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UniProtKB - Q9UKV5 (AMFR_HUMAN)

Entry version 184 (10 Feb 2021)
Sequence version 2 (01 Jun 2003)
Previous versions | rss
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Protein

E3 ubiquitin-protein ligase AMFR

Gene

AMFR

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

E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins, such as CD3D, CYP3A4, CFTR, INSIG1, SOAT2/ACAT2 and APOB for proteasomal degradation (PubMed:10456327, PubMed:11724934, PubMed:12670940, PubMed:19103148, PubMed:24424410, PubMed:28604676). Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD) (PubMed:10456327, PubMed:11724934, PubMed:19103148, PubMed:24424410). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG1 complex at the ER membrane (PubMed:16168377, PubMed:22143767). In addition, interaction of AMFR with AUP1 facilitates interaction of AMFR with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase RNF139, leading to sterol-induced HMGCR ubiquitination (PubMed:23223569). The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction (PubMed:16168377, PubMed:22143767, PubMed:23223569). In addition to ubiquitination on lysine residues, catalyzes ubiquitination on cysteine residues: together with INSIG1, mediates polyubiquitination of SOAT2/ACAT2 at 'Cys-277', leading to its degradation when the lipid levels are low (PubMed:28604676). Catalyzes ubiquitination and subsequent degradation of INSIG1 when cells are depleted of sterols (PubMed:17043353). Mediates polyubiquitination of INSIG2 at 'Cys-215' in some tissues, leading to its degradation (PubMed:31953408). Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex (PubMed:21636303). Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation (PubMed:21636303). Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor (PubMed:10456327). In association with LMBR1L and UBAC2, negatively regulates the canonical Wnt signaling pathway in the lymphocytes by promoting the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (PubMed:31073040).13 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.Curated EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri341 – 379RING-typePROSITE-ProRule annotationAdd BLAST39

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionReceptor, Transferase
Biological processUbl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.2.B10, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9UKV5

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-HSA-901032, ER Quality Control Compartment (ERQC)

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9UKV5

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

<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%5Fand%5Ftaxonomy%5Fsection">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:
E3 ubiquitin-protein ligase AMFR (EC:2.3.2.27Curated)
Alternative name(s):
Autocrine motility factor receptor1 Publication
Short name:
AMF receptor1 Publication
RING finger protein 45
gp781 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:AMFR1 PublicationImported
Synonyms:RNF45Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 16

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:463, AMFR

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603243, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UKV5

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000159461.14

<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%5Flocation%5Fsection">'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>Transmembranei82 – 102HelicalSequence analysisAdd BLAST21
Transmembranei122 – 142HelicalSequence analysisAdd BLAST21
Transmembranei145 – 165HelicalSequence analysisAdd BLAST21
Transmembranei186 – 206HelicalSequence analysisAdd BLAST21
Transmembranei215 – 235HelicalSequence analysisAdd BLAST21
Transmembranei276 – 296HelicalSequence analysisAdd BLAST21
Transmembranei429 – 449HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi341 – 344CAIC → AAIA: Decreased palmitoylation. 1 Publication4
Mutagenesisi356C → A: Decreased palmitoylation. No degradation of HMGCR. 2 Publications1
Mutagenesisi364C → A: Decreased palmitoylation. 1 Publication1
Mutagenesisi375 – 378CPTC → APTA: Decreased palmitoylation. 1 Publication4

Organism-specific databases

DisGeNET

More...DisGeNETi		267

Open Targets

More...OpenTargetsi		ENSG00000159461

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24768

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9UKV5, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		AMFR

Domain mapping of disease mutations (DMDM)

More...DMDMi		34922250

<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 describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000645791 – 643E3 ubiquitin-protein ligase AMFRAdd BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei516PhosphoserineCombined sources1
Modified residuei523PhosphoserineCombined sources1
Modified residuei542PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Palmitoylation of the RING-type zing finger by ZDHHC6 promotes localization to the peripheral endoplasmic reticulum.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9UKV5

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9UKV5

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9UKV5

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9UKV5

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9UKV5

PeptideAtlas

More...PeptideAtlasi		Q9UKV5

PRoteomics IDEntifications database

More...PRIDEi		Q9UKV5

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		54350
84893

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UKV5

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9UKV5

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q9UKV5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000159461, Expressed in testis and 237 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9UKV5, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9UKV5, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000159461, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with RNF5 (By similarity). Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation (By similarity).

Interacts with DERL1 (PubMed:16186510).

Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7 (PubMed:11724934).

Component of the VCP/p97-AMFR/gp78 complex that enhances VCP/p97 binding to polyubiquitinated proteins for their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).

Interacts (via the VIM) with VCP/p97 (PubMed:16168377, PubMed:16186510).

Interacts (via its membrane domain) with INSIG1; the interaction initiates the sterol-mediated ubiquitination and degradation of HMGCR by the ERAD pathway (PubMed:16168377, PubMed:22143767).

Interacts with AUP1, UBE2G2 and RNF139/TRC8; interaction with AUP1 facilitates interaction of AMFR with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase RNF139, leading to sterol-induced ubiquitination of HMGCR and its subsequent proteasomal degradation (PubMed:23223569).

Interacts with BAG6 (PubMed:21636303).

Interacts with USP13 (via UBA 2 domain); the interaction is direct (PubMed:24424410).

Interacts with LMBR1L (PubMed:31073040).

Interacts with UBAC2 and CTNNB1 (By similarity).

Interacts with C18orf32 (PubMed:29275994).

By similarity1 Publication9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106764, 150 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9UKV5

Database of interacting proteins

More...DIPi		DIP-29060N

Protein interaction database and analysis system

More...IntActi		Q9UKV5, 70 interactors

Molecular INTeraction database

More...MINTi		Q9UKV5

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000290649

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9UKV5, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q9UKV5

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9UKV5

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9UKV5

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini456 – 498CUEPROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni622 – 640VCP/p97-interacting motif (VIM)1 PublicationAdd BLAST19

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The CUE domain is required for recognition of misfolded proteins such as mutant CFTR.By similarity
The VCP/p97-interacting motif (VIM) is sufficient for binding VCP/p97 to form a complex capable of transferring VCP/p97 from the cytosol to microsomes.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri341 – 379RING-typePROSITE-ProRule annotationAdd BLAST39

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0802, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156482

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_015061_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9UKV5

Identification of Orthologs from Complete Genome Data

More...OMAi		GHVIMRY

Database of Orthologous Groups

More...OrthoDBi		897451at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9UKV5

TreeFam database of animal gene trees

More...TreeFami		TF320052

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00226

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR040675, AMFR_Ube2g2-bd
IPR003892, CUE
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02845, CUE, 1 hit
PF18442, G2BR, 1 hit
PF13639, zf-RING_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00546, CUE, 1 hit
SM00184, RING, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51140, CUE, 1 hit
PS50089, ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q9UKV5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPLLFLERFP WPSLRTYTGL SGLALLGTII SAYRALSQPE AGPGEPDQLT 
        60         70         80         90        100
ASLQPEPPAP ARPSAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK 
       110        120        130        140        150
LIQCIVFGPL RVSERQHLKD KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL 
       160        170        180        190        200
WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM SSHGRVLSLL VAMLLSCCGL 
       210        220        230        240        250
AAVCSITGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH LWDLNHEGTW 
       260        270        280        290        300
EGKGTYVYYT DFVMELTLLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY 
       310        320        330        340        350
LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA 
       360        370        380        390        400
ARKLPCGHLF HNSCLRSWLE QDTSCPTCRM SLNIADNNRV REEHQGENLD 
       410        420        430        440        450
ENLVPVAAAE GRPRLNQHNH FFHFDGSRIA SWLPSFSVEV MHTTNILGIT 
       460        470        480        490        500
QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL QLTRSVEITT DNILEGRIQV 
       510        520        530        540        550
PFPTQRSDSI RPALNSPVER PSSDQEEGET SAQTERVPLD LSPRLEETLD 
       560        570        580        590        600
FGEVEVEPSE VEDFEARGSR FSKSADERQR MLVQRKDELL QQARKRFLNK 
       610        620        630        640 
SSEDDAASES FLPSEGASSD PVTLRRRMLA AAAERRLQKQ QTS
Length:643
Mass (Da):72,996
Last modified:June 1, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8782324609C0E62A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
R4GNG2R4GNG2_HUMAN
E3 ubiquitin-protein ligase AMFR
AMFR
299Annotation score:

Annotation score:2 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>
H3BRK9H3BRK9_HUMAN
E3 ubiquitin-protein ligase AMFR
AMFR
288Annotation score:

Annotation score:1 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>
H3BQM3H3BQM3_HUMAN
E3 ubiquitin-protein ligase AMFR
AMFR
165Annotation score:

Annotation score:1 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>
H3BSK3H3BSK3_HUMAN
E3 ubiquitin-protein ligase AMFR
AMFR
229Annotation score:

Annotation score:1 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA36671 differs from that shown. Several sequencing errors.Curated
The sequence AAA79362 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti406V → D in AAA79362 (PubMed:7626106).Curated1
Sequence conflicti491D → V in AAA79362 (PubMed:7626106).Curated1
Sequence conflicti500V → L in AAA79362 (PubMed:7626106).Curated1
Sequence conflicti614S → L in AAD56722 (PubMed:10456327).Curated1

Natural variant

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_035790605D → V in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs373191257Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF124145 mRNA Translation: AAD56722.1
BC069197 mRNA Translation: AAH69197.1
L35233 mRNA Translation: AAA79362.1 Frameshift.
M63175 mRNA Translation: AAA36671.1 Sequence problems.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10758.1

Protein sequence database of the Protein Information Resource

More...PIRi		A39877

NCBI Reference Sequences

More...RefSeqi		NP_001135.3, NM_001144.5
NP_001310441.1, NM_001323512.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000290649; ENSP00000290649; ENSG00000159461

Database of genes from NCBI RefSeq genomes

More...GeneIDi		267

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:267

UCSC genome browser

More...UCSCi		uc002eiy.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124145 mRNA Translation: AAD56722.1
BC069197 mRNA Translation: AAH69197.1
L35233 mRNA Translation: AAA79362.1 Frameshift.
M63175 mRNA Translation: AAA36671.1 Sequence problems.
CCDSiCCDS10758.1
PIRiA39877
RefSeqiNP_001135.3, NM_001144.5
NP_001310441.1, NM_001323512.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EJSNMR-A452-502[»]
2LVNNMR-C453-504[»]
2LVONMR-C453-504[»]
2LVPNMR-C453-504[»]
2LVQNMR-D453-504[»]
2LXHNMR-C313-393[»]
2LXPNMR-B574-600[»]
C327-384[»]
3FSHX-ray2.76C574-601[»]
3H8KX-ray1.80B573-600[»]
3TIWX-ray1.80C/D622-640[»]
4G3OX-ray1.60A456-498[»]
4LADX-ray2.30B313-393[»]
B574-600[»]
BMRBiQ9UKV5
SMRiQ9UKV5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106764, 150 interactors
CORUMiQ9UKV5
DIPiDIP-29060N
IntActiQ9UKV5, 70 interactors
MINTiQ9UKV5
STRINGi9606.ENSP00000290649

PTM databases

iPTMnetiQ9UKV5
PhosphoSitePlusiQ9UKV5
SwissPalmiQ9UKV5

Genetic variation databases

BioMutaiAMFR
DMDMi34922250

Proteomic databases

EPDiQ9UKV5
jPOSTiQ9UKV5
MassIVEiQ9UKV5
MaxQBiQ9UKV5
PaxDbiQ9UKV5
PeptideAtlasiQ9UKV5
PRIDEiQ9UKV5
ProteomicsDBi54350
84893

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		14770, 276 antibodies

Genome annotation databases

EnsembliENST00000290649; ENSP00000290649; ENSG00000159461
GeneIDi267
KEGGihsa:267
UCSCiuc002eiy.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		267
DisGeNETi267

GeneCards: human genes, protein and diseases

More...GeneCardsi		AMFR
HGNCiHGNC:463, AMFR
HPAiENSG00000159461, Low tissue specificity
MIMi603243, gene
neXtProtiNX_Q9UKV5
OpenTargetsiENSG00000159461
PharmGKBiPA24768
VEuPathDBiHostDB:ENSG00000159461.14

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0802, Eukaryota
GeneTreeiENSGT00940000156482
HOGENOMiCLU_015061_0_0_1
InParanoidiQ9UKV5
OMAiGHVIMRY
OrthoDBi897451at2759
PhylomeDBiQ9UKV5
TreeFamiTF320052

Enzyme and pathway databases

UniPathwayiUPA00143
BRENDAi2.3.2.B10, 2681
PathwayCommonsiQ9UKV5
ReactomeiR-HSA-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-HSA-901032, ER Quality Control Compartment (ERQC)
SIGNORiQ9UKV5

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		267, 18 hits in 873 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		AMFR, human
EvolutionaryTraceiQ9UKV5

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		AMFR

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		267
PharosiQ9UKV5, Tbio

Protein Ontology

More...PROi		PR:Q9UKV5
RNActiQ9UKV5, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000159461, Expressed in testis and 237 other tissues
ExpressionAtlasiQ9UKV5, baseline and differential
GenevisibleiQ9UKV5, HS

Family and domain databases

Gene3Di3.30.40.10, 1 hit
IDEALiIID00226
InterProiView protein in InterPro
IPR040675, AMFR_Ube2g2-bd
IPR003892, CUE
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF02845, CUE, 1 hit
PF18442, G2BR, 1 hit
PF13639, zf-RING_2, 1 hit
SMARTiView protein in SMART
SM00546, CUE, 1 hit
SM00184, RING, 1 hit
PROSITEiView protein in PROSITE
PS51140, CUE, 1 hit
PS50089, ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMFR_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UKV5
Secondary accession number(s): P26442, Q8IZ70
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2003
Last modified: February 10, 2021
This is version 184 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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