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Protein

Zinc phosphodiesterase ELAC protein 1

Gene

ELAC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Zinc 1; catalyticBy similarity
Metal bindingi64 – 641Zinc 1; catalyticBy similarity
Active sitei66 – 661Proton acceptorSequence analysis
Metal bindingi66 – 661Zinc 2; catalyticBy similarity
Metal bindingi67 – 671Zinc 2; catalyticBy similarity
Metal bindingi182 – 1821Zinc 1; catalyticBy similarity
Metal bindingi253 – 2531Zinc 1; catalyticBy similarity
Metal bindingi253 – 2531Zinc 2; catalyticBy similarity
Metal bindingi313 – 3131Zinc 2; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

PharmGKBiPA27738.

Polymorphism and mutation databases

BioMutaiELAC1.
DMDMi41017799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Zinc phosphodiesterase ELAC protein 1PRO_0000155825Add
BLAST

Proteomic databases

EPDiQ9H777.
MaxQBiQ9H777.
PaxDbiQ9H777.
PRIDEiQ9H777.

PTM databases

iPTMnetiQ9H777.
PhosphoSiteiQ9H777.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9H777.
CleanExiHS_ELAC1.
ExpressionAtlasiQ9H777. baseline and differential.
GenevisibleiQ9H777. HS.

Organism-specific databases

HPAiHPA040483.
HPA040867.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000269466.

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi11 – 144Combined sources
Beta strandi17 – 193Combined sources
Beta strandi21 – 288Combined sources
Beta strandi31 – 355Combined sources
Helixi41 – 477Combined sources
Beta strandi48 – 503Combined sources
Helixi52 – 543Combined sources
Beta strandi55 – 595Combined sources
Helixi65 – 673Combined sources
Turni68 – 703Combined sources
Helixi71 – 8111Combined sources
Beta strandi91 – 966Combined sources
Helixi99 – 10911Combined sources
Beta strandi118 – 1236Combined sources
Helixi127 – 1293Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi171 – 18414Combined sources
Beta strandi186 – 1938Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi255 – 2573Combined sources
Helixi261 – 2655Combined sources
Turni266 – 2683Combined sources
Beta strandi270 – 2756Combined sources
Helixi280 – 2823Combined sources
Helixi283 – 2886Combined sources
Helixi294 – 30310Combined sources
Beta strandi307 – 3126Combined sources
Beta strandi347 – 3504Combined sources
Beta strandi356 – 3583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZWFX-ray1.70A/B3-363[»]
ProteinModelPortaliQ9H777.
SMRiQ9H777. Positions 3-361.
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.
PhylomeDBiQ9H777.
TreeFamiTF324462.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
HAMAPiMF_01818. RNase_Z_BN.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti314 – 3141F → S in BAB15021 (PubMed:14702039).Curated
Sequence conflicti358 – 3581S → G in BAB15021 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti355 – 3551M → V.1 Publication
Corresponds to variant rs34524743 [ dbSNP | Ensembl ].
VAR_017424

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZWFX-ray1.70A/B3-363[»]
ProteinModelPortaliQ9H777.
SMRiQ9H777. Positions 3-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000269466.

PTM databases

iPTMnetiQ9H777.
PhosphoSiteiQ9H777.

Polymorphism and mutation databases

BioMutaiELAC1.
DMDMi41017799.

Proteomic databases

EPDiQ9H777.
MaxQBiQ9H777.
PaxDbiQ9H777.
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.
GeneCardsiELAC1.
HGNCiHGNC:14197. ELAC1.
HPAiHPA040483.
HPA040867.
MIMi608079. gene.
neXtProtiNX_Q9H777.
PharmGKBiPA27738.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.1.26.11. 2681.

Miscellaneous databases

ChiTaRSiELAC1. human.
GeneWikiiELAC1.
GenomeRNAii55520.
NextBioi59936.
PROiQ9H777.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H777.
CleanExiHS_ELAC1.
ExpressionAtlasiQ9H777. baseline and differential.
GenevisibleiQ9H777. HS.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
HAMAPiMF_01818. RNase_Z_BN.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Physical and transcriptional map of a 311-kb segment of chromosome 18q21, a candidate lung tumor suppressor locus."
    Yanaihara N., Kohno T., Takakura S., Takei K., Otsuka A., Sunaga N., Takahashi M., Yamazaki M., Tashiro H., Fukuzumi Y., Fujimori Y., Hagiwara K., Tanaka T., Yokota J.
    Genomics 72:169-179(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT VAL-355.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Smooth muscle.
  4. "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: Muscle.
  5. "A candidate prostate cancer susceptibility gene encodes tRNA 3' processing endoribonuclease."
    Takaku H., Minagawa A., Takagi M., Nashimoto M.
    Nucleic Acids Res. 31:2272-2278(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  6. "Involvement of human ELAC2 gene product in 3' end processing of mitochondrial tRNAs."
    Brzezniak L.K., Bijata M., Szczesny R.J., Stepien P.P.
    RNA Biol. 8:616-626(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

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: May 11, 2016
This is version 122 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.