Search Results

Overview

Uniprot IDQ9H814
Protein NamePhosphorylated adapter RNA export protein
Gene NamePHAX
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
158 TYNYLLAKKLRKESQ
159 YNYLLAKKLRKESQE
198 ENGQGHLKRKRPVKD
332 RRTQVLGKKMKQAIK
339 KKMKQAIKSLNFQED

Function

A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus (PubMed:39011894). Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Also binds to telomerase RNA

Protein Sequence

10 MALEVGDMED 20 GQLSDSDSDM 30 TVAPSDRPLQ 40 LPKVLGGDSA 50 MRAFQNTATA 60 CAPVSHYRAV 70 ESVDSSEESF 80 SDSDDDSCLW 90 KRKRQKCFNP 100 PPKPEPFQFG 110 QSSQKPPVAG 120 GKKINNIWGA 130 VLQEQNQDAV 140 ATELGILGME 150 GTIDRSRQSE 160 TYNYLLAKKL 170 RKESQEHTKD 180 LDKELDEYMH 190 GGKKMGSKEE 200 ENGQGHLKRK 210 RPVKDRLGNR 220 PEMNYKGRYE 230 ITAEDSQEKV 240 ADEISFRLQE 250 PKKDLIARVV 260 RIIGNKKAIE 270 LLMETAEVEQ 280 NGGLFIMNGS 290 RRRTPGGVFL 300 NLLKNTPSIS 310 EEQIKDIFYI 320 ENQKEYENKK 330 AARKRRTQVL 340 GKKMKQAIKS 350 LNFQEDDDTS 360 RETFASDTNE 370 ALASLDESQE 380 GHAEAKLEAE 390 EAIEVDHSHD LDIF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015030 Cajal body
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0140262 mRNA cap binding complex binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0015643 toxic substance binding
Biological Process GO:0015031 protein transport
Biological Process GO:0043489 RNA stabilization
Biological Process GO:0006408 snRNA export from nucleus

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] 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.