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Protein

Nuclease EXOG, mitochondrial

Gene

EXOG

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

Functioni

Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity.1 Publication

Cofactori

a divalent metal cation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei140Proton acceptor1
Metal bindingi171Divalent metal cation; catalyticBy similarity1

GO - Molecular functioni

  • 5'-3' exonuclease activity Source: HGNC
  • endonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157036-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclease EXOG, mitochondrial (EC:3.1.30.-)
Alternative name(s):
Endonuclease G-like 1
Short name:
Endo G-like 1
Gene namesi
Name:EXOG
Synonyms:ENDOGL1, ENDOGL2, ENGL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3347. EXOG.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: HGNC
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137S → D: No effect on catalytic activity. 1 Publication1
Mutagenesisi140H → A: Abolishes catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi9941.
OpenTargetsiENSG00000157036.
PharmGKBiPA27784.

Polymorphism and mutation databases

BioMutaiEXOG.
DMDMi193806336.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 41MitochondrionSequence analysisAdd BLAST41
ChainiPRO_000017866942 – 368Nuclease EXOG, mitochondrialAdd BLAST327

Proteomic databases

EPDiQ9Y2C4.
PaxDbiQ9Y2C4.
PeptideAtlasiQ9Y2C4.
PRIDEiQ9Y2C4.

PTM databases

iPTMnetiQ9Y2C4.
PhosphoSitePlusiQ9Y2C4.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000157036.
ExpressionAtlasiQ9Y2C4. baseline and differential.
GenevisibleiQ9Y2C4. HS.

Organism-specific databases

HPAiHPA013609.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi115267. 13 interactors.
STRINGi9606.ENSP00000287675.

Structurei

Secondary structure

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni60 – 65Combined sources6
Beta strandi73 – 76Combined sources4
Beta strandi78 – 85Combined sources8
Turni86 – 89Combined sources4
Beta strandi90 – 98Combined sources9
Turni100 – 103Combined sources4
Helixi109 – 111Combined sources3
Turni122 – 124Combined sources3
Helixi128 – 131Combined sources4
Turni132 – 135Combined sources4
Beta strandi137 – 142Combined sources6
Helixi144 – 146Combined sources3
Helixi151 – 156Combined sources6
Helixi160 – 162Combined sources3
Beta strandi163 – 166Combined sources4
Helixi168 – 172Combined sources5
Helixi174 – 184Combined sources11
Helixi185 – 187Combined sources3
Beta strandi190 – 199Combined sources10
Turni218 – 221Combined sources4
Beta strandi226 – 236Combined sources11
Beta strandi244 – 254Combined sources11
Beta strandi258 – 260Combined sources3
Helixi262 – 265Combined sources4
Helixi269 – 276Combined sources8
Turni286 – 288Combined sources3
Beta strandi289 – 292Combined sources4
Helixi293 – 295Combined sources3
Helixi304 – 315Combined sources12
Helixi325 – 333Combined sources9
Helixi341 – 344Combined sources4
Beta strandi347 – 349Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A1NX-ray2.80A42-368[»]
ProteinModelPortaliQ9Y2C4.
SMRiQ9Y2C4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3721. Eukaryota.
COG1864. LUCA.
GeneTreeiENSGT00530000063772.
HOGENOMiHOG000214172.
HOVERGENiHBG107857.
InParanoidiQ9Y2C4.
KOiK15050.
OMAiFNEDYVG.
OrthoDBiEOG091G0BHG.
PhylomeDBiQ9Y2C4.
TreeFamiTF105386.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
InterProiIPR001604. DNA/RNA_non-sp_Endonuclease.
IPR020821. Extracellular_endonuc_su_A.
[Graphical view]
PfamiPF01223. Endonuclease_NS. 1 hit.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2C4-1) [UniParc]FASTAAdd to basket
Also known as: ENGL-a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAIKSIASRL RGSRRFLSGF VAGAVVGAAG AGLAALQFFR SQGAEGALTG
60 70 80 90 100
KQPDGSAEKA VLEQFGFPLT GTEARCYTNH ALSYDQAKRV PRWVLEHISK
110 120 130 140 150
SKIMGDADRK HCKFKPDPNI PPTFSAFNED YVGSGWSRGH MAPAGNNKFS
160 170 180 190 200
SKAMAETFYL SNIVPQDFDN NSGYWNRIEM YCRELTERFE DVWVVSGPLT
210 220 230 240 250
LPQTRGDGKK IVSYQVIGED NVAVPSHLYK VILARRSSVS TEPLALGAFV
260 270 280 290 300
VPNEAIGFQP QLTEFQVSLQ DLEKLSGLVF FPHLDRTSDI RNICSVDTCK
310 320 330 340 350
LLDFQEFTLY LSTRKIEGAR SVLRLEKIME NLKNAEIEPD DYFMSRYEKK
360
LEELKAKEQS GTQIRKPS
Length:368
Mass (Da):41,085
Last modified:July 1, 2008 - v2
Checksum:i432E046A6F4ADF0E
GO
Isoform 2 (identifier: Q9Y2C4-2) [UniParc]FASTAAdd to basket
Also known as: ENDOGL2, ENGL-b

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: Missing.
     231-289: VILARRSSVS...FFPHLDRTSD → DHAGCCVESP...RISGRIGCRV
     290-368: Missing.

Note: No experimental confirmation available. Probably inactive since it lacks the active site.
Show »
Length:149
Mass (Da):16,571
Checksum:i119E20B841F28349
GO
Isoform 3 (identifier: Q9Y2C4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: Missing.

Note: Probably inactive since it lacks the active site.
Show »
Length:228
Mass (Da):26,017
Checksum:iD1490E95B8A8F5B3
GO
Isoform 4 (identifier: Q9Y2C4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-104: Missing.

Show »
Length:318
Mass (Da):35,437
Checksum:i65D1A335CFAC7CA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti309L → S in BAF82796 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_044320277G → V Abolishes catalytic activity. 2 PublicationsCorresponds to variant rs1141223dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0345061 – 140Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST140
Alternative sequenceiVSP_04121455 – 104Missing in isoform 4. CuratedAdd BLAST50
Alternative sequenceiVSP_034507231 – 289VILAR…DRTSD → DHAGCCVESPLGTRTSEEAT ARIQERDDGGSDQRSGLVEL GIYFEGRANRISGRIGCRV in isoform 2. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_034508290 – 368Missing in isoform 2. 1 PublicationAdd BLAST79

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020523 mRNA. Translation: BAA76752.1.
AB020735 mRNA. Translation: BAA76753.1.
AK289602 mRNA. Translation: BAF82291.1.
AK290107 mRNA. Translation: BAF82796.1.
AK301067 mRNA. Translation: BAG62674.1.
AK315814 mRNA. Translation: BAF98705.1.
CH471055 Genomic DNA. Translation: EAW64538.1.
BC104212 mRNA. Translation: AAI04213.1.
BC104213 mRNA. Translation: AAI04214.1.
CCDSiCCDS2680.1. [Q9Y2C4-1]
CCDS46795.1. [Q9Y2C4-4]
RefSeqiNP_001138936.1. NM_001145464.1. [Q9Y2C4-4]
NP_001305883.1. NM_001318954.1. [Q9Y2C4-3]
NP_001305884.1. NM_001318955.1. [Q9Y2C4-3]
NP_001305885.1. NM_001318956.1. [Q9Y2C4-3]
NP_001305886.1. NM_001318957.1. [Q9Y2C4-3]
NP_001305887.1. NM_001318958.1. [Q9Y2C4-3]
NP_001305888.1. NM_001318959.1. [Q9Y2C4-3]
NP_005098.2. NM_005107.3. [Q9Y2C4-1]
XP_005265690.1. XM_005265633.3. [Q9Y2C4-3]
XP_006713507.1. XM_006713444.3. [Q9Y2C4-3]
XP_016863073.1. XM_017007584.1. [Q9Y2C4-3]
XP_016863074.1. XM_017007585.1. [Q9Y2C4-3]
XP_016863075.1. XM_017007586.1. [Q9Y2C4-3]
XP_016863076.1. XM_017007587.1. [Q9Y2C4-3]
XP_016863077.1. XM_017007588.1. [Q9Y2C4-3]
XP_016863078.1. XM_017007589.1. [Q9Y2C4-3]
XP_016863079.1. XM_017007590.1. [Q9Y2C4-3]
XP_016863080.1. XM_017007591.1. [Q9Y2C4-3]
XP_016863081.1. XM_017007592.1. [Q9Y2C4-3]
XP_016863082.1. XM_017007593.1. [Q9Y2C4-3]
UniGeneiHs.517897.

Genome annotation databases

EnsembliENST00000287675; ENSP00000287675; ENSG00000157036. [Q9Y2C4-1]
ENST00000422077; ENSP00000404305; ENSG00000157036. [Q9Y2C4-4]
GeneIDi9941.
KEGGihsa:9941.
UCSCiuc003cih.3. human. [Q9Y2C4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020523 mRNA. Translation: BAA76752.1.
AB020735 mRNA. Translation: BAA76753.1.
AK289602 mRNA. Translation: BAF82291.1.
AK290107 mRNA. Translation: BAF82796.1.
AK301067 mRNA. Translation: BAG62674.1.
AK315814 mRNA. Translation: BAF98705.1.
CH471055 Genomic DNA. Translation: EAW64538.1.
BC104212 mRNA. Translation: AAI04213.1.
BC104213 mRNA. Translation: AAI04214.1.
CCDSiCCDS2680.1. [Q9Y2C4-1]
CCDS46795.1. [Q9Y2C4-4]
RefSeqiNP_001138936.1. NM_001145464.1. [Q9Y2C4-4]
NP_001305883.1. NM_001318954.1. [Q9Y2C4-3]
NP_001305884.1. NM_001318955.1. [Q9Y2C4-3]
NP_001305885.1. NM_001318956.1. [Q9Y2C4-3]
NP_001305886.1. NM_001318957.1. [Q9Y2C4-3]
NP_001305887.1. NM_001318958.1. [Q9Y2C4-3]
NP_001305888.1. NM_001318959.1. [Q9Y2C4-3]
NP_005098.2. NM_005107.3. [Q9Y2C4-1]
XP_005265690.1. XM_005265633.3. [Q9Y2C4-3]
XP_006713507.1. XM_006713444.3. [Q9Y2C4-3]
XP_016863073.1. XM_017007584.1. [Q9Y2C4-3]
XP_016863074.1. XM_017007585.1. [Q9Y2C4-3]
XP_016863075.1. XM_017007586.1. [Q9Y2C4-3]
XP_016863076.1. XM_017007587.1. [Q9Y2C4-3]
XP_016863077.1. XM_017007588.1. [Q9Y2C4-3]
XP_016863078.1. XM_017007589.1. [Q9Y2C4-3]
XP_016863079.1. XM_017007590.1. [Q9Y2C4-3]
XP_016863080.1. XM_017007591.1. [Q9Y2C4-3]
XP_016863081.1. XM_017007592.1. [Q9Y2C4-3]
XP_016863082.1. XM_017007593.1. [Q9Y2C4-3]
UniGeneiHs.517897.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A1NX-ray2.80A42-368[»]
ProteinModelPortaliQ9Y2C4.
SMRiQ9Y2C4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115267. 13 interactors.
STRINGi9606.ENSP00000287675.

PTM databases

iPTMnetiQ9Y2C4.
PhosphoSitePlusiQ9Y2C4.

Polymorphism and mutation databases

BioMutaiEXOG.
DMDMi193806336.

Proteomic databases

EPDiQ9Y2C4.
PaxDbiQ9Y2C4.
PeptideAtlasiQ9Y2C4.
PRIDEiQ9Y2C4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287675; ENSP00000287675; ENSG00000157036. [Q9Y2C4-1]
ENST00000422077; ENSP00000404305; ENSG00000157036. [Q9Y2C4-4]
GeneIDi9941.
KEGGihsa:9941.
UCSCiuc003cih.3. human. [Q9Y2C4-1]

Organism-specific databases

CTDi9941.
DisGeNETi9941.
GeneCardsiEXOG.
H-InvDBHIX0003181.
HGNCiHGNC:3347. EXOG.
HPAiHPA013609.
MIMi604051. gene.
neXtProtiNX_Q9Y2C4.
OpenTargetsiENSG00000157036.
PharmGKBiPA27784.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3721. Eukaryota.
COG1864. LUCA.
GeneTreeiENSGT00530000063772.
HOGENOMiHOG000214172.
HOVERGENiHBG107857.
InParanoidiQ9Y2C4.
KOiK15050.
OMAiFNEDYVG.
OrthoDBiEOG091G0BHG.
PhylomeDBiQ9Y2C4.
TreeFamiTF105386.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157036-MONOMER.

Miscellaneous databases

GenomeRNAii9941.
PROiQ9Y2C4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157036.
ExpressionAtlasiQ9Y2C4. baseline and differential.
GenevisibleiQ9Y2C4. HS.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
InterProiIPR001604. DNA/RNA_non-sp_Endonuclease.
IPR020821. Extracellular_endonuc_su_A.
[Graphical view]
PfamiPF01223. Endonuclease_NS. 1 hit.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEXOG_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2C4
Secondary accession number(s): A8K242
, B4DVG2, Q3SXM9, Q9Y2C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 1, 2008
Last modified: November 2, 2016
This is version 116 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

Miscellaneous

The active site contains 1 hydrated divalent metal cation that has only 1 direct interaction with the protein; all other interactions are via water molecules.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.