CPLM-023308

Genbank Nucleotide ID

Protein Synonyms/Alias

hExo1; Exonuclease I; hExoI

Homo sapiens (Human)

Position	Peptide	Type	References
185	GCKKVILKMDQFGNG	ubiquitination	[1]
214	GDVFTEEKFRYMCIL	ubiquitination	[1, 2]
240	IGLAKACKVLRLANN	ubiquitination	[1]
292	QLVFDPIKRKLIPLN	ubiquitination	[1, 2, 3]
391	VSDAPQLKENPSTVG	ubiquitination	[2, 3]
406	VERVISTKGLNLPRK	ubiquitination	[1]
482	TPPRTRNKFATFLQR	acetylation	[4]
548	EYGDQEGKRLVDTDV	ubiquitination	[2]
796	IKLNELWKNFGFKKD	ubiquitination	[5, 6]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch- containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis.

REGION 1 99 N-domain.
REGION 129 387 Interaction with MSH3.
REGION 138 229 I-domain.
REGION 388 490 Interaction with MLH1.
REGION 418 421 Nuclear localization signal.
REGION 600 846 Interaction with MSH2.
REGION 787 846 Interaction with MLH1.
METAL 30 30 Magnesium 1 (By similarity).
METAL 78 78 Magnesium 1 (By similarity).
METAL 150 150 Magnesium 1 (By similarity).
METAL 152 152 Magnesium 1 (By similarity).
METAL 171 171 Magnesium 2 (By similarity).
METAL 173 173 Magnesium 2 (By similarity).
METAL 225 225 Magnesium 2 (By similarity).
MOD_RES 376 376 Phosphoserine.
MOD_RES 422 422 Phosphoserine.
MOD_RES 454 454 Phosphoserine.
MOD_RES 482 482 N6-acetyllysine.
MOD_RES 581 581 Phosphothreonine.
MOD_RES 598 598 Phosphoserine.
MOD_RES 621 621 Phosphothreonine.
MOD_RES 623 623 Phosphoserine.
MOD_RES 639 639 Phosphoserine.
MOD_RES 660 660 Phosphoserine.
MOD_RES 674 674 Phosphoserine.
MOD_RES 714 714 Phosphoserine; by ATR.
MOD_RES 746 746 Phosphoserine.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease; Excision nuclease; Exonuclease; Hydrolase; Immunity; Magnesium; Meiosis; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0003677; F:DNA binding; IDA:UniProtKB.
GO:0051908; F:double-stranded DNA specific 5'-3' exodeoxyribonuclease activity; IDA:UniProtKB.
GO:0048256; F:flap endonuclease activity; IDA:UniProtKB.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0004523; F:ribonuclease H activity; TAS:ProtInc.
GO:0045145; F:single-stranded DNA specific 5'-3' exodeoxyribonuclease activity; IDA:UniProtKB.
GO:0043566; F:structure-specific DNA binding; IEA:Compara.
GO:0006310; P:DNA recombination; IGI:UniProtKB.
GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IEA:Compara.
GO:0045190; P:isotype switching; IEA:Compara.
GO:0007126; P:meiosis; IEA:UniProtKB-KW.
GO:0006298; P:mismatch repair; IDA:UniProtKB.
GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Compara.

IPR020045; 5-3_exonuclease_C.
IPR008918; HhH2.
IPR006086; XPG-I_dom.
IPR006084; XPG/Rad2.
IPR019974; XPG_CS.
IPR006085; XPG_DNA_repair_N.

PF00867; XPG_I
PF00752; XPG_N

SM00279; HhH2
SM00484; XPGI
SM00485; XPGN

PS00841; XPG_1
PS00842; XPG_2

PR00853; XPGRADSUPER.