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Protein

Mitogen-activated protein kinase 8

Gene

MAPK8

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

Functioni

Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity (PubMed:10747973).2 Publications
JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7 phosphorylates Tyr-183 preferentially. Inhibited by dual specificity phosphatases, such as DUSP1. Inhibited by SERPINB3.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei55ATPPROSITE-ProRule annotation1
Active sitei151Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 40ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • histone deacetylase regulator activity Source: BHF-UCL
  • JUN kinase activity Source: UniProtKB
  • kinase activity Source: Reactome
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • cellular response to amino acid starvation Source: CAFA
  • cellular response to cadmium ion Source: CAFA
  • cellular response to cytokine stimulus Source: Reactome
  • cellular response to lipopolysaccharide Source: MGI
  • cellular response to mechanical stimulus Source: UniProtKB
  • cellular response to reactive oxygen species Source: CAFA
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • JNK cascade Source: UniProtKB
  • JUN phosphorylation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of protein binding Source: UniProtKB
  • neuron development Source: GO_Central
  • peptidyl-serine phosphorylation Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of apoptotic process Source: GO_Central
  • positive regulation of cyclase activity Source: CACAO
  • positive regulation of deacetylase activity Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  • positive regulation of protein metabolic process Source: CACAO
  • protein phosphorylation Source: CAFA
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of DNA replication origin binding Source: CAFA
  • regulation of macroautophagy Source: ParkinsonsUK-UCL
  • regulation of protein localization Source: BHF-UCL
  • response to UV Source: MGI
  • rhythmic process Source: UniProtKB-KW
  • stress-activated MAPK cascade Source: CAFA

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processBiological rhythms
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24 2681
ReactomeiR-HSA-111446 Activation of BIM and translocation to mitochondria
R-HSA-139910 Activation of BMF and translocation to mitochondria
R-HSA-193648 NRAGE signals death through JNK
R-HSA-205043 NRIF signals cell death from the nucleus
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-376172 DSCAM interactions
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-450341 Activation of the AP-1 family of transcription factors
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-9007892 Interleukin-38 signaling
SignaLinkiP45983
SIGNORiP45983

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 8 (EC:2.7.11.24)
Short name:
MAP kinase 8
Short name:
MAPK 8
Alternative name(s):
JNK-46
Stress-activated protein kinase 1c
Short name:
SAPK1c
Stress-activated protein kinase JNK1
c-Jun N-terminal kinase 1
Gene namesi
Name:MAPK8
Synonyms:JNK1, PRKM8, SAPK1, SAPK1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000107643.15
HGNCiHGNC:6881 MAPK8
MIMi601158 gene
neXtProtiNX_P45983

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi183T → A: Phosphorylation blocked. 1 Publication1
Mutagenesisi185Y → F: Phosphorylation blocked. 1 Publication1

Organism-specific databases

DisGeNETi5599
OpenTargetsiENSG00000107643
PharmGKBiPA283

Chemistry databases

ChEMBLiCHEMBL2276
DrugBankiDB07268 2-({2-[(3-HYDROXYPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)BENZAMIDE
GuidetoPHARMACOLOGYi1496

Polymorphism and mutation databases

BioMutaiMAPK8
DMDMi2507195

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001862621 – 427Mitogen-activated protein kinase 8Add BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116S-nitrosocysteineBy similarity1
Modified residuei183Phosphothreonine; by MAP2K71 Publication1
Modified residuei185Phosphotyrosine; by MAP2K41 Publication1
Modified residuei377PhosphoserineBy similarity1
Isoform 5 (identifier: P45983-5)
Modified residuei301PhosphoserineCombined sources1
Isoform 1 (identifier: P45983-2)
Modified residuei377PhosphoserineCombined sources1
Isoform 3 (identifier: P45983-3)
Modified residuei377PhosphoserineCombined sources1

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme (PubMed:11062067). Phosphorylated by TAOK2 (PubMed:17158878). May be phosphorylated at Thr-183 and Tyr-185 by MAP3K1/MEKK1 (PubMed:17761173).3 Publications

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP45983
MaxQBiP45983
PaxDbiP45983
PeptideAtlasiP45983
PRIDEiP45983

PTM databases

iPTMnetiP45983
PhosphoSitePlusiP45983

Expressioni

Gene expression databases

BgeeiENSG00000107643
CleanExiHS_MAPK8
ExpressionAtlasiP45983 baseline and differential
GenevisibleiP45983 HS

Organism-specific databases

HPAiCAB004463
CAB069396

Interactioni

Subunit structurei

Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4 (PubMed:15693750). These proteins also bind other components of the JNK signaling pathway. Interacts with TP53 and WWOX (PubMed:12514174). Interacts with JAMP (By similarity). Forms a complex with MAPK8IP1 and ARHGEF28 (By similarity). Interacts with HSF1 (via D domain and preferentially with hyperphosphorylated form); this interaction occurs under both normal growth conditions and immediately upon heat shock (PubMed:10747973). Interacts (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in undifferentiated cells (By similarity). Interacts with NFATC4 (PubMed:17875713). Interacts with MECOM; regulates JNK signaling (PubMed:10856240). Interacts with PIN1; this interaction mediates MAPK8 conformational changes leading to the binding of MAPK8 to its substrates (PubMed:21660049). Interacts with GRIPAP1 (PubMed:17761173).By similarity9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111585, 186 interactors
DIPiDIP-249N
ELMiP45983
IntActiP45983, 90 interactors
MINTiP45983
STRINGi9606.ENSP00000353483

Chemistry databases

BindingDBiP45983

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Beta strandi10 – 15Combined sources6
Beta strandi18 – 23Combined sources6
Beta strandi26 – 34Combined sources9
Beta strandi36 – 45Combined sources10
Turni46 – 49Combined sources4
Beta strandi50 – 58Combined sources9
Helixi60 – 62Combined sources3
Helixi64 – 79Combined sources16
Beta strandi83 – 85Combined sources3
Beta strandi88 – 92Combined sources5
Beta strandi94 – 97Combined sources4
Turni98 – 100Combined sources3
Beta strandi103 – 109Combined sources7
Beta strandi112 – 114Combined sources3
Helixi115 – 120Combined sources6
Helixi125 – 144Combined sources20
Helixi154 – 156Combined sources3
Beta strandi157 – 159Combined sources3
Turni161 – 163Combined sources3
Beta strandi165 – 167Combined sources3
Beta strandi174 – 177Combined sources4
Beta strandi178 – 180Combined sources3
Beta strandi182 – 184Combined sources3
Beta strandi185 – 187Combined sources3
Helixi189 – 191Combined sources3
Helixi194 – 197Combined sources4
Helixi206 – 220Combined sources15
Helixi230 – 241Combined sources12
Helixi246 – 249Combined sources4
Helixi254 – 261Combined sources8
Helixi271 – 274Combined sources4
Helixi277 – 279Combined sources3
Helixi285 – 301Combined sources17
Helixi306 – 308Combined sources3
Helixi312 – 317Combined sources6
Helixi319 – 322Combined sources4
Helixi327 – 330Combined sources4
Turni339 – 342Combined sources4
Helixi349 – 363Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UKHX-ray2.35A1-363[»]
1UKIX-ray2.70A1-363[»]
2G01X-ray3.50A/B1-364[»]
2GMXX-ray3.50A/B1-364[»]
2H96X-ray3.00A/B1-364[»]
2NO3X-ray3.20A/B1-364[»]
2XRWX-ray1.33A2-364[»]
2XS0X-ray2.60A1-379[»]
3ELJX-ray1.80A1-364[»]
3O17X-ray3.00A/B1-364[»]
3O2MX-ray2.70A/B1-364[»]
3PZEX-ray2.00A7-364[»]
3V3VX-ray2.70A1-366[»]
3VUDX-ray3.50A1-364[»]
3VUGX-ray3.24A1-364[»]
3VUHX-ray2.70A1-364[»]
3VUIX-ray2.80A1-364[»]
3VUKX-ray2.95A1-364[»]
3VULX-ray2.81A1-364[»]
3VUMX-ray2.69A1-364[»]
4AWIX-ray1.91A1-364[»]
4E73X-ray2.27A1-363[»]
4G1WX-ray2.45A1-363[»]
4HYSX-ray2.42A1-363[»]
4HYUX-ray2.15A1-363[»]
4IZYX-ray2.30A1-363[»]
4L7FX-ray1.95A7-362[»]
4QTDX-ray1.50A1-363[»]
4UX9X-ray2.34A/B/C/D1-364[»]
4YR8X-ray2.40A/C/E/F1-363[»]
5LW1X-ray3.20B/E/H2-363[»]
6F5EX-ray2.70B2-363[»]
ProteinModelPortaliP45983
SMRiP45983
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45983

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 321Protein kinasePROSITE-ProRule annotationAdd BLAST296

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi183 – 185TXY3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0665 Eukaryota
ENOG410XSHI LUCA
GeneTreeiENSGT00550000074271
HOGENOMiHOG000233024
HOVERGENiHBG014652
InParanoidiP45983
KOiK04440
OMAiPKQPFSE
PhylomeDBiP45983
TreeFamiTF105100

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR003527 MAP_kinase_CS
IPR008351 MAPK_JNK
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PRINTSiPR01772 JNKMAPKINASE
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS01351 MAPK, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P45983-1) [UniParc]FASTAAdd to basket
Also known as: JNK1-alpha-2

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
MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER
60 70 80 90 100
NVAIKKLSRP FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE
110 120 130 140 150
FQDVYIVMEL MDANLCQVIQ MELDHERMSY LLYQMLCGIK HLHSAGIIHR
160 170 180 190 200
DLKPSNIVVK SDCTLKILDF GLARTAGTSF MMTPYVVTRY YRAPEVILGM
210 220 230 240 250
GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ LGTPCPEFMK
260 270 280 290 300
KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
310 320 330 340 350
MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE
360 370 380 390 400
EWKELIYKEV MDLEERTKNG VIRGQPSPLG AAVINGSQHP SSSSSVNDVS
410 420
SMSTDPTLAS DTDSSLEAAA GPLGCCR
Length:427
Mass (Da):48,296
Last modified:November 1, 1997 - v2
Checksum:i94FB6BE0358B9B60
GO
Isoform 1 (identifier: P45983-2) [UniParc]FASTAAdd to basket
Also known as: JNK1-alpha-1

The sequence of this isoform differs from the canonical sequence as follows:
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

Show »
Length:384
Mass (Da):44,229
Checksum:iA7320EF933E9CF85
GO
Isoform 3 (identifier: P45983-3) [UniParc]FASTAAdd to basket
Also known as: JNK1-beta-1

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: L → I
     219-230: VCHKILFPGRDY → IKGGVLFPGTDH
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

Show »
Length:384
Mass (Da):44,022
Checksum:i76E49A950E64C1A1
GO
Isoform 4 (identifier: P45983-4) [UniParc]FASTAAdd to basket
Also known as: JNK1-beta-2

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: L → I
     219-230: VCHKILFPGRDY → IKGGVLFPGTDH

Show »
Length:427
Mass (Da):48,088
Checksum:i3F5CC3F6A4F3EF2D
GO
Isoform 5 (identifier: P45983-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     206-281: Missing.
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

Show »
Length:308
Mass (Da):35,333
Checksum:i914B803A1223601D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042258171G → S in a renal clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042259177G → R in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_050592365E → K. Corresponds to variant dbSNP:rs45483593Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054554206 – 281Missing in isoform 5. 1 PublicationAdd BLAST76
Alternative sequenceiVSP_004831208L → I in isoform 3 and isoform 4. 1 Publication1
Alternative sequenceiVSP_004832219 – 230VCHKI…PGRDY → IKGGVLFPGTDH in isoform 3 and isoform 4. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_004833380 – 427GAAVI…LGCCR → AQVQQ in isoform 1, isoform 3 and isoform 5. 3 PublicationsAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26318 mRNA Translation: AAA36131.1
U34822 mRNA Translation: AAC50607.1
U35004 mRNA Translation: AAC50610.1
U35005 mRNA Translation: AAC50611.1
DQ234352 mRNA Translation: ABB29981.1
AC016397 Genomic DNA No translation available.
AC074325 Genomic DNA No translation available.
AB451231 mRNA Translation: BAG70045.1
CH471187 Genomic DNA Translation: EAW93132.1
CH471187 Genomic DNA Translation: EAW93129.1
CH471187 Genomic DNA Translation: EAW93130.1
CH471187 Genomic DNA Translation: EAW93133.1
CH471187 Genomic DNA Translation: EAW93134.1
CH471187 Genomic DNA Translation: EAW93136.1
BC144063 mRNA Translation: AAI44064.1
CCDSiCCDS60527.1 [P45983-5]
CCDS7223.1 [P45983-4]
CCDS7224.1 [P45983-1]
CCDS7225.1 [P45983-2]
CCDS7226.1 [P45983-3]
PIRiS71097
S71099
RefSeqiNP_001265476.1, NM_001278547.1 [P45983-4]
NP_001265477.1, NM_001278548.1 [P45983-5]
NP_001310231.1, NM_001323302.1 [P45983-2]
NP_001310250.1, NM_001323321.1 [P45983-3]
NP_001310251.1, NM_001323322.1 [P45983-4]
NP_001310252.1, NM_001323323.1 [P45983-4]
NP_001310253.1, NM_001323324.1 [P45983-2]
NP_001310254.1, NM_001323325.1 [P45983-3]
NP_001310255.1, NM_001323326.1 [P45983-2]
NP_001310256.1, NM_001323327.1 [P45983-2]
NP_001310257.1, NM_001323328.1 [P45983-1]
NP_001310258.1, NM_001323329.1 [P45983-1]
NP_001310259.1, NM_001323330.1 [P45983-4]
NP_001310260.1, NM_001323331.1 [P45983-1]
NP_620634.1, NM_139046.3 [P45983-3]
NP_620637.1, NM_139049.3 [P45983-1]
UniGeneiHs.138211
Hs.522924

Genome annotation databases

EnsembliENST00000360332; ENSP00000353483; ENSG00000107643 [P45983-5]
ENST00000374176; ENSP00000363291; ENSG00000107643 [P45983-4]
ENST00000374179; ENSP00000363294; ENSG00000107643 [P45983-3]
ENST00000374182; ENSP00000363297; ENSG00000107643 [P45983-2]
ENST00000374189; ENSP00000363304; ENSG00000107643 [P45983-1]
ENST00000395611; ENSP00000378974; ENSG00000107643 [P45983-4]
GeneIDi5599
KEGGihsa:5599
UCSCiuc001jgm.5 human [P45983-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMK08_HUMAN
AccessioniPrimary (citable) accession number: P45983
Secondary accession number(s): B5BTZ5
, B7ZLV4, D3DX88, D3DX92, Q15709, Q15712, Q15713, Q308M2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: May 23, 2018
This is version 202 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, Reference proteome

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