MTR10/YOR160W Protein Information Help

Standard Name Mtr10p
Systematic Name Yor160wp
Alias Kap111p
ORF Classification Verified
Description Nuclear import receptor; mediates the nuclear localization of proteins involved in mRNA-nucleus export; promotes dissociation of mRNAs from the nucleus-cytoplasm mRNA shuttling protein Npl3p; required for retrograde import of mature tRNAs; relocalizes from cytoplasm to the nuclear periphery upon DNA replication stress (1, 2, 3, 4, 5)
Name Description Mrna TRansport defective 6
Experimental Data
Molecules/cell 6340 7
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 972
Molecular Weight (Da) 110,744
Isoelectric Point (pI) 4.51

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Mtr10p (InterPro)
Physical Interactions There are 31 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052F60 | Q99189
MIPS: YOR160W
NCBI: 1293720 | 1420397 | 2498597 | 6324734 | NP_014803.1
GenBank/EMBL/DDBJ: DAA10933.1 | U55020 | Z75068
Amino Acid Sequence (or in FASTA format)
       1  MDNLQVSDIE TALQCISSTA SQDDKNKALQ FLEQFQRSTV AWSICNEILS
      51  KEDPTNALLE LNIFAAQTLR NKVTYDLSQL ENNLPQFKDS LLTLLLSHNQ
     101  KLIITQLNVA LARLAIQFLE WQNPIFEIIS LLNSSPSILL NFLRILPEET
     151  LDIASTSLTE VEFNSRIHEL IDPIAEDVLK FLVSCIDLLQ NTDGNSSSSI
     201  SLEQILRCLN SWSYEFPVEQ LLTVQPLINL VFETISNGNE SDMEAFDSAI
     251  DCLCVILRES RDTTNEQLIS ALFHQLMLLQ EKLLPTLFTD HPLNDEYDDD
     301  LLEGMTRLFV EAGEAWSVVI SKNPDFFKPM VLVLLMLTCK NEDLDVVSYT
     351  FPFWFNFKQS LVLPRYQESR KAYSDIFVKL INGIITHLQY PSGQFSSKEE
     401  EDKFKDFRYH MGDVLKDCTA VVGTSEALSQ PLIRIKSAIE NNNSWQIMEA
     451  PLFSLRTMAK EISLTENTIL PEIIKIICNL PEQAKIRYAS TLVLGRYTEW
     501  TAKHPELLEV QLQYIFNGFQ LHEGSSDMQS IITASSHALM FFCSDCSKLL
     551  VGYIDQLINF FLNVQSSIDI ESQFELCQGL SAVINNQPEA KVSVIFQKLV
     601  DDNLRQIEAL IPQWKANPTL LAPQIADKID LLYALFEELK PRYNYPQQGS
     651  EPLLPRIEFI WKALRTLLVD AGAMTDSIIV ERVAKLLRRI FERFHVFCEP
     701  ILPSVAEFLI QGYLTTGFGS YLWCSGSLIV IFGDDESFPI SPSLKDAVWK
     751  FALSQCETFI LNFNKFDKLQ LNDYHEAIID FFSLISDLIM FYPGAFLNST
     801  ELLGPVLNVA LECVNKLDNY DAYICILRCL DDIISWGFKT PPISTVSIEI
     851  VPDEWRKQVI NEVVIAHGNQ LILVLFIGLV TTFENTAHSD AISCIVKCLR
     901  ILTEANNNDA TICIDWIYKV VEQLGQVTLN ERDNLAKAVV EGLNSKDYRK
     951  VREGIRAFVG WYSRKNINSR FE*                             

external links for Mtr10p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Mtr10p
1) Pemberton LF, et al.  (1997) A distinct and parallel pathway for the nuclear import of an mRNA-binding protein. J Cell Biol 139(7):1645-53
2) Senger B, et al.  (1998) Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. EMBO J 17(8):2196-207
3) Windgassen M, et al.  (2004) Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the translating mRNPs, and Npl3p can function as a translational repressor. Mol Cell Biol 24(23):10479-91
4) Murthi A, et al.  (2010) Regulation of tRNA Bidirectional Nuclear-Cytoplasmic Trafficking in Saccharomyces cerevisiae. Mol Biol Cell 21(4):639-49
5) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
6) Kadowaki T, et al.  (1994) Isolation and characterization of Saccharomyces cerevisiae mRNA transport-defective (mtr) mutants. J Cell Biol 126(3):649-59
7) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41