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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei140 – 1401Proton acceptor
Metal bindingi171 – 1711Divalent metal cation; catalyticBy similarity

GO - Molecular functioni

  • endonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro

GO - Biological processi

  • nucleic acid phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Metal-binding

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: UniProtKB-SubCell
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371S → D: No effect on catalytic activity. 1 Publication
Mutagenesisi140 – 1401H → A: Abolishes catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA27784.

Polymorphism and mutation databases

BioMutaiEXOG.
DMDMi193806336.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence analysisAdd
BLAST
Chaini42 – 368327Nuclease EXOG, mitochondrialPRO_0000178669Add
BLAST

Proteomic databases

EPDiQ9Y2C4.
MaxQBiQ9Y2C4.
PaxDbiQ9Y2C4.
PRIDEiQ9Y2C4.

PTM databases

iPTMnetiQ9Y2C4.
PhosphoSiteiQ9Y2C4.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9Y2C4.
ExpressionAtlasiQ9Y2C4. baseline and differential.
GenevisibleiQ9Y2C4. HS.

Organism-specific databases

HPAiHPA013609.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi115267. 13 interactions.
STRINGi9606.ENSP00000287675.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni60 – 656Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 858Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 989Combined sources
Turni100 – 1034Combined sources
Helixi109 – 1113Combined sources
Turni122 – 1243Combined sources
Helixi128 – 1314Combined sources
Turni132 – 1354Combined sources
Beta strandi137 – 1426Combined sources
Helixi144 – 1463Combined sources
Helixi151 – 1566Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 1664Combined sources
Helixi168 – 1725Combined sources
Helixi174 – 18411Combined sources
Helixi185 – 1873Combined sources
Beta strandi190 – 19910Combined sources
Turni218 – 2214Combined sources
Beta strandi226 – 23611Combined sources
Beta strandi244 – 25411Combined sources
Beta strandi258 – 2603Combined sources
Helixi262 – 2654Combined sources
Helixi269 – 2768Combined sources
Turni286 – 2883Combined sources
Beta strandi289 – 2924Combined sources
Helixi293 – 2953Combined sources
Helixi304 – 31512Combined sources
Helixi325 – 3339Combined sources
Helixi341 – 3444Combined sources
Beta strandi347 – 3493Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A1NX-ray2.80A42-368[»]
ProteinModelPortaliQ9Y2C4.
SMRiQ9Y2C4. Positions 59-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3721. Eukaryota.
COG1864. LUCA.
GeneTreeiENSGT00530000063772.
HOGENOMiHOG000214172.
HOVERGENiHBG107857.
InParanoidiQ9Y2C4.
KOiK15050.
OMAiFNEDYVG.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091L → S in BAF82796 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771G → V Abolishes catalytic activity. 2 Publications
Corresponds to variant rs1141223 [ dbSNP | Ensembl ].
VAR_044320

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 140140Missing in isoform 2 and isoform 3. 3 PublicationsVSP_034506Add
BLAST
Alternative sequencei55 – 10450Missing in isoform 4. CuratedVSP_041214Add
BLAST
Alternative sequencei231 – 28959VILAR…DRTSD → DHAGCCVESPLGTRTSEEAT ARIQERDDGGSDQRSGLVEL GIYFEGRANRISGRIGCRV in isoform 2. 1 PublicationVSP_034507Add
BLAST
Alternative sequencei290 – 36879Missing in isoform 2. 1 PublicationVSP_034508Add
BLAST

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_005265633.2. [Q9Y2C4-3]
XP_006713507.1. XM_006713444.2. [Q9Y2C4-3]
XP_006713508.1. XM_006713445.2. [Q9Y2C4-3]
XP_006713509.1. XM_006713446.2. [Q9Y2C4-3]
XP_006713510.1. XM_006713447.2. [Q9Y2C4-3]
XP_011532622.1. XM_011534320.1. [Q9Y2C4-3]
XP_011532623.1. XM_011534321.1. [Q9Y2C4-3]
XP_011532625.1. XM_011534323.1. [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_005265633.2. [Q9Y2C4-3]
XP_006713507.1. XM_006713444.2. [Q9Y2C4-3]
XP_006713508.1. XM_006713445.2. [Q9Y2C4-3]
XP_006713509.1. XM_006713446.2. [Q9Y2C4-3]
XP_006713510.1. XM_006713447.2. [Q9Y2C4-3]
XP_011532622.1. XM_011534320.1. [Q9Y2C4-3]
XP_011532623.1. XM_011534321.1. [Q9Y2C4-3]
XP_011532625.1. XM_011534323.1. [Q9Y2C4-3]
UniGeneiHs.517897.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A1NX-ray2.80A42-368[»]
ProteinModelPortaliQ9Y2C4.
SMRiQ9Y2C4. Positions 59-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115267. 13 interactions.
STRINGi9606.ENSP00000287675.

PTM databases

iPTMnetiQ9Y2C4.
PhosphoSiteiQ9Y2C4.

Polymorphism and mutation databases

BioMutaiEXOG.
DMDMi193806336.

Proteomic databases

EPDiQ9Y2C4.
MaxQBiQ9Y2C4.
PaxDbiQ9Y2C4.
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.
GeneCardsiEXOG.
H-InvDBHIX0003181.
HGNCiHGNC:3347. EXOG.
HPAiHPA013609.
MIMi604051. gene.
neXtProtiNX_Q9Y2C4.
PharmGKBiPA27784.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

GenomeRNAii9941.
PROiQ9Y2C4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2C4.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT VAL-277.
  2. "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] (ISOFORM 3).
    Tissue: Spleen and Subthalamic nucleus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 3).
  5. "EXOG, a novel paralog of endonuclease G in higher eukaryotes."
    Cymerman I.A., Chung I., Beckmann B.M., Bujnicki J.M., Meiss G.
    Nucleic Acids Res. 36:1369-1379(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-137 AND HIS-140, CHARACTERIZATION OF VARIANT VAL-277.
  6. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 8, 2016
This is version 112 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.