ULS1/YOR191W Protein Information Help

Standard Name Uls1p 1
Systematic Name Yor191wp
Alias Dis1p 2 , Tid4p 3 , Ris1p
ORF Classification Verified
Description Protein involved in proteolytic control of sumoylated substrates; contains RING finger domain; interacts with SUMO (Smt3p); member of the SWI/SNF family of DNA-dependent ATPases; plays a role in antagonizing silencing during mating-type switching; relocalizes from nucleus to cytoplasm upon DNA replication stress (1, 2, 4)
Name Description Ubiquitin Ligase for SUMO conjugates 1
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,619
Molecular Weight (Da) 184,404
Isoelectric Point (pI) 7.47

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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 Uls1p (InterPro)
Physical Interactions There are 36 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000006BC7F | Q08562
MIPS: YOR191W
NCBI: 1420457 | 6324765 | 74676476 | NP_014834.1 | NM_001183610.1
GenBank/EMBL/DDBJ: DAA10963.1 | Z75099
External Classifications EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
EC: 3.6.4.-
Amino Acid Sequence (or in FASTA format)
 
       1  MAAVPTIDLT LADSDNEDIF HSFSSSTSVD KIDIRKENGK LRMAGLEVAQ
      51  SNDDAARQAF HVFKTNISNN ETFDTILSKS KTITDSTFNN EKSSNEVKQQ
     101  QVLKEETMGS SNDEKKTQES SPSAEMIKLF YENDDVPLSD SFKQKEEGKR
     151  INQDEQVKEN ICGISSSYVS KDYDGVEDDF EPNTCQDSNL DFQEEKLNLN
     201  NKPSQQQFSD PETKDNSLKS ENKDQIKGVT TTSYRDLPIE SSAFQDSETQ
     251  NNSKNTIPNI VNEKRTPALP SNLSSVESSL KNETAKVEGK TTVRLPGLQN
     301  NVALLEQEQS ELFKHFSEQP VDISDFGRKI KRKHSGDFAD NKILKRPILP
     351  SKNMDHTTHN SHDSEQKNSS IIILSDEDES GAGINDIESP LKVSEPNTAD
     401  ALRSSVPEVI SLLDLPNIDL NNSVIKEASG SNSIPTSETD AQSSSSSVLQ
     451  GTIMTEQATQ SSQHECNSSL DTLKKNHQKL LKDLNSRESE LRNALSCCKT
     501  NSEILRRKLS RREKEVSDAE KHWQLLLTSM ARGGRTISST QQILVDEAEN
     551  QLNKLKEKRQ LTKSKLDSIN LKMYNYNEQW KSFVHSKNIN LQKSLAALER
     601  SARDSKASAT VNKRNECLAE KEKLDQMLKE GTLSFSTYKQ LTGEIQQKLN
     651  DLKLGDQRTT DINSVLPIVR QPLAKRDLFI KSIDTAKDLL AKNTSRTEMT
     701  KRILYRHLDN LVSYKNFFED GRSLIDINRR HVAHESAQIL FTNGVKMPIV
     751  FETLQDYGIK FSNPAIVNPD RRAQYFKSIE VARDLISKST RSEDAKRKIT
     801  RFLNIIEEFR KDIDTGFPPT PLKREGVGKA VVGLRQQGLK MDRLYENLRR
     851  YKIPITSEEL LQQSYLFPVN ADQRPPSNWN IVENTEDTSS TANDLSMQDE
     901  FHISNMHAAE DQEQIRALLE NVKQSESIID GEALTPEDMT VNLLKHQRLG
     951  LHWLLQVENS AKKGGLLADD MGLGKTIQAI ALMLANRSEE SKCKTNLIVA
    1001  PVSVLRVWKG ELETKVKKRA KFTTFIFGGS GNGKVKHWRD LARYDAVLVS
    1051  YQTLANEFKK HWPKKLDGEQ NQLPAVPHIQ ALNRLKTSNE YYSPFFCNDS
    1101  TFYRILLDEG QNIKNKNTRA SKACCTINGM YRWVLSGTPI QNSMDELYSL
    1151  IRFLRIPPYH KEQRFKLDIG RFFQRNKQYQ YDNEDRKNAL RKVRVLLNAI
    1201  MLRRSKADKI DGKPLLELPP KIVEVDESRL KGEELKFYTA LESKNQALAK
    1251  KLLNNSTRGS YSSVLTLLLR LRQACCHSEL VVMGEKKAEG TKVANGKSFE
    1301  DDWLRLYYKI THMSGEAQAQ VITSMNSMTC FWCMEQLEPE AMSVLTGCGH
    1351  LICDTCIEPF IEESSMLPQA KKTKGGAFAI PCKDCQRLTN EKDIVSHKLY
    1401  DQVINQGFTE EDLHAEYLSE MEKQKIQQKN VYVPNFESLE PSTKIEQCIQ
    1451  VIQRVFDESA TEKIIIFSQF TTFFEILEHF LKNKLNFPYL KYIGSMNAQR
    1501  RSDVINEFYR DPEKRILLIS MKAGNSGLTL TCANHVVIVD PFWNPYVEEQ
    1551  AQDRCYRISQ TKKVQVHKLF IKDSVEDRIS ELQKRKKEMV DSAMDPGKIK
    1601  EVNSLGRREL GFLFGLNAL*

external links for Uls1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
YGOB BioPIXIE MIPS YeastRC Public Image Repository
YOGY CYC2008 (complexes) Pfam domains

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Uls1p
1) Uzunova K, et al.  (2007) Ubiquitin-dependent Proteolytic Control of SUMO Conjugates. J Biol Chem 282(47):34167-75
2) Zhang Z and Buchman AR  (1997) Identification of a member of a DNA-dependent ATPase family that causes interference with silencing. Mol Cell Biol 17(9):5461-72
3) Dresser ME, et al.  (1997) DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is largely independent of the RAD51 pathway. Genetics 147(2):533-44
4) 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