Overview
| Uniprot ID | Q9UGP5 |
|---|
| Protein Name | DNA polymerase lambda |
|---|
| Gene Name | POLL |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 27 |
ASSKVLAKIPRREEG |
| 8 |
MDPRGILKAFPKRQK |
Function
DNA polymerase that functions in several pathways of DNA repair (PubMed:11457865, PubMed:19806195, PubMed:20693240, PubMed:30250067). Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA (PubMed:11457865, PubMed:19806195). Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination (PubMed:19806195, PubMed:20693240, PubMed:30250067). Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities (PubMed:10887191, PubMed:10982892, PubMed:12809503, PubMed:14627824, PubMed:15537631, PubMed:19806195). Also has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity (PubMed:11457865, PubMed:19806195)
Protein Sequence
10
MDPRGILKAF
20
PKRQKIHADA
30
SSKVLAKIPR
40
REEGEEAEEW
50
LSSLRAHVVR
60
TGIGRARAEL
70
FEKQIVQHGG
80
QLCPAQGPGV
90
THIVVDEGMD
100
YERALRLLRL
110
PQLPPGAQLV
120
KSAWLSLCLQ
130
ERRLVDVAGF
140
SIFIPSRYLD
150
HPQPSKAEQD
160
ASIPPGTHEA
170
LLQTALSPPP
180
PPTRPVSPPQ
190
KAKEAPNTQA
200
QPISDDEASD
210
GEETQVSAAD
220
LEALISGHYP
230
TSLEGDCEPS
240
PAPAVLDKWV
250
CAQPSSQKAT
260
NHNLHITEKL
270
EVLAKAYSVQ
280
GDKWRALGYA
290
KAINALKSFH
300
KPVTSYQEAC
310
SIPGIGKRMA
320
EKIIEILESG
330
HLRKLDHISE
340
SVPVLELFSN
350
IWGAGTKTAQ
360
MWYQQGFRSL
370
EDIRSQASLT
380
TQQAIGLKHY
390
SDFLERMPRE
400
EATEIEQTVQ
410
KAAQAFNSGL
420
LCVACGSYRR
430
GKATCGDVDV
440
LITHPDGRSH
450
RGIFSRLLDS
460
LRQEGFLTDD
470
LVSQEENGQQ
480
QKYLGVCRLP
490
GPGRRHRRLD
500
IIVVPYSEFA
510
CALLYFTGSA
520
HFNRSMRALA
530
KTKGMSLSEH
540
ALSTAVVRNT
550
HGCKVGPGRV
560
LPTPTEKDVF
570
RLLGLPYREP
AERDW
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0035861 |
site of double-strand break |
| Molecular Function |
GO:0051575 |
5'-deoxyribose-5-phosphate lyase activity |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0003887 |
DNA-directed DNA polymerase activity |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Biological Process |
GO:0006287 |
base-excision repair, gap-filling |
| Biological Process |
GO:0071897 |
DNA biosynthetic process |
| Biological Process |
GO:0006260 |
DNA replication |
| Biological Process |
GO:0000724 |
double-strand break repair via homologous recombination |
| Biological Process |
GO:0006303 |
double-strand break repair via nonhomologous end joining |
| Biological Process |
GO:0006289 |
nucleotide-excision repair |
| Biological Process |
GO:0016446 |
somatic hypermutation of immunoglobulin genes |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.