Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P13489 (RINI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease inhibitor
Alternative name(s):
Placental ribonuclease inhibitor
Short name=Placental RNase inhibitor
Ribonuclease/angiogenin inhibitor 1
Short name=RAI
Gene names
Name:RNH1
Synonyms:PRI, RNH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. Ref.3 Ref.10 Ref.11

Subunit structure

Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.

Subcellular location

Cytoplasm.

Domain

The LRR domain forms a horseshoe-shaped structure that interacts tightly with target RNases via a large protein interaction surface on its interior side. Ref.18 Ref.19 Ref.20

Post-translational modification

The N-terminus is blocked.

At least 30 of the 32 cysteine residues are in the reduced form.

Sequence similarities

Contains 15 LRR (leucine-rich) repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ANGP039502EBI-1237106,EBI-525291
RNASE1P079982EBI-1237106,EBI-2823523
RNASE1P618233EBI-1237106,EBI-908364From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.16
Chain2 – 461460Ribonuclease inhibitor
PRO_0000097343

Regions

Repeat20 – 4829LRR 1
Repeat49 – 7628LRR 2
Repeat77 – 10529LRR 3
Repeat106 – 13328LRR 4
Repeat134 – 16229LRR 5
Repeat163 – 19028LRR 6
Repeat191 – 21929LRR 7
Repeat220 – 24728LRR 8
Repeat248 – 27629LRR 9
Repeat277 – 30428LRR 10
Repeat305 – 33329LRR 11
Repeat334 – 36128LRR 12
Repeat362 – 39029LRR 13
Repeat391 – 41828LRR 14
Repeat419 – 44729LRR 15
Region2 – 11102 X 5 AA tandem repeats of S-L-D-I-Q

Amino acid modifications

Modified residue21N-acetylserine Ref.16 Ref.17
Modified residue821Phosphothreonine Ref.12
Modified residue911Phosphoserine Ref.13

Natural variations

Natural variant1701P → L.
Corresponds to variant rs17585 [ dbSNP | Ensembl ].
VAR_014726

Experimental info

Mutagenesis2621W → A: Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-264 and A-319. Ref.9 Ref.10
Mutagenesis2641W → A: Substantially decreased binding affinity for RNASE2. Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-262 and A-319. Ref.9 Ref.10
Mutagenesis3191W → A: Substantially decreased binding affinity for RNASE2. Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-262 and A-264. Ref.9 Ref.10
Mutagenesis3761W → A: 40-fold reduction in binding affinity for RNASE2. Ref.9 Ref.19
Mutagenesis435 – 4362YD → AA: Substantially decreases binding affinity for RNASE1, ANG and RNASE2. Ref.9
Mutagenesis4581R → A: 25-fold reduction in binding affinity for RNASE2. Ref.9 Ref.19
Mutagenesis4611Missing: A significant decrease in binding affinity with RNASE1, slight decrease for the ANG ligand, no real change in binding affinity for RNASE2. Ref.8 Ref.9 Ref.10
Sequence conflict1881R → H in AAH03506. Ref.5
Sequence conflict3591R → A in AAL60586. Ref.3
Sequence conflict3651L → P in AAL60586. Ref.3
Sequence conflict423 – 4242RQ → SE in CAA32151. Ref.2
Sequence conflict423 – 4242RQ → SE in AAA60249. Ref.2

Secondary structure

.................................................................................. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13489 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5E88CDAC95BAE5B3

FASTA46149,973
        10         20         30         40         50         60 
MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS ALRVNPALAE 

        70         80         90        100        110        120 
LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA GCGVLSSTLR TLPTLQELHL 

       130        140        150        160        170        180 
SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE YCSLSAASCE PLASVLRAKP DFKELTVSNN 

       190        200        210        220        230        240 
DINEAGVRVL CQGLKDSPCQ LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG 

       250        260        270        280        290        300 
DVGMAELCPG LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG 

       310        320        330        340        350        360 
ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN NRLEDAGVRE 

       370        380        390        400        410        420 
LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL RELDLSNNCL GDAGILQLVE 

       430        440        450        460 
SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL EKDKPSLRVI S 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human placental ribonuclease inhibitor."
Lee F.S., Fox E.A., Zhou H.-M., Strydom D.J., Vallee B.L.
Biochemistry 27:8545-8553(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-28; 35-44; 47-62; 65-72; 87-130; 147-181; 189-200; 206-226; 231-235; 239-268; 272-276; 288-295; 297-299; 303-316; 353-364; 374-394; 402-412; 424-449 AND 453-461, OXIDATION STATE OF THE CYSTEINES.
Tissue: Placenta.
[2]"The primary structure of human ribonuclease/angiogenin inhibitor (RAI) discloses a novel highly diversified protein superfamily with a common repetitive module."
Schneider R., Schneider-Scherzer E., Thurnher M., Auer B., Schweiger M.
EMBO J. 7:4151-4156(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 444-462.
[3]"Expression of a human ribonuclease inhibitor variant in Escherichia coli and silkworm insect cell (Bombyx mori)."
Huang G.H., Yang G.Z., Chen J.Y., Wu X.F.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:960-963(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"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: Brain, Colon, Lymph and Ovary.
[6]"Purification and characterization of human brain ribonuclease inhibitor."
Nadano D., Yasuda T., Takeshita H., Uchide K., Kishi K.
Arch. Biochem. Biophys. 312:421-428(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Brain.
[7]"Characterisation of a tryptic peptide from human placental ribonuclease inhibitor which inhibits ribonuclease activity."
Crevel-Thieffry I., Cotterill S., Schuller E.
Biochim. Biophys. Acta 1122:107-112(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 174-195 AND 288-302, INTERACTION WITH RNASE1.
[8]"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 SER-461, INTERACTION WITH ANG AND RNASE1.
[9]"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: MUTAGENESIS OF 435-TYR-ASP-436, INTERACTION WITH ANG AND RNASE1.
[10]"Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2)."
Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.
Biochemistry 42:1451-1459(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-262; TRP-264; TRP-319; 435-TYR-ASP-436 AND SER-461, INTERACTION WITH RNASE2.
[11]"The cytosolic ribonuclease inhibitor contributes to intracellular redox homeostasis."
Monti D.M., Montesano Gesualdi N., Matousek J., Esposito F., D'Alessio G.
FEBS Lett. 581:930-934(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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 2-461 IN COMPLEX WITH ANG, INTERACTION WITH ANG, DOMAIN.
[19]"Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor."
Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.
J. Mol. Biol. 347:637-655(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH RNASE2, DOMAIN, INTERACTION WITH RNASE2, MUTAGENESIS OF TRP-376 AND ARG-458.
[20]"Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein."
Johnson R.J., McCoy J.G., Bingman C.A., Phillips G.N. Jr., Raines R.T.
J. Mol. Biol. 368:434-449(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RNASE1, DOMAIN, INTERACTION WITH RNASE1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22414 mRNA. Translation: AAA59130.1.
M36717 mRNA. Translation: AAA60249.1.
X13973 mRNA. Translation: CAA32151.1.
AY071904 mRNA. Translation: AAL60586.1.
AL161967 mRNA. Translation: CAB82310.1.
BC000677 mRNA. Translation: AAH00677.1.
BC003506 mRNA. Translation: AAH03506.1.
BC011186 mRNA. Translation: AAH11186.1.
BC011500 mRNA. Translation: AAH11500.1.
BC014629 mRNA. Translation: AAH14629.1.
BC024037 mRNA. Translation: AAH24037.1.
BC047730 mRNA. Translation: AAH47730.1.
CCDSCCDS7697.1.
PIRA31858.
RefSeqNP_002930.2. NM_002939.3.
NP_976317.1. NM_203383.1.
NP_976318.1. NM_203384.1.
NP_976319.1. NM_203385.1.
NP_976320.1. NM_203386.2.
NP_976321.1. NM_203387.2.
NP_976322.1. NM_203388.2.
NP_976323.1. NM_203389.2.
UniGeneHs.530687.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4YX-ray2.00A/D2-461[»]
1Z7XX-ray1.95W/Y1-461[»]
2BEXX-ray1.99A/B2-461[»]
2Q4GX-ray1.95W/Y1-461[»]
ProteinModelPortalP13489.
SMRP13489. Positions 2-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111977. 24 interactions.
IntActP13489. 18 interactions.
MINTMINT-5000705.
STRING9606.ENSP00000346402.

PTM databases

PhosphoSiteP13489.

Polymorphism databases

DMDM132573.

2D gel databases

REPRODUCTION-2DPAGEIPI00550069.

Proteomic databases

MaxQBP13489.
PaxDbP13489.
PeptideAtlasP13489.
PRIDEP13489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354420; ENSP00000346402; ENSG00000023191.
ENST00000356187; ENSP00000348515; ENSG00000023191.
ENST00000397604; ENSP00000380729; ENSG00000023191.
ENST00000397614; ENSP00000380738; ENSG00000023191.
ENST00000397615; ENSP00000380739; ENSG00000023191.
ENST00000438658; ENSP00000416589; ENSG00000023191.
ENST00000533410; ENSP00000435594; ENSG00000023191.
ENST00000534797; ENSP00000433999; ENSG00000023191.
GeneID6050.
KEGGhsa:6050.
UCSCuc001lpk.1. human.

Organism-specific databases

CTD6050.
GeneCardsGC11M000485.
HGNCHGNC:10074. RNH1.
HPAHPA039223.
HPA040781.
MIM173320. gene.
neXtProtNX_P13489.
PharmGKBPA34447.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308334.
HOGENOMHOG000140402.
HOVERGENHBG001059.
InParanoidP13489.
KOK16634.
OMAVQELCQG.
OrthoDBEOG7P5T07.
PhylomeDBP13489.

Gene expression databases

ArrayExpressP13489.
BgeeP13489.
CleanExHS_RNH1.
GenevestigatorP13489.

Family and domain databases

InterProIPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
[Graphical view]
SMARTSM00368. LRR_RI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNH1. human.
EvolutionaryTraceP13489.
GeneWikiRNH1.
GenomeRNAi6050.
NextBio23577.
PROP13489.
SOURCESearch...

Entry information

Entry nameRINI_HUMAN
AccessionPrimary (citable) accession number: P13489
Secondary accession number(s): Q8IZK8 expand/collapse secondary AC list , Q96FD7, Q9BQ80, Q9UDK6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 163 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM