Search Results

Overview

Uniprot IDP52948
Protein NameNuclear pore complex protein Nup98-Nup96
Gene NameNUP98
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1019 RFSRLPSKADTSQEI
1040 ISASHSSKTRSLVGG
542 PTNPAAQKALTTPTH
551 LTTPTHYKLTPRPAT
563 PATRVRPKALQTTGT
603 SIKKLVLKNLNNSNL
757 LAKITNEKGECIVSD
831 DGVWPTDKTSRCLIK
858 RLEAVSRKQGAQFKE

Function

Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134)

Protein Sequence

10 MFNKSFGTPF 20 GGGTGGFGTT 30 STFGQNTGFG 40 TTSGGAFGTS 50 AFGSSNNTGG 60 LFGNSQTKPG 70 GLFGTSSFSQ 80 PATSTSTGFG 90 FGTSTGTANT 100 LFGTASTGTS 110 LFSSQNNAFA 120 QNKPTGFGNF 130 GTSTSSGGLF 140 GTTNTTSNPF 150 GSTSGSLFGP 160 SSFTAAPTGT 170 TIKFNPPTGT 180 DTMVKAGVST 190 NISTKHQCIT 200 AMKEYESKSL 210 EELRLEDYQA 220 NRKGPQNQVG 230 AGTTTGLFGS 240 SPATSSATGL 250 FSSSTTNSGF 260 AYGQNKTAFG 270 TSTTGFGTNP 280 GGLFGQQNQQ 290 TTSLFSKPFG 300 QATTTQNTGF 310 SFGNTSTIGQ 320 PSTNTMGLFG 330 VTQASQPGGL 340 FGTATNTSTG 350 TAFGTGTGLF 360 GQTNTGFGAV 370 GSTLFGNNKL 380 TTFGSSTTSA 390 PSFGTTSGGL 400 FGNKPTLTLG 410 TNTNTSNFGF 420 GTNTSGNSIF 430 GSKPAPGTLG 440 TGLGAGFGTA 450 LGAGQASLFG 460 NNQPKIGGPL 470 GTGAFGAPGF 480 NTTTATLGFG 490 APQAPVALTD 500 PNASAAQQAV 510 LQQHINSLTY 520 SPFGDSPLFR 530 NPMSDPKKKE 540 ERLKPTNPAA 550 QKALTTPTHY 560 KLTPRPATRV 570 RPKALQTTGT 580 AKSHLFDGLD 590 DDEPSLANGA 600 FMPKKSIKKL 610 VLKNLNNSNL 620 FSPVNRDSEN 630 LASPSEYPEN 640 GERFSFLSKP 650 VDENHQQDGD 660 EDSLVSHFYT 670 NPIAKPIPQT 680 PESAGNKHSN 690 SNSVDDTIVA 700 LNMRAALRNG 710 LEGSSEETSF 720 HDESLQDDRE 730 EIENNSYHMH 740 PAGIILTKVG 750 YYTIPSMDDL 760 AKITNEKGEC 770 IVSDFTIGRK 780 GYGSIYFEGD 790 VNLTNLNLDD 800 IVHIRRKEVV 810 VYLDDNQKPP 820 VGEGLNRKAE 830 VTLDGVWPTD 840 KTSRCLIKSP 850 DRLADINYEG 860 RLEAVSRKQG 870 AQFKEYRPET 880 GSWVFKVSHF 890 SKYGLQDSDE 900 EEEEHPSKTS 910 TKKLKTAPLP 920 PASQTTPLQM 930 ALNGKPAPPP 940 QSQSPEVEQL 950 GRVVELDSDM 960 VDITQEPVLD 970 TMLEESMPED 980 QEPVSASTHI 990 ASSLGINPHV 1000 LQIMKASLLT 1010 DEEDVDMALD 1020 QRFSRLPSKA 1030 DTSQEICSPR 1040 LPISASHSSK 1050 TRSLVGGLLQ 1060 SKFTSGAFLS 1070 PSVSVQECRT 1080 PRAASLMNIP 1090 STSSWSVPPP 1100 LTSVFTMPSP 1110 APEVPLKTVG 1120 TRRQLGLVPR 1130 EKSVTYGKGK 1140 LLMDMALFMG 1150 RSFRVGWGPN 1160 WTLANSGEQL 1170 NGSHELENHQ 1180 IADSMEFGFL 1190 PNPVAVKPLT 1200 ESPFKVHLEK 1210 LSLRQRKPDE 1220 DMKLYQTPLE 1230 LKLKHSTVHV 1240 DELCPLIVPN 1250 LGVAVIHDYA 1260 DWVKEASGDL 1270 PEAQIVKHWS 1280 LTWTLCEALW 1290 GHLKELDSQL 1300 NEPREYIQIL 1310 ERRRAFSRWL 1320 SCTATPQIEE 1330 EVSLTQKNSP 1340 VEAVFSYLTG 1350 KRISEACSLA 1360 QQSGDHRLAL 1370 LLSQFVGSQS 1380 VRELLTMQLV 1390 DWHQLQADSF 1400 IQDERLRIFA 1410 LLAGKPVWQL 1420 SEKKQINVCS 1430 QLDWKRSLAI 1440 HLWYLLPPTA 1450 SISRALSMYE 1460 EAFQNTSDSD 1470 RYACSPLPSY 1480 LEGSGCVIAE 1490 EQNSQTPLRD 1500 VCFHLLKLYS 1510 DRHYDLNQLL 1520 EPRSITADPL 1530 DYRLSWHLWE 1540 VLRALNYTHL 1550 SAQCEGVLQA 1560 SYAGQLESEG 1570 LWEWAIFVLL 1580 HIDNSGIREK 1590 AVRELLTRHC 1600 QLLETPESWA 1610 KETFLTQKLR 1620 VPAKWIHEAK 1630 AVRAHMESDK 1640 HLEALCLFKA 1650 EHWNRCHKLI 1660 IRHLASDAII 1670 NENYDYLKGF 1680 LEDLAPPERS 1690 SLIQDWETSG 1700 LVYLDYIRVI 1710 EMLRHIQQVD 1720 CSGNDLEQLH 1730 IKVTSLCSRI 1740 EQIQCYSAKD 1750 RLAQSDMAKR 1760 VANLLRVVLS 1770 LHHPPDRTSD 1780 STPDPQRVPL 1790 RLLAPHIGRL 1800 PMPEDYAMDE 1810 LRSLTQSYLR ELAVGSL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Biological Process GO:0051292 nuclear pore complex assembly
Biological Process GO:0006999 nuclear pore organization
Biological Process GO:0006913 nucleocytoplasmic transport
Biological Process GO:0048026 positive regulation of mRNA splicing, via spliceosome
Biological Process GO:0000973 post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery
Biological Process GO:0006606 protein import into nucleus
Biological Process GO:0006508 proteolysis
Biological Process GO:0006405 RNA export from nucleus
Biological Process GO:0034398 telomere tethering at nuclear periphery
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0042405 nuclear inclusion body
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0034399 nuclear periphery
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0044614 nuclear pore cytoplasmic filaments
Cellular Component GO:0044615 nuclear pore nuclear basket
Cellular Component GO:0031080 nuclear pore outer ring
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0140693 molecular condensate scaffold activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0008139 nuclear localization sequence binding
Molecular Function GO:1990841 promoter-specific chromatin binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008236 serine-type peptidase activity
Molecular Function GO:0017056 structural constituent of nuclear pore
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0051028 mRNA transport

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] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] 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.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[7] 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.

[8] 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.