Search Results

Overview

Uniprot IDP49792
Protein NameE3 SUMO-protein ligase RanBP2
Gene NameRANBP2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1121 NMGSSQQKNSGFRRS
1350 NFEFQVAKKEGSWWH
1414 RFALVTPKKEGHWDC
1446 QNTKSANKSGSSFVH
1530 FGTSETSKTLKSGFE
1533 SETSKTLKSGFEDMF
1593 FGTSETSKAPKSGFE
1596 SETSKAPKSGFEGMF
1652 PASSETSKAPKSGFE
1655 SETSKAPKSGFEGMF
1714 SETSKAPKSGFEGMF
1769 PASSEISKAPKSGFE
1842 SQVGTGFKSNFSEKA
1848 FKSNFSEKASKFGNT
1851 NFSEKASKFGNTEQG
1886 NTEFKSTKEGFSIPV
1963 GEGFQFGKKDPNFKG
1964 EGFQFGKKDPNFKGF
1977 GFSGAGEKLFSSQYG
1985 LFSSQYGKMANKANT
1989 QYGKMANKANTSGDF
2165 VDTGRAAKLIQRAEE
2531 IFSSEKSKPFAFGNS
2576 ESKVEPKKCELSKNS
2592 IEQSSDSKVKNLFAS
619 LLKIIKKKNSIPEPI
794 LSPSKSYKYSPKTPP
997 ASRSAESKTIEFGKT

Function

E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830)

Protein Sequence

10 MRRSKADVER 20 YIASVQGSTP 30 SPRQKSMKGF 40 YFAKLYYEAK 50 EYDLAKKYIC 60 TYINVQERDP 70 KAHRFLGLLY 80 ELEENTDKAV 90 ECYRRSVELN 100 PTQKDLVLKI 110 AELLCKNDVT 120 DGRAKYWLER 130 AAKLFPGSPA 140 IYKLKEQLLD 150 CEGEDGWNKL 160 FDLIQSELYV 170 RPDDVHVNIR 180 LVEVYRSTKR 190 LKDAVAHCHE 200 AERNIALRSS 210 LEWNSCVVQT 220 LKEYLESLQC 230 LESDKSDWRA 240 TNTDLLLAYA 250 NLMLLTLSTR 260 DVQESRELLQ 270 SFDSALQSVK 280 SLGGNDELSA 290 TFLEMKGHFY 300 MHAGSLLLKM 310 GQHSSNVQWR 320 ALSELAALCY 330 LIAFQVPRPK 340 IKLIKGEAGQ 350 NLLEMMACDR 360 LSQSGHMLLN 370 LSRGKQDFLK 380 EIVETFANKS 390 GQSALYDALF 400 SSQSPKDTSF 410 LGSDDIGNID 420 VREPELEDLT 430 RYDVGAIRAH 440 NGSLQHLTWL 450 GLQWNSLPAL 460 PGIRKWLKQL 470 FHHLPHETSR 480 LETNAPESIC 490 ILDLEVFLLG 500 VVYTSHLQLK 510 EKCNSHHSSY 520 QPLCLPLPVC 530 KQLCTERQKS 540 WWDAVCTLIH 550 RKAVPGNVAK 560 LRLLVQHEIN 570 TLRAQEKHGL 580 QPALLVHWAE 590 CLQKTGSGLN 600 SFYDQREYIG 610 RSVHYWKKVL 620 PLLKIIKKKN 630 SIPEPIDPLF 640 KHFHSVDIQA 650 SEIVEYEEDA 660 HITFAILDAV 670 NGNIEDAVTA 680 FESIKSVVSY 690 WNLALIFHRK 700 AEDIENDALS 710 PEEQEECKNY 720 LRKTRDYLIK 730 IIDDSDSNLS 740 VVKKLPVPLE 750 SVKEMLNSVM 760 QELEDYSEGG 770 PLYKNGSLRN 780 ADSEIKHSTP 790 SPTRYSLSPS 800 KSYKYSPKTP 810 PRWAEDQNSL 820 LKMICQQVEA 830 IKKEMQELKL 840 NSSNSASPHR 850 WPTENYGPDS 860 VPDGYQGSQT 870 FHGAPLTVAT 880 TGPSVYYSQS 890 PAYNSQYLLR 900 PAANVTPTKG 910 PVYGMNRLPP 920 QQHIYAYPQQ 930 MHTPPVQSSS 940 ACMFSQEMYG 950 PPALRFESPA 960 TGILSPRGDD 970 YFNYNVQQTS 980 TNPPLPEPGY 990 FTKPPIAAHA 1000 SRSAESKTIE 1010 FGKTNFVQPM 1020 PGEGLRPSLP 1030 TQAHTTQPTP 1040 FKFNSNFKSN 1050 DGDFTFSSPQ 1060 VVTQPPPAAY 1070 SNSESLLGLL 1080 TSDKPLQGDG 1090 YSGAKPIPGG 1100 QTIGPRNTFN 1110 FGSKNVSGIS 1120 FTENMGSSQQ 1130 KNSGFRRSDD 1140 MFTFHGPGKS 1150 VFGTPTLETA 1160 NKNHETDGGS 1170 AHGDDDDDGP 1180 HFEPVVPLPD 1190 KIEVKTGEED 1200 EEEFFCNRAK 1210 LFRFDVESKE 1220 WKERGIGNVK 1230 ILRHKTSGKI 1240 RLLMRREQVL 1250 KICANHYISP 1260 DMKLTPNAGS 1270 DRSFVWHALD 1280 YADELPKPEQ 1290 LAIRFKTPEE 1300 AALFKCKFEE 1310 AQSILKAPGT 1320 NVAMASNQAV 1330 RIVKEPTSHD 1340 NKDICKSDAG 1350 NLNFEFQVAK 1360 KEGSWWHCNS 1370 CSLKNASTAK 1380 KCVSCQNLNP 1390 SNKELVGPPL 1400 AETVFTPKTS 1410 PENVQDRFAL 1420 VTPKKEGHWD 1430 CSICLVRNEP 1440 TVSRCIACQN 1450 TKSANKSGSS 1460 FVHQASFKFG 1470 QGDLPKPINS 1480 DFRSVFSTKE 1490 GQWDCSACLV 1500 QNEGSSTKCA 1510 ACQNPRKQSL 1520 PATSIPTPAS 1530 FKFGTSETSK 1540 TLKSGFEDMF 1550 AKKEGQWDCS 1560 SCLVRNEANA 1570 TRCVACQNPD 1580 KPSPSTSVPA 1590 PASFKFGTSE 1600 TSKAPKSGFE 1610 GMFTKKEGQW 1620 DCSVCLVRNE 1630 ASATKCIACQ 1640 NPGKQNQTTS 1650 AVSTPASSET 1660 SKAPKSGFEG 1670 MFTKKEGQWD 1680 CSVCLVRNEA 1690 SATKCIACQN 1700 PGKQNQTTSA 1710 VSTPASSETS 1720 KAPKSGFEGM 1730 FTKKEGQWDC 1740 SVCLVRNEAS 1750 ATKCIACQCP 1760 SKQNQTTAIS 1770 TPASSEISKA 1780 PKSGFEGMFI 1790 RKGQWDCSVC 1800 CVQNESSSLK 1810 CVACDASKPT 1820 HKPIAEAPSA 1830 FTLGSEMKLH 1840 DSSGSQVGTG 1850 FKSNFSEKAS 1860 KFGNTEQGFK 1870 FGHVDQENSP 1880 SFMFQGSSNT 1890 EFKSTKEGFS 1900 IPVSADGFKF 1910 GISEPGNQEK 1920 KSEKPLENGT 1930 GFQAQDISGQ 1940 KNGRGVIFGQ 1950 TSSTFTFADL 1960 AKSTSGEGFQ 1970 FGKKDPNFKG 1980 FSGAGEKLFS 1990 SQYGKMANKA 2000 NTSGDFEKDD 2010 DAYKTEDSDD 2020 IHFEPVVQMP 2030 EKVELVTGEE 2040 DEKVLYSQRV 2050 KLFRFDAEVS 2060 QWKERGLGNL 2070 KILKNEVNGK 2080 LRMLMRREQV 2090 LKVCANHWIT 2100 TTMNLKPLSG 2110 SDRAWMWLAS 2120 DFSDGDAKLE 2130 QLAAKFKTPE 2140 LAEEFKQKFE 2150 ECQRLLLDIP 2160 LQTPHKLVDT 2170 GRAAKLIQRA 2180 EEMKSGLKDF 2190 KTFLTNDQTK 2200 VTEEENKGSG 2210 TGAAGASDTT 2220 IKPNPENTGP 2230 TLEWDNYDLR 2240 EDALDDSVSS 2250 SSVHASPLAS 2260 SPVRKNLFRF 2270 GESTTGFNFS 2280 FKSALSPSKS 2290 PAKLNQSGTS 2300 VGTDEESDVT 2310 QEEERDGQYF 2320 EPVVPLPDLV 2330 EVSSGEENEQ 2340 VVFSHRAKLY 2350 RYDKDVGQWK 2360 ERGIGDIKIL 2370 QNYDNKQVRI 2380 VMRRDQVLKL 2390 CANHRITPDM 2400 TLQNMKGTER 2410 VWLWTACDFA 2420 DGERKVEHLA 2430 VRFKLQDVAD 2440 SFKKIFDEAK 2450 TAQEKDSLIT 2460 PHVSRSSTPR 2470 ESPCGKIAVA 2480 VLEETTRERT 2490 DVIQGDDVAD 2500 ATSEVEVSST 2510 SETTPKAVVS 2520 PPKFVFGSES 2530 VKSIFSSEKS 2540 KPFAFGNSSA 2550 TGSLFGFSFN 2560 APLKSNNSET 2570 SSVAQSGSES 2580 KVEPKKCELS 2590 KNSDIEQSSD 2600 SKVKNLFASF 2610 PTEESSINYT 2620 FKTPEKAKEK 2630 KKPEDSPSDD 2640 DVLIVYELTP 2650 TAEQKALATK 2660 LKLPPTFFCY 2670 KNRPDYVSEE 2680 EEDDEDFETA 2690 VKKLNGKLYL 2700 DGSEKCRPLE 2710 ENTADNEKEC 2720 IIVWEKKPTV 2730 EEKAKADTLK 2740 LPPTFFCGVC 2750 SDTDEDNGNG 2760 EDFQSELQKV 2770 QEAQKSQTEE 2780 ITSTTDSVYT 2790 GGTEVMVPSF 2800 CKSEEPDSIT 2810 KSISSPSVSS 2820 ETMDKPVDLS 2830 TRKEIDTDST 2840 SQGESKIVSF 2850 GFGSSTGLSF 2860 ADLASSNSGD 2870 FAFGSKDKNF 2880 QWANTGAAVF 2890 GTQSVGTQSA 2900 GKVGEDEDGS 2910 DEEVVHNEDI 2920 HFEPIVSLPE 2930 VEVKSGEEDE 2940 EILFKERAKL 2950 YRWDRDVSQW 2960 KERGVGDIKI 2970 LWHTMKNYYR 2980 ILMRRDQVFK 2990 VCANHVITKT 3000 MELKPLNVSN 3010 NALVWTASDY 3020 ADGEAKVEQL 3030 AVRFKTKEVA 3040 DCFKKTFEEC 3050 QQNLMKLQKG 3060 HVSLAAELSK 3070 ETNPVVFFDV 3080 CADGEPLGRI 3090 TMELFSNIVP 3100 RTAENFRALC 3110 TGEKGFGFKN 3120 SIFHRVIPDF 3130 VCQGGDITKH 3140 DGTGGQSIYG 3150 DKFEDENFDV 3160 KHTGPGLLSM 3170 ANQGQNTNNS 3180 QFVITLKKAE 3190 HLDFKHVVFG 3200 FVKDGMDTVK 3210 KIESFGSPKG 3220 SVCRRITITE CGQI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016020 membrane
Cellular Component GO:0005642 annulate lamellae
Cellular Component GO:1990723 cytoplasmic periphery of the nuclear pore complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0042405 nuclear inclusion body
Cellular Component GO:0031965 nuclear membrane
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:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0019209 kinase activator activity
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0031267 small GTPase binding
Molecular Function GO:0061665 SUMO ligase activity
Molecular Function GO:0019789 SUMO transferase activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0051642 centrosome localization
Biological Process GO:0051028 mRNA transport
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0006607 NLS-bearing protein import into nucleus
Biological Process GO:0051168 nuclear export
Biological Process GO:0006913 nucleocytoplasmic transport
Biological Process GO:0006457 protein folding
Biological Process GO:0016925 protein sumoylation
Biological Process GO:0001975 response to amphetamine

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] 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] 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.

[5] 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.

[6] 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.

[7] 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.