATPPROSITE-ProRule annotation9
DNA bindingi259 – 277Add BLAST19

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Repressor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01956-MONOMER.
BRENDAi2.7.11.24. 2681.
ReactomeiR-HSA-111995. phospho-PLA2 pathway.
R-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-112411. MAPK1 (ERK2) activation.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-437239. Recycling pathway of L1.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-444257. RSK activation.
R-HSA-445144. Signal transduction by L1.
R-HSA-450341. Activation of the AP-1 family of transcription factors.
R-HSA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5674499. Negative feedback regulation of MAPK pathway.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-74749. Signal attenuation.
R-HSA-879415. Advanced glycosylation endproduct receptor signaling.
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP28482.
SIGNORiP28482.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 1 (EC:2.7.11.24)
Short name:
MAP kinase 1
Short name:
MAPK 1
Alternative name(s):
ERT1
Extracellular signal-regulated kinase 2
Short name:
ERK-2
MAP kinase isoform p42
Short name:
p42-MAPK
Mitogen-activated protein kinase 2
Short name:
MAP kinase 2
Short name:
MAPK 2
Gene namesi
Name:MAPK1
Synonyms:ERK2, PRKM1, PRKM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:6871. MAPK1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: Ensembl
  • caveola Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: Ensembl
  • early endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • late endosome Source: UniProtKB
  • microtubule cytoskeleton Source: HPA
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • protein complex Source: Ensembl
  • pseudopodium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54K → R: Does not inhibit interaction with MAP2K1. 1 Publication1
Mutagenesisi176 – 179Missing : Inhibits homodimerization and interaction with TPR. 1 Publication4
Mutagenesisi185T → A: Inhibits interaction with TPR; when associated with A-187. 1 Publication1
Mutagenesisi187Y → A: Inhibits interaction with TPR; when associated with A-185. 1 Publication1
Mutagenesisi234L → A: Inhibits interaction with TPR. 1 Publication1
Mutagenesisi318D → A: Loss of dephosphorylation by PTPRJ. 2 Publications1
Mutagenesisi318D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-321. 2 Publications1
Mutagenesisi321D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-318. 1 Publication1

Organism-specific databases

DisGeNETi5594.
MalaCardsiMAPK1.
OpenTargetsiENSG00000100030.
Orphaneti261330. Distal 22q11.2 microdeletion syndrome.
PharmGKBiPA30616.

Chemistry databases

ChEMBLiCHEMBL4040.
DrugBankiDB01169. Arsenic trioxide.
DB01064. Isoprenaline.
GuidetoPHARMACOLOGYi1495.

Polymorphism and mutation databases

BioMutaiMAPK1.
DMDMi119554.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001862472 – 360Mitogen-activated protein kinase 1Add BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei29Phosphoserine; by SGK11 Publication1
Modified residuei181PhosphothreonineBy similarity1
Modified residuei185Phosphothreonine; by MAP2K1 and MAP2K2Combined sources1
Modified residuei187Phosphotyrosine; by MAP2K1 and MAP2K2Combined sources2 Publications1
Modified residuei190Phosphothreonine; by autocatalysis1 Publication1
Modified residuei246Phosphoserine1 Publication1
Modified residuei248Phosphoserine1 Publication1
Modified residuei284PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated upon KIT and FLT3 signaling (By similarity). Dually phosphorylated on Thr-185 and Tyr-187, which activates the enzyme. Undergoes regulatory phosphorylation on additional residues such as Ser-246 and Ser-248 in the kinase insert domain (KID) These phosphorylations, which are probably mediated by more than one kinase, are important for binding of MAPK1/ERK2 to importin-7 (IPO7) and its nuclear translocation. In addition, autophosphorylation of Thr-190 was shown to affect the subcellular localization of MAPK1/ERK2 as well. Ligand-activated ALK induces tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-187. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. DUSP3 and DUSP6 dephosphorylate specifically MAPK1/ERK2 and MAPK3/ERK1 whereas DUSP9 dephosphorylates a broader range of MAPKs.By similarity7 Publications
ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP28482.
PaxDbiP28482.
PeptideAtlasiP28482.
PRIDEiP28482.

2D gel databases

OGPiP28482.

PTM databases

iPTMnetiP28482.
PhosphoSitePlusiP28482.
SwissPalmiP28482.

Expressioni

Gene expression databases

BgeeiENSG00000100030.
CleanExiHS_MAPK1.
ExpressionAtlasiP28482. baseline and differential.
GenevisibleiP28482. HS.

Organism-specific databases

HPAiCAB004229.
HPA003995.
HPA005700.
HPA030069.

Interactioni

Subunit structurei

Binds both upstream activators and downstream substrates in multimolecular complexes. Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine-kinase activity. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with MORG1, PEA15 and MKNK2 (By similarity). MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation (By similarity). Interacts with DCC (By similarity). The phosphorylated form interacts with PML (isoform PML-4). Interacts with STYX.By similarity22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-959949,EBI-959949
ARRB2P321213EBI-959949,EBI-714559
cicQ9U1H02EBI-959949,EBI-98330From a different organism.
COPS6Q7L5N12EBI-959949,EBI-486838
DUSP1P285624EBI-959949,EBI-975493
Dusp2Q059222EBI-959949,EBI-7898692From a different organism.
DUSP5Q166904EBI-959949,EBI-7487376
ETS1P149213EBI-959949,EBI-913209
MAP2K1Q027502EBI-959949,EBI-492564
MAPK14Q16539-35EBI-959949,EBI-6932370
MAPK3P273613EBI-959949,EBI-73995
MBPP026872EBI-959949,EBI-908215From a different organism.
PPM1AP3581319EBI-959949,EBI-989143
PTPN7P352366EBI-959949,EBI-2265723
PTPRJQ129137EBI-959949,EBI-2264500
PTPRRQ152563EBI-959949,EBI-2265659
RPS6KA3P518123EBI-959949,EBI-1046616
U24Q695592EBI-959949,EBI-8015758From a different organism.

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111580. 223 interactors.
DIPiDIP-519N.
IntActiP28482. 76 interactors.
MINTiMINT-144006.
STRINGi9606.ENSP00000215832.

Chemistry databases

BindingDBiP28482.

Structurei

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 14Combined sources3
Beta strandi17 – 19Combined sources3
Turni22 – 24Combined sources3
Beta strandi25 – 34Combined sources10
Beta strandi37 – 44Combined sources8
Turni45 – 48Combined sources4
Beta strandi49 – 56Combined sources8
Beta strandi59 – 61Combined sources3
Helixi62 – 77Combined sources16
Beta strandi81 – 83Combined sources3
Beta strandi88 – 90Combined sources3
Turni95 – 97Combined sources3
Beta strandi101 – 106Combined sources6
Beta strandi109 – 111Combined sources3
Helixi112 – 118Combined sources7
Helixi123 – 142Combined sources20
Helixi152 – 154Combined sources3
Beta strandi155 – 157Combined sources3
Turni159 – 161Combined sources3
Beta strandi163 – 165Combined sources3
Helixi168 – 170Combined sources3
Helixi176 – 178Combined sources3
Turni181 – 185Combined sources5
Helixi191 – 193Combined sources3
Helixi196 – 200Combined sources5
Beta strandi201 – 203Combined sources3
Helixi208 – 223Combined sources16
Helixi235 – 244Combined sources10
Helixi249 – 253Combined sources5
Helixi258 – 265Combined sources8
Helixi275 – 278Combined sources4
Beta strandi279 – 282Combined sources4
Helixi284 – 293Combined sources10
Turni298 – 300Combined sources3
Helixi304 – 308Combined sources5
Helixi311 – 313Combined sources3
Turni314 – 316Combined sources3
Helixi319 – 321Combined sources3
Beta strandi331 – 333Combined sources3
Helixi335 – 337Combined sources3
Helixi340 – 351Combined sources12
Helixi352 – 354Combined sources3
Turni356 – 358Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMEX-ray2.00A1-360[»]
1TVOX-ray2.50A1-360[»]
1WZYX-ray2.50A1-360[»]
2OJGX-ray2.00A2-360[»]
2OJIX-ray2.60A2-360[»]
2OJJX-ray2.40A2-360[»]
2Y9QX-ray1.55A1-360[»]
3D42X-ray2.46B184-191[»]
3D44X-ray1.90B184-191[»]
3I5ZX-ray2.20A1-360[»]
3I60X-ray2.50A1-360[»]
3SA0X-ray1.59A1-360[»]
3TEIX-ray2.40A1-360[»]
3W55X-ray3.00A1-360[»]
4FMQX-ray2.10A1-360[»]
4FUXX-ray2.20A1-360[»]
4FUYX-ray2.00A1-360[»]
4FV0X-ray2.10A1-360[»]
4FV1X-ray1.99A1-360[»]
4FV2X-ray2.00A1-360[»]
4FV3X-ray2.20A1-360[»]
4FV4X-ray2.50A1-360[»]
4FV5X-ray2.40A1-360[»]
4FV6X-ray2.50A1-360[»]
4FV7X-ray1.90A1-360[»]
4FV8X-ray2.00A1-360[»]
4FV9X-ray2.11A1-360[»]
4G6NX-ray2.00A1-360[»]
4G6OX-ray2.20A1-360[»]
4H3PX-ray2.30A/D1-360[»]
4H3QX-ray2.20A1-360[»]
4IZ5X-ray3.19A/B/C/D8-360[»]
4IZ7X-ray1.80A/C8-360[»]
4IZAX-ray1.93A/C8-360[»]
4N0SX-ray1.80A1-360[»]
4NIFX-ray2.15B/E1-360[»]
4O6EX-ray1.95A13-360[»]
4QP1X-ray2.70A/B1-360[»]
4QP2X-ray2.23A/B1-360[»]
4QP3X-ray2.60A/B1-360[»]
4QP4X-ray2.20A/B1-360[»]
4QP6X-ray3.10A/B1-360[»]
4QP7X-ray2.25A/B1-360[»]
4QP8X-ray2.45A/B1-360[»]
4QP9X-ray2.00A1-360[»]
4QPAX-ray2.85A/B1-360[»]
4QTAX-ray1.45A1-360[»]
4QTEX-ray1.50A1-360[»]
4XJ0X-ray2.58A/B12-360[»]
4ZXTX-ray2.00A1-360[»]
4ZZMX-ray1.89A11-360[»]
4ZZNX-ray1.33A11-360[»]
4ZZOX-ray1.63A11-360[»]
5AX3X-ray2.98A1-360[»]
5BUEX-ray2.40A2-360[»]
5BUIX-ray2.12A2-360[»]
5BUJX-ray1.85A2-360[»]
5BVDX-ray1.90A2-360[»]
5BVEX-ray2.00A2-360[»]
5BVFX-ray1.90A2-360[»]
5K4IX-ray1.76A9-360[»]
5LCJX-ray1.78A1-360[»]
5LCKX-ray1.89A1-360[»]
ProteinModelPortaliP28482.
SMRiP28482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28482.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 313Protein kinasePROSITE-ProRule annotationAdd BLAST289

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni105 – 108Inhibitor-binding4
Regioni153 – 154Inhibitor-binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi185 – 187TXY3
Motifi318 – 322Cytoplasmic retention motif5
Motifi327 – 333Nuclear translocation motif7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 9Poly-Ala8

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP28482.
KOiK04371.
OMAiEEAESHH.
OrthoDBiEOG091G08QL.
PhylomeDBiP28482.
TreeFamiTF105097.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01770. ERK1ERK2MAPK.
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

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. AlignAdd to basket

Isoform 1 (identifier: P28482-1) [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
MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR
60 70 80 90 100
VAIKKISPFE HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD
110 120 130 140 150
VYIVQDLMET DLYKLLKTQH LSNDHICYFL YQILRGLKYI HSANVLHRDL
160 170 180 190 200
KPSNLLLNTT CDLKICDFGL ARVADPDHDH TGFLTEYVAT RWYRAPEIML
210 220 230 240 250
NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI LGILGSPSQE
260 270 280 290 300
DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK
310 320 330 340 350
RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE
360
TARFQPGYRS
Length:360
Mass (Da):41,390
Last modified:January 23, 2007 - v3
Checksum:iE85D0B2A5D2D724E
GO
Isoform 2 (identifier: P28482-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     242-285: Missing.

Show »
Length:316
Mass (Da):36,432
Checksum:i6076E1767B603945
GO

Sequence cautioni

The sequence CAA77753 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91R → Q in CAA77752 (PubMed:1319925).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_047815242 – 285Missing in isoform 2. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84489 mRNA. Translation: AAA58459.1.
Z11694 mRNA. Translation: CAA77752.1.
Z11695 mRNA. Translation: CAA77753.1. Different initiation.
DQ399292 mRNA. Translation: ABD60303.1.
AP000553 Genomic DNA. No translation available.
AP000554 Genomic DNA. No translation available.
AP000555 Genomic DNA. No translation available.
BC017832 mRNA. Translation: AAH17832.1.
CCDSiCCDS13795.1. [P28482-1]
PIRiJQ1400.
RefSeqiNP_002736.3. NM_002745.4. [P28482-1]
NP_620407.1. NM_138957.3. [P28482-1]
UniGeneiHs.431850.

Genome annotation databases

EnsembliENST00000215832; ENSP00000215832; ENSG00000100030. [P28482-1]
ENST00000398822; ENSP00000381803; ENSG00000100030. [P28482-1]
ENST00000544786; ENSP00000440842; ENSG00000100030. [P28482-2]
GeneIDi5594.
KEGGihsa:5594.
UCSCiuc010gtk.2. human. [P28482-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Extracellular signal-regulated kinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84489 mRNA. Translation: AAA58459.1.
Z11694 mRNA. Translation: CAA77752.1.
Z11695 mRNA. Translation: CAA77753.1. Different initiation.
DQ399292 mRNA. Translation: ABD60303.1.
AP000553 Genomic DNA. No translation available.
AP000554 Genomic DNA. No translation available.
AP000555 Genomic DNA. No translation available.
BC017832 mRNA. Translation: AAH17832.1.
CCDSiCCDS13795.1. [P28482-1]
PIRiJQ1400.
RefSeqiNP_002736.3. NM_002745.4. [P28482-1]
NP_620407.1. NM_138957.3. [P28482-1]
UniGeneiHs.431850.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMEX-ray2.00A1-360[»]
1TVOX-ray2.50A1-360[»]
1WZYX-ray2.50A1-360[»]
2OJGX-ray2.00A2-360[»]
2OJIX-ray2.60A2-360[»]
2OJJX-ray2.40A2-360[»]
2Y9QX-ray1.55A1-360[»]
3D42X-ray2.46B184-191[»]
3D44X-ray1.90B184-191[»]
3I5ZX-ray2.20A1-360[»]
3I60X-ray2.50A1-360[»]
3SA0X-ray1.59A1-360[»]
3TEIX-ray2.40A1-360[»]
3W55X-ray3.00A1-360[»]
4FMQX-ray2.10A1-360[»]
4FUXX-ray2.20A1-360[»]
4FUYX-ray2.00A1-360[»]
4FV0X-ray2.10A1-360[»]
4FV1X-ray1.99A1-360[»]
4FV2X-ray2.00A1-360[»]
4FV3X-ray2.20A1-360[»]
4FV4X-ray2.50A1-360[»]
4FV5X-ray2.40A1-360[»]
4FV6X-ray2.50A1-360[»]
4FV7X-ray1.90A1-360[»]
4FV8X-ray2.00A1-360[»]
4FV9X-ray2.11A1-360[»]
4G6NX-ray2.00A1-360[»]
4G6OX-ray2.20A1-360[»]
4H3PX-ray2.30A/D1-360[»]
4H3QX-ray2.20A1-360[»]
4IZ5X-ray3.19A/B/C/D8-360[»]
4IZ7X-ray1.80A/C8-360[»]
4IZAX-ray1.93A/C8-360[»]
4N0SX-ray1.80A1-360[»]
4NIFX-ray2.15B/E1-360[»]
4O6EX-ray1.95A13-360[»]
4QP1X-ray2.70A/B1-360[»]
4QP2X-ray2.23A/B1-360[»]
4QP3X-ray2.60A/B1-360[»]
4QP4X-ray2.20A/B1-360[»]
4QP6X-ray3.10A/B1-360[»]
4QP7X-ray2.25A/B1-360[»]
4QP8X-ray2.45A/B1-360[»]
4QP9X-ray2.00A1-360[»]
4QPAX-ray2.85A/B1-360[»]
4QTAX-ray1.45A1-360[»]
4QTEX-ray1.50A1-360[»]
4XJ0X-ray2.58A/B12-360[»]
4ZXTX-ray2.00A1-360[»]
4ZZMX-ray1.89A11-360[»]
4ZZNX-ray1.33A11-360[»]
4ZZOX-ray1.63A11-360[»]
5AX3X-ray2.98A1-360[»]
5BUEX-ray2.40A2-360[»]
5BUIX-ray2.12A2-360[»]
5BUJX-ray1.85A2-360[»]
5BVDX-ray1.90A2-360[»]
5BVEX-ray2.00A2-360[»]
5BVFX-ray1.90A2-360[»]
5K4IX-ray1.76A9-360[»]
5LCJX-ray1.78A1-360[»]
5LCKX-ray1.89A1-360[»]
ProteinModelPortaliP28482.
SMRiP28482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111580. 223 interactors.
DIPiDIP-519N.
IntActiP28482. 76 interactors.
MINTiMINT-144006.
STRINGi9606.ENSP00000215832.

Chemistry databases

BindingDBiP28482.
ChEMBLiCHEMBL4040.
DrugBankiDB01169. Arsenic trioxide.
DB01064. Isoprenaline.
GuidetoPHARMACOLOGYi1495.

PTM databases

iPTMnetiP28482.
PhosphoSitePlusiP28482.
SwissPalmiP28482.

Polymorphism and mutation databases

BioMutaiMAPK1.
DMDMi119554.

2D gel databases

OGPiP28482.

Proteomic databases

EPDiP28482.
PaxDbiP28482.
PeptideAtlasiP28482.
PRIDEiP28482.

Protocols and materials databases

DNASUi5594.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215832; ENSP00000215832; ENSG00000100030. [P28482-1]
ENST00000398822; ENSP00000381803; ENSG00000100030. [P28482-1]
ENST00000544786; ENSP00000440842; ENSG00000100030. [P28482-2]
GeneIDi5594.
KEGGihsa:5594.
UCSCiuc010gtk.2. human. [P28482-1]

Organism-specific databases

CTDi5594.
DisGeNETi5594.
GeneCardsiMAPK1.
HGNCiHGNC:6871. MAPK1.
HPAiCAB004229.
HPA003995.
HPA005700.
HPA030069.
MalaCardsiMAPK1.
MIMi176948. gene.
neXtProtiNX_P28482.
OpenTargetsiENSG00000100030.
Orphaneti261330. Distal 22q11.2 microdeletion syndrome.
PharmGKBiPA30616.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP28482.
KOiK04371.
OMAiEEAESHH.
OrthoDBiEOG091G08QL.
PhylomeDBiP28482.
TreeFamiTF105097.

Enzyme and pathway databases

BioCyciZFISH:HS01956-MONOMER.
BRENDAi2.7.11.24. 2681.
ReactomeiR-HSA-111995. phospho-PLA2 pathway.
R-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-112411. MAPK1 (ERK2) activation.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-437239. Recycling pathway of L1.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-444257. RSK activation.
R-HSA-445144. Signal transduction by L1.
R-HSA-450341. Activation of the AP-1 family of transcription factors.
R-HSA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5674499. Negative feedback regulation of MAPK pathway.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-74749. Signal attenuation.
R-HSA-879415. Advanced glycosylation endproduct receptor signaling.
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP28482.
SIGNORiP28482.

Miscellaneous databases

ChiTaRSiMAPK1. human.
EvolutionaryTraceiP28482.
GeneWikiiMAPK1.
GenomeRNAii5594.
PROiP28482.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100030.
CleanExiHS_MAPK1.
ExpressionAtlasiP28482. baseline and differential.
GenevisibleiP28482. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01770. ERK1ERK2MAPK.
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMK01_HUMAN
AccessioniPrimary (citable) accession number: P28482
Secondary accession number(s): A8CZ64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 197 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.