Search Results

Overview

Uniprot IDQ9BXW9
Protein NameFanconi anemia group D2 protein
Gene NameFANCD2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1390 AFWLGNLKNRDLQGE
22 SLTEDASKTRKQPLS
322 RLQASQVKLKSKGRA
34 PLSKKTKKSHIANEV
9 VSKRRLSKSEDKESL

Function

Required for maintenance of chromosomal stability (PubMed:11239453, PubMed:14517836). Promotes accurate and efficient pairing of homologs during meiosis (PubMed:14517836). Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing (PubMed:15671039, PubMed:15650050, PubMed:30335751, PubMed:36385258). The FANCI-FANCD2 complex binds and scans double-stranded DNA (dsDNA) for DNA damage; this complex stalls at DNA junctions between double-stranded DNA and single-stranded DNA (By similarity). May participate in S phase and G2 phase checkpoint activation upon DNA damage (PubMed:15377654). Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (PubMed:15454491, PubMed:15661754). Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress (PubMed:15661754, PubMed:19465921). Promotes BRCA2/FANCD1 loading onto damaged chromatin (PubMed:11239454, PubMed:12239151, PubMed:12086603, PubMed:15115758, PubMed:15199141, PubMed:15671039, PubMed:18212739). May also be involved in B-cell immunoglobulin isotype switching

Protein Sequence

10 MVSKRRLSKS 20 EDKESLTEDA 30 SKTRKQPLSK 40 KTKKSHIANE 50 VEENDSIFVK 60 LLKISGIILK 70 TGESQNQLAV 80 DQIAFQKKLF 90 QTLRRHPSYP 100 KIIEEFVSGL 110 ESYIEDEDSF 120 RNCLLSCERL 130 QDEEASMGAS 140 YSKSLIKLLL 150 GIDILQPAII 160 KTLFEKLPEY 170 FFENKNSDEI 180 NIPRLIVSQL 190 KWLDRVVDGK 200 DLTTKIMQLI 210 SIAPENLQHD 220 IITSLPEILG 230 DSQHADVGKE 240 LSDLLIENTS 250 LTVPILDVLS 260 SLRLDPNFLL 270 KVRQLVMDKL 280 SSIRLEDLPV 290 IIKFILHSVT 300 AMDTLEVISE 310 LREKLDLQHC 320 VLPSRLQASQ 330 VKLKSKGRAS 340 SSGNQESSGQ 350 SCIILLFDVI 360 KSAIRYEKTI 370 SEAWIKAIEN 380 TASVSEHKVF 390 DLVMLFIIYS 400 TNTQTKKYID 410 RVLRNKIRSG 420 CIQEQLLQST 430 FSVHYLVLKD 440 MCSSILSLAQ 450 SLLHSLDQSI 460 ISFGSLLYKY 470 AFKFFDTYCQ 480 QEVVGALVTH 490 ICSGNEAEVD 500 TALDVLLELV 510 VLNPSAMMMN 520 AVFVKGILDY 530 LDNISPQQIR 540 KLFYVLSTLA 550 FSKQNEASSH 560 IQDDMHLVIR 570 KQLSSTVFKY 580 KLIGIIGAVT 590 MAGIMAADRS 600 ESPSLTQERA 610 NLSDEQCTQV 620 TSLLQLVHSC 630 SEQSPQASAL 640 YYDEFANLIQ 650 HEKLDPKALE 660 WVGHTICNDF 670 QDAFVVDSCV 680 VPEGDFPFPV 690 KALYGLEEYD 700 TQDGIAINLL 710 PLLFSQDFAK 720 DGGPVTSQES 730 GQKLVSPLCL 740 APYFRLLRLC 750 VERQHNGNLE 760 EIDGLLDCPI 770 FLTDLEPGEK 780 LESMSAKERS 790 FMCSLIFLTL 800 NWFREIVNAF 810 CQETSPEMKG 820 KVLTRLKHIV 830 ELQIILEKYL 840 AVTPDYVPPL 850 GNFDVETLDI 860 TPHTVTAISA 870 KIRKKGKIER 880 KQKTDGSKTS 890 SSDTLSEEKN 900 SECDPTPSHR 910 GQLNKEFTGK 920 EEKTSLLLHN 930 SHAFFRELDI 940 EVFSILHCGL 950 VTKFILDTEM 960 HTEATEVVQL 970 GPPELLFLLE 980 DLSQKLESML 990 TPPIARRVPF 1000 LKNKGSRNIG 1010 FSHLQQRSAQ 1020 EIVHCVFQLL 1030 TPMCNHLENI 1040 HNYFQCLAAE 1050 NHGVVDGPGV 1060 KVQEYHIMSS 1070 CYQRLLQIFH 1080 GLFAWSGFSQ 1090 PENQNLLYSA 1100 LHVLSSRLKQ 1110 GEHSQPLEEL 1120 LSQSVHYLQN 1130 FHQSIPSFQC 1140 ALYLIRLLMV 1150 ILEKSTASAQ 1160 NKEKIASLAR 1170 QFLCRVWPSG 1180 DKEKSNISND 1190 QLHALLCIYL 1200 EHTESILKAI 1210 EEIAGVGVPE 1220 LINSPKDASS 1230 STFPTLTRHT 1240 FVVFFRVMMA 1250 ELEKTVKKIE 1260 PGTAADSQQI 1270 HEEKLLYWNM 1280 AVRDFSILIN 1290 LIKVFDSHPV 1300 LHVCLKYGRL 1310 FVEAFLKQCM 1320 PLLDFSFRKH 1330 REDVLSLLET 1340 FQLDTRLLHH 1350 LCGHSKIHQD 1360 TRLTQHVPLL 1370 KKTLELLVCR 1380 VKAMLTLNNC 1390 REAFWLGNLK 1400 NRDLQGEEIK 1410 SQNSQESTAD 1420 ESEDDMSSQA 1430 SKSKATEDGE 1440 EDEVSAGEKE 1450 QDSDESYDDS D

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000793 condensed chromosome
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0070182 DNA polymerase binding
Biological Process GO:1990918 double-strand break repair involved in meiotic recombination
Biological Process GO:0007129 homologous chromosome pairing at meiosis
Biological Process GO:0036297 interstrand cross-link repair
Biological Process GO:0031573 mitotic intra-S DNA damage checkpoint signaling
Biological Process GO:0010332 response to gamma radiation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] 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.