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Protein

Ribonuclease inhibitor

Gene

RNH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • ribonuclease inhibitor activity Source: UniProtKB

GO - Biological processi

  • mRNA catabolic process Source: UniProtKB
  • 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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000023191.16
HGNCiHGNC:10074 RNH1
MIMi173320 gene
neXtProtiNX_P13489

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi262W → A: Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-264 and A-319. 1 Publication1
Mutagenesisi264W → 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 Publication1
Mutagenesisi319W → 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 Publication1
Mutagenesisi376W → A: 40-fold reduction in binding affinity for RNASE2. 1 Publication1
Mutagenesisi435 – 436YD → AA: Substantially decreases binding affinity for RNASE1, ANG and RNASE2. 2 Publications2
Mutagenesisi458R → A: 25-fold reduction in binding affinity for RNASE2. 1 Publication1
Mutagenesisi461Missing : A significant decrease in binding affinity with RNASE1, slight decrease for the ANG ligand, no real change in binding affinity for RNASE2. 2 Publications1

Organism-specific databases

DisGeNETi6050
OpenTargetsiENSG00000023191
PharmGKBiPA34447

Polymorphism and mutation databases

BioMutaiRNH1
DMDMi132573

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000973432 – 461Ribonuclease inhibitorAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei82PhosphothreonineCombined sources1
Modified residuei91PhosphoserineCombined sources1

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

EPDiP13489
MaxQBiP13489
PaxDbiP13489
PeptideAtlasiP13489
PRIDEiP13489

2D gel databases

REPRODUCTION-2DPAGEiIPI00550069

PTM databases

iPTMnetiP13489
PhosphoSitePlusiP13489
SwissPalmiP13489

Expressioni

Gene expression databases

BgeeiENSG00000023191
CleanExiHS_RNH1
ExpressionAtlasiP13489 baseline and differential
GenevisibleiP13489 HS

Organism-specific databases

HPAiHPA039223
HPA040781

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi11197768 interactors.
CORUMiP13489
IntActiP13489 37 interactors.
MINTiP13489
STRINGi9606.ENSP00000346402

Structurei

Secondary structure

1461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 12Combined sources10
Helixi17 – 27Combined sources11
Beta strandi31 – 38Combined sources8
Helixi42 – 53Combined sources12
Beta strandi60 – 62Combined sources3
Helixi69 – 78Combined sources10
Beta strandi89 – 91Combined sources3
Helixi99 – 101Combined sources3
Helixi102 – 108Combined sources7
Beta strandi117 – 119Combined sources3
Beta strandi122 – 124Combined sources3
Helixi126 – 137Combined sources12
Beta strandi146 – 148Combined sources3
Helixi156 – 158Combined sources3
Helixi159 – 168Combined sources10
Beta strandi174 – 176Combined sources3
Beta strandi179 – 181Combined sources3
Helixi183 – 196Combined sources14
Beta strandi203 – 205Combined sources3
Helixi215 – 225Combined sources11
Beta strandi231 – 233Combined sources3
Beta strandi236 – 238Combined sources3
Helixi240 – 251Combined sources12
Beta strandi260 – 262Combined sources3
Helixi270 – 282Combined sources13
Beta strandi288 – 290Combined sources3
Helixi297 – 308Combined sources12
Beta strandi310 – 312Combined sources3
Beta strandi317 – 319Combined sources3
Helixi327 – 329Combined sources3
Helixi330 – 339Combined sources10
Beta strandi345 – 347Combined sources3
Beta strandi350 – 352Combined sources3
Helixi354 – 365Combined sources12
Beta strandi374 – 376Combined sources3
Helixi384 – 396Combined sources13
Beta strandi402 – 404Combined sources3
Beta strandi407 – 409Combined sources3
Helixi412 – 422Combined sources11
Beta strandi431 – 433Combined sources3
Helixi441 – 453Combined sources13
Beta strandi457 – 460Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13489

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati20 – 48LRR 1Add BLAST29
Repeati49 – 76LRR 2Add BLAST28
Repeati77 – 105LRR 3Add BLAST29
Repeati106 – 133LRR 4Add BLAST28
Repeati134 – 162LRR 5Add BLAST29
Repeati163 – 190LRR 6Add BLAST28
Repeati191 – 219LRR 7Add BLAST29
Repeati220 – 247LRR 8Add BLAST28
Repeati248 – 276LRR 9Add BLAST29
Repeati277 – 304LRR 10Add BLAST28
Repeati305 – 333LRR 11Add BLAST29
Repeati334 – 361LRR 12Add BLAST28
Repeati362 – 390LRR 13Add BLAST29
Repeati391 – 418LRR 14Add BLAST28
Repeati419 – 447LRR 15Add BLAST29

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 112 X 5 AA tandem repeats of S-L-D-I-Q10

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

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4308 Eukaryota
ENOG410ZBX3 LUCA
GeneTreeiENSGT00900000140813
HOGENOMiHOG000140402
HOVERGENiHBG001059
InParanoidiP13489
KOiK16634
OMAiLWLWECD
OrthoDBiEOG091G01CG
PhylomeDBiP13489

Family and domain databases

Gene3Di3.80.10.101 hit
InterProiView protein in InterPro
IPR001611 Leu-rich_rpt
IPR006553 Leu-rich_rpt_Cys-con_subtyp
IPR032675 LRR_dom_sf
PfamiView protein in Pfam
PF13516 LRR_6, 6 hits
SMARTiView protein in SMART
SM00367 LRR_CC, 5 hits

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)DescriptionActionsGraphical viewLength
Sequence conflicti188R → H in AAH03506 (PubMed:15489334).Curated1
Sequence conflicti359R → A in AAL60586 (PubMed:14515218).Curated1
Sequence conflicti365L → P in AAL60586 (PubMed:14515218).Curated1
Sequence conflicti423 – 424RQ → SE in CAA32151 (PubMed:3243277).Curated2
Sequence conflicti423 – 424RQ → SE in AAA60249 (PubMed:3243277).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014726170P → L. Corresponds to variant dbSNP:rs17585Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
XP_011518557.1, XM_011520255.1
XP_011518559.1, XM_011520257.2
XP_011518560.1, XM_011520258.2
XP_011518561.1, XM_011520259.2
XP_011518562.1, XM_011520260.2
XP_011518563.1, XM_011520261.2
XP_011518564.1, XM_011520262.2
XP_011518565.1, XM_011520263.1
XP_016873595.1, XM_017018106.1
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
ENST00000612988; ENSP00000479004; ENSG00000276230
ENST00000617351; ENSP00000484572; ENSG00000276230
ENST00000618184; ENSP00000478664; ENSG00000276230
ENST00000619599; ENSP00000479966; ENSG00000276230
ENST00000621211; ENSP00000480036; ENSG00000276230
ENST00000632527; ENSP00000487940; ENSG00000276230
ENST00000632954; ENSP00000487753; ENSG00000276230
ENST00000633287; ENSP00000488734; ENSG00000276230
GeneIDi6050
KEGGihsa:6050
UCSCiuc001lpk.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRINI_HUMAN
AccessioniPrimary (citable) accession number: P13489
Secondary accession number(s): Q8IZK8
, Q96FD7, Q9BQ80, Q9UDK6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 199 of the entry and version 2 of the sequence. See 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