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UniProtKB - Q02750 (MP2K1_HUMAN)

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Protein

Dual specificity mitogen-activated protein kinase kinase 1

Gene

MAP2K1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of 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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Ras proteins such as HRAS mediate the activation of RAF proteins such as RAF1 or BRAF which in turn activate extracellular signal-regulated kinases (ERK) through MAPK (mitogen-activated protein kinases) and ERK kinases MAP2K1/MEK1 and MAP2K2/MEK2. Activation occurs through phosphorylation of Ser-218 and Ser-222. MAP2K1/MEK1 is also the target of negative feed-back regulation by its substrate kinases, such as MAPK1/ERK2. These phosphorylate MAP2K1/MEK1 on Thr-292, thereby facilitating dephosphorylation of the activating residues Ser-218 and Ser-222. Inhibited by serine/threonine phosphatase 2A (By similarity). Many inhibitors have been identified including pyrrole derivatives, TAK-733 (one of a series of 8-methylpyrido[2,3-d]pyrimidine-4,7(3H,8H)-dione derivatives), CH4987655 and RDEA119/BAY 869766.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei77Inhibitor; via carbonyl oxygen8 Publications1
Binding sitei78Inhibitor; via amide nitrogen and carbonyl oxygen8 Publications1
Binding sitei97ATPPROSITE-ProRule annotation6 Publications1
Binding sitei97Inhibitor8 Publications1
Active sitei190Proton acceptorPROSITE-ProRule annotation1
Binding sitei190Inhibitor8 Publications1
Binding sitei194Inhibitor; via carbonyl oxygen8 Publications1
Binding sitei208ATPPROSITE-ProRule annotation6 Publications1
Binding sitei208Inhibitor8 Publications1
Binding sitei212Inhibitor; via amide nitrogen8 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi74 – 82ATPPROSITE-ProRule annotation6 Publications9
Nucleotide bindingi143 – 146ATPPROSITE-ProRule annotation6 Publications4
Nucleotide bindingi150 – 153ATPPROSITE-ProRule annotation6 Publications4
Nucleotide bindingi192 – 195ATPPROSITE-ProRule annotation6 Publications4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase kinase activity Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • protein kinase activity Source: ProtInc
  • protein N-terminus binding Source: MGI
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome
  • protein tyrosine kinase activity Source: UniProtKB-KW
  • signal transducer, downstream of receptor, with protein tyrosine phosphatase activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  • activation of MAPK activity Source: AgBase
  • Bergmann glial cell differentiation Source: Ensembl
  • cell cycle arrest Source: BHF-UCL
  • cell motility Source: Ensembl
  • cellular senescence Source: BHF-UCL
  • cerebellar cortex formation Source: Ensembl
  • chemotaxis Source: ProtInc
  • epithelial cell proliferation involved in lung morphogenesis Source: Ensembl
  • ERK1 and ERK2 cascade Source: Ensembl
  • face development Source: Ensembl
  • heart development Source: Ensembl
  • keratinocyte differentiation Source: Ensembl
  • labyrinthine layer development Source: Ensembl
  • MAPK cascade Source: Reactome
  • movement of cell or subcellular component Source: ProtInc
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of gene expression Source: UniProtKB
  • neuron differentiation Source: Ensembl
  • placenta blood vessel development Source: Ensembl
  • positive regulation of axonogenesis Source: Ensembl
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCL
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • proteolysis in other organism Source: Reactome
  • regulation of apoptotic process Source: GO_Central
  • regulation of axon regeneration Source: Ensembl
  • regulation of early endosome to late endosome transport Source: UniProtKB
  • regulation of Golgi inheritance Source: UniProtKB
  • regulation of mitotic cell cycle Source: GO_Central
  • regulation of stress-activated MAPK cascade Source: UniProtKB
  • signal transduction Source: ProtInc
  • thymus development Source: Ensembl
  • thyroid gland development Source: Ensembl
  • trachea formation Source: Ensembl
Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.2. 2681.
ReactomeiR-HSA-110056. MAPK3 (ERK1) activation.
R-HSA-445144. Signal transduction by L1.
R-HSA-5210891. Uptake and function of anthrax toxins.
R-HSA-5673000. RAF activation.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5674499. Negative feedback regulation of MAPK pathway.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
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.
SignaLinkiQ02750.
SIGNORiQ02750.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity mitogen-activated protein kinase kinase 1 (EC:2.7.12.2)
Short name:
MAP kinase kinase 1
Short name:
MAPKK 1
Short name:
MKK1
Alternative name(s):
ERK activator kinase 1
MAPK/ERK kinase 1
Short name:
MEK 1
Gene namesi
Name:MAP2K1
Synonyms:MEK1, PRKMK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:6840. MAP2K1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: HPA
  • early endosome Source: UniProtKB
  • endoplasmic reticulum Source: MGI
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • late endosome Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cardiofaciocutaneous syndrome 3 (CFC3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. Distinctive features of CFC3 include macrostomia and horizontal shape of palpebral fissures.
See also OMIM:615279
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03509353F → S in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908594Ensembl.1
Natural variantiVAR_069780128G → V in CFC3. 1 PublicationCorresponds to variant dbSNP:rs730880508Ensembl.1
Natural variantiVAR_035094130Y → C in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908595Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97K → R: Inactivation. 1 Publication1
Mutagenesisi150S → A: No loss of activity. 1 Publication1
Mutagenesisi212S → A: No loss of activity. 1 Publication1
Mutagenesisi218S → A: Inactivation. 1 Publication1
Mutagenesisi222S → A: Inactivation. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Ectodermal dysplasia, Mental retardation

Organism-specific databases

DisGeNETi5604.
MalaCardsiMAP2K1.
MIMi615279. phenotype.
OpenTargetsiENSG00000169032.
Orphaneti1340. Cardiofaciocutaneous syndrome.
PharmGKBiPA30584.

Chemistry databases

ChEMBLiCHEMBL3587.
DrugBankiDB06616. Bosutinib.
DB05239. Cobimetinib.
DB02152. K-252a.
DB08911. Trametinib.
GuidetoPHARMACOLOGYi2062.

Polymorphism and mutation databases

BioMutaiMAP2K1.
DMDMi400274.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000863652 – 393Dual specificity mitogen-activated protein kinase kinase 1Add BLAST392

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei218Phosphoserine; by RAF2 Publications1
Modified residuei222Phosphoserine; by RAF1 Publication1
Modified residuei286PhosphothreonineCombined sources1
Modified residuei292Phosphothreonine; by MAPK1By similarity1
Modified residuei298Phosphoserine; by PAK1 Publication1

Post-translational modificationi

Phosphorylation at Ser-218 and Ser-222 by MAP kinase kinase kinases (RAF or MEKK1) positively regulates kinase activity. Also phosphorylated at Thr-292 by MAPK1/ERK2 and at Ser-298 by PAK. MAPK1/ERK2 phosphorylation of Thr-292 occurs in response to cellular adhesion and leads to inhibition of Ser-298 phosphorylation by PAK.2 Publications
Acetylation by Yersinia yopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei8 – 9Cleavage; by anthrax lethal factor2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ02750.
MaxQBiQ02750.
PaxDbiQ02750.
PeptideAtlasiQ02750.
PRIDEiQ02750.

PTM databases

iPTMnetiQ02750.
PhosphoSitePlusiQ02750.

Miscellaneous databases

PMAP-CutDBiQ02750.

Expressioni

Tissue specificityi

Widely expressed, with extremely low levels in brain.1 Publication

Gene expression databases

BgeeiENSG00000169032.
CleanExiHS_MAP2K1.
ExpressionAtlasiQ02750. baseline and differential.
GenevisibleiQ02750. HS.

Organism-specific databases

HPAiCAB003834.
HPA026430.

Interactioni

Subunit structurei

Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3/ERK1 and RGS14. Forms a heterodimer with MAP2K2/MEK2. Forms heterodimers with KSR2 which further dimerize to form tetramers. Interacts with ARBB2, LAMTOR3, MAPK1/ERK2, MORG1 and RAF1 (By similarity). Interacts with PPARG and with isoform 1 of VRK2 (PubMed:20679487, PubMed:17101779). Interacts with Yersinia yopJ (PubMed:16728640). Interacts with SGK1 (PubMed:19447520). Interacts with BIRC6/bruce (PubMed:18329369). Interacts with KSR1 (PubMed:10409742).By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein C-terminus binding Source: MGI
  • protein N-terminus binding Source: MGI
Complete GO annotation...

Protein-protein interaction databases

BioGridi111590. 69 interactors.
DIPiDIP-201N.
IntActiQ02750. 64 interactors.
MINTiMINT-99632.
STRINGi9606.ENSP00000302486.

Chemistry databases

BindingDBiQ02750.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 58Combined sources15
Helixi65 – 67Combined sources3
Beta strandi68 – 76Combined sources9
Beta strandi81 – 87Combined sources7
Turni88 – 90Combined sources3
Beta strandi93 – 100Combined sources8
Helixi105 – 115Combined sources11
Helixi116 – 120Combined sources5
Beta strandi129 – 135Combined sources7
Beta strandi138 – 143Combined sources6
Helixi151 – 158Combined sources8
Helixi163 – 184Combined sources22
Helixi193 – 195Combined sources3
Beta strandi196 – 198Combined sources3
Turni200 – 202Combined sources3
Beta strandi204 – 206Combined sources3
Helixi213 – 218Combined sources6
Helixi221 – 223Combined sources3
Helixi227 – 229Combined sources3
Helixi232 – 235Combined sources4
Helixi242 – 258Combined sources17
Helixi268 – 275Combined sources8
Helixi310 – 319Combined sources10
Turni327 – 329Combined sources3
Helixi332 – 342Combined sources11
Turni346 – 348Combined sources3
Helixi352 – 356Combined sources5
Helixi359 – 366Combined sources8
Helixi371 – 379Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S9JX-ray2.40A62-393[»]
2P55X-ray2.80A62-393[»]
3DV3X-ray2.30A62-382[»]
3DY7X-ray2.70A62-393[»]
3E8NX-ray2.50A62-393[»]
3EQBX-ray2.62A62-393[»]
3EQCX-ray1.80A35-393[»]
3EQDX-ray2.10A35-393[»]
3EQFX-ray2.70A35-393[»]
3EQGX-ray2.50A35-393[»]
3EQHX-ray2.00A35-393[»]
3EQIX-ray1.90A35-393[»]
3MBLX-ray2.60A62-382[»]
3ORNX-ray2.80A62-393[»]
3OS3X-ray2.80A62-393[»]
3PP1X-ray2.70A62-382[»]
3SLSX-ray2.30A/B45-263[»]
A/B308-383[»]
3V01X-ray2.70A62-393[»]
3V04X-ray2.70A62-393[»]
3VVHX-ray2.00A/B/C62-393[»]
3W8QX-ray2.20A39-382[»]
3WIGX-ray2.70A62-393[»]
3ZLSX-ray2.50A37-383[»]
3ZLWX-ray2.12A37-383[»]
3ZLXX-ray2.20A37-383[»]
3ZLYX-ray2.11A37-383[»]
3ZM4X-ray2.37A37-383[»]
4AN2X-ray2.50A61-392[»]
4AN3X-ray2.10A61-392[»]
4AN9X-ray2.80A61-392[»]
4ANBX-ray2.20A61-392[»]
4ARKX-ray2.60A62-393[»]
4LMNX-ray2.80A62-393[»]
4MNEX-ray2.85A/D/E/H62-393[»]
4U7ZX-ray2.80A62-393[»]
4U80X-ray2.80A62-393[»]
4U81X-ray2.70A62-393[»]
5BX0X-ray2.93A37-383[»]
5EYMX-ray2.70A/B35-393[»]
5HZEX-ray2.40A37-383[»]
ProteinModelPortaliQ02750.
SMRiQ02750.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02750.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 361Protein kinasePROSITE-ProRule annotationAdd BLAST294

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 78Inhibitor binding2
Regioni144 – 146Inhibitor binding3
Regioni208 – 212Inhibitor binding5
Regioni270 – 307RAF1-bindingBy similarityAdd BLAST38

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi262 – 307Pro-richAdd BLAST46

Domaini

The proline-rich region localized between residues 270 and 307 is important for binding to RAF1 and activation of MAP2K1/MEK1.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.Curated

Phylogenomic databases

eggNOGiKOG0581. Eukaryota.
ENOG410XQ5A. LUCA.
GeneTreeiENSGT00760000119199.
HOGENOMiHOG000234206.
HOVERGENiHBG108518.
InParanoidiQ02750.
KOiK04368.
OMAiELMFGCP.
OrthoDBiEOG091G0DEC.
PhylomeDBiQ02750.
TreeFamiTF105137.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 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. AlignAdd to basket

Isoform 1 (identifier: Q02750-1) [UniParc]FASTAAdd to basket
Also known as: MKK1a

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
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL 
        60         70         80         90        100
EAFLTQKQKV GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH 
       110        120        130        140        150
LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS 
       160        170        180        190        200
LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD VKPSNILVNS 
       210        220        230        240        250
RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG 
       260        270        280        290        300
LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLSSY 
       310        320        330        340        350
GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA 
       360        370        380        390 
DLKQLMVHAF IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA AGV
Length:393
Mass (Da):43,439
Last modified:January 23, 2007 - v2
Checksum:i0344118FFC842D51
GO
Isoform 2 (identifier: Q02750-2) [UniParc]FASTAAdd to basket
Also known as: MKK1b

The sequence of this isoform differs from the canonical sequence as follows:
     147-172: Missing.

Show »
Length:367
Mass (Da):40,764
Checksum:i9944432D8705DEFD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52A → R AA sequence (PubMed:10409742).Curated1
Sequence conflicti180Missing AA sequence (PubMed:10409742).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03509353F → S in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908594Ensembl.1
Natural variantiVAR_069780128G → V in CFC3. 1 PublicationCorresponds to variant dbSNP:rs730880508Ensembl.1
Natural variantiVAR_035094130Y → C in CFC3. 1 PublicationCorresponds to variant dbSNP:rs121908595Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_040500147 – 172Missing in isoform 2. 1 PublicationAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05624 mRNA. Translation: AAA36318.1.
L11284 mRNA. No translation available.
CCDSiCCDS10216.1. [Q02750-1]
PIRiA45100.
RefSeqiNP_002746.1. NM_002755.3. [Q02750-1]
XP_016877900.1. XM_017022411.1. [Q02750-2]
UniGeneiHs.145442.
Hs.677223.

Genome annotation databases

EnsembliENST00000307102; ENSP00000302486; ENSG00000169032. [Q02750-1]
GeneIDi5604.
KEGGihsa:5604.
UCSCiuc010bhq.4. human. [Q02750-1]

Keywords - Coding sequence diversityi

Alternative splicing

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.

Entry informationi

Entry nameiMP2K1_HUMAN
AccessioniPrimary (citable) accession number: Q02750
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 194 of the entry and version 2 of the sequence. See 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 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families