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P13489

- RINI_HUMAN

UniProt

P13489 - RINI_HUMAN

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Protein

Ribonuclease inhibitor

Gene

RNH1

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

Functioni

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

GO - Molecular functioni

  1. ribonuclease inhibitor activity Source: UniProtKB

GO - Biological processi

  1. mRNA catabolic process Source: UniProtKB
  2. negative regulation of catalytic activity Source: GOC
  3. regulation of angiogenesis Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease inhibitor
Alternative name(s):
Placental ribonuclease inhibitor
Short name:
Placental RNase inhibitor
Ribonuclease/angiogenin inhibitor 1
Short name:
RAI
Gene namesi
Name:RNH1
Synonyms:PRI, RNH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10074. RNH1.

Subcellular locationi

GO - Cellular componenti

  1. angiogenin-PRI complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi262 – 2621W → A: Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-264 and A-319. 1 Publication
Mutagenesisi264 – 2641W → 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. 1 Publication
Mutagenesisi319 – 3191W → 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. 1 Publication
Mutagenesisi376 – 3761W → A: 40-fold reduction in binding affinity for RNASE2. 1 Publication
Mutagenesisi435 – 4362YD → AA: Substantially decreases binding affinity for RNASE1, ANG and RNASE2. 2 Publications
Mutagenesisi458 – 4581R → A: 25-fold reduction in binding affinity for RNASE2. 1 Publication
Mutagenesisi461 – 4611Missing: A significant decrease in binding affinity with RNASE1, slight decrease for the ANG ligand, no real change in binding affinity for RNASE2. 2 Publications

Organism-specific databases

PharmGKBiPA34447.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 461460Ribonuclease inhibitorPRO_0000097343Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei82 – 821Phosphothreonine1 Publication
Modified residuei91 – 911Phosphoserine1 Publication

Post-translational modificationi

The N-terminus is blocked.
At least 30 of the 32 cysteine residues are in the reduced form.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13489.
PaxDbiP13489.
PeptideAtlasiP13489.
PRIDEiP13489.

2D gel databases

REPRODUCTION-2DPAGEIPI00550069.

PTM databases

PhosphoSiteiP13489.

Expressioni

Gene expression databases

BgeeiP13489.
CleanExiHS_RNH1.
ExpressionAtlasiP13489. baseline and differential.
GenevestigatoriP13489.

Organism-specific databases

HPAiHPA039223.
HPA040781.

Interactioni

Subunit structurei

Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANGP039502EBI-1237106,EBI-525291
RNASE1P079982EBI-1237106,EBI-2823523
RNASE1P618233EBI-1237106,EBI-908364From a different organism.

Protein-protein interaction databases

BioGridi111977. 28 interactions.
IntActiP13489. 18 interactions.
MINTiMINT-5000705.
STRINGi9606.ENSP00000346402.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210
Helixi17 – 2711
Beta strandi31 – 388
Helixi42 – 5312
Beta strandi60 – 623
Helixi69 – 7810
Beta strandi89 – 913
Helixi99 – 1013
Helixi102 – 1087
Beta strandi117 – 1193
Beta strandi122 – 1243
Helixi126 – 13712
Beta strandi146 – 1483
Helixi156 – 1583
Helixi159 – 16810
Beta strandi174 – 1763
Beta strandi179 – 1813
Helixi183 – 19614
Beta strandi203 – 2053
Helixi215 – 22511
Beta strandi231 – 2333
Beta strandi236 – 2383
Helixi240 – 25112
Beta strandi260 – 2623
Helixi270 – 28213
Beta strandi288 – 2903
Helixi297 – 30812
Beta strandi310 – 3123
Beta strandi317 – 3193
Helixi327 – 3293
Helixi330 – 33910
Beta strandi345 – 3473
Beta strandi350 – 3523
Helixi354 – 36512
Beta strandi374 – 3763
Helixi384 – 39613
Beta strandi402 – 4043
Beta strandi407 – 4093
Helixi412 – 42211
Beta strandi431 – 4333
Helixi441 – 45313
Beta strandi457 – 4604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4YX-ray2.00A/D2-461[»]
1Z7XX-ray1.95W/Y1-461[»]
2BEXX-ray1.99A/B2-461[»]
2Q4GX-ray1.95W/Y1-461[»]
ProteinModelPortaliP13489.
SMRiP13489. Positions 2-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13489.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati20 – 4829LRR 1Add
BLAST
Repeati49 – 7628LRR 2Add
BLAST
Repeati77 – 10529LRR 3Add
BLAST
Repeati106 – 13328LRR 4Add
BLAST
Repeati134 – 16229LRR 5Add
BLAST
Repeati163 – 19028LRR 6Add
BLAST
Repeati191 – 21929LRR 7Add
BLAST
Repeati220 – 24728LRR 8Add
BLAST
Repeati248 – 27629LRR 9Add
BLAST
Repeati277 – 30428LRR 10Add
BLAST
Repeati305 – 33329LRR 11Add
BLAST
Repeati334 – 36128LRR 12Add
BLAST
Repeati362 – 39029LRR 13Add
BLAST
Repeati391 – 41828LRR 14Add
BLAST
Repeati419 – 44729LRR 15Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 11102 X 5 AA tandem repeats of S-L-D-I-Q

Domaini

The LRR domain forms a horseshoe-shaped structure that interacts tightly with target RNases via a large protein interaction surface on its interior side.3 Publications

Sequence similaritiesi

Contains 15 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG308334.
GeneTreeiENSGT00760000118770.
HOGENOMiHOG000140402.
HOVERGENiHBG001059.
InParanoidiP13489.
KOiK16634.
OMAiVQELCQG.
OrthoDBiEOG7P5T07.
PhylomeDBiP13489.

Family and domain databases

InterProiIPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
[Graphical view]
SMARTiSM00368. LRR_RI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13489-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS
60 70 80 90 100
ALRVNPALAE LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA
110 120 130 140 150
GCGVLSSTLR TLPTLQELHL SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE
160 170 180 190 200
YCSLSAASCE PLASVLRAKP DFKELTVSNN DINEAGVRVL CQGLKDSPCQ
210 220 230 240 250
LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG DVGMAELCPG
260 270 280 290 300
LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG
310 320 330 340 350
ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN
360 370 380 390 400
NRLEDAGVRE LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL
410 420 430 440 450
RELDLSNNCL GDAGILQLVE SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL
460
EKDKPSLRVI S
Length:461
Mass (Da):49,973
Last modified:January 23, 2007 - v2
Checksum:i5E88CDAC95BAE5B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881R → H in AAH03506. (PubMed:15489334)Curated
Sequence conflicti359 – 3591R → A in AAL60586. (PubMed:14515218)Curated
Sequence conflicti365 – 3651L → P in AAL60586. (PubMed:14515218)Curated
Sequence conflicti423 – 4242RQ → SE in CAA32151. (PubMed:3243277)Curated
Sequence conflicti423 – 4242RQ → SE in AAA60249. (PubMed:3243277)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701P → L.
Corresponds to variant rs17585 [ dbSNP | Ensembl ].
VAR_014726

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7697.1.
PIRiA31858.
RefSeqiNP_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.
UniGeneiHs.530687.

Genome annotation databases

EnsembliENST00000354420; ENSP00000346402; ENSG00000023191.
ENST00000356187; ENSP00000348515; ENSG00000023191.
ENST00000397604; ENSP00000380729; ENSG00000023191.
ENST00000397614; ENSP00000380738; ENSG00000023191.
ENST00000397615; ENSP00000380739; ENSG00000023191.
ENST00000438658; ENSP00000416589; ENSG00000023191.
ENST00000533410; ENSP00000435594; ENSG00000023191.
ENST00000534797; ENSP00000433999; ENSG00000023191.
GeneIDi6050.
KEGGihsa:6050.
UCSCiuc001lpk.1. human.

Polymorphism databases

DMDMi132573.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS7697.1.
PIRi A31858.
RefSeqi NP_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.
UniGenei Hs.530687.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4Y X-ray 2.00 A/D 2-461 [» ]
1Z7X X-ray 1.95 W/Y 1-461 [» ]
2BEX X-ray 1.99 A/B 2-461 [» ]
2Q4G X-ray 1.95 W/Y 1-461 [» ]
ProteinModelPortali P13489.
SMRi P13489. Positions 2-461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111977. 28 interactions.
IntActi P13489. 18 interactions.
MINTi MINT-5000705.
STRINGi 9606.ENSP00000346402.

PTM databases

PhosphoSitei P13489.

Polymorphism databases

DMDMi 132573.

2D gel databases

REPRODUCTION-2DPAGE IPI00550069.

Proteomic databases

MaxQBi P13489.
PaxDbi P13489.
PeptideAtlasi P13489.
PRIDEi P13489.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354420 ; ENSP00000346402 ; ENSG00000023191 .
ENST00000356187 ; ENSP00000348515 ; ENSG00000023191 .
ENST00000397604 ; ENSP00000380729 ; ENSG00000023191 .
ENST00000397614 ; ENSP00000380738 ; ENSG00000023191 .
ENST00000397615 ; ENSP00000380739 ; ENSG00000023191 .
ENST00000438658 ; ENSP00000416589 ; ENSG00000023191 .
ENST00000533410 ; ENSP00000435594 ; ENSG00000023191 .
ENST00000534797 ; ENSP00000433999 ; ENSG00000023191 .
GeneIDi 6050.
KEGGi hsa:6050.
UCSCi uc001lpk.1. human.

Organism-specific databases

CTDi 6050.
GeneCardsi GC11M000485.
HGNCi HGNC:10074. RNH1.
HPAi HPA039223.
HPA040781.
MIMi 173320. gene.
neXtProti NX_P13489.
PharmGKBi PA34447.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG308334.
GeneTreei ENSGT00760000118770.
HOGENOMi HOG000140402.
HOVERGENi HBG001059.
InParanoidi P13489.
KOi K16634.
OMAi VQELCQG.
OrthoDBi EOG7P5T07.
PhylomeDBi P13489.

Miscellaneous databases

ChiTaRSi RNH1. human.
EvolutionaryTracei P13489.
GeneWikii RNH1.
GenomeRNAii 6050.
NextBioi 23577.
PROi P13489.
SOURCEi Search...

Gene expression databases

Bgeei P13489.
CleanExi HS_RNH1.
ExpressionAtlasi P13489. baseline and differential.
Genevestigatori P13489.

Family and domain databases

InterProi IPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
[Graphical view ]
SMARTi SM00368. LRR_RI. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiRINI_HUMAN
AccessioniPrimary (citable) accession number: P13489
Secondary accession number(s): Q8IZK8
, Q96FD7, Q9BQ80, Q9UDK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 166 of the entry and version 2 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

External Data

Dasty 3