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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Transportin-3

UniprotKB/SwissProt ID: Q9Y5L0 (Q9Y5L0)

Gene Name: TNPO3

Organism: Homo sapiens (Human)

Function: Importin, which transports target proteins into the nucleus (PubMed:10366588, PubMed:10713112, PubMed:11517331, PubMed:12628928, PubMed:24449914). Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains (PubMed:10366588, PubMed:10713112, PubMed:11517331, PubMed:12628928, PubMed:24449914). Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 phosphorylation (PubMed:30916345, PubMed:31465518). The nuclear import process is regulated by the small GTPase Ran that partitions between cytoplasm and nucleus in the predominantly GDP- and GTP-bound form, respectively (PubMed:23878195, PubMed:24449914). Importin associates with target cargo proteins in the cytoplasm, and the competitive binding of GTP-bound Ran induces the release of cargos in the nucleus (PubMed:23878195, PubMed:24449914) (Microbial infection) Involved in immunodeficiency virus (HIV-1) infection by importing the pre-integration complex (PIC) into the nucleus (PubMed:18722123, PubMed:21901095, PubMed:22398280, PubMed:29329553). Required for a nuclear maturation step of HIV-1 prior to integration (PubMed:21901095, PubMed:22398280)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus envelope. Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR013598 Exportin-1/Importin-b-like
IPR051345 Importin_beta-like_NTR

The S-nitrosylation sites of Q9Y5L0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 125 LALQMPSWKG C VQTLVEKYSN   
2 296 REDLDKVLNY C RIFTELCETF   
3 303 LNYCRIFTEL C ETFLEKIVCT   
4 312 LCETFLEKIV C TPGQGLGDLR   
5 380 QRLLHALARH C QLEPDHEGVP   
6 511 PVLGYLMKGL C EKPLASAAAK   
7 60 LLQIRQDVES C YFAAQTMKMK   
8 634 PIVENGQTHP C QKVIQEIWPV   
9 908 FHKQVTSAEE C KQVCWALRDF