Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Angiogenin

Gene

ANG

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

Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo.4 Publications

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei37Proton acceptor1
Active sitei138Proton donor1

<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

  • actin binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • endonuclease activity Source: UniProtKB
  • heparin binding Source: UniProtKB
  • peptide binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ribonuclease activity Source: UniProtKB
  • rRNA binding Source: UniProtKB
  • signaling receptor binding Source: UniProtKB

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, DNA-binding, Endonuclease, Hydrolase, Nuclease, Protein synthesis inhibitor
Biological processAngiogenesis, Differentiation, Stress response

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-418990 Adherens junctions interactions

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P03950

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P03950

<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:
Angiogenin (EC:3.1.27.-)
Alternative name(s):
Ribonuclease 5
Short name:
RNase 5
<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:ANG
Synonyms:RNASE5
<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 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000214274.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:483 ANG

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
105850 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P03950

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasmic vesicle, 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

Amyotrophic lateral sclerosis 9 (ALS9)8 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
See also OMIM:611895
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_04414512F → S in ALS9. 1 Publication1
Natural variantiVAR_04414620P → S in ALS9. 2 Publications1
Natural variantiVAR_04414736Q → L in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; wild type far-UV CD spectra. 2 PublicationsCorresponds to variant dbSNP:rs121909535EnsemblClinVar.1
Natural variantiVAR_07302138Y → H in ALS9. 1 PublicationCorresponds to variant dbSNP:rs1032422334Ensembl.1
Natural variantiVAR_04414841K → E in ALS9; reduced ribonucleolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs121909537EnsemblClinVar.1
Natural variantiVAR_04414941K → I in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation. 4 PublicationsCorresponds to variant dbSNP:rs121909536EnsemblClinVar.1
Natural variantiVAR_07302246D → G in ALS9; homodimerization is similar to wild-type; localization in the nucleus is similar to the wild-type; reduces strongly ribonucleolytic activity. 2 Publications1
Natural variantiVAR_04415052S → N in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. 1 PublicationCorresponds to variant dbSNP:rs121909542EnsemblClinVar.1
Natural variantiVAR_04415155R → K in ALS9; marginally reduced ribonucleolytic activity; wild type far-UV CD spectra. 2 PublicationsCorresponds to variant dbSNP:rs121909538EnsemblClinVar.1
Natural variantiVAR_04415263C → W in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability. 2 PublicationsCorresponds to variant dbSNP:rs121909539EnsemblClinVar.1
Natural variantiVAR_04415364K → I in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; moderate reduction of thermal stability. 3 PublicationsCorresponds to variant dbSNP:rs121909540EnsemblClinVar.1
Natural variantiVAR_044155136P → L in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. 1 PublicationCorresponds to variant dbSNP:rs121909543EnsemblClinVar.1
Natural variantiVAR_044156137V → I in ALS9. 1 PublicationCorresponds to variant dbSNP:rs121909544EnsemblClinVar.1
Natural variantiVAR_044157138H → R in ALS9. 1 Publication1

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>Mutagenesisi29R → A: Significantly decreases binding affinity for RNH1. 1 Publication1
Mutagenesisi32H → A: Significantly decreases binding affinity for RNH1. 1 Publication1
Mutagenesisi36Q → A: Slightly decreases binding affinity for RNH1. 1 Publication1
Mutagenesisi59L → P: Homodimerization is similar to wild-type; causes mislocalization in the cytoplasm; reduces strongly ribonucleolytic activity. 1 Publication1
Mutagenesisi64K → Q: Significantly decreases binding affinity for RNH1. 2 Publications1
Mutagenesisi92N → A: Slightly decreases binding affinity for RNH1. 1 Publication1
Mutagenesisi109 – 110GG → RR: Significantly decreases binding affinity for RNH1. 1 Publication2
Mutagenesisi132E → A: Slightly decreases binding affinity for RNH1. 1 Publication1
Mutagenesisi140D → H, S or A: 15- to 18-fold increase in RNase activity. 1 Publication1
Mutagenesisi141Q → G: Over 18-fold increase in RNase activity. 1 Publication1
Mutagenesisi143 – 144IF → AA: 3- to 5-fold increase in RNase activity. 1 Publication2

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET

More...
DisGeNETi
283

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
ANG

MalaCards human disease database

More...
MalaCardsi
ANG
MIMi611895 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000214274

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

More...
Orphaneti
803 Amyotrophic lateral sclerosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24790

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5829

Drug and drug target database

More...
DrugBanki
DB04272 Citric Acid
DB03088 Pyroglutamic Acid

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ANG

Domain mapping of disease mutations (DMDM)

More...
DMDMi
113873

<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 – 241 PublicationAdd 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_000003084325 – 147Angiogenin2 PublicationsAdd BLAST123

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 residuei25Pyrrolidone carboxylic acid1 Publication1
<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 bondi50 ↔ 1051 Publication
Disulfide bondi63 ↔ 1161 Publication
Disulfide bondi81 ↔ 1311 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P03950

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

More...
PaxDbi
P03950

PeptideAtlas

More...
PeptideAtlasi
P03950

PRoteomics IDEntifications database

More...
PRIDEi
P03950

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51619

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P03950

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P03950

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

More...
PhosphoSitePlusi
P03950

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed predominantly in the liver. Also detected in endothelial cells and spinal cord neurons.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Low level expression in the developing fetus, increased in the neonate, and maximal in the adult.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000214274 Expressed in 180 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_ANG

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P03950 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P03950 HS

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:25372031). Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur.5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
106780, 9 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P03950

Protein interaction database and analysis system

More...
IntActi
P03950, 123 interactors

Molecular INTeraction database

More...
MINTi
P03950

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000336762

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P03950

<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

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P03950

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

More...
SMRi
P03950

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03950

<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

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>Regioni64 – 68Substrate binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi55 – 59Nucleolar localization signal5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410J3ET Eukaryota
ENOG410Y4FD LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000162981

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000276883

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG008396

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P03950

KEGG Orthology (KO)

More...
KOi
K16631

Identification of Orthologs from Complete Genome Data

More...
OMAi
GSIKAIC

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0YDD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P03950

TreeFam database of animal gene trees

More...
TreeFami
TF333393

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.130.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001427 RNaseA
IPR036816 RNaseA-like_dom_sf
IPR023411 RNaseA_AS
IPR023412 RNaseA_domain

The PANTHER Classification System

More...
PANTHERi
PTHR11437 PTHR11437, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00074 RnaseA, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00794 RIBONUCLEASE

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD000535 RNaseA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00092 RNAse_Pc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54076 SSF54076, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00127 RNASE_PANCREATIC, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P03950-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVMGLGVLLL VFVLGLGLTP PTLAQDNSRY THFLTQHYDA KPQGRDDRYC
60 70 80 90 100
ESIMRRRGLT SPCKDINTFI HGNKRSIKAI CENKNGNPHR ENLRISKSSF
110 120 130 140
QVTTCKLHGG SPWPPCQYRA TAGFRNVVVA CENGLPVHLD QSIFRRP
Length:147
Mass (Da):16,550
Last modified:October 23, 1986 - v1
<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:i9C462DA3C8D39ACC
GO

<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 AAH20704 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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 conflicti59L → P in AAH62698 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04414512F → S in ALS9. 1 Publication1
Natural variantiVAR_04414620P → S in ALS9. 2 Publications1
Natural variantiVAR_04414736Q → L in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; wild type far-UV CD spectra. 2 PublicationsCorresponds to variant dbSNP:rs121909535EnsemblClinVar.1
Natural variantiVAR_07302138Y → H in ALS9. 1 PublicationCorresponds to variant dbSNP:rs1032422334Ensembl.1
Natural variantiVAR_04414841K → E in ALS9; reduced ribonucleolytic activity. 2 PublicationsCorresponds to variant dbSNP:rs121909537EnsemblClinVar.1
Natural variantiVAR_04414941K → I in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation. 4 PublicationsCorresponds to variant dbSNP:rs121909536EnsemblClinVar.1
Natural variantiVAR_07302246D → G in ALS9; homodimerization is similar to wild-type; localization in the nucleus is similar to the wild-type; reduces strongly ribonucleolytic activity. 2 Publications1
Natural variantiVAR_04415052S → N in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. 1 PublicationCorresponds to variant dbSNP:rs121909542EnsemblClinVar.1
Natural variantiVAR_04415155R → K in ALS9; marginally reduced ribonucleolytic activity; wild type far-UV CD spectra. 2 PublicationsCorresponds to variant dbSNP:rs121909538EnsemblClinVar.1
Natural variantiVAR_04415263C → W in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability. 2 PublicationsCorresponds to variant dbSNP:rs121909539EnsemblClinVar.1
Natural variantiVAR_04415364K → I in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; moderate reduction of thermal stability. 3 PublicationsCorresponds to variant dbSNP:rs121909540EnsemblClinVar.1
Natural variantiVAR_04415470I → V in some ALS9 patients; pathogenicity uncertain; reduced ribonucleolytic activity; moderate reduction of thermal stability. 3 PublicationsCorresponds to variant dbSNP:rs121909541EnsemblClinVar.1
Natural variantiVAR_01314884K → E1 PublicationCorresponds to variant dbSNP:rs17560EnsemblClinVar.1
Natural variantiVAR_044155136P → L in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. 1 PublicationCorresponds to variant dbSNP:rs121909543EnsemblClinVar.1
Natural variantiVAR_044156137V → I in ALS9. 1 PublicationCorresponds to variant dbSNP:rs121909544EnsemblClinVar.1
Natural variantiVAR_044157138H → R in ALS9. 1 Publication1

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
M11567 Genomic DNA Translation: AAA51678.1
AF449647 Genomic DNA Translation: AAL67710.1
AF449648 Genomic DNA Translation: AAL67711.1
AF449649 Genomic DNA Translation: AAL67712.1
AF449650 Genomic DNA Translation: AAL67713.1
AF449651 Genomic DNA Translation: AAL67714.1
FJ236304 mRNA Translation: ACI45236.1
CR407633 mRNA Translation: CAG28561.1
AK313989 mRNA Translation: BAG36701.1
CH471078 Genomic DNA Translation: EAW66450.1
CH471078 Genomic DNA Translation: EAW66451.1
BC020704 mRNA Translation: AAH20704.1 Different initiation.
BC054880 mRNA Translation: AAH54880.1
BC062698 mRNA Translation: AAH62698.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9554.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A90498 NRHUAG

NCBI Reference Sequences

More...
RefSeqi
NP_001091046.1, NM_001097577.2
NP_001136.1, NM_001145.4

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.283749

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000336811; ENSP00000336762; ENSG00000214274
ENST00000397990; ENSP00000381077; ENSG00000214274

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
283

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:283

Keywords - Coding sequence diversityi

Polymorphism

<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_references_section">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

Functional Glycomics Gateway - Glycan Binding

Angiogenin

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11567 Genomic DNA Translation: AAA51678.1
AF449647 Genomic DNA Translation: AAL67710.1
AF449648 Genomic DNA Translation: AAL67711.1
AF449649 Genomic DNA Translation: AAL67712.1
AF449650 Genomic DNA Translation: AAL67713.1
AF449651 Genomic DNA Translation: AAL67714.1
FJ236304 mRNA Translation: ACI45236.1
CR407633 mRNA Translation: CAG28561.1
AK313989 mRNA Translation: BAG36701.1
CH471078 Genomic DNA Translation: EAW66450.1
CH471078 Genomic DNA Translation: EAW66451.1
BC020704 mRNA Translation: AAH20704.1 Different initiation.
BC054880 mRNA Translation: AAH54880.1
BC062698 mRNA Translation: AAH62698.1
CCDSiCCDS9554.1
PIRiA90498 NRHUAG
RefSeqiNP_001091046.1, NM_001097577.2
NP_001136.1, NM_001145.4
UniGeneiHs.283749

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
1A4YX-ray2.00B/E25-147[»]
1ANGX-ray2.40A25-147[»]
1AWZNMR-A25-147[»]
1B1EX-ray2.00A25-147[»]
1B1IX-ray1.80A26-147[»]
1B1JX-ray2.00A25-147[»]
1GV7X-ray2.10A26-145[»]
1H0DX-ray2.00C26-147[»]
1H52X-ray2.00A25-147[»]
1H53X-ray2.00A26-147[»]
1HBYX-ray2.00A25-147[»]
1K58X-ray2.70A25-147[»]
1K59X-ray1.80A25-147[»]
1K5AX-ray2.33A25-147[»]
1K5BX-ray1.80A25-144[»]
1UN3X-ray1.70A26-147[»]
1UN4X-ray2.10A26-147[»]
1UN5X-ray2.60A25-147[»]
2ANGX-ray2.00A25-147[»]
4AHDX-ray2.47A/B25-147[»]
4AHEX-ray2.08A25-147[»]
4AHFX-ray2.12A25-147[»]
4AHGX-ray2.45A25-147[»]
4AHHX-ray2.50A25-147[»]
4AHIX-ray2.80A25-147[»]
4AHJX-ray2.03A25-147[»]
4AHKX-ray1.97A/B25-147[»]
4AHLX-ray2.05A25-147[»]
4AHMX-ray1.96A25-147[»]
4AHNX-ray2.98A25-147[»]
4AOHX-ray1.04A24-147[»]
4B36X-ray1.76A/B25-147[»]
5EOPX-ray1.35A26-146[»]
5EPZX-ray1.85A26-145[»]
5EQOX-ray2.40A25-145[»]
5M9AX-ray1.95A25-147[»]
5M9CX-ray2.05A25-147[»]
5M9GX-ray2.28A25-147[»]
5M9JX-ray1.90A25-147[»]
5M9MX-ray1.65A/B/C/D25-147[»]
5M9PX-ray1.80A25-147[»]
5M9QX-ray1.35A25-147[»]
5M9RX-ray1.44A/B25-147[»]
5M9SX-ray1.85A25-147[»]
5M9TX-ray2.20A/B25-147[»]
5M9VX-ray1.70A25-147[»]
ProteinModelPortaliP03950
SMRiP03950
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106780, 9 interactors
CORUMiP03950
IntActiP03950, 123 interactors
MINTiP03950
STRINGi9606.ENSP00000336762

Chemistry databases

BindingDBiP03950
ChEMBLiCHEMBL5829
DrugBankiDB04272 Citric Acid
DB03088 Pyroglutamic Acid

PTM databases

iPTMnetiP03950
PhosphoSitePlusiP03950

Polymorphism and mutation databases

BioMutaiANG
DMDMi113873

Proteomic databases

EPDiP03950
PaxDbiP03950
PeptideAtlasiP03950
PRIDEiP03950
ProteomicsDBi51619
TopDownProteomicsiP03950

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
283
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336811; ENSP00000336762; ENSG00000214274
ENST00000397990; ENSP00000381077; ENSG00000214274
GeneIDi283
KEGGihsa:283

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
283
DisGeNETi283
EuPathDBiHostDB:ENSG00000214274.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ANG
GeneReviewsiANG
HGNCiHGNC:483 ANG
MalaCardsiANG
MIMi105850 gene
611895 phenotype
neXtProtiNX_P03950
OpenTargetsiENSG00000214274
Orphaneti803 Amyotrophic lateral sclerosis
PharmGKBiPA24790

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410J3ET Eukaryota
ENOG410Y4FD LUCA
GeneTreeiENSGT00940000162981
HOGENOMiHOG000276883
HOVERGENiHBG008396
InParanoidiP03950
KOiK16631
OMAiGSIKAIC
OrthoDBiEOG091G0YDD
PhylomeDBiP03950
TreeFamiTF333393

Enzyme and pathway databases

ReactomeiR-HSA-418990 Adherens junctions interactions
SABIO-RKiP03950
SIGNORiP03950

Miscellaneous databases

EvolutionaryTraceiP03950

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Angiogenin

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

More...
GenomeRNAii
283

Protein Ontology

More...
PROi
PR:P03950

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000214274 Expressed in 180 organ(s), highest expression level in liver
CleanExiHS_ANG
ExpressionAtlasiP03950 baseline and differential
GenevisibleiP03950 HS

Family and domain databases

Gene3Di3.10.130.10, 1 hit
InterProiView protein in InterPro
IPR001427 RNaseA
IPR036816 RNaseA-like_dom_sf
IPR023411 RNaseA_AS
IPR023412 RNaseA_domain
PANTHERiPTHR11437 PTHR11437, 1 hit
PfamiView protein in Pfam
PF00074 RnaseA, 1 hit
PRINTSiPR00794 RIBONUCLEASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000535 RNaseA, 1 hit
SMARTiView protein in SMART
SM00092 RNAse_Pc, 1 hit
SUPFAMiSSF54076 SSF54076, 1 hit
PROSITEiView protein in PROSITE
PS00127 RNASE_PANCREATIC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiANGI_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: P03950
Secondary accession number(s): Q05CV1
, Q53X86, Q6P5T2, Q8WXE7
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: December 5, 2018
This is version 216 of the entry and version 1 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again