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Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

ERN1

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

Functioni

Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11779464, PubMed:11175748, PubMed:12637535, PubMed:9637683, PubMed:21317875). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP (PubMed:21317875). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:21317875). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:24508390, PubMed:21317875). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11779464, PubMed:24508390, PubMed:21317875).1 Publication5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+2 Publications

Enzyme regulationi

The kinase domain is activated by trans-autophosphorylation following homodimerization (PubMed:12637535, PubMed:9637683). Kinase activity is required for activation of the endoribonuclease domain (PubMed:12637535, PubMed:9637683). Endoribonuclease activity is specifically inhibited by hydroxy-aryl-aldehydes (HAA) (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei599ATPPROSITE-ProRule annotationCombined sources2 Publications1
Active sitei688Proton acceptorPROSITE-ProRule annotationBy similarity1
Binding sitei711ATPCombined sources1 Publication1
Binding sitei892Hydroxy-aryl-aldehyde inhibitorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi577 – 585ATPPROSITE-ProRule annotationBy similarity9
Nucleotide bindingi643 – 645ATPCombined sources1 Publication3
Nucleotide bindingi690 – 693ATPCombined sources1 Publication4

GO - Molecular functioni

  • ADP binding Source: ParkinsonsUK-UCL
  • ATP binding Source: UniProtKB
  • endoribonuclease activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • Hsp70 protein binding Source: ParkinsonsUK-UCL
  • Hsp90 protein binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • magnesium ion binding Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • activation of JUN kinase activity Source: ParkinsonsUK-UCL
  • cell cycle arrest Source: UniProtKB
  • cellular response to glucose stimulus Source: ParkinsonsUK-UCL
  • cellular response to unfolded protein Source: ParkinsonsUK-UCL
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • endothelial cell proliferation Source: UniProtKB
  • insulin metabolic process Source: ParkinsonsUK-UCL
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  • IRE1-mediated unfolded protein response Source: UniProtKB
  • mRNA catabolic process Source: ParkinsonsUK-UCL
  • mRNA cleavage Source: UniProtKB
  • mRNA cleavage involved in mRNA processing Source: ParkinsonsUK-UCL
  • mRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
  • peptidyl-serine autophosphorylation Source: ParkinsonsUK-UCL
  • peptidyl-serine trans-autophosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  • positive regulation of RNA splicing Source: UniProtKB
  • positive regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • protein autophosphorylation Source: ParkinsonsUK-UCL
  • protein phosphorylation Source: UniProtKB
  • regulation of macroautophagy Source: ParkinsonsUK-UCL
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionHydrolase, Kinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Transcription, Transcription regulation, Unfolded protein response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-381070 IRE1alpha activates chaperones
SignaLinkiO75460
SIGNORiO75460

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase/endoribonuclease IRE1Curated
Alternative name(s):
Endoplasmic reticulum-to-nucleus signaling 11 Publication
Inositol-requiring protein 11 Publication
Short name:
hIRE1p1 Publication
Ire1-alpha1 Publication
Short name:
IRE1a1 Publication
Including the following 2 domains:
Serine/threonine-protein kinase (EC:2.7.11.12 Publications)
Endoribonuclease (EC:3.1.26.-1 Publication)
Gene namesi
Name:ERN1Imported
Synonyms:IRE1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000178607.15
HGNCiHGNC:3449 ERN1
MIMi604033 gene
neXtProtiNX_O75460

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 443LumenalSequence analysisAdd BLAST425
Transmembranei444 – 464HelicalSequence analysisAdd BLAST21
Topological domaini465 – 977CytoplasmicSequence analysisAdd BLAST513

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105Q → E: Impaired ability to homodimerize. 1 Publication1
Mutagenesisi109C → S: No effect on dimerization. 1 Publication1
Mutagenesisi123D → P: Abolishes ability to homodimerize. 1 Publication1
Mutagenesisi125W → A: Abolishes ability to homodimerize. 1 Publication1
Mutagenesisi148C → S: No effect on dimerization. Weakens dimer; when associated with S-332. Abolishes interaction with PDIA6. Prolonged splicing of XBP1, probably due to prolonged activation of PDIA6. Inhibits formation of oxidized multimeric forms of ERN1 in response to ER stress. 2 Publications1
Mutagenesisi332C → S: No effect on dimerization. Weakens dimer; when associated with S-148. 1 Publication1
Mutagenesisi599K → A: Loss of autophosphorylation and of endoribonuclease activity. Inhibition of growth arrest. 2 Publications1

Organism-specific databases

DisGeNETi2081
OpenTargetsiENSG00000178607
PharmGKBiPA27861

Chemistry databases

ChEMBLiCHEMBL1163101
GuidetoPHARMACOLOGYi2020

Polymorphism and mutation databases

BioMutaiERN1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002432719 – 977Serine/threonine-protein kinase/endoribonuclease IRE1Add BLAST959

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei973PhosphothreonineCombined sources1

Post-translational modificationi

Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain.3 Publications
ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities.1 Publication

Keywords - PTMi

ADP-ribosylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO75460
MaxQBiO75460
PaxDbiO75460
PeptideAtlasiO75460
PRIDEiO75460
ProteomicsDBi50021
50022 [O75460-2]

PTM databases

iPTMnetiO75460
PhosphoSitePlusiO75460

Expressioni

Tissue specificityi

Ubiquitously expressed. High levels observed in pancreatic tissue.1 Publication

Gene expression databases

BgeeiENSG00000178607
CleanExiHS_ERN1
GenevisibleiO75460 HS

Organism-specific databases

HPAiCAB009495
HPA027730

Interactioni

Subunit structurei

Monomer (PubMed:29198525, PubMed:16973740). Homodimer; disulfide-linked; homodimerization takes place in response to endoplasmic reticulum stress and promotes activation of the kinase and endoribonuclease activities (PubMed:12637535, PubMed:24508390, PubMed:16973740, PubMed:21317875). Dimer formation is driven by hydrophobic interactions within the N-terminal luminal domains and stabilized by disulfide bridges (PubMed:12637535). Interacts (via the luminal region) with DNAJB9/ERdj4; interaction takes place in unstressed cells and promotes recruitment of HSPA5/BiP (PubMed:29198525). Interacts (via the luminal region) with HSPA5/BiP; HSPA5/BiP is a negative regulator of the unfolded protein response (UPR) that prevents homodimerization of ERN1/IRE1 and subsequent activation of the protein (PubMed:12637535, PubMed:29198525). Interacts with PDIA6, a negative regulator of the UPR; the interaction is direct and disrupts homodimerization (PubMed:24508390). Interacts with DAB2IP (via PH domain); the interaction occurs in a endoplasmic reticulum stress-induced dependent manner and is required for subsequent recruitment of TRAF2 to ERN1/IRE1 (By similarity). Interacts with TAOK3 and TRAF2 (PubMed:11278723).By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • Hsp70 protein binding Source: ParkinsonsUK-UCL
  • Hsp90 protein binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi108391, 33 interactors
DIPiDIP-31711N
IntActiO75460, 22 interactors
MINTiO75460
STRINGi9606.ENSP00000401445

Chemistry databases

BindingDBiO75460

Structurei

Secondary structure

1977
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Beta strandi40 – 46Combined sources7
Turni47 – 49Combined sources3
Beta strandi52 – 57Combined sources6
Beta strandi73 – 75Combined sources3
Turni77 – 79Combined sources3
Beta strandi82 – 84Combined sources3
Beta strandi93 – 95Combined sources3
Helixi100 – 104Combined sources5
Beta strandi120 – 128Combined sources9
Beta strandi154 – 164Combined sources11
Beta strandi168 – 172Combined sources5
Beta strandi176 – 182Combined sources7
Beta strandi197 – 201Combined sources5
Beta strandi205 – 209Combined sources5
Turni211 – 213Combined sources3
Beta strandi216 – 221Combined sources6
Beta strandi226 – 231Combined sources6
Beta strandi238 – 240Combined sources3
Beta strandi243 – 246Combined sources4
Helixi247 – 264Combined sources18
Helixi273 – 279Combined sources7
Beta strandi280 – 284Combined sources5
Beta strandi286 – 288Combined sources3
Beta strandi297 – 300Combined sources4
Turni359 – 361Combined sources3
Beta strandi564 – 566Combined sources3
Beta strandi567 – 580Combined sources14
Turni581 – 583Combined sources3
Beta strandi584 – 591Combined sources8
Beta strandi594 – 601Combined sources8
Helixi603 – 605Combined sources3
Helixi606 – 617Combined sources12
Beta strandi628 – 633Combined sources6
Beta strandi638 – 642Combined sources5
Beta strandi645 – 648Combined sources4
Helixi649 – 655Combined sources7
Helixi657 – 661Combined sources5
Helixi665 – 681Combined sources17
Turni691 – 693Combined sources3
Beta strandi694 – 697Combined sources4
Turni701 – 703Combined sources3
Beta strandi707 – 709Combined sources3
Helixi712 – 714Combined sources3
Helixi740 – 743Combined sources4
Helixi754 – 768Combined sources15
Helixi778 – 780Combined sources3
Helixi781 – 787Combined sources7
Beta strandi793 – 795Combined sources3
Helixi800 – 812Combined sources13
Helixi817 – 819Combined sources3
Helixi823 – 827Combined sources5
Helixi830 – 832Combined sources3
Helixi835 – 849Combined sources15
Beta strandi854 – 856Combined sources3
Helixi857 – 865Combined sources9
Helixi867 – 870Combined sources4
Beta strandi874 – 878Combined sources5
Helixi880 – 887Combined sources8
Beta strandi888 – 890Combined sources3
Helixi897 – 909Combined sources13
Helixi911 – 913Combined sources3
Helixi916 – 922Combined sources7
Helixi927 – 936Combined sources10
Helixi940 – 947Combined sources8
Helixi948 – 951Combined sources4
Beta strandi952 – 954Combined sources3
Helixi955 – 957Combined sources3
Turni958 – 960Combined sources3

3D structure databases

ProteinModelPortaliO75460
SMRiO75460
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75460

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini571 – 832Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini835 – 963KENPROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni906 – 907Hydroxy-aryl-aldehyde inhibitor bindingBy similarity2

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1027 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00390000015684
HOGENOMiHOG000012929
HOVERGENiHBG051506
InParanoidiO75460
KOiK08852
OMAiMDWRENI
OrthoDBiEOG091G049V
PhylomeDBiO75460
TreeFamiTF313986

Family and domain databases

Gene3Di1.20.1440.180, 1 hit
2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR010513 KEN_dom
IPR038357 KEN_sf
IPR011009 Kinase-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR000719 Prot_kinase_dom
IPR018997 PUB_domain
IPR011047 Quinoprotein_ADH-like_supfam
IPR008271 Ser/Thr_kinase_AS
IPR015943 WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PF06479 Ribonuc_2-5A, 1 hit
SMARTiView protein in SMART
SM00564 PQQ, 5 hits
SM00580 PUG, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF50998 SSF50998, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51392 KEN, 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: O75460-1) [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
MPARRLLLLL TLLLPGLGIF GSTSTVTLPE TLLFVSTLDG SLHAVSKRTG
60 70 80 90 100
SIKWTLKEDP VLQVPTHVEE PAFLPDPNDG SLYTLGSKNN EGLTKLPFTI
110 120 130 140 150
PELVQASPCR SSDGILYMGK KQDIWYVIDL LTGEKQQTLS SAFADSLCPS
160 170 180 190 200
TSLLYLGRTE YTITMYDTKT RELRWNATYF DYAASLPEDD VDYKMSHFVS
210 220 230 240 250
NGDGLVVTVD SESGDVLWIQ NYASPVVAFY VWQREGLRKV MHINVAVETL
260 270 280 290 300
RYLTFMSGEV GRITKWKYPF PKETEAKSKL TPTLYVGKYS TSLYASPSMV
310 320 330 340 350
HEGVAVVPRG STLPLLEGPQ TDGVTIGDKG ECVITPSTDV KFDPGLKSKN
360 370 380 390 400
KLNYLRNYWL LIGHHETPLS ASTKMLERFP NNLPKHRENV IPADSEKKSF
410 420 430 440 450
EEVINLVDQT SENAPTTVSR DVEEKPAHAP ARPEAPVDSM LKDMATIILS
460 470 480 490 500
TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ KELEKIQLLQ QQQQQLPFHP
510 520 530 540 550
PGDTAQDGEL LDTSGPYSES SGTSSPSTSP RASNHSLCSG SSASKAGSSP
560 570 580 590 600
SLEQDDGDEE TSVVIVGKIS FCPKDVLGHG AEGTIVYRGM FDNRDVAVKR
610 620 630 640 650
ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ
660 670 680 690 700
EYVEQKDFAH LGLEPITLLQ QTTSGLAHLH SLNIVHRDLK PHNILISMPN
710 720 730 740 750
AHGKIKAMIS DFGLCKKLAV GRHSFSRRSG VPGTEGWIAP EMLSEDCKEN
760 770 780 790 800
PTYTVDIFSA GCVFYYVISE GSHPFGKSLQ RQANILLGAC SLDCLHPEKH
810 820 830 840 850
EDVIARELIE KMIAMDPQKR PSAKHVLKHP FFWSLEKQLQ FFQDVSDRIE
860 870 880 890 900
KESLDGPIVK QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL
910 920 930 940 950
LRAMRNKKHH YRELPAEVRE TLGSLPDDFV CYFTSRFPHL LAHTYRAMEL
960 970
CSHERLFQPY YFHEPPEPQP PVTPDAL
Length:977
Mass (Da):109,735
Last modified:July 1, 2008 - v2
Checksum:iA2DF808CCE015536
GO
Isoform 2 (identifier: O75460-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-70: IFGSTSTVTL...VLQVPTHVEE → VSDRGAWGGG...SPAVGGSGRA
     71-977: Missing.

Show »
Length:70
Mass (Da):6,649
Checksum:iC93BA0CB092E6204
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti190 – 191DV → EG in AAC25991 (PubMed:9637683).Curated2
Sequence conflicti768I → V in AAC25991 (PubMed:9637683).Curated1
Sequence conflicti816D → G in BAF85092 (PubMed:14702039).Curated1
Sequence conflicti824 – 825KH → ND in AAC25991 (PubMed:9637683).Curated2
Sequence conflicti880V → D in AAC25991 (PubMed:9637683).Curated1
Sequence conflicti904M → T in BAF85092 (PubMed:14702039).Curated1
Sequence conflicti924S → T in AAC25991 (PubMed:9637683).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040488244N → S in a renal clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040489418V → M1 PublicationCorresponds to variant dbSNP:rs55869215Ensembl.1
Natural variantiVAR_040490474L → R in a lung adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs186305118Ensembl.1
Natural variantiVAR_040491635R → W in a gastric adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs146710304Ensembl.1
Natural variantiVAR_040492700N → S1 PublicationCorresponds to variant dbSNP:rs918253870Ensembl.1
Natural variantiVAR_040493769S → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_040494830P → L in an ovarian serous carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03458219 – 70IFGST…THVEE → VSDRGAWGGGQLATAGSGPG QRRGAGAGVRAGSATAAARC PVSPAVGGSGRA in isoform 2. 2 PublicationsAdd BLAST52
Alternative sequenceiVSP_03458371 – 977Missing in isoform 2. 2 PublicationsAdd BLAST907

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059198 mRNA Translation: AAC25991.1
AK292403 mRNA Translation: BAF85092.1
DA254477 mRNA No translation available.
AB209869 mRNA Translation: BAD93106.1
AC005803 Genomic DNA No translation available.
AC025362 Genomic DNA No translation available.
CH471109 Genomic DNA Translation: EAW94214.1
BC130405 mRNA Translation: AAI30406.1
BC130407 mRNA Translation: AAI30408.1
BI912495 mRNA No translation available.
CCDSiCCDS45762.1 [O75460-1]
RefSeqiNP_001424.3, NM_001433.3 [O75460-1]
UniGeneiHs.133982
Hs.700027
Hs.744953

Genome annotation databases

EnsembliENST00000433197; ENSP00000401445; ENSG00000178607 [O75460-1]
ENST00000606895; ENSP00000475519; ENSG00000178607 [O75460-2]
GeneIDi2081
KEGGihsa:2081
UCSCiuc002jdz.3 human [O75460-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiERN1_HUMAN
AccessioniPrimary (citable) accession number: O75460
Secondary accession number(s): A1L457
, A8K8N8, A8MXS7, Q59EE2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 1, 2008
Last modified: July 18, 2018
This is version 183 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

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

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