Full text data of RNH1
RNH1
(PRI, RNH)
[Confidence: low (only semi-automatic identification from reviews)]
Ribonuclease inhibitor (Placental ribonuclease inhibitor; Placental RNase inhibitor; Ribonuclease/angiogenin inhibitor 1; RAI)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribonuclease inhibitor (Placental ribonuclease inhibitor; Placental RNase inhibitor; Ribonuclease/angiogenin inhibitor 1; RAI)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P13489
ID RINI_HUMAN Reviewed; 461 AA.
AC P13489; Q8IZK8; Q96FD7; Q9BQ80; Q9UDK6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 157.
DE RecName: Full=Ribonuclease inhibitor;
DE AltName: Full=Placental ribonuclease inhibitor;
DE Short=Placental RNase inhibitor;
DE AltName: Full=Ribonuclease/angiogenin inhibitor 1;
DE Short=RAI;
GN Name=RNH1; Synonyms=PRI, RNH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-28; 35-44; 47-62;
RP 65-72; 87-130; 147-181; 189-200; 206-226; 231-235; 239-268; 272-276;
RP 288-295; 297-299; 303-316; 353-364; 374-394; 402-412; 424-449 AND
RP 453-461, AND OXIDATION STATE OF THE CYSTEINES.
RC TISSUE=Placenta;
RX PubMed=3219362; DOI=10.1021/bi00423a007;
RA Lee F.S., Fox E.A., Zhou H.-M., Strydom D.J., Vallee B.L.;
RT "Primary structure of human placental ribonuclease inhibitor.";
RL Biochemistry 27:8545-8553(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 444-462.
RX PubMed=3243277;
RA Schneider R., Schneider-Scherzer E., Thurnher M., Auer B.,
RA Schweiger M.;
RT "The primary structure of human ribonuclease/angiogenin inhibitor
RT (RAI) discloses a novel highly diversified protein superfamily with a
RT common repetitive module.";
RL EMBO J. 7:4151-4156(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=14515218;
RA Huang G.H., Yang G.Z., Chen J.Y., Wu X.F.;
RT "Expression of a human ribonuclease inhibitor variant in Escherichia
RT coli and silkworm insect cell (Bombyx mori).";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:960-963(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, Lymph, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Brain;
RX PubMed=8037455; DOI=10.1006/abbi.1994.1328;
RA Nadano D., Yasuda T., Takeshita H., Uchide K., Kishi K.;
RT "Purification and characterization of human brain ribonuclease
RT inhibitor.";
RL Arch. Biochem. Biophys. 312:421-428(1994).
RN [7]
RP PROTEIN SEQUENCE OF 174-195 AND 288-302, AND INTERACTION WITH RNASE1.
RX PubMed=1633192; DOI=10.1016/0167-4838(92)90134-Y;
RA Crevel-Thieffry I., Cotterill S., Schuller E.;
RT "Characterisation of a tryptic peptide from human placental
RT ribonuclease inhibitor which inhibits ribonuclease activity.";
RL Biochim. Biophys. Acta 1122:107-112(1992).
RN [8]
RP MUTAGENESIS OF SER-461, AND INTERACTION WITH ANG AND RNASE1.
RX PubMed=9050852; DOI=10.1073/pnas.94.5.1761;
RA Chen C.Z., Shapiro R.;
RT "Site-specific mutagenesis reveals differences in the structural bases
RT for tight binding of RNase inhibitor to angiogenin and RNase A.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1761-1766(1997).
RN [9]
RP MUTAGENESIS OF 435-TYR-ASP-436, AND INTERACTION WITH ANG AND RNASE1.
RX PubMed=10413501; DOI=10.1021/bi990762a;
RA Chen C.Z., Shapiro R.;
RT "Superadditive and subadditive effects of 'hot spot' mutations within
RT the interfaces of placental ribonuclease inhibitor with angiogenin and
RT ribonuclease A.";
RL Biochemistry 38:9273-9285(1999).
RN [10]
RP FUNCTION, MUTAGENESIS OF TRP-262; TRP-264; TRP-319; 435-TYR-ASP-436
RP AND SER-461, AND INTERACTION WITH RNASE2.
RX PubMed=12578357; DOI=10.1021/bi026852o;
RA Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.;
RT "Mutational analysis of the complex of human RNase inhibitor and human
RT eosinophil-derived neurotoxin (RNase 2).";
RL Biochemistry 42:1451-1459(2003).
RN [11]
RP FUNCTION.
RX PubMed=17292889; DOI=10.1016/j.febslet.2007.01.072;
RA Monti D.M., Montesano Gesualdi N., Matousek J., Esposito F.,
RA D'Alessio G.;
RT "The cytosolic ribonuclease inhibitor contributes to intracellular
RT redox homeostasis.";
RL FEBS Lett. 581:930-934(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH ANG,
RP INTERACTION WITH ANG, AND DOMAIN.
RX PubMed=9311977; DOI=10.1093/emboj/16.17.5162;
RA Papageorgiou A.C., Shapiro R., Acharya K.R.;
RT "Molecular recognition of human angiogenin by placental ribonuclease
RT inhibitor -- an X-ray crystallographic study at 2.0-A resolution.";
RL EMBO J. 16:5162-5177(1997).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH RNASE2,
RP DOMAIN, INTERACTION WITH RNASE2, AND MUTAGENESIS OF TRP-376 AND
RP ARG-458.
RX PubMed=15755456; DOI=10.1016/j.jmb.2005.01.035;
RA Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.;
RT "Molecular recognition of human eosinophil-derived neurotoxin (RNase
RT 2) by placental ribonuclease inhibitor.";
RL J. Mol. Biol. 347:637-655(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RNASE1, DOMAIN,
RP AND INTERACTION WITH RNASE1.
RX PubMed=17350650; DOI=10.1016/j.jmb.2007.02.005;
RA Johnson R.J., McCoy J.G., Bingman C.A., Phillips G.N. Jr.,
RA Raines R.T.;
RT "Inhibition of human pancreatic ribonuclease by the human ribonuclease
RT inhibitor protein.";
RL J. Mol. Biol. 368:434-449(2007).
CC -!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and
CC ANG. May play a role in redox homeostasis.
CC -!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and
CC RNASE2.
CC -!- INTERACTION:
CC P03950:ANG; NbExp=2; IntAct=EBI-1237106, EBI-525291;
CC P07998:RNASE1; NbExp=2; IntAct=EBI-1237106, EBI-2823523;
CC P61823:RNASE1 (xeno); NbExp=3; IntAct=EBI-1237106, EBI-908364;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The LRR domain forms a horseshoe-shaped structure that
CC interacts tightly with target RNases via a large protein
CC interaction surface on its interior side.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: At least 30 of the 32 cysteine residues are in the reduced
CC form.
CC -!- SIMILARITY: Contains 15 LRR (leucine-rich) repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M22414; AAA59130.1; -; mRNA.
DR EMBL; M36717; AAA60249.1; -; mRNA.
DR EMBL; X13973; CAA32151.1; -; mRNA.
DR EMBL; AY071904; AAL60586.1; -; mRNA.
DR EMBL; AL161967; CAB82310.1; -; mRNA.
DR EMBL; BC000677; AAH00677.1; -; mRNA.
DR EMBL; BC003506; AAH03506.1; -; mRNA.
DR EMBL; BC011186; AAH11186.1; -; mRNA.
DR EMBL; BC011500; AAH11500.1; -; mRNA.
DR EMBL; BC014629; AAH14629.1; -; mRNA.
DR EMBL; BC024037; AAH24037.1; -; mRNA.
DR EMBL; BC047730; AAH47730.1; -; mRNA.
DR PIR; A31858; A31858.
DR RefSeq; NP_002930.2; NM_002939.3.
DR RefSeq; NP_976317.1; NM_203383.1.
DR RefSeq; NP_976318.1; NM_203384.1.
DR RefSeq; NP_976319.1; NM_203385.1.
DR RefSeq; NP_976320.1; NM_203386.2.
DR RefSeq; NP_976321.1; NM_203387.2.
DR RefSeq; NP_976322.1; NM_203388.2.
DR RefSeq; NP_976323.1; NM_203389.2.
DR RefSeq; XP_005253106.1; XM_005253049.1.
DR RefSeq; XP_005253107.1; XM_005253050.1.
DR RefSeq; XP_005253108.1; XM_005253051.1.
DR UniGene; Hs.530687; -.
DR PDB; 1A4Y; X-ray; 2.00 A; A/D=2-461.
DR PDB; 1Z7X; X-ray; 1.95 A; W/Y=1-461.
DR PDB; 2BEX; X-ray; 1.99 A; A/B=2-461.
DR PDB; 2Q4G; X-ray; 1.95 A; W/Y=1-461.
DR PDBsum; 1A4Y; -.
DR PDBsum; 1Z7X; -.
DR PDBsum; 2BEX; -.
DR PDBsum; 2Q4G; -.
DR ProteinModelPortal; P13489; -.
DR SMR; P13489; 2-461.
DR IntAct; P13489; 18.
DR MINT; MINT-5000705; -.
DR STRING; 9606.ENSP00000346402; -.
DR PhosphoSite; P13489; -.
DR DMDM; 132573; -.
DR REPRODUCTION-2DPAGE; IPI00550069; -.
DR PaxDb; P13489; -.
DR PeptideAtlas; P13489; -.
DR PRIDE; P13489; -.
DR Ensembl; ENST00000354420; ENSP00000346402; ENSG00000023191.
DR Ensembl; ENST00000356187; ENSP00000348515; ENSG00000023191.
DR Ensembl; ENST00000397604; ENSP00000380729; ENSG00000023191.
DR Ensembl; ENST00000397614; ENSP00000380738; ENSG00000023191.
DR Ensembl; ENST00000397615; ENSP00000380739; ENSG00000023191.
DR Ensembl; ENST00000438658; ENSP00000416589; ENSG00000023191.
DR Ensembl; ENST00000533410; ENSP00000435594; ENSG00000023191.
DR Ensembl; ENST00000534797; ENSP00000433999; ENSG00000023191.
DR GeneID; 6050; -.
DR KEGG; hsa:6050; -.
DR UCSC; uc001lpk.1; human.
DR CTD; 6050; -.
DR GeneCards; GC11M000485; -.
DR HGNC; HGNC:10074; RNH1.
DR HPA; HPA039223; -.
DR HPA; HPA040781; -.
DR MIM; 173320; gene.
DR neXtProt; NX_P13489; -.
DR PharmGKB; PA34447; -.
DR eggNOG; NOG308334; -.
DR HOGENOM; HOG000140402; -.
DR HOVERGEN; HBG001059; -.
DR InParanoid; P13489; -.
DR KO; K16634; -.
DR OMA; MEDRLQA; -.
DR OrthoDB; EOG7P5T07; -.
DR PhylomeDB; P13489; -.
DR ChiTaRS; RNH1; human.
DR EvolutionaryTrace; P13489; -.
DR GeneWiki; RNH1; -.
DR GenomeRNAi; 6050; -.
DR NextBio; 23577; -.
DR PRO; PR:P13489; -.
DR ArrayExpress; P13489; -.
DR Bgee; P13489; -.
DR CleanEx; HS_RNH1; -.
DR Genevestigator; P13489; -.
DR GO; GO:0032311; C:angiogenin-PRI complex; IPI:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; NAS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
DR InterPro; IPR003590; Leu-rich_rpt_RNase_inh_sub-typ.
DR SMART; SM00368; LRR_RI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Leucine-rich repeat; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 461 Ribonuclease inhibitor.
FT /FTId=PRO_0000097343.
FT REPEAT 20 48 LRR 1.
FT REPEAT 49 76 LRR 2.
FT REPEAT 77 105 LRR 3.
FT REPEAT 106 133 LRR 4.
FT REPEAT 134 162 LRR 5.
FT REPEAT 163 190 LRR 6.
FT REPEAT 191 219 LRR 7.
FT REPEAT 220 247 LRR 8.
FT REPEAT 248 276 LRR 9.
FT REPEAT 277 304 LRR 10.
FT REPEAT 305 333 LRR 11.
FT REPEAT 334 361 LRR 12.
FT REPEAT 362 390 LRR 13.
FT REPEAT 391 418 LRR 14.
FT REPEAT 419 447 LRR 15.
FT REGION 2 11 2 X 5 AA tandem repeats of S-L-D-I-Q.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 82 82 Phosphothreonine.
FT MOD_RES 91 91 Phosphoserine.
FT VARIANT 170 170 P -> L (in dbSNP:rs17585).
FT /FTId=VAR_014726.
FT MUTAGEN 262 262 W->A: Binding affinity decreased 5000-
FT fold over the wild type for RNASE2; when
FT associated with A-264 and A-319.
FT MUTAGEN 264 264 W->A: Substantially decreased binding
FT affinity for RNASE2. Binding affinity
FT decreased 5000-fold over the wild type
FT for RNASE2; when associated with A-262
FT and A-319.
FT MUTAGEN 319 319 W->A: Substantially decreased binding
FT affinity for RNASE2. Binding affinity
FT decreased 5000-fold over the wild type
FT for RNASE2; when associated with A-262
FT and A-264.
FT MUTAGEN 376 376 W->A: 40-fold reduction in binding
FT affinity for RNASE2.
FT MUTAGEN 435 436 YD->AA: Substantially decreases binding
FT affinity for RNASE1, ANG and RNASE2.
FT MUTAGEN 458 458 R->A: 25-fold reduction in binding
FT affinity for RNASE2.
FT MUTAGEN 461 461 Missing: A significant decrease in
FT binding affinity with RNASE1, slight
FT decrease for the ANG ligand, no real
FT change in binding affinity for RNASE2.
FT CONFLICT 188 188 R -> H (in Ref. 5; AAH03506).
FT CONFLICT 359 359 R -> A (in Ref. 3; AAL60586).
FT CONFLICT 365 365 L -> P (in Ref. 3; AAL60586).
FT CONFLICT 423 424 RQ -> SE (in Ref. 2; CAA32151/AAA60249).
FT STRAND 3 12
FT HELIX 17 27
FT STRAND 31 38
FT HELIX 42 53
FT STRAND 60 62
FT HELIX 69 78
FT STRAND 89 91
FT HELIX 99 101
FT HELIX 102 108
FT STRAND 117 119
FT STRAND 122 124
FT HELIX 126 137
FT STRAND 146 148
FT HELIX 156 158
FT HELIX 159 168
FT STRAND 174 176
FT STRAND 179 181
FT HELIX 183 196
FT STRAND 203 205
FT HELIX 215 225
FT STRAND 231 233
FT STRAND 236 238
FT HELIX 240 251
FT STRAND 260 262
FT HELIX 270 282
FT STRAND 288 290
FT HELIX 297 308
FT STRAND 310 312
FT STRAND 317 319
FT HELIX 327 329
FT HELIX 330 339
FT STRAND 345 347
FT STRAND 350 352
FT HELIX 354 365
FT STRAND 374 376
FT HELIX 384 396
FT STRAND 402 404
FT STRAND 407 409
FT HELIX 412 422
FT STRAND 431 433
FT HELIX 441 453
FT STRAND 457 460
SQ SEQUENCE 461 AA; 49973 MW; 5E88CDAC95BAE5B3 CRC64;
MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS ALRVNPALAE
LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA GCGVLSSTLR TLPTLQELHL
SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE YCSLSAASCE PLASVLRAKP DFKELTVSNN
DINEAGVRVL CQGLKDSPCQ LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG
DVGMAELCPG LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG
ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN NRLEDAGVRE
LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL RELDLSNNCL GDAGILQLVE
SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL EKDKPSLRVI S
//
ID RINI_HUMAN Reviewed; 461 AA.
AC P13489; Q8IZK8; Q96FD7; Q9BQ80; Q9UDK6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 157.
DE RecName: Full=Ribonuclease inhibitor;
DE AltName: Full=Placental ribonuclease inhibitor;
DE Short=Placental RNase inhibitor;
DE AltName: Full=Ribonuclease/angiogenin inhibitor 1;
DE Short=RAI;
GN Name=RNH1; Synonyms=PRI, RNH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-28; 35-44; 47-62;
RP 65-72; 87-130; 147-181; 189-200; 206-226; 231-235; 239-268; 272-276;
RP 288-295; 297-299; 303-316; 353-364; 374-394; 402-412; 424-449 AND
RP 453-461, AND OXIDATION STATE OF THE CYSTEINES.
RC TISSUE=Placenta;
RX PubMed=3219362; DOI=10.1021/bi00423a007;
RA Lee F.S., Fox E.A., Zhou H.-M., Strydom D.J., Vallee B.L.;
RT "Primary structure of human placental ribonuclease inhibitor.";
RL Biochemistry 27:8545-8553(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 444-462.
RX PubMed=3243277;
RA Schneider R., Schneider-Scherzer E., Thurnher M., Auer B.,
RA Schweiger M.;
RT "The primary structure of human ribonuclease/angiogenin inhibitor
RT (RAI) discloses a novel highly diversified protein superfamily with a
RT common repetitive module.";
RL EMBO J. 7:4151-4156(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=14515218;
RA Huang G.H., Yang G.Z., Chen J.Y., Wu X.F.;
RT "Expression of a human ribonuclease inhibitor variant in Escherichia
RT coli and silkworm insect cell (Bombyx mori).";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:960-963(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, Lymph, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Brain;
RX PubMed=8037455; DOI=10.1006/abbi.1994.1328;
RA Nadano D., Yasuda T., Takeshita H., Uchide K., Kishi K.;
RT "Purification and characterization of human brain ribonuclease
RT inhibitor.";
RL Arch. Biochem. Biophys. 312:421-428(1994).
RN [7]
RP PROTEIN SEQUENCE OF 174-195 AND 288-302, AND INTERACTION WITH RNASE1.
RX PubMed=1633192; DOI=10.1016/0167-4838(92)90134-Y;
RA Crevel-Thieffry I., Cotterill S., Schuller E.;
RT "Characterisation of a tryptic peptide from human placental
RT ribonuclease inhibitor which inhibits ribonuclease activity.";
RL Biochim. Biophys. Acta 1122:107-112(1992).
RN [8]
RP MUTAGENESIS OF SER-461, AND INTERACTION WITH ANG AND RNASE1.
RX PubMed=9050852; DOI=10.1073/pnas.94.5.1761;
RA Chen C.Z., Shapiro R.;
RT "Site-specific mutagenesis reveals differences in the structural bases
RT for tight binding of RNase inhibitor to angiogenin and RNase A.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1761-1766(1997).
RN [9]
RP MUTAGENESIS OF 435-TYR-ASP-436, AND INTERACTION WITH ANG AND RNASE1.
RX PubMed=10413501; DOI=10.1021/bi990762a;
RA Chen C.Z., Shapiro R.;
RT "Superadditive and subadditive effects of 'hot spot' mutations within
RT the interfaces of placental ribonuclease inhibitor with angiogenin and
RT ribonuclease A.";
RL Biochemistry 38:9273-9285(1999).
RN [10]
RP FUNCTION, MUTAGENESIS OF TRP-262; TRP-264; TRP-319; 435-TYR-ASP-436
RP AND SER-461, AND INTERACTION WITH RNASE2.
RX PubMed=12578357; DOI=10.1021/bi026852o;
RA Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.;
RT "Mutational analysis of the complex of human RNase inhibitor and human
RT eosinophil-derived neurotoxin (RNase 2).";
RL Biochemistry 42:1451-1459(2003).
RN [11]
RP FUNCTION.
RX PubMed=17292889; DOI=10.1016/j.febslet.2007.01.072;
RA Monti D.M., Montesano Gesualdi N., Matousek J., Esposito F.,
RA D'Alessio G.;
RT "The cytosolic ribonuclease inhibitor contributes to intracellular
RT redox homeostasis.";
RL FEBS Lett. 581:930-934(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH ANG,
RP INTERACTION WITH ANG, AND DOMAIN.
RX PubMed=9311977; DOI=10.1093/emboj/16.17.5162;
RA Papageorgiou A.C., Shapiro R., Acharya K.R.;
RT "Molecular recognition of human angiogenin by placental ribonuclease
RT inhibitor -- an X-ray crystallographic study at 2.0-A resolution.";
RL EMBO J. 16:5162-5177(1997).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-461 IN COMPLEX WITH RNASE2,
RP DOMAIN, INTERACTION WITH RNASE2, AND MUTAGENESIS OF TRP-376 AND
RP ARG-458.
RX PubMed=15755456; DOI=10.1016/j.jmb.2005.01.035;
RA Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.;
RT "Molecular recognition of human eosinophil-derived neurotoxin (RNase
RT 2) by placental ribonuclease inhibitor.";
RL J. Mol. Biol. 347:637-655(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH RNASE1, DOMAIN,
RP AND INTERACTION WITH RNASE1.
RX PubMed=17350650; DOI=10.1016/j.jmb.2007.02.005;
RA Johnson R.J., McCoy J.G., Bingman C.A., Phillips G.N. Jr.,
RA Raines R.T.;
RT "Inhibition of human pancreatic ribonuclease by the human ribonuclease
RT inhibitor protein.";
RL J. Mol. Biol. 368:434-449(2007).
CC -!- FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and
CC ANG. May play a role in redox homeostasis.
CC -!- SUBUNIT: Forms high-affinity heterodimers with RNASE1, ANG and
CC RNASE2.
CC -!- INTERACTION:
CC P03950:ANG; NbExp=2; IntAct=EBI-1237106, EBI-525291;
CC P07998:RNASE1; NbExp=2; IntAct=EBI-1237106, EBI-2823523;
CC P61823:RNASE1 (xeno); NbExp=3; IntAct=EBI-1237106, EBI-908364;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The LRR domain forms a horseshoe-shaped structure that
CC interacts tightly with target RNases via a large protein
CC interaction surface on its interior side.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: At least 30 of the 32 cysteine residues are in the reduced
CC form.
CC -!- SIMILARITY: Contains 15 LRR (leucine-rich) repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M22414; AAA59130.1; -; mRNA.
DR EMBL; M36717; AAA60249.1; -; mRNA.
DR EMBL; X13973; CAA32151.1; -; mRNA.
DR EMBL; AY071904; AAL60586.1; -; mRNA.
DR EMBL; AL161967; CAB82310.1; -; mRNA.
DR EMBL; BC000677; AAH00677.1; -; mRNA.
DR EMBL; BC003506; AAH03506.1; -; mRNA.
DR EMBL; BC011186; AAH11186.1; -; mRNA.
DR EMBL; BC011500; AAH11500.1; -; mRNA.
DR EMBL; BC014629; AAH14629.1; -; mRNA.
DR EMBL; BC024037; AAH24037.1; -; mRNA.
DR EMBL; BC047730; AAH47730.1; -; mRNA.
DR PIR; A31858; A31858.
DR RefSeq; NP_002930.2; NM_002939.3.
DR RefSeq; NP_976317.1; NM_203383.1.
DR RefSeq; NP_976318.1; NM_203384.1.
DR RefSeq; NP_976319.1; NM_203385.1.
DR RefSeq; NP_976320.1; NM_203386.2.
DR RefSeq; NP_976321.1; NM_203387.2.
DR RefSeq; NP_976322.1; NM_203388.2.
DR RefSeq; NP_976323.1; NM_203389.2.
DR RefSeq; XP_005253106.1; XM_005253049.1.
DR RefSeq; XP_005253107.1; XM_005253050.1.
DR RefSeq; XP_005253108.1; XM_005253051.1.
DR UniGene; Hs.530687; -.
DR PDB; 1A4Y; X-ray; 2.00 A; A/D=2-461.
DR PDB; 1Z7X; X-ray; 1.95 A; W/Y=1-461.
DR PDB; 2BEX; X-ray; 1.99 A; A/B=2-461.
DR PDB; 2Q4G; X-ray; 1.95 A; W/Y=1-461.
DR PDBsum; 1A4Y; -.
DR PDBsum; 1Z7X; -.
DR PDBsum; 2BEX; -.
DR PDBsum; 2Q4G; -.
DR ProteinModelPortal; P13489; -.
DR SMR; P13489; 2-461.
DR IntAct; P13489; 18.
DR MINT; MINT-5000705; -.
DR STRING; 9606.ENSP00000346402; -.
DR PhosphoSite; P13489; -.
DR DMDM; 132573; -.
DR REPRODUCTION-2DPAGE; IPI00550069; -.
DR PaxDb; P13489; -.
DR PeptideAtlas; P13489; -.
DR PRIDE; P13489; -.
DR Ensembl; ENST00000354420; ENSP00000346402; ENSG00000023191.
DR Ensembl; ENST00000356187; ENSP00000348515; ENSG00000023191.
DR Ensembl; ENST00000397604; ENSP00000380729; ENSG00000023191.
DR Ensembl; ENST00000397614; ENSP00000380738; ENSG00000023191.
DR Ensembl; ENST00000397615; ENSP00000380739; ENSG00000023191.
DR Ensembl; ENST00000438658; ENSP00000416589; ENSG00000023191.
DR Ensembl; ENST00000533410; ENSP00000435594; ENSG00000023191.
DR Ensembl; ENST00000534797; ENSP00000433999; ENSG00000023191.
DR GeneID; 6050; -.
DR KEGG; hsa:6050; -.
DR UCSC; uc001lpk.1; human.
DR CTD; 6050; -.
DR GeneCards; GC11M000485; -.
DR HGNC; HGNC:10074; RNH1.
DR HPA; HPA039223; -.
DR HPA; HPA040781; -.
DR MIM; 173320; gene.
DR neXtProt; NX_P13489; -.
DR PharmGKB; PA34447; -.
DR eggNOG; NOG308334; -.
DR HOGENOM; HOG000140402; -.
DR HOVERGEN; HBG001059; -.
DR InParanoid; P13489; -.
DR KO; K16634; -.
DR OMA; MEDRLQA; -.
DR OrthoDB; EOG7P5T07; -.
DR PhylomeDB; P13489; -.
DR ChiTaRS; RNH1; human.
DR EvolutionaryTrace; P13489; -.
DR GeneWiki; RNH1; -.
DR GenomeRNAi; 6050; -.
DR NextBio; 23577; -.
DR PRO; PR:P13489; -.
DR ArrayExpress; P13489; -.
DR Bgee; P13489; -.
DR CleanEx; HS_RNH1; -.
DR Genevestigator; P13489; -.
DR GO; GO:0032311; C:angiogenin-PRI complex; IPI:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; NAS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
DR InterPro; IPR003590; Leu-rich_rpt_RNase_inh_sub-typ.
DR SMART; SM00368; LRR_RI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Leucine-rich repeat; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 461 Ribonuclease inhibitor.
FT /FTId=PRO_0000097343.
FT REPEAT 20 48 LRR 1.
FT REPEAT 49 76 LRR 2.
FT REPEAT 77 105 LRR 3.
FT REPEAT 106 133 LRR 4.
FT REPEAT 134 162 LRR 5.
FT REPEAT 163 190 LRR 6.
FT REPEAT 191 219 LRR 7.
FT REPEAT 220 247 LRR 8.
FT REPEAT 248 276 LRR 9.
FT REPEAT 277 304 LRR 10.
FT REPEAT 305 333 LRR 11.
FT REPEAT 334 361 LRR 12.
FT REPEAT 362 390 LRR 13.
FT REPEAT 391 418 LRR 14.
FT REPEAT 419 447 LRR 15.
FT REGION 2 11 2 X 5 AA tandem repeats of S-L-D-I-Q.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 82 82 Phosphothreonine.
FT MOD_RES 91 91 Phosphoserine.
FT VARIANT 170 170 P -> L (in dbSNP:rs17585).
FT /FTId=VAR_014726.
FT MUTAGEN 262 262 W->A: Binding affinity decreased 5000-
FT fold over the wild type for RNASE2; when
FT associated with A-264 and A-319.
FT MUTAGEN 264 264 W->A: Substantially decreased binding
FT affinity for RNASE2. Binding affinity
FT decreased 5000-fold over the wild type
FT for RNASE2; when associated with A-262
FT and A-319.
FT MUTAGEN 319 319 W->A: Substantially decreased binding
FT affinity for RNASE2. Binding affinity
FT decreased 5000-fold over the wild type
FT for RNASE2; when associated with A-262
FT and A-264.
FT MUTAGEN 376 376 W->A: 40-fold reduction in binding
FT affinity for RNASE2.
FT MUTAGEN 435 436 YD->AA: Substantially decreases binding
FT affinity for RNASE1, ANG and RNASE2.
FT MUTAGEN 458 458 R->A: 25-fold reduction in binding
FT affinity for RNASE2.
FT MUTAGEN 461 461 Missing: A significant decrease in
FT binding affinity with RNASE1, slight
FT decrease for the ANG ligand, no real
FT change in binding affinity for RNASE2.
FT CONFLICT 188 188 R -> H (in Ref. 5; AAH03506).
FT CONFLICT 359 359 R -> A (in Ref. 3; AAL60586).
FT CONFLICT 365 365 L -> P (in Ref. 3; AAL60586).
FT CONFLICT 423 424 RQ -> SE (in Ref. 2; CAA32151/AAA60249).
FT STRAND 3 12
FT HELIX 17 27
FT STRAND 31 38
FT HELIX 42 53
FT STRAND 60 62
FT HELIX 69 78
FT STRAND 89 91
FT HELIX 99 101
FT HELIX 102 108
FT STRAND 117 119
FT STRAND 122 124
FT HELIX 126 137
FT STRAND 146 148
FT HELIX 156 158
FT HELIX 159 168
FT STRAND 174 176
FT STRAND 179 181
FT HELIX 183 196
FT STRAND 203 205
FT HELIX 215 225
FT STRAND 231 233
FT STRAND 236 238
FT HELIX 240 251
FT STRAND 260 262
FT HELIX 270 282
FT STRAND 288 290
FT HELIX 297 308
FT STRAND 310 312
FT STRAND 317 319
FT HELIX 327 329
FT HELIX 330 339
FT STRAND 345 347
FT STRAND 350 352
FT HELIX 354 365
FT STRAND 374 376
FT HELIX 384 396
FT STRAND 402 404
FT STRAND 407 409
FT HELIX 412 422
FT STRAND 431 433
FT HELIX 441 453
FT STRAND 457 460
SQ SEQUENCE 461 AA; 49973 MW; 5E88CDAC95BAE5B3 CRC64;
MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS ALRVNPALAE
LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA GCGVLSSTLR TLPTLQELHL
SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE YCSLSAASCE PLASVLRAKP DFKELTVSNN
DINEAGVRVL CQGLKDSPCQ LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG
DVGMAELCPG LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG
ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN NRLEDAGVRE
LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL RELDLSNNCL GDAGILQLVE
SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL EKDKPSLRVI S
//
MIM
173320
*RECORD*
*FIELD* NO
173320
*FIELD* TI
*173320 RIBONUCLEASE/ANGIOGENIN INHIBITOR; RNH
;;PLACENTAL RIBONUCLEASE INHIBITOR
*FIELD* TX
read more
DESCRIPTION
Placental ribonuclease inhibitor (PRI) is a member of a family of
proteinaceous cytoplasmic RNase inhibitors that occur in many tissues
and bind to both intracellular and extracellular RNases. In addition to
control of intracellular RNases, the inhibitor may have a role in the
regulation of angiogenin (105850). Ribonuclease inhibitor, of 50,000 Da,
binds to ribonucleases and holds them in a latent form. Since neutral
and alkaline ribonucleases probably play a critical role in the turnover
of RNA in eukaryotic cells, RNH may be essential for control of mRNA
turnover; the interaction of eukaryotic cells with ribonuclease may be
reversible in vivo (summary by Lee et al., 1988).
CLONING
Lee et al. (1988) determined the primary structure of PRI from the cDNA.
The mature protein encodes a 460-amino acid polypeptide with a molecular
mass of 49,847 kD. The amino acid sequence contains 7 direct internal
repeat units, each 57 amino acids in length. These repeat units comprise
87% of the molecule. The average degree of identity between any 2 is
39%.
MAPPING
By study of human-rodent somatic cell hybrids and by in situ
hybridization, Weremowicz et al. (1990) mapped the PRI gene to 11p15.
The localization was further refined to 11p15.5, distal to the IGF2
gene, by in situ hybridization to metaphase chromosomes from a cell line
with a well-characterized translocation involving a breakpoint between
IGF2 (147470) and HRAS (190020). Zneimer et al. (1990) localized the RNH
gene to 11p15.5 by in situ hybridization.
*FIELD* RF
1. Lee, F. S.; Fox, E. A.; Zhou, H.-M.; Strydom, D. J.; Vallee, B.
L.: Primary structure of human placental ribonuclease inhibitor. Biochemistry 27:
8545-8553, 1988. Note: Erratum: Biochemistry 28: 7138 only, 1989.
2. Weremowicz, S.; Fox, E. A.; Morton, C. C.; Vallee, B. L.: The
placental ribonuclease inhibitor (RNH) gene is located on chromosome
subband 11p15.5. Genomics 8: 717-721, 1990.
3. Zneimer, S. M.; Crawford, D.; Schneider, N. R.; Beutler, B.: Mapping
of the human ribonuclease inhibitor gene (RNH) to chromosome 11p15
by in situ hybridization. Genomics 8: 175-178, 1990.
*FIELD* CD
Victor A. McKusick: 1/5/1989
*FIELD* ED
terry: 11/27/2012
alopez: 3/7/2012
alopez: 3/5/2012
alopez: 7/8/2010
carol: 7/9/2003
dholmes: 9/15/1997
supermim: 3/16/1992
carol: 12/6/1990
carol: 9/8/1990
carol: 8/20/1990
supermim: 3/20/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
173320
*FIELD* TI
*173320 RIBONUCLEASE/ANGIOGENIN INHIBITOR; RNH
;;PLACENTAL RIBONUCLEASE INHIBITOR
*FIELD* TX
read more
DESCRIPTION
Placental ribonuclease inhibitor (PRI) is a member of a family of
proteinaceous cytoplasmic RNase inhibitors that occur in many tissues
and bind to both intracellular and extracellular RNases. In addition to
control of intracellular RNases, the inhibitor may have a role in the
regulation of angiogenin (105850). Ribonuclease inhibitor, of 50,000 Da,
binds to ribonucleases and holds them in a latent form. Since neutral
and alkaline ribonucleases probably play a critical role in the turnover
of RNA in eukaryotic cells, RNH may be essential for control of mRNA
turnover; the interaction of eukaryotic cells with ribonuclease may be
reversible in vivo (summary by Lee et al., 1988).
CLONING
Lee et al. (1988) determined the primary structure of PRI from the cDNA.
The mature protein encodes a 460-amino acid polypeptide with a molecular
mass of 49,847 kD. The amino acid sequence contains 7 direct internal
repeat units, each 57 amino acids in length. These repeat units comprise
87% of the molecule. The average degree of identity between any 2 is
39%.
MAPPING
By study of human-rodent somatic cell hybrids and by in situ
hybridization, Weremowicz et al. (1990) mapped the PRI gene to 11p15.
The localization was further refined to 11p15.5, distal to the IGF2
gene, by in situ hybridization to metaphase chromosomes from a cell line
with a well-characterized translocation involving a breakpoint between
IGF2 (147470) and HRAS (190020). Zneimer et al. (1990) localized the RNH
gene to 11p15.5 by in situ hybridization.
*FIELD* RF
1. Lee, F. S.; Fox, E. A.; Zhou, H.-M.; Strydom, D. J.; Vallee, B.
L.: Primary structure of human placental ribonuclease inhibitor. Biochemistry 27:
8545-8553, 1988. Note: Erratum: Biochemistry 28: 7138 only, 1989.
2. Weremowicz, S.; Fox, E. A.; Morton, C. C.; Vallee, B. L.: The
placental ribonuclease inhibitor (RNH) gene is located on chromosome
subband 11p15.5. Genomics 8: 717-721, 1990.
3. Zneimer, S. M.; Crawford, D.; Schneider, N. R.; Beutler, B.: Mapping
of the human ribonuclease inhibitor gene (RNH) to chromosome 11p15
by in situ hybridization. Genomics 8: 175-178, 1990.
*FIELD* CD
Victor A. McKusick: 1/5/1989
*FIELD* ED
terry: 11/27/2012
alopez: 3/7/2012
alopez: 3/5/2012
alopez: 7/8/2010
carol: 7/9/2003
dholmes: 9/15/1997
supermim: 3/16/1992
carol: 12/6/1990
carol: 9/8/1990
carol: 8/20/1990
supermim: 3/20/1990
ddp: 10/27/1989