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P13489

- RINI_HUMAN

UniProt

P13489 - RINI_HUMAN

Protein

Ribonuclease inhibitor

Gene

RNH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. 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

    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: UniProt

    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. 2 Publications
    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. 2 Publications
    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. 2 Publications
    Mutagenesisi376 – 3761W → A: 40-fold reduction in binding affinity for RNASE2. 2 Publications
    Mutagenesisi435 – 4362YD → AA: Substantially decreases binding affinity for RNASE1, ANG and RNASE2. 1 Publication
    Mutagenesisi458 – 4581R → A: 25-fold reduction in binding affinity for RNASE2. 2 Publications
    Mutagenesisi461 – 4611Missing: A significant decrease in binding affinity with RNASE1, slight decrease for the ANG ligand, no real change in binding affinity for RNASE2. 3 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

    ArrayExpressiP13489.
    BgeeiP13489.
    CleanExiHS_RNH1.
    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. 25 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.
    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

    MSLDIQSLDI QCEELSDARW AELLPLLQQC QVVRLDDCGL TEARCKDISS    50
    ALRVNPALAE LNLRSNELGD VGVHCVLQGL QTPSCKIQKL SLQNCCLTGA 100
    GCGVLSSTLR TLPTLQELHL SDNLLGDAGL QLLCEGLLDP QCRLEKLQLE 150
    YCSLSAASCE PLASVLRAKP DFKELTVSNN DINEAGVRVL CQGLKDSPCQ 200
    LEALKLESCG VTSDNCRDLC GIVASKASLR ELALGSNKLG DVGMAELCPG 250
    LLHPSSRLRT LWIWECGITA KGCGDLCRVL RAKESLKELS LAGNELGDEG 300
    ARLLCETLLE PGCQLESLWV KSCSFTAACC SHFSSVLAQN RFLLELQISN 350
    NRLEDAGVRE LCQGLGQPGS VLRVLWLADC DVSDSSCSSL AATLLANHSL 400
    RELDLSNNCL GDAGILQLVE SVRQPGCLLE QLVLYDIYWS EEMEDRLQAL 450
    EKDKPSLRVI S 461
    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. 25 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.
    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

    ArrayExpressi P13489.
    Bgeei P13489.
    CleanExi HS_RNH1.
    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

    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 1, 2014
    This is version 165 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