TOM1/YDR457W Protein Information Help

Standard Name Tom1p 1
Systematic Name Ydr457wp
ORF Classification Verified
Description E3 ubiquitin ligase of the hect-domain class; has a role in mRNA export from the nucleus and may regulate transcriptional coactivators; involved in degradation of excess histones; interacts with Dia2p and is required for Dia2p degradation; required to target Cdc6p for ubiquitin-mediated destruction during G1 phase (2, 3, 4, 5, 6, 7, 8)
Name Description Temperature dependent Organization in Mitotic nucleus
Experimental Data
Molecules/cell 358 9
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 3,268
Molecular Weight (Da) 374,180
Isoelectric Point (pI) 4.92

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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 Tom1p (InterPro)
Physical Interactions There are 34 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000006BC10 | Q03280
MIPS: YDR457W
NCBI: 2257705 | 398366613 | 50401412 | 927738 | NP_010745.3
GenBank/EMBL/DDBJ: DAA12291.1 | D63905 | U33050
External Classifications EC: 6.3.2.- [Acid-Amino-Acid Ligases (Peptide Synthases)]
Amino Acid Sequence (or in FASTA format)
       1  MVLFTRCEKA RKEKLAAGYK PLVDYLIDCD TPTFLERIEA IQEWDRSRDD
      51  LYVWIPILDR MDGLLLKVAE KYKYKQDPKK ECEVKLVEME AHDVDYCLKM
     101  LKFTRRLLLN TENRFVYSSG DVLMYLLNCP NFTIKLAVMR ILAILGERFV
     151  IAREKIVAHN IFGDHNLRKK TLKLALSLSS SVMDEDGEHF SLVDLYFDKK
     201  KVPQKWRKLR FTHYTSNDFK KSSQQKNNIN ETQTSIKKVT MTTQELCEHS
     251  LQQIFDKGMA LLPAESWFDF SIKASVAKAF SDDSGENIDL RNIIIETKLN
     301  AIAFVNTIFS PPQVSSKLFE LDPYAFNSLT DLISLSETKI PKELRTDALF
     351  TLECISLKHV WCSDIIRNLG GNISHGLLFQ ILRYIAKTLR EATDEIDEEY
     401  NVRFFYLISN LADVKPLHES LFAAGLIPTL LEIVSIRNCP YKRTLASATH
     451  LLETFIDNSE TTTEFIENDG FTMLITSVAN EIDFTLAHPE TWQPPKYSVV
     501  YYSISFRELA YIRSLLKLVL KLLSTDSGDR IRNLIDSPIL VSLKKILENK
     551  LVFGLTLITY TLDVVQKVIN SEPTIYPVLV EAGLIPYVID NFPKLIGPSA
     601  ELLSLLPDVV SAICLNPEGL KQVKEKGLIN NLFDFLLDAD HARILTGGDR
     651  STEYGTDIDE LARHYPDLKA NIVEALCNVI RKMPSTFRNE REFLFTSPKD
     701  QKYFFHRKNE EILTDKEEHE PAYWELLDKG TMLDTFTSVL FGMSLGNGSF
     751  SQVPQHLEAR DFLAIIFMEN PPYEYFTSVA ISNVTEVLQY LDEKYEDYAF
     801  MDVMKVLNDQ LENLNDFLNS PNDRSFFLER DGENSVRSCH SKLCRLAAIL
     851  NIVTNVYIDL TTLSCKRIMQ IYSYFDKRGF SLIKNLKLLF QKCALEEMYI
     901  RQHMPDSVIT ETMPLPIVDV SGDGPPLQIY IDDPKKGDQK GKITSVKTRN
     951  TLQMRTILYT LQSNTAILFR CFLRLSHSRN MDLEHKDLTT EVHIFENVVE
    1001  NVIEMLKATE LEGHLPYILV LLNFNTFVFT IPKASPNSTE ILQTIPAYIF
    1051  YQKGGYLLYL HIIRDLFTRM TKIKDLSSLD NINYIDESNG ILTLSCLINA
    1101  LTFYNKSMQT ETMENVQSIG KYYVSIDDDY NIMKALTVPI KVMALAMILD
    1151  LDKSDSLFKT QSRNVPYSVF KQLLSMLKNI FTNVNIYTKE LYELHWDLIF
    1201  PPIKKISLFE QVGIPGDVAA NYLTDTGDDL PADNSIGLFS PEQWEKYKKL
    1251  IGEDKSIYYP QPMQAQYYKG CSSKELDELR DTFFNDGLPS RIFTVLPFYP
    1301  KLVNAFAKTL LQIFTKYDEP TEVFAGRILD RILETDLDDP ATLSSLIHLF
    1351  GIFLNEKYIY QKASHLMQRF IEYLEKSLKP EHVNTPWFSK ALYVYEIILA
    1401  KSELPHLEEL SKDVLLRYPL LSMAKVFRIP DPMKQKLFDI LIRVSDISNF
    1451  YSALATSRIL IFYSRDELYA NNIARSGILS RLLKVIGSFQ KLDKINFLES
    1501  SFLLLTRRCF ETTENVDALI RAEINRSFTA RPLGGGDDAV RELTTILEEK
    1551  AHVVMRSPSQ FIDVLCETAR FHEFDDQGAL VDYSLKRFLG EKDKNTQASS
    1601  TEKSDIYERT GIMHLLLSQL MAASEKDWLS EPANSSDLPE NKKAQLDPSR
    1651  NPVCAYMIFL LKLLVELVSS YNQCKFEFLT FSRRNTYAER PRPRTTAINF
    1701  FLYRLLDKPV GTDHDKHEAK RREVIGMLAR SVIIGFLATV QDDRTTKTDV
    1751  KLADPHMNFI RKFAIEAIIK AIRNATSSSK LLESNHLKLD MWFRIITSMV
    1801  YVQAPYLRQL LDSNKVEADQ YQLCKLVIDL GLPSVITEAM ASIDLNYPFS
    1851  KKIFNVAVEA LNTISSTRNN FSEHFKIEDH DEVEDEVDES DKEEIPDMFK
    1901  NSALGMYDVE DIEEDDDDDT SLIGDDDAMA FVDSDNGFEV VFSDEDDDMG
    1951  EEDADDARSD SEENELSSEM QSSTADGTDV DYEVDDADGL IINIDQPSGD
    2001  DEEMADYDAN ISHSSHSENE DDASMDVIEV YDDELSSGYD VDLSDYDVDE
    2051  SDWDSGLSSL SISDEDSESS EDEPINSTRM GDSRRRWLIA EGVELTDDSQ
    2101  GESEEDDRGV FRGIEHIFSN ENEPLFRVHD EMRHRNHHRS INRTHFHSAM
    2151  SAPSLSLLNR GRRNQSNLIN PLGPTGLEQV ENDISDQVTV AGSGSRPRSH
    2201  HLHFSEVLVS GSFFDEPVLD GIILKSTVSR WKDIFDMFYD SKTYANCIIP
    2251  TVINRLYKVS LALQKDLENK REQEKLKNKN LLFNEAKVES HNSSDAISVE
    2301  QDDIQESNVT HDDHEPVYVT IQGSEVDIGG TDIDPEFMNA LPDDIRADVF
    2351  AQHVRERRAE ARLNSDHNVH SREIDSDFLE AIPEDIREGI LDTEAEEQRM
    2401  FGRIGSSADV IRADDDVSNN DEEVENGLDH GNSNDRNNAD PEKKKPARIY
    2451  FAPLIDRAGI ASLMKSVFIS KPYIQREIYH ELFYRLCSSK QNRNDLMNTF
    2501  LFILSEGIID QHSLEKVYNI ISSRAMGHAK TTTVRQLPSD CTPLTVANQT
    2551  IEILQSLIDA DSRLKYFLIA EHDNLIVNKA NNKSRKEALP DKKLRWPLWH
    2601  LFSLLDRKLI TDESVLMDLL TRILQVCTKT LAVLSTSSNG KENLSKKFHL
    2651  PSFDEDDLMK ILSIIMLDSC TTRVFQQTLN IIYNLSKLQG CMSIFTKHLV
    2701  SLAISIMSKL KSALDGLSRE VGTITTGMEI NSELLQKFTL PSSDQAKLLK
    2751  ILTTVDFLYT HKRKEEERNV KDLQSLYDKM NGGPVWSSLS ECLSQFEKSQ
    2801  AINTSATILL PLIESLMVVC RRSDLSQNRN TAVKYEDAKL LDFSKTRVEN
    2851  LFFPFTDAHK KLLNQMIRSN PKLMSGPFAL LVKNPKVLDF DNKRYFFNAK
    2901  LKSDNQERPK LPITVRREQV FLDSYRALFF KTNDEIKNSK LEITFKGESG
    2951  VDAGGVTREW YQVLSRQMFN PDYALFLPVP SDKTTFHPNR TSGINPEHLS
    3001  FFKFIGMIIG KAIRDQCFLD CHFSREVYKN ILGRPVSLKD MESLDPDYYK
    3051  SLVWILENDI TDIIEETFSV ETDDYGEHKV INLIEGGKDI IVTEANKQDY
    3101  VKKVVEYKLQ TSVKEQMDNF LVGFYALISK DLITIFDEQE LELLISGLPD
    3151  IDVDDWKNNT TYVNYTATCK EVSYFWRAVR SFDAEERAKL LQFVTGTSKV
    3201  PLNGFKELSG VNGVCKFSIH RDFGSSERLP SSHTCFNQLN LPPYESYETL
    3251  RGSLLLAINE GHEGFGLA*                                  

external links for Tom1p
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 Tom1p
1) Utsugi T, et al.  (1995) A high dose of the STM1 gene suppresses the temperature sensitivity of the tom1 and htr1 mutants in Saccharomyces cerevisiae. Biochim Biophys Acta 1263(3):285-8
2) Utsugi T, et al.  (1999) Yeast tom1 mutant exhibits pleiotropic defects in nuclear division, maintenance of nuclear structure and nucleocytoplasmic transport at high temperatures. Gene 234(2):285-95
3) Davey M, et al.  (2000) The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1. Mol Gen Genet 263(3):520-6
4) Saleh A, et al.  (1998) TOM1p, a yeast hect-domain protein which mediates transcriptional regulation through the ADA/SAGA coactivator complexes. J Mol Biol 282(5):933-46
5) Duncan K, et al.  (2000) A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr Biol 10(12):687-96
6) Singh RK, et al.  (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33
7) Kim DH and Koepp DM  (2012) Hect E3 ubiquitin ligase Tom1 controls Dia2 degradation during the cell cycle. Mol Biol Cell 23(21):4203-11
8) Kim DH, et al.  (2012) The Hect domain E3 ligase Tom1 and the F-box protein Dia2 control Cdc6 degradation in G1 phase. J Biol Chem 287(53):44212-20
9) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41