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Reviewed, UniProtKB/Swiss-Prot P13489 (RINI_HUMAN)

Last modified June 16, 2009. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ribonuclease inhibitor
Alternative name(s):
    Ribonuclease/angiogenin inhibitor 1
      Short name=RAI
    Placental ribonuclease inhibitor
      Short name=RNase inhibitor
      Short name=RI
Gene names
Name: RNH1
Synonyms: PRI, RNH
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

Inhibitor of pancreatic RNase and angiogenin. May also function in the modulation of cellular activities.

Subunit structure

Forms a tight one-to-one complex with the RNase.

Subcellular location

Cytoplasm.

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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainLeucine-rich repeat
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processmRNA catabolic process

Non-traceable author statement. Source: UniProtKB

regulation of angiogenesis

Inferred from direct assay. Source: UniProtKB

   Cellular componentangiogenin-PRI complex

Inferred from physical interaction. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: UniProtKB

ribonuclease inhibitor activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
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 residue821Phosphothreonine Ref.6

Natural variations

Natural variant1701P → L: dbSNP rs17585.
VAR_014726

Experimental info

Sequence conflict423 – 4242RQ → SE in CAA32151. Ref.2
Sequence conflict423 – 4242RQ → SE in AAA60249. Ref.2

Secondary structure

1 ............................................................................ 461
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13489-1 [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

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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: 3219362] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, 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: 3243277] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 444-462.
[3]"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lymph and Ovary.
[5]"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: 8037455] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Brain.
[6]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, MASS SPECTROMETRY.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"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: 9311977] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH ANGIOGENIN.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M22414 mRNA. Translation: AAA59130.1.
X13973 mRNA. Translation: CAA32151.1.
M36717 mRNA. Translation: AAA60249.1.
AL161967 mRNA. Translation: CAB82310.1.
BC011500 mRNA. Translation: AAH11500.1.
BC014629 mRNA. Translation: AAH14629.1.
BC047730 mRNA. Translation: AAH47730.1.
IPIIPI00550069.
PIRA31858.
RefSeqNP_002930.2.
NP_976317.1.
NP_976318.1.
NP_976319.1.
NP_976320.1.
NP_976321.1.
NP_976322.1.
NP_976323.1.
UniGeneHs.530687

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A4YX-ray2.00A/D2-461[»]
1Z7XX-ray1.95W/Y1-461[»]
2BEXX-ray1.99A/B2-461[»]
2Q4GX-ray1.95W/Y1-461[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6061N.

PTM databases

PhosphoSiteP13489.

2-D gel databases

REPRODUCTION-2DPAGEIPI00550069.

Proteomic databases

PeptideAtlasP13489.
PRIDEP13489.

Genome annotation databases

EnsemblENSG00000023191. Homo sapiens. [Contig view]
GeneID6050.
KEGGhsa:6050.

Organism-specific databases

GeneCardsGC11M000485.
H-InvDBHIX0009337.
HGNCHGNC:10074. RNH1.
MIM173320. gene.
PharmGKBPA34447.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP13489.
HOVERGENP13489.
OMAP13489. CRLEKLQ.

Gene expression databases

ArrayExpressP13489.
BgeeP13489.
CleanExHS_RNH1.
GermOnlineENSG00000023191. Homo sapiens.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
[Graphical view]
SMARTSM00368. LRR_RI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio23577.
SOURCESearch...

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Entry information

Entry nameRINI_HUMAN
AccessionPrimary (citable) accession number: P13489
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents