Search Results

Overview

Uniprot IDP62826
Protein NameGTP-binding nuclear protein Ran
Gene NameRAN
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
123 PIVLCGNKVDIKDRK
127 CGNKVDIKDRKVKAK
134 KDRKVKAKSIVFHRK
141 KSIVFHRKKNLQYYD
142 SIVFHRKKNLQYYDI
23 VGDGGTGKTTFVKRH
37 HLTGEFEKKYVATLG
38 LTGEFEKKYVATLGV
60 HTNRGPIKFNVWDTA
71 WDTAGQEKFGGLRDG
99 VTSRVTYKNVPNWHR

Function

GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:10400640, PubMed:17209048, PubMed:26272610, PubMed:27306458, PubMed:8276887, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis (PubMed:11336674, PubMed:26272610, PubMed:29040603, PubMed:7819259, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport (PubMed:8896452, PubMed:9351834, PubMed:9428644). Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation (PubMed:10408446, PubMed:29040603). Required for normal progress through mitosis (PubMed:12194828, PubMed:29040603, PubMed:8421051). The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). Acts as a negative regulator of the kinase activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases (PubMed:10400640)

Protein Sequence

10 MAAQGEPQVQ 20 FKLVLVGDGG 30 TGKTTFVKRH 40 LTGEFEKKYV 50 ATLGVEVHPL 60 VFHTNRGPIK 70 FNVWDTAGQE 80 KFGGLRDGYY 90 IQAQCAIIMF 100 DVTSRVTYKN 110 VPNWHRDLVR 120 VCENIPIVLC 130 GNKVDIKDRK 140 VKAKSIVFHR 150 KKNLQYYDIS 160 AKSNYNFEKP 170 FLWLARKLIG 180 DPNLEFVAMP 190 ALAPPEVVMD 200 PALAAQYEHD 210 LEVAQTTALP DEDDDL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005814 centriole
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0001673 male germ cell nucleus
Cellular Component GO:0002177 manchette
Cellular Component GO:0042470 melanosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0030496 midbody
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0055037 recycling endosome
Cellular Component GO:0042565 RNA nuclear export complex
Cellular Component GO:0036126 sperm flagellum
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0045505 dynein intermediate chain binding
Molecular Function GO:0003925 G protein activity
Molecular Function GO:0019003 GDP binding
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0061676 importin-alpha family protein binding
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0051301 cell division
Biological Process GO:0071389 cellular response to mineralocorticoid stimulus
Biological Process GO:0006259 DNA metabolic process
Biological Process GO:0046039 GTP metabolic process
Biological Process GO:0021766 hippocampus development
Biological Process GO:0000278 mitotic cell cycle
Biological Process GO:0000070 mitotic sister chromatid segregation
Biological Process GO:0007052 mitotic spindle organization
Biological Process GO:0042307 positive regulation of protein import into nucleus
Biological Process GO:0035281 pre-miRNA export from nucleus
Biological Process GO:0006611 protein export from nucleus
Biological Process GO:0006606 protein import into nucleus
Biological Process GO:1902570 protein localization to nucleolus
Biological Process GO:0000055 ribosomal large subunit export from nucleus
Biological Process GO:0000056 ribosomal small subunit export from nucleus
Biological Process GO:0000054 ribosomal subunit export from nucleus
Biological Process GO:0061015 snRNA import into nucleus
Biological Process GO:0007286 spermatid development
Biological Process GO:0016032 viral process

Reference

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[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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] 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.

[10] 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.

[11] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[12] 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.