Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc phosphodiesterase ELAC protein 1

Gene

ELAC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.

Catalytic activityi

Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.1 Publication

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62Zinc 1; catalyticBy similarity1
Metal bindingi64Zinc 1; catalyticBy similarity1
Active sitei66Proton acceptorSequence analysis1
Metal bindingi66Zinc 2; catalyticBy similarity1
Metal bindingi67Zinc 2; catalyticBy similarity1
Metal bindingi182Zinc 1; catalyticBy similarity1
Metal bindingi253Zinc 1; catalyticBy similarity1
Metal bindingi253Zinc 2; catalyticBy similarity1
Metal bindingi313Zinc 2; catalyticBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS13902-MONOMER.
BRENDAi3.1.26.11. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc phosphodiesterase ELAC protein 1 (EC:3.1.26.11)
Alternative name(s):
Deleted in Ma29
ElaC homolog protein 1
Ribonuclease Z 1
Short name:
RNase Z 1
tRNA 3 endonuclease 1
tRNase Z 1
Gene namesi
Name:ELAC1
Synonyms:D29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:14197. ELAC1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi55520.
OpenTargetsiENSG00000141642.
PharmGKBiPA27738.

Polymorphism and mutation databases

BioMutaiELAC1.
DMDMi41017799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001558251 – 363Zinc phosphodiesterase ELAC protein 1Add BLAST363

Proteomic databases

EPDiQ9H777.
MaxQBiQ9H777.
PaxDbiQ9H777.
PeptideAtlasiQ9H777.
PRIDEiQ9H777.

PTM databases

iPTMnetiQ9H777.
PhosphoSitePlusiQ9H777.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiENSG00000141642.
CleanExiHS_ELAC1.
ExpressionAtlasiQ9H777. baseline and differential.
GenevisibleiQ9H777. HS.

Organism-specific databases

HPAiHPA040483.
HPA040867.
HPA066483.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000269466.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi11 – 14Combined sources4
Beta strandi17 – 19Combined sources3
Beta strandi21 – 28Combined sources8
Beta strandi31 – 35Combined sources5
Helixi41 – 47Combined sources7
Beta strandi48 – 50Combined sources3
Helixi52 – 54Combined sources3
Beta strandi55 – 59Combined sources5
Helixi65 – 67Combined sources3
Turni68 – 70Combined sources3
Helixi71 – 81Combined sources11
Beta strandi91 – 96Combined sources6
Helixi99 – 109Combined sources11
Beta strandi118 – 123Combined sources6
Helixi127 – 129Combined sources3
Turni160 – 163Combined sources4
Beta strandi164 – 169Combined sources6
Beta strandi171 – 184Combined sources14
Beta strandi186 – 193Combined sources8
Beta strandi247 – 251Combined sources5
Beta strandi255 – 257Combined sources3
Helixi261 – 265Combined sources5
Turni266 – 268Combined sources3
Beta strandi270 – 275Combined sources6
Helixi280 – 282Combined sources3
Helixi283 – 288Combined sources6
Helixi294 – 303Combined sources10
Beta strandi307 – 312Combined sources6
Beta strandi347 – 350Combined sources4
Beta strandi356 – 358Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZWFX-ray1.70A/B3-363[»]
ProteinModelPortaliQ9H777.
SMRiQ9H777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase Z family.Curated

Phylogenomic databases

eggNOGiKOG2121. Eukaryota.
COG1234. LUCA.
GeneTreeiENSGT00730000111224.
HOGENOMiHOG000272419.
HOVERGENiHBG050040.
InParanoidiQ9H777.
KOiK00784.
OMAiPVPGKMD.
OrthoDBiEOG091G0KQW.
PhylomeDBiQ9H777.
TreeFamiTF324462.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
HAMAPiMF_01818. RNase_Z_BN. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR013471. RNase_Z/BN.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
PF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 2 hits.
TIGRFAMsiTIGR02651. RNase_Z. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9H777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMDVTFLGT GAAYPSPTRG ASAVVLRCEG ECWLFDCGEG TQTQLMKSQL
60 70 80 90 100
KAGRITKIFI THLHGDHFFG LPGLLCTISL QSGSMVSKQP IEIYGPVGLR
110 120 130 140 150
DFIWRTMELS HTELVFHYVV HELVPTADQC PAEELKEFAH VNRADSPPKE
160 170 180 190 200
EQGRTILLDS EENSYLLFDD EQFVVKAFRL FHRIPSFGFS VVEKKRPGKL
210 220 230 240 250
NAQKLKDLGV PPGPAYGKLK NGISVVLENG VTISPQDVLK KPIVGRKICI
260 270 280 290 300
LGDCSGVVGD GGVKLCFEAD LLIHEATLDD AQMDKAKEHG HSTPQMAATF
310 320 330 340 350
AKLCRAKRLV LTHFSQRYKP VALAREGETD GIAELKKQAE SVLDLQEVTL
360
AEDFMVISIP IKK
Length:363
Mass (Da):40,019
Last modified:January 16, 2004 - v2
Checksum:i125A8416502D4C79
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti314F → S in BAB15021 (PubMed:14702039).Curated1
Sequence conflicti358S → G in BAB15021 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017424355M → V.1 PublicationCorresponds to variant rs34524743dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029151 mRNA. Translation: BAA96799.1.
AF308695 mRNA. Translation: AAG24917.1.
AK024822 mRNA. Translation: BAB15021.1.
BC014624 mRNA. Translation: AAH14624.1.
CCDSiCCDS11949.1.
RefSeqiNP_061166.1. NM_018696.2.
UniGeneiHs.657360.

Genome annotation databases

EnsembliENST00000269466; ENSP00000269466; ENSG00000141642.
GeneIDi55520.
KEGGihsa:55520.
UCSCiuc002lez.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029151 mRNA. Translation: BAA96799.1.
AF308695 mRNA. Translation: AAG24917.1.
AK024822 mRNA. Translation: BAB15021.1.
BC014624 mRNA. Translation: AAH14624.1.
CCDSiCCDS11949.1.
RefSeqiNP_061166.1. NM_018696.2.
UniGeneiHs.657360.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZWFX-ray1.70A/B3-363[»]
ProteinModelPortaliQ9H777.
SMRiQ9H777.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000269466.

PTM databases

iPTMnetiQ9H777.
PhosphoSitePlusiQ9H777.

Polymorphism and mutation databases

BioMutaiELAC1.
DMDMi41017799.

Proteomic databases

EPDiQ9H777.
MaxQBiQ9H777.
PaxDbiQ9H777.
PeptideAtlasiQ9H777.
PRIDEiQ9H777.

Protocols and materials databases

DNASUi55520.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269466; ENSP00000269466; ENSG00000141642.
GeneIDi55520.
KEGGihsa:55520.
UCSCiuc002lez.4. human.

Organism-specific databases

CTDi55520.
DisGeNETi55520.
GeneCardsiELAC1.
HGNCiHGNC:14197. ELAC1.
HPAiHPA040483.
HPA040867.
HPA066483.
MIMi608079. gene.
neXtProtiNX_Q9H777.
OpenTargetsiENSG00000141642.
PharmGKBiPA27738.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2121. Eukaryota.
COG1234. LUCA.
GeneTreeiENSGT00730000111224.
HOGENOMiHOG000272419.
HOVERGENiHBG050040.
InParanoidiQ9H777.
KOiK00784.
OMAiPVPGKMD.
OrthoDBiEOG091G0KQW.
PhylomeDBiQ9H777.
TreeFamiTF324462.

Enzyme and pathway databases

BioCyciZFISH:HS13902-MONOMER.
BRENDAi3.1.26.11. 2681.

Miscellaneous databases

ChiTaRSiELAC1. human.
GeneWikiiELAC1.
GenomeRNAii55520.
PROiQ9H777.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141642.
CleanExiHS_ELAC1.
ExpressionAtlasiQ9H777. baseline and differential.
GenevisibleiQ9H777. HS.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
HAMAPiMF_01818. RNase_Z_BN. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR013471. RNase_Z/BN.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
PF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 2 hits.
TIGRFAMsiTIGR02651. RNase_Z. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRNZ1_HUMAN
AccessioniPrimary (citable) accession number: Q9H777
Secondary accession number(s): Q9NS99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: November 2, 2016
This is version 127 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, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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

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 one 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.