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Protein

Angiogenin

Gene

ANG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Sites

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

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
  • receptor binding Source: UniProtKB
  • ribonuclease activity Source: UniProtKB
  • rRNA binding Source: UniProtKB

GO - Biological processi

  • actin filament polymerization Source: UniProtKB
  • activation of phospholipase A2 activity Source: UniProtKB
  • activation of phospholipase C activity Source: UniProtKB
  • activation of protein kinase B activity Source: UniProtKB
  • adherens junction organization Source: Reactome
  • angiogenesis Source: UniProtKB
  • antibacterial humoral response Source: UniProtKB
  • antifungal humoral response Source: UniProtKB
  • cell communication Source: UniProtKB
  • cell migration Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • diacylglycerol biosynthetic process Source: UniProtKB
  • homeostatic process Source: UniProtKB
  • innate immune response Source: UniProtKB
  • negative regulation of smooth muscle cell proliferation Source: UniProtKB
  • negative regulation of translation Source: UniProtKB-KW
  • oocyte maturation Source: UniProtKB
  • ovarian follicle development Source: UniProtKB
  • placenta development Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of phosphorylation Source: UniProtKB
  • positive regulation of protein secretion Source: UniProtKB
  • response to hormone Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • response to yeast Source: UniProtKB
  • rRNA transcription Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Endonuclease, Hydrolase, Nuclease, Protein synthesis inhibitor

Keywords - Biological processi

Angiogenesis, Differentiation, Stress response

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:HS09945-MONOMER.
ReactomeiR-HSA-418990. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiogenin (EC:3.1.27.-)
Alternative name(s):
Ribonuclease 5
Short name:
RNase 5
Gene namesi
Name:ANG
Synonyms:RNASE5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:483. ANG.

Subcellular locationi

GO - Cellular componenti

  • angiogenin-PRI complex Source: UniProtKB
  • basal lamina Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • growth cone Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 9 (ALS9)7 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
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 rs121909535dbSNPEnsembl.1
Natural variantiVAR_07302138Y → H in ALS9. 1 Publication1
Natural variantiVAR_04414841K → E in ALS9; reduced ribonucleolytic activity. 2 PublicationsCorresponds to variant rs121909537dbSNPEnsembl.1
Natural variantiVAR_04414941K → I in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation. 4 PublicationsCorresponds to variant rs121909536dbSNPEnsembl.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 rs121909542dbSNPEnsembl.1
Natural variantiVAR_04415155R → K in ALS9; marginally reduced ribonucleolytic activity; wild type far-UV CD spectra. 2 PublicationsCorresponds to variant rs121909538dbSNPEnsembl.1
Natural variantiVAR_04415263C → W in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability. 2 PublicationsCorresponds to variant rs121909539dbSNPEnsembl.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 rs121909540dbSNPEnsembl.1
Natural variantiVAR_04415470I → V in some ALS9 patients; pathogenicity uncertain; reduced ribonucleolytic activity; moderate reduction of thermal stability. 3 PublicationsCorresponds to variant rs121909541dbSNPEnsembl.1
Natural variantiVAR_044155136P → L in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. 1 PublicationCorresponds to variant rs121909543dbSNPEnsembl.1
Natural variantiVAR_044156137V → I in ALS9. 1 PublicationCorresponds to variant rs121909544dbSNPEnsembl.1
Natural variantiVAR_044157138H → R in ALS9. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi283.
MalaCardsiANG.
MIMi611895. phenotype.
OpenTargetsiENSG00000214274.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA24790.

Chemistry databases

ChEMBLiCHEMBL5829.

Polymorphism and mutation databases

BioMutaiANG.
DMDMi113873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000003084325 – 147Angiogenin2 PublicationsAdd BLAST123

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi50 ↔ 1051 Publication
Disulfide bondi63 ↔ 1161 Publication
Disulfide bondi81 ↔ 1311 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP03950.
PeptideAtlasiP03950.
PRIDEiP03950.
TopDownProteomicsiP03950.

PTM databases

iPTMnetiP03950.
PhosphoSitePlusiP03950.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiENSG00000214274.
CleanExiHS_ANG.
ExpressionAtlasiP03950. baseline and differential.
GenevisibleiP03950. HS.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN2P356094EBI-525291,EBI-77797
ANXA2P073556EBI-525291,EBI-352622
FSTP198833EBI-525291,EBI-1571188
PLAURQ034055EBI-525291,EBI-716505
RNH1P134892EBI-525291,EBI-1237106
S100A10P609038EBI-525291,EBI-717048

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106780. 7 interactors.
IntActiP03950. 11 interactors.
STRINGi9606.ENSP00000336762.

Chemistry databases

BindingDBiP03950.

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 37Combined sources10
Helixi47 – 56Combined sources10
Turni60 – 63Combined sources4
Beta strandi65 – 70Combined sources6
Helixi74 – 78Combined sources5
Helixi79 – 81Combined sources3
Turni83 – 85Combined sources3
Beta strandi86 – 89Combined sources4
Turni90 – 92Combined sources3
Beta strandi93 – 98Combined sources6
Beta strandi100 – 110Combined sources11
Beta strandi112 – 115Combined sources4
Beta strandi117 – 125Combined sources9
Beta strandi128 – 132Combined sources5
Beta strandi135 – 139Combined sources5
Helixi141 – 144Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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/B25-107[»]
A/B116-147[»]
5EOPX-ray1.35A26-146[»]
5EPZX-ray1.85A26-145[»]
5EQOX-ray2.40A25-145[»]
ProteinModelPortaliP03950.
SMRiP03950.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03950.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 68Substrate binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi55 – 59Nucleolar localization signal5

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J3ET. Eukaryota.
ENOG410Y4FD. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP03950.
KOiK16631.
OMAiFIHGNKG.
OrthoDBiEOG091G0YDD.
PhylomeDBiP03950.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i9C462DA3C8D39ACC
GO

Sequence cautioni

The sequence AAH20704 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 rs121909535dbSNPEnsembl.1
Natural variantiVAR_07302138Y → H in ALS9. 1 Publication1
Natural variantiVAR_04414841K → E in ALS9; reduced ribonucleolytic activity. 2 PublicationsCorresponds to variant rs121909537dbSNPEnsembl.1
Natural variantiVAR_04414941K → I in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation. 4 PublicationsCorresponds to variant rs121909536dbSNPEnsembl.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 rs121909542dbSNPEnsembl.1
Natural variantiVAR_04415155R → K in ALS9; marginally reduced ribonucleolytic activity; wild type far-UV CD spectra. 2 PublicationsCorresponds to variant rs121909538dbSNPEnsembl.1
Natural variantiVAR_04415263C → W in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability. 2 PublicationsCorresponds to variant rs121909539dbSNPEnsembl.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 rs121909540dbSNPEnsembl.1
Natural variantiVAR_04415470I → V in some ALS9 patients; pathogenicity uncertain; reduced ribonucleolytic activity; moderate reduction of thermal stability. 3 PublicationsCorresponds to variant rs121909541dbSNPEnsembl.1
Natural variantiVAR_01314884K → E.1 PublicationCorresponds to variant rs17560dbSNPEnsembl.1
Natural variantiVAR_044155136P → L in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. 1 PublicationCorresponds to variant rs121909543dbSNPEnsembl.1
Natural variantiVAR_044156137V → I in ALS9. 1 PublicationCorresponds to variant rs121909544dbSNPEnsembl.1
Natural variantiVAR_044157138H → R in ALS9. 1 Publication1

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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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:
PDBei
RCSB PDBi
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/B25-107[»]
A/B116-147[»]
5EOPX-ray1.35A26-146[»]
5EPZX-ray1.85A26-145[»]
5EQOX-ray2.40A25-145[»]
ProteinModelPortaliP03950.
SMRiP03950.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106780. 7 interactors.
IntActiP03950. 11 interactors.
STRINGi9606.ENSP00000336762.

Chemistry databases

BindingDBiP03950.
ChEMBLiCHEMBL5829.

PTM databases

iPTMnetiP03950.
PhosphoSitePlusiP03950.

Polymorphism and mutation databases

BioMutaiANG.
DMDMi113873.

Proteomic databases

PaxDbiP03950.
PeptideAtlasiP03950.
PRIDEiP03950.
TopDownProteomicsiP03950.

Protocols and materials databases

DNASUi283.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi283.
DisGeNETi283.
GeneCardsiANG.
GeneReviewsiANG.
HGNCiHGNC:483. ANG.
MalaCardsiANG.
MIMi105850. gene.
611895. phenotype.
neXtProtiNX_P03950.
OpenTargetsiENSG00000214274.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA24790.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J3ET. Eukaryota.
ENOG410Y4FD. LUCA.
GeneTreeiENSGT00840000129759.
HOGENOMiHOG000276883.
HOVERGENiHBG008396.
InParanoidiP03950.
KOiK16631.
OMAiFIHGNKG.
OrthoDBiEOG091G0YDD.
PhylomeDBiP03950.
TreeFamiTF333393.

Enzyme and pathway databases

BioCyciZFISH:HS09945-MONOMER.
ReactomeiR-HSA-418990. Adherens junctions interactions.

Miscellaneous databases

EvolutionaryTraceiP03950.
GeneWikiiAngiogenin.
GenomeRNAii283.
PROiP03950.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000214274.
CleanExiHS_ANG.
ExpressionAtlasiP03950. baseline and differential.
GenevisibleiP03950. HS.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANGI_HUMAN
AccessioniPrimary (citable) accession number: P03950
Secondary accession number(s): Q05CV1
, Q53X86, Q6P5T2, Q8WXE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: November 30, 2016
This is version 196 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.