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Protein

Ribonuclease pancreatic

Gene

RNASE1

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

Functioni

Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.1 Publication

Catalytic activityi

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351SubstrateBy similarity
Binding sitei38 – 381SubstrateBy similarity
Active sitei40 – 401Proton acceptor
Binding sitei94 – 941SubstrateBy similarity
Binding sitei113 – 1131SubstrateBy similarity
Active sitei147 – 1471Proton donor

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. pancreatic ribonuclease activity Source: ProtInc

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease pancreatic (EC:3.1.27.5)
Alternative name(s):
HP-RNase
RIB-1
RNase UpI-1
Ribonuclease 1
Short name:
RNase 1
Ribonuclease A
Short name:
RNase A
Gene namesi
Name:RNASE1
Synonyms:RIB1, RNS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:10044. RNASE1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119. 1 Publication
Mutagenesisi95 – 951N → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119. 1 Publication
Mutagenesisi116 – 1172NG → RS: No effect on inhibition by RNH1. 1 Publication
Mutagenesisi116 – 1161N → A: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119. 1 Publication
Mutagenesisi117 – 1171G → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119. 1 Publication
Mutagenesisi119 – 1191R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117. 1 Publication

Organism-specific databases

PharmGKBiPA34412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28286 PublicationsAdd
BLAST
Chaini29 – 156128Ribonuclease pancreaticPRO_0000030921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 112
Glycosylationi62 – 621N-linked (GlcNAc...); partial1 Publication
Disulfide bondi68 ↔ 123
Disulfide bondi86 ↔ 138
Disulfide bondi93 ↔ 100
Glycosylationi104 – 1041N-linked (GlcNAc...)1 Publication
Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-linked glycans are of complex type.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP07998.
PeptideAtlasiP07998.
PRIDEiP07998.

PTM databases

PhosphoSiteiP07998.

Expressioni

Tissue specificityi

Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).

Gene expression databases

BgeeiP07998.
CleanExiHS_RNASE1.
ExpressionAtlasiP07998. baseline and differential.
GenevestigatoriP07998.

Organism-specific databases

HPAiHPA001140.

Interactioni

Subunit structurei

Monomer. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RNH1P134892EBI-2823523,EBI-1237106

Protein-protein interaction databases

BioGridi111964. 1 interaction.
IntActiP07998. 6 interactions.
MINTiMINT-4845964.
STRINGi9606.ENSP00000344193.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 409Combined sources
Turni47 – 504Combined sources
Helixi53 – 608Combined sources
Turni61 – 644Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 756Combined sources
Helixi79 – 835Combined sources
Helixi84 – 874Combined sources
Beta strandi88 – 925Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi125 – 13915Combined sources
Turni140 – 1434Combined sources
Beta strandi144 – 1529Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZAX-ray1.65A/B28-156[»]
1E21X-ray1.90A29-156[»]
1H8XX-ray2.00A/B29-156[»]
1Z7XX-ray1.95X/Z29-156[»]
2E0JX-ray1.60A/B29-156[»]
2E0LX-ray1.60A/B29-156[»]
2E0MX-ray1.70A/B29-156[»]
2E0OX-ray2.00A/B29-156[»]
2K11NMR-A29-155[»]
2Q4GX-ray1.95X/Z29-156[»]
3F8GX-ray2.60A/B29-153[»]
4KXHX-ray2.70A/B/C/D29-156[»]
ProteinModelPortaliP07998.
SMRiP07998. Positions 36-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07998.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 735Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40319.
HOVERGENiHBG008396.
InParanoidiP07998.
KOiK01168.
OMAiNCAYRTS.
OrthoDBiEOG7J1826.
PhylomeDBiP07998.
TreeFamiTF333393.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07998-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS
60 70 80 90 100
STYCNQMMRR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC
110 120 130 140 150
YKSNSSMHIT DCRLTNGSRY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA

SVEDST
Length:156
Mass (Da):17,644
Last modified:February 1, 1996 - v4
Checksum:iF63B17B8B55115F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → G in CAA55817. (PubMed:8588814)Curated
Sequence conflicti4 – 41Missing in AAB35096. (PubMed:7649283)Curated
Sequence conflicti9 – 113RLL → VLP in AAB35096. (PubMed:7649283)Curated
Sequence conflicti16 – 227ILLVLGW → VLLLVR in AAB35096. (PubMed:7649283)Curated
Sequence conflicti67 – 671R → L in CAG29314. 1 PublicationCurated
Sequence conflicti151 – 1511S → T in CAA55817. (PubMed:8588814)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26129 mRNA. Translation: BAA05124.1.
DQ494867 Genomic DNA. Translation: ABF00144.1.
AK312100 mRNA. Translation: BAG35036.1.
CR450318 mRNA. Translation: CAG29314.1.
CH471078 Genomic DNA. Translation: EAW66437.1.
CH471078 Genomic DNA. Translation: EAW66438.1.
BC005324 mRNA. Translation: AAH05324.1.
BC022882 mRNA. Translation: AAH22882.1.
X79235 Genomic DNA. Translation: CAA55817.1.
S79281 mRNA. Translation: AAB35096.1.
X62946 Genomic DNA. Translation: CAA44718.1.
CCDSiCCDS9559.1.
PIRiI53530.
S45003. NRHU1.
RefSeqiNP_002924.1. NM_002933.4.
NP_937875.1. NM_198232.2.
NP_937877.1. NM_198234.2.
NP_937878.1. NM_198235.2.
UniGeneiHs.78224.

Genome annotation databases

EnsembliENST00000340900; ENSP00000344193; ENSG00000129538.
ENST00000397967; ENSP00000381057; ENSG00000129538.
ENST00000397970; ENSP00000381060; ENSG00000129538.
ENST00000412779; ENSP00000399493; ENSG00000129538.
GeneIDi6035.
KEGGihsa:6035.
UCSCiuc001vyf.3. human.

Polymorphism databases

DMDMi1350818.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26129 mRNA. Translation: BAA05124.1.
DQ494867 Genomic DNA. Translation: ABF00144.1.
AK312100 mRNA. Translation: BAG35036.1.
CR450318 mRNA. Translation: CAG29314.1.
CH471078 Genomic DNA. Translation: EAW66437.1.
CH471078 Genomic DNA. Translation: EAW66438.1.
BC005324 mRNA. Translation: AAH05324.1.
BC022882 mRNA. Translation: AAH22882.1.
X79235 Genomic DNA. Translation: CAA55817.1.
S79281 mRNA. Translation: AAB35096.1.
X62946 Genomic DNA. Translation: CAA44718.1.
CCDSiCCDS9559.1.
PIRiI53530.
S45003. NRHU1.
RefSeqiNP_002924.1. NM_002933.4.
NP_937875.1. NM_198232.2.
NP_937877.1. NM_198234.2.
NP_937878.1. NM_198235.2.
UniGeneiHs.78224.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZAX-ray1.65A/B28-156[»]
1E21X-ray1.90A29-156[»]
1H8XX-ray2.00A/B29-156[»]
1Z7XX-ray1.95X/Z29-156[»]
2E0JX-ray1.60A/B29-156[»]
2E0LX-ray1.60A/B29-156[»]
2E0MX-ray1.70A/B29-156[»]
2E0OX-ray2.00A/B29-156[»]
2K11NMR-A29-155[»]
2Q4GX-ray1.95X/Z29-156[»]
3F8GX-ray2.60A/B29-153[»]
4KXHX-ray2.70A/B/C/D29-156[»]
ProteinModelPortaliP07998.
SMRiP07998. Positions 36-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111964. 1 interaction.
IntActiP07998. 6 interactions.
MINTiMINT-4845964.
STRINGi9606.ENSP00000344193.

Chemistry

BindingDBiP07998.
ChEMBLiCHEMBL5425.
DrugBankiDB00536. Guanidine.
DB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteiP07998.

Polymorphism databases

DMDMi1350818.

Proteomic databases

PaxDbiP07998.
PeptideAtlasiP07998.
PRIDEiP07998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340900; ENSP00000344193; ENSG00000129538.
ENST00000397967; ENSP00000381057; ENSG00000129538.
ENST00000397970; ENSP00000381060; ENSG00000129538.
ENST00000412779; ENSP00000399493; ENSG00000129538.
GeneIDi6035.
KEGGihsa:6035.
UCSCiuc001vyf.3. human.

Organism-specific databases

CTDi6035.
GeneCardsiGC14M021269.
HGNCiHGNC:10044. RNASE1.
HPAiHPA001140.
MIMi180440. gene.
neXtProtiNX_P07998.
PharmGKBiPA34412.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40319.
HOVERGENiHBG008396.
InParanoidiP07998.
KOiK01168.
OMAiNCAYRTS.
OrthoDBiEOG7J1826.
PhylomeDBiP07998.
TreeFamiTF333393.

Miscellaneous databases

ChiTaRSiRNASE1. human.
EvolutionaryTraceiP07998.
GeneWikiiRNASE1.
GenomeRNAii6035.
NextBioi23515.
PROiP07998.
SOURCEiSearch...

Gene expression databases

BgeeiP07998.
CleanExiHS_RNASE1.
ExpressionAtlasiP07998. baseline and differential.
GenevestigatoriP07998.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR001427. RNaseA.
IPR023411. RNaseA_AS.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00092. RNAse_Pc. 1 hit.
[Graphical view]
SUPFAMiSSF54076. SSF54076. 1 hit.
PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence encoding human pancreatic ribonuclease."
    Seno M., Fatami J.I., Kosaka M., Seno S., Yamada H.
    Biochim. Biophys. Acta 1218:466-468(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  2. "Duplication and divergence of two distinct pancreatic ribonuclease genes in leaf-eating African and Asian colobine monkeys."
    Schienman J.E., Holt R.A., Auerbach M.R., Stewart C.B.
    Mol. Biol. Evol. 23:1465-1479(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Pancreas and Prostate.
  7. "Primary structure of the coding part of the gene for human pancreatic ribonuclease and its chromosomal location."
    Kochetov A.V., Lukasheva V.V., Filipenko M.L., Mertvetsov N.P., Rivkin M.I.
    Bioorg. Khim. 21:691-694(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
    Tissue: Placenta.
  8. "Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease."
    Russo N., de Nigris M., Ciardiello A., Di Donato A., D'Alessio G.
    FEBS Lett. 369:352-352(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-155.
  9. "The DNA sequences of the human and hamster secretory ribonucleases determined with the polymerase chain reaction (PCR)."
    Haugg M., Schein C.H.
    Nucleic Acids Res. 20:612-612(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-149.
    Tissue: Placenta.
  10. "The amino acid sequence of human pancreatic ribonuclease."
    Beintema J.J., Wietzes P., Weickmann J.L., Glitz D.G.
    Anal. Biochem. 136:48-64(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-156.
    Tissue: Pancreas.
  11. "Differences in glycosylation pattern of human secretory ribonucleases."
    Beintema J.J., Blank A., Schieven G.L., Dekker C.A., Sorrentino S., Libonati M.
    Biochem. J. 255:501-505(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-156, GLYCOSYLATION AT ASN-62; ASN-104 AND ASN-116.
  12. "Purification and characterization of three ribonucleases from human kidney: comparison with urine ribonucleases."
    Mizuta K., Awazu S., Yasuda T., Kishi K.
    Arch. Biochem. Biophys. 281:144-151(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-47.
  13. "A putative mouse oocyte maturation inhibitory protein from urine of pregnant women: N-terminal sequence homology with human nonsecretory ribonuclease."
    Sakakibara R., Hashida K., Tominaga N., Sakai K., Ishiguro M., Imamura S., Ohmatsu F., Sato E.
    Chem. Pharm. Bull. 39:146-149(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-43.
  14. "Characterization of a unique nonsecretory ribonuclease from urine of pregnant women."
    Sakakibara R., Hashida K., Kitahara T., Ishiguro M.
    J. Biochem. 111:325-330(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-48.
    Tissue: Urine.
  15. "Two distinct secretory ribonucleases from human cerebrum: purification, characterization and relationships to other ribonucleases."
    Yasuda T., Nadano D., Takeshita H., Kishi K.
    Biochem. J. 296:617-625(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-49.
  16. "Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases."
    Pous J., Canals A., Terzyan S.S., Guasch A., Benito A., Ribo M., Vilanova M., Coll M.
    J. Mol. Biol. 303:49-60(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-156, MUTAGENESIS OF 116-ASN-GLY-117.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-156.
  18. "The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization."
    Canals A., Pous J., Guasch A., Benito A., Ribo M., Vilanova M., Coll M.
    Structure 9:967-976(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-156, DISULFIDE BONDS.
  19. "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) OF 29-156 IN COMPLEX WITH RNH1, FUNCTION, SUBUNIT, INTERACTION WITH RNH1, DISULFIDE BONDS, MUTAGENESIS OF ARG-67; ASN-95; ASN-116; GLY-117 AND ARG-119.
  20. "'Crystal lattice engineering,' an approach to engineer protein crystal contacts by creating intermolecular symmetry: crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines."
    Yamada H., Tamada T., Kosaka M., Miyata K., Fujiki S., Tano M., Moriya M., Yamanishi M., Honjo E., Tada H., Ino T., Yamaguchi H., Futami J., Seno M., Nomoto T., Hirata T., Yoshimura M., Kuroki R.
    Protein Sci. 16:1389-1397(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-156, DISULFIDE BONDS.

Entry informationi

Entry nameiRNAS1_HUMAN
AccessioniPrimary (citable) accession number: P07998
Secondary accession number(s): B2R589
, D3DS06, Q16830, Q16869, Q1KHR2, Q6ICS5, Q9UCB4, Q9UCB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 163 of the entry and version 4 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.