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Entry version 262 (08 May 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Plays a role in enhancing learning and memory performance (By similarity).By similarity20 Publications
Isoform 2 may act as an antagonist of EGF action.
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei745ATPCombined sources2 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei837Proton acceptorPROSITE-ProRule annotation1
Binding sitei855ATPCombined sources2 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1016Important for interaction with PIK3C2B1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi718 – 726ATPCombined sources1 Publication9
Nucleotide bindingi790 – 791ATPCombined sources2 Publications2

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Host cell receptor for virus entry, Kinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1227986 Signaling by ERBB2
R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1236394 Signaling by ERBB4
R-HSA-1250196 SHC1 events in ERBB2 signaling
R-HSA-1251932 PLCG1 events in ERBB2 signaling
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-177929 Signaling by EGFR
R-HSA-179812 GRB2 events in EGFR signaling
R-HSA-180292 GAB1 signalosome
R-HSA-180336 SHC1 events in EGFR signaling
R-HSA-182971 EGFR downregulation
R-HSA-1963640 GRB2 events in ERBB2 signaling
R-HSA-1963642 PI3K events in ERBB2 signaling
R-HSA-212718 EGFR interacts with phospholipase C-gamma
R-HSA-2179392 EGFR Transactivation by Gastrin
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-445144 Signal transduction by L1
R-HSA-5637810 Constitutive Signaling by EGFRvIII
R-HSA-5638303 Inhibition of Signaling by Overexpressed EGFR
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6785631 ERBB2 Regulates Cell Motility
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8847993 ERBB2 Activates PTK6 Signaling
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8857538 PTK6 promotes HIF1A stabilization
R-HSA-8863795 Downregulation of ERBB2 signaling
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
R-HSA-9009391 Non-genomic estrogen signaling
R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-HSA-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P00533

SIGNOR Signaling Network Open Resource

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SIGNORi
P00533

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P00533 Predicted

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Epidermal growth factor receptor (EC:2.7.10.1)
Alternative name(s):
Proto-oncogene c-ErbB-1
Receptor tyrosine-protein kinase erbB-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EGFR
Synonyms:ERBB, ERBB1, HER1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3236 EGFR

Online Mendelian Inheritance in Man (OMIM)

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MIMi
131550 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P00533

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

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini25 – 645ExtracellularSequence analysisAdd BLAST621
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei646 – 668HelicalSequence analysisAdd BLAST23
Topological domaini669 – 1210CytoplasmicSequence analysisAdd BLAST542

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus, Secreted

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Lung cancer (LNCR)3 Publications
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.
See also OMIM:211980
Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized.
See also OMIM:616069
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072435428G → D in NISBD2; loss of function; the mutant does not localize to the cell membrane; has diffuse cytoplasmic localization. 1 PublicationCorresponds to variant dbSNP:rs606231253EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi275Y → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication1
Mutagenesisi287F → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication1
Mutagenesisi309R → S: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287. 1 Publication1
Mutagenesisi429R → E: Abolishes autophosphorylation and activation of downstream kinases. 1 Publication1
Mutagenesisi587 – 590DGPH → AGPA: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication4
Mutagenesisi609K → A: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication1
Mutagenesisi688L → A: Strongly reduced phosphorylation. 2 Publications1
Mutagenesisi689V → A: Reduced autophosphorylation. 1 Publication1
Mutagenesisi689V → M: Constitutively activated kinase. 1 Publication1
Mutagenesisi690E → A: Reduced phosphorylation. 2 Publications1
Mutagenesisi692L → A or P: Strongly reduced phosphorylation. 2 Publications1
Mutagenesisi693T → A: Increased phosphorylation. 1 Publication1
Mutagenesisi693T → D: Strongly reduced phosphorylation. 1 Publication1
Mutagenesisi694P → A: Strongly reduced phosphorylation. 1 Publication1
Mutagenesisi699P → A: Reduced phosphorylation. 1 Publication1
Mutagenesisi700N → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi704L → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi705R → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi706I → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi745K → A or M: Abolishes kinase activity. 1 Publication1
Mutagenesisi974D → A: Strongly reduced phosphorylation. 1
Mutagenesisi977R → A: Reduced phosphorylation. 1 Publication1
Mutagenesisi1005 – 1006ED → RK: Constitutively activated kinase. 1 Publication2
Mutagenesisi1016Y → F: 50% decrease in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1197. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1092. 1 Publication1
Mutagenesisi1048 – 1210Missing : Abolishes palmitoylation. 1 PublicationAdd BLAST163
Mutagenesisi1049C → A: Decreased palmitoylation. 1 Publication1
Mutagenesisi1067Q → G: No effect on interaction with CBLC. 1 Publication1
Mutagenesisi1068R → G: Strongly decreases interaction with CBLC. 1 Publication1
Mutagenesisi1069Y → F: Abolishes interaction with CBLC. 1 Publication1
Mutagenesisi1092Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. 1 Publication1
Mutagenesisi1110Y → F: No change in interaction with PIK3C2B. 1 Publication1
Mutagenesisi1146C → A: Decreased palmitoylation. 1 Publication1
Mutagenesisi1172Y → F: No change in interaction with PIK3C2B. 1 Publication1
Mutagenesisi1197Y → F: No change in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1016. Abolishes interaction with PIK3C2B; when associated with F-1092 and F-1016. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
1956

MalaCards human disease database

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MalaCardsi
EGFR
MIMi211980 phenotype
616069 phenotype

Open Targets

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OpenTargetsi
ENSG00000146648

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
251579 Giant cell glioblastoma
251576 Gliosarcoma
294023 Neonatal inflammatory skin and bowel disease
357191 Selection of therapeutic option in non-small cell lung carcinoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA7360

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL203

Drug and drug target database

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DrugBanki
DB08916 Afatinib
DB00002 Cetuximab
DB05424 CI-1033
DB00530 Erlotinib
DB03496 Flavopiridol
DB00317 Gefitinib
DB05324 HuMax-EGFr
DB11737 Icotinib
DB04988 IGN311
DB05774 IMC-11F8
DB05900 INSM-18
DB01259 Lapatinib
DB00281 Lidocaine
DB05101 Matuzumab
DB07662 N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE
DB09559 Necitumumab
DB13164 Olmutinib
DB09330 Osimertinib
DB01269 Panitumumab
DB05374 Rindopepimut
DB07602 S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE
DB00072 Trastuzumab
DB05294 Vandetanib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1797

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EGFR

Domain mapping of disease mutations (DMDM)

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DMDMi
2811086

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 243 PublicationsAdd BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001666525 – 1210Epidermal growth factor receptorAdd BLAST1186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi31 ↔ 58Combined sources3 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_00022756N-linked (GlcNAc...) (complex) asparagine; atypical; partialCombined sources6 Publications1
Glycosylationi73N-linked (GlcNAc...) asparagine; atypicalCombined sources1 Publication1
Glycosylationi128N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi157 ↔ 187Combined sources5 Publications
Glycosylationi175N-linked (GlcNAc...) asparagineCombined sources5 Publications1
Disulfide bondi190 ↔ 199Combined sources5 Publications
Disulfide bondi194 ↔ 207Combined sources5 Publications
Glycosylationi196N-linked (GlcNAc...) asparagineCombined sources5 Publications1
Disulfide bondi215 ↔ 223Combined sources5 Publications
Disulfide bondi219 ↔ 231Combined sources5 Publications
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei229Phosphoserine1 Publication1
Disulfide bondi232 ↔ 240Combined sources5 Publications
Disulfide bondi236 ↔ 248Combined sources5 Publications
Disulfide bondi251 ↔ 260Combined sources5 Publications
Disulfide bondi264 ↔ 291Combined sources5 Publications
Disulfide bondi295 ↔ 307Combined sources
Disulfide bondi311 ↔ 326Combined sources5 Publications
Disulfide bondi329 ↔ 333Combined sources
Disulfide bondi337 ↔ 362Combined sources5 Publications
Glycosylationi352N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Glycosylationi361N-linked (GlcNAc...) asparagineCombined sources6 Publications1
Glycosylationi413N-linked (GlcNAc...) asparagineCombined sources4 Publications1
Glycosylationi444N-linked (GlcNAc...) asparagineCombined sources6 Publications1
Disulfide bondi470 ↔ 499Combined sources
Disulfide bondi506 ↔ 515Combined sources5 Publications
Disulfide bondi510 ↔ 523Combined sources5 Publications
Disulfide bondi526 ↔ 535Combined sources4 Publications
Glycosylationi528N-linked (GlcNAc...) asparagineCombined sources5 Publications1
Disulfide bondi539 ↔ 555Combined sources3 Publications
Disulfide bondi558 ↔ 571Combined sources3 Publications
Disulfide bondi562 ↔ 579Combined sources3 Publications
Glycosylationi568N-linked (GlcNAc...) asparagine; partialCombined sources5 Publications1
Disulfide bondi582 ↔ 591Combined sources3 Publications
Disulfide bondi595 ↔ 617Combined sources3 Publications
Glycosylationi603N-linked (GlcNAc...) asparagine; partialCombined sources4 Publications1
Disulfide bondi620 ↔ 628Combined sources3 Publications
Glycosylationi623N-linked (GlcNAc...) (high mannose) asparagine1 Publication1
Disulfide bondi624 ↔ 636Combined sources3 Publications
Modified residuei678Phosphothreonine; by PKC and PKD/PRKD11 Publication1
Modified residuei693Phosphothreonine; by PKD/PRKD1Combined sources3 Publications1
Modified residuei695PhosphoserineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei991PhosphoserineCombined sources1 Publication1
Modified residuei995PhosphoserineCombined sources1
Modified residuei998Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei1016Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1026PhosphoserineCombined sources1 Publication1
Modified residuei1039PhosphoserineCombined sources1
Modified residuei1041PhosphothreonineCombined sources1
Modified residuei1042PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi1049S-palmitoyl cysteine1 Publication1
Modified residuei1064PhosphoserineCombined sources1
Modified residuei1069Phosphotyrosine1 Publication1
Modified residuei1070Phosphoserine1 Publication1
Modified residuei1071Phosphoserine1 Publication1
Modified residuei1081PhosphoserineCombined sources1
Modified residuei1092Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1110Phosphotyrosine; by autocatalysis2 Publications