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Overview

Uniprot ID	Q9H6Z4
Protein Name	Ran-binding protein 3
Gene Name	RANBP3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
21	PPVFVFQKDKGQKSP
23	VFVFQKDKGQKSPAE
378	ESAAAYTKATARKCL

Function

Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export

Protein Sequence

10 MADLANEEKP 20 AIAPPVFVFQ 30 KDKGQKSPAE 40 QKNLSDSGEE 50 PRGEAEAPHH 60 GTGHPESAGE 70 HALEPPAPAG 80 ASASTPPPPA 90 PEAQLPPFPR 100 ELAGRSAGGS 110 SPEGGEDSDR 120 EDGNYCPPVK 130 RERTSSLTQF 140 PPSQSEERSS 150 GFRLKPPTLI 160 HGQAPSAGLP 170 SQKPKEQQRS 180 VLRPAVLQAP 190 QPKALSQTVP 200 SSGTNGVSLP 210 ADCTGAVPAA 220 SPDTAAWRSP 230 SEAADEVCAL 240 EEKEPQKNES 250 SNASEEEACE 260 KKDPATQQAF 270 VFGQNLRDRV 280 KLINESVDEA 290 DMENAGHPSA 300 DTPTATNYFL 310 QYISSSLENS 320 TNSADASSNK 330 FVFGQNMSER 340 VLSPPKLNEV 350 SSDANRENAA 360 AESGSESSSQ 370 EATPEKESLA 380 ESAAAYTKAT 390 ARKCLLEKVE 400 VITGEEAESN 410 VLQMQCKLFV 420 FDKTSQSWVE 430 RGRGLLRLND 440 MASTDDGTLQ 450 SRLVMRTQGS 460 LRLILNTKLW 470 AQMQIDKASE 480 KSIRITAMDT 490 EDQGVKVFLI 500 SASSKDTGQL 510 YAALHHRILA 520 LRSRVEQEQE 530 AKMPAPEPGA 540 APSNEEDDSD 550 DDDVLAPSGA 560 TAAGAGDEGD GQTTGST

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005643	nuclear pore
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0070412	R-SMAD binding
Molecular Function	GO:0031267	small GTPase binding
Biological Process	GO:0006611	protein export from nucleus

Reference

[1] 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.

[2] 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.

[3] 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.