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P03950 (ANGI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiogenin

EC=3.1.27.-
Alternative name(s):
Ribonuclease 5
Short name=RNase 5
Gene names
Name:ANG
Synonyms:RNASE5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.14 Ref.15 Ref.16

Subunit structure

Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur. Ref.13 Ref.15 Ref.18

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Nucleusnucleolus. Note: Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA. Ref.11 Ref.14

Tissue specificity

Expressed predominantly in the liver. Also detected in endothelial cells and spinal cord neurons. Ref.9 Ref.28

Developmental stage

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

Involvement in disease

Amyotrophic lateral sclerosis 9 (ALS9) [MIM:611895]: A 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Caution

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

Sequence caution

The sequence AAH20704.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Stress response
   Cellular componentBasement membrane
Extracellular matrix
Nucleus
Secreted
   Coding sequence diversityPolymorphism
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   DomainSignal
   LigandDNA-binding
   Molecular functionDevelopmental protein
Endonuclease
Hydrolase
Nuclease
Protein synthesis inhibitor
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis

Inferred from direct assay PubMed 2424496PubMed 2730651. Source: GOC

actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of phospholipase A2 activity

Inferred from mutant phenotype PubMed 2646638. Source: UniProtKB

activation of phospholipase C activity

Inferred from mutant phenotype PubMed 2457905. Source: UniProtKB

activation of protein kinase B activity

Inferred from mutant phenotype PubMed 17125737. Source: UniProtKB

angiogenesis

Inferred from mutant phenotype PubMed 17125737PubMed 2479414. Source: UniProtKB

cell communication

Non-traceable author statement PubMed 10103013. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype PubMed 17125737. Source: UniProtKB

diacylglycerol biosynthetic process

Inferred from direct assay PubMed 2457905. Source: UniProtKB

homeostatic process

Non-traceable author statement PubMed 15166501. Source: UniProtKB

negative regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 10103013. Source: UniProtKB

negative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid phosphodiester bond hydrolysis

Traceable author statement PubMed 10103013. Source: GOC

oocyte maturation

Non-traceable author statement PubMed 11438326. Source: UniProtKB

ovarian follicle development

Non-traceable author statement PubMed 12770725. Source: UniProtKB

placenta development

Non-traceable author statement PubMed 11984825. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 9122172PubMed 9707554. Source: UniProtKB

positive regulation of phosphorylation

Inferred from direct assay PubMed 17125737. Source: UniProtKB

positive regulation of protein secretion

Inferred from direct assay PubMed 2646638. Source: UniProtKB

rRNA transcription

Inferred from mutant phenotype PubMed 15735021. Source: UniProtKB

response to hormone

Inferred from direct assay PubMed 10999833. Source: UniProtKB

response to hypoxia

Inferred from direct assay PubMed 10999833PubMed 15979542PubMed 16490744. Source: UniProtKB

   Cellular_componentangiogenin-PRI complex

Inferred from physical interaction PubMed 3470787. Source: UniProtKB

basal lamina

Inferred from direct assay PubMed 15166501. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 16461950PubMed 16490744PubMed 3663649. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 10649442PubMed 15735021. Source: UniProtKB

   Molecular_functionDNA binding

Inferred by curator PubMed 10649442. Source: UniProtKB

actin binding

Inferred from direct assay PubMed 11782452PubMed 7679494. Source: UniProtKB

copper ion binding

Inferred from direct assay PubMed 9245697. Source: UniProtKB

endonuclease activity

Traceable author statement PubMed 10103013. Source: UniProtKB

endoribonuclease activity, producing 3'-phosphomonoesters

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from direct assay PubMed 10103013. Source: UniProtKB

peptide binding

Inferred from direct assay PubMed 11782452. Source: UniProtKB

rRNA binding

Traceable author statement PubMed 2457905. Source: UniProtKB

receptor binding

Inferred from direct assay PubMed 9122172. Source: UniProtKB

ribonuclease activity

Inferred from direct assay PubMed 2424496PubMed 2730651. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.8
Chain25 – 147123Angiogenin Ref.1 Ref.8
PRO_0000030843

Regions

Region64 – 685Substrate binding
Motif55 – 595Nucleolar localization signal

Sites

Active site371Proton acceptor
Active site1381Proton donor

Amino acid modifications

Modified residue251Pyrrolidone carboxylic acid Ref.8
Disulfide bond50 ↔ 105 Ref.8
Disulfide bond63 ↔ 116 Ref.8
Disulfide bond81 ↔ 131 Ref.8

Natural variations

Natural variant121F → S in ALS9. Ref.30
VAR_044145
Natural variant201P → S in ALS9. Ref.28 Ref.30
VAR_044146
Natural variant361Q → L in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; wild type far-UV CD spectra. Ref.27 Ref.29
VAR_044147
Natural variant411K → E in ALS9; reduced ribonucleolytic activity. Ref.27 Ref.29
VAR_044148
Natural variant411K → I in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation. Ref.27 Ref.28 Ref.29
VAR_044149
Natural variant521S → N in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. Ref.28
VAR_044150
Natural variant551R → K in ALS9; marginally reduced ribonucleolytic activity; wild type far-UV CD spectra. Ref.27 Ref.29
VAR_044151
Natural variant631C → W in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability. Ref.27 Ref.29
VAR_044152
Natural variant641K → I in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; moderate reduction of thermal stability. Ref.26 Ref.27 Ref.29
VAR_044153
Natural variant701I → V in some ALS9 patients; pathogenicity uncertain; reduced ribonucleolytic activity; moderate reduction of thermal stability. Ref.27 Ref.29 Ref.30
VAR_044154
Natural variant841K → E. Ref.2
Corresponds to variant rs17560 [ dbSNP | Ensembl ].
VAR_013148
Natural variant1361P → L in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus. Ref.28
VAR_044155
Natural variant1371V → I in ALS9. Ref.30
VAR_044156
Natural variant1381H → R in ALS9. Ref.30
VAR_044157

Experimental info

Mutagenesis291R → A: Significantly decreases binding affinity for RNH1. Ref.13 Ref.15
Mutagenesis321H → A: Significantly decreases binding affinity for RNH1. Ref.12 Ref.15
Mutagenesis361Q → A: Slightly decreases binding affinity for RNH1. Ref.12 Ref.15
Mutagenesis641K → Q: Significantly decreases binding affinity for RNH1. Ref.12 Ref.13 Ref.15
Mutagenesis921N → A: Slightly decreases binding affinity for RNH1. Ref.12 Ref.15
Mutagenesis109 – 1102GG → RR: Significantly decreases binding affinity for RNH1. Ref.15
Mutagenesis1321E → A: Slightly decreases binding affinity for RNH1. Ref.12 Ref.15
Mutagenesis1401D → H, S or A: 15- to 18-fold increase in RNase activity. Ref.15 Ref.21
Mutagenesis1411Q → G: Over 18-fold increase in RNase activity. Ref.15 Ref.21
Mutagenesis143 – 1442IF → AA: 3- to 5-fold increase in RNase activity. Ref.15
Sequence conflict591L → P in AAH62698. Ref.7

Secondary structure

............................. 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03950 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: 9C462DA3C8D39ACC

FASTA14716,550
        10         20         30         40         50         60 
MVMGLGVLLL VFVLGLGLTP PTLAQDNSRY THFLTQHYDA KPQGRDDRYC ESIMRRRGLT 

        70         80         90        100        110        120 
SPCKDINTFI HGNKRSIKAI CENKNGNPHR ENLRISKSSF QVTTCKLHGG SPWPPCQYRA 

       130        140 
TAGFRNVVVA CENGLPVHLD QSIFRRP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor."
Kurachi K., Davie E.W., Strydom D.J., Riordan J.F., Vallee B.L.
Biochemistry 24:5494-5499(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Diversifying selection of the tumor-growth promoter angiogenin in primate evolution."
Zhang J., Rosenberg H.F.
Mol. Biol. Evol. 19:438-445(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-84.
[3]Li J., Wang H.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"NEDO functional analysis of protein and research application project."
Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[8]"Amino acid sequence of human tumor derived angiogenin."
Strydom D.J., Fett J.W., Lobb R.R., Alderman E.M., Bethune J.L., Riordan J.F., Vallee B.L.
Biochemistry 24:5486-5494(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-147, DISULFIDE BONDS.
[9]"Tissue distribution and developmental expression of the messenger RNA encoding angiogenin."
Weiner H.L., Weiner L.H., Swain J.L.
Science 237:280-282(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily."
Saxena S.K., Rybak S.M., Davey R.T. Jr., Youle R.J., Ackerman E.J.
J. Biol. Chem. 267:21982-21986(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Identification of the nucleolar targeting signal of human angiogenin."
Moroianu J., Riordan J.F.
Biochem. Biophys. Res. Commun. 203:1765-1772(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEOLAR LOCALIZATION SIGNAL.
[12]"Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A."
Chen C.Z., Shapiro R.
Proc. Natl. Acad. Sci. U.S.A. 94:1761-1766(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-32; GLN-36; LYS-64; ASN-92 AND GLU-132.
[13]"Superadditive and subadditive effects of 'hot spot' mutations within the interfaces of placental ribonuclease inhibitor with angiogenin and ribonuclease A."
Chen C.Z., Shapiro R.
Biochemistry 38:9273-9285(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNH1, MUTAGENESIS OF ARG-29 AND LYS-64.
[14]"The nuclear function of angiogenin in endothelial cells is related to rRNA production."
Xu Z.P., Tsuji T., Riordan J.F., Hu G.F.
Biochem. Biophys. Res. Commun. 294:287-292(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING.
[15]"Ribonuclease inhibitor regulates neovascularization by human angiogenin."
Dickson K.A., Kang D.K., Kwon Y.S., Kim J.C., Leland P.A., Kim B.M., Chang S.I., Raines R.T.
Biochemistry 48:3804-3806(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RNH1, MUTAGENESIS OF 109-GLY-GLY-110.
[16]"Angiogenin-induced tRNA fragments inhibit translation initiation."
Ivanov P., Emara M.M., Villen J., Gygi S.P., Anderson P.
Mol. Cell 43:613-623(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease."
Acharya K.R., Shapiro R., Allen S.C., Riordan J.F., Vallee B.L.
Proc. Natl. Acad. Sci. U.S.A. 91:2915-2919(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-147.
[18]"Molecular recognition of human angiogenin by placental ribonuclease inhibitor -- an X-ray crystallographic study at 2.0-A resolution."
Papageorgiou A.C., Shapiro R., Acharya K.R.
EMBO J. 16:5162-5177(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-147 IN COMPLEX WITH RNH1 AND SUBUNIT.
[19]"Refined crystal structures of native human angiogenin and two active site variants: implications for the unique functional properties of an enzyme involved in neovascularisation during tumour growth."
Leonidas D.D., Shapiro R., Allen S.C., Subbarao G.V., Veluraja K., Acharya K.R.
J. Mol. Biol. 285:1209-1233(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-147.
[20]"Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography."
Leonidas D.D., Chavali G.B., Jardine A.M., Li S., Shapiro R., Acharya K.R.
Protein Sci. 10:1669-1676(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 26-147 OF MUTANT GLY-141 IN COMPLEX WITH PHOSPHATE AND PYROPHOSPHATE.
[21]"Crystallographic studies on the role of the C-terminal segment of human angiogenin in defining enzymatic potency."
Leonidas D.D., Shapiro R., Subbarao G.V., Russo A., Acharya K.R.
Biochemistry 41:2552-2562(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-147, MUTAGENESIS OF ASP-140; GLN-141 AND 143-ILE-PHE-144.
[22]"The crystal structure of human angiogenin in complex with an antitumor neutralizing antibody."
Chavali G.B., Papageorgiou A.C., Olson K.A., Fett J.W., Hu G., Shapiro R., Acharya K.R.
Structure 11:875-885(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 26-147.
[23]"Crystallographic studies on structural features that determine the enzymatic specificity and potency of human angiogenin: Thr44, Thr80, and residues 38-41."
Holloway D.E., Chavali G.B., Hares M.C., Baker M.D., Subbarao G.V., Shapiro R., Acharya K.R.
Biochemistry 43:1230-1241(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ASP-68 AND ALA-104.
[24]"Three-dimensional solution structure of human angiogenin determined by 1H,15N-NMR spectroscopy -- characterization of histidine protonation states and pKa values."
Lequin O., Thuering H., Robin M., Lallemand J.-Y.
Eur. J. Biochem. 250:712-726(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[25]"Mechanisms of loss of functions of human angiogenin variants implicated in amyotrophic lateral sclerosis."
Padhi A.K., Kumar H., Vasaikar S.V., Jayaram B., Gomes J.
PLoS ONE 7:E32479-E32479(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[26]"A novel candidate region for ALS on chromosome 14q11.2."
Greenway M.J., Alexander M.D., Ennis S., Traynor B.J., Corr B., Frost E., Green A., Hardiman O.
Neurology 63:1936-1938(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS9 ILE-64.
[27]"ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis."
Greenway M.J., Andersen P.M., Russ C., Ennis S., Cashman S., Donaghy C., Patterson V., Swingler R., Kieran D., Prehn J., Morrison K.E., Green A., Acharya K.R., Brown R.H. Jr., Hardiman O.
Nat. Genet. 38:411-413(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS9 LEU-36; ILE-41; GLU-41; LYS-55; TRP-63 AND ILE-64, VARIANT VAL-70.
[28]"Angiogenin loss-of-function mutations in amyotrophic lateral sclerosis."
Wu D., Yu W., Kishikawa H., Folkerth R.D., Iafrate A.J., Shen Y., Xin W., Sims K., Hu G.-F.
Ann. Neurol. 62:609-617(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS9 SER-20; ILE-41; ASN-52 AND LEU-136, CHARACTERIZATION OF VARIANTS ALS9 ILE-41; ASN-52 AND LEU-136, TISSUE SPECIFICITY.
[29]"Characterization of human angiogenin variants implicated in amyotrophic lateral sclerosis."
Crabtree B., Thiyagarajan N., Prior S.H., Wilson P., Iyer S., Ferns T., Shapiro R., Brew K., Subramanian V., Acharya K.R.
Biochemistry 46:11810-11818(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ALS9 LEU-36; ILE-41; GLU-41; LYS-55; TRP-63 AND ILE-64, CHARACTERIZATION OF VARIANT VAL-70.
[30]"Identification of new ANG gene mutations in a large cohort of Italian patients with amyotrophic lateral sclerosis."
Gellera C., Colombrita C., Ticozzi N., Castellotti B., Bragato C., Ratti A., Taroni F., Silani V.
Neurogenetics 9:33-40(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS9 SER-12; SER-20; ILE-137 AND ARG-138, VARIANT VAL-70.
[31]"A novel angiogenin gene mutation in a sporadic patient with amyotrophic lateral sclerosis from southern Italy."
Conforti F.L., Sprovieri T., Mazzei R., Ungaro C., La Bella V., Tessitore A., Patitucci A., Magariello A., Gabriele A.L., Tedeschi G., Simone I.L., Majorana G., Valentino P., Condino F., Bono F., Monsurro M.R., Muglia M., Quattrone A.
Neuromuscul. Disord. 18:68-70(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ALS9.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRNRHUAG. A90498.
RefSeqNP_001091046.1. NM_001097577.2.
NP_001136.1. NM_001145.4.
UniGeneHs.283749.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.00A26-147[»]
1H53X-ray2.00A26-147[»]
1HBYX-ray2.00A26-147[»]
1K58X-ray2.70A26-147[»]
1K59X-ray1.80A26-147[»]
1K5AX-ray2.33A25-147[»]
1K5BX-ray1.80A26-144[»]
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[»]
ProteinModelPortalP03950.
SMRP03950. Positions 24-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106780. 7 interactions.
IntActP03950. 7 interactions.
STRING9606.ENSP00000336762.

Chemistry

BindingDBP03950.
ChEMBLCHEMBL5829.

PTM databases

PhosphoSiteP03950.

Polymorphism databases

DMDM113873.

Proteomic databases

PaxDbP03950.
PeptideAtlasP03950.
PRIDEP03950.

Protocols and materials databases

DNASU283.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336811; ENSP00000336762; ENSG00000214274.
ENST00000397990; ENSP00000381077; ENSG00000214274.
GeneID283.
KEGGhsa:283.
UCSCuc001vxw.4. human.

Organism-specific databases

CTD283.
GeneCardsGC14P021152.
HGNCHGNC:483. ANG.
MIM105850. gene.
611895. phenotype.
neXtProtNX_P03950.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA24790.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283332.
HOGENOMHOG000276883.
HOVERGENHBG008396.
InParanoidP03950.
KOK16631.
OMAPCKYRAT.
OrthoDBEOG7J1826.
PhylomeDBP03950.
TreeFamTF333393.

Gene expression databases

BgeeP03950.
CleanExHS_ANG.
GenevestigatorP03950.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMSSF54076. SSF54076. 1 hit.
PROSITEPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03950.
GeneWikiAngiogenin.
GenomeRNAi283.
NextBio1141.
PROP03950.
SOURCESearch...

Entry information

Entry nameANGI_HUMAN
AccessionPrimary (citable) accession number: P03950
Secondary accession number(s): Q05CV1 expand/collapse secondary AC list , Q53X86, Q6P5T2, Q8WXE7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: April 16, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM