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UniProtKB/Swiss-Prot entry Q8L6Y1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UBP14_ARATH
Primary accession number Q8L6Y1
Secondary accession numbers Q0WV77 Q9FPT0 Q9LJT6
Integrated into Swiss-Prot on August 30, 2005
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name Ubiquitin carboxyl-terminal hydrolase 14
Synonyms EC 3.1.2.15
Ubiquitin thioesterase 14
Ubiquitin-specific-processing protease 14
Deubiquitinating enzyme 14
AtUBP14
TITAN-6 protein
Gene name
Name: UBP14
Synonyms: TTN6
OrderedLocusNames: At3g20630/At3g20625
ORFNames: F3H11_1, K10D20.17, K10D20.26
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
DOI=10.1104/pp.124.4.1828; PubMed=11115897 [NCBI, ExPASy, EBI, Israel, Japan]
Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D.;
"The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine.";
Plant Physiol. 124:1828-1843(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/7.3.217; PubMed=10907853 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11576424 [NCBI, ExPASy, EBI, Israel, Japan]
Doelling J.H., Yan N., Kurepa J., Walker J., Vierstra R.D.;
"The ubiquitin-specific protease UBP14 is essential for early embryo development in Arabidopsis thaliana.";
Plant J. 27:393-405(2001).
[6]
FUNCTION.
DOI=10.1104/pp.128.1.38; PubMed=11788751 [NCBI, ExPASy, EBI, Israel, Japan]
Tzafrir I., McElver J.A., Liu C.-M., Yang L.J., Wu J.Q., Martinez A., Patton D.A., Meinke D.W.;
"Diversity of TITAN functions in Arabidopsis seed development.";
Plant Physiol. 128:38-51(2002).
[7]
STRUCTURE BY NMR OF 594-665.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-011, a UBA domain from Arabidopsis cDNA.";
Submitted (SEP-2004) to the PDB data bank.
[8]
STRUCTURE BY NMR OF 651-710.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-023, a UBA domain from Arabidopsis cDNA.";
Submitted (NOV-2004) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF302664; AAG42755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000410; BAB01171.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP002034; BAB01171.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY140096; AAM98237.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK226894; BAE98971.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_566666.2; -.
UniGene At.16942
3D structure databases
PDB
1VEK; NMR; -; A=594-665.[ExPASy / RCSB / EBI]
1WIV; NMR; -; A=651-710.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1VEK; -.
1WIV; -.
SMR Q8L6Y1; 157-272.
ModBase Q8L6Y1.
Protein family/group databases
MEROPS C19.084; -.
Organism-specific databases
TAIR At3g20630; -.
Ontologies
GO
GO:0004221; Molecular function: ubiquitin thiolesterase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001394; Peptidase_C19.
IPR000449; UBA/transl_elong_EF1B_N.
IPR015940; UBA/transl_elong_EF1B_N_euk.
IPR016652; Ubiquitinyl_hydrolase.
IPR001607; Znf_UBP.
Graphical view of domain structure.
Pfam PF00627; UBA; 2.
PF00443; UCH; 1.
PF02148; zf-UBP; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF016308; UBP; 1.
SMART SM00165; UBA; 2.
SM00290; ZnF_UBP; 1.
SMART graphical view of domain structure.
PROSITE PS50030; UBA; 2.
PS00972; UCH_2_1; 1.
PS00973; UCH_2_2; 1.
PS50235; UCH_2_3; 1.
PS50271; ZF_UBP; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8L6Y1.
Genome annotation databases
GeneID 821610; -.
GenomeReviews BA000014_GR; AT3G20630.
KEGG ath:AT3G20630; -.
NMPDR fig|3702.1.peg.14295; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Hydrolase; Metal-binding; Protease; Repeat; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   797  797     Ubiquitin carboxyl-terminal hydrolase 14. PRO_0000080697
DOMAIN   613   654  42     UBA 1. 
DOMAIN   670   710  41     UBA 2. 
ZN_FING   178   252  75     UBP-type. 
ACT_SITE   317   317        By similarity. 
ACT_SITE   749   749        By similarity. 
ACT_SITE   758   758        By similarity. 
CONFLICT   601   601        G -> A (in Ref. 1; AAG42755). 
STRAND   603   605  3      
HELIX   616   625  10      
HELIX   629   638  10      
TURN   639   641  3      
HELIX   644   654  11      
TURN   659   661  3      
HELIX   673   682  10      
HELIX   686   695  10      
HELIX   700   709  10      
Sequence information
Length: 797 AA [This is the length of the unprocessed precursor] Molecular weight: 88374 Da [This is the MW of the unprocessed precursor] CRC64: B827C513A6D5C4E2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELLRSNLSR VQIPEPTHRI YKHECCISFD TPRSEGGLFV DMNSFLAFGK DYVSWNYEKT 

        70         80         90        100        110        120 
GNPVYLHIKQ TRKSIPEDRP LKKPTLLAIG VDGGFDNNEP EYEESYSIVI LPDFVSLPFP 

       130        140        150        160        170        180 
SVELPEKVRI AVDTVVNAVG AERKEQVAAW TAEKKLISEH ALTLQQIKSG IVIPPSGWKC 

       190        200        210        220        230        240 
SKCDKTENLW LNLTDGMILC GRKNWDGTGG NNHAVEHYKE TAYPLAVKLG TITADLEAAD 

       250        260        270        280        290        300 
VYSYPEDDSV LDPLLAEHLA HFGIDFSSMQ KTEMTTAERE LDQNTNFDWN RIQESGKELV 

       310        320        330        340        350        360 
PVFGPGYTGL VNLGNSCYLA ATMQIVFSTH SFISRYFSHQ SLKMAFEMAP ADPTLDLNMQ 

       370        380        390        400        410        420 
LTKLGHGLLS GKYSMPATQK DATTGDPRQE GIPPRMFKNV IAASHAEFSS MRQQDALDFF 

       430        440        450        460        470        480 
LHLVGKVERA SNTTPDLDPS RSFKFGIEEK ILCPSGKVGY NKREDCILSL NIPLHEATNK 

       490        500        510        520        530        540 
DELEAFHKQK AGKGLEENDM RSSDEIVRPR VPLEACLANF ASSEPIEDYY SSALKGMTTA 

       550        560        570        580        590        600 
IKTTGLTSFP DYLVLHMRKF VMEEGWVPKK LDVYIDVPDV IDISHMRSKG LQPGEELLPD 

       610        620        630        640        650        660 
GVPEEVMESA QPVANEEIVA QLVSMGFSQL HCQKAAINTS NAGVEEAMNW LLSHMDDPDI 

       670        680        690        700        710        720 
DAPISHQTSD IDQSSVDTLL SFGFAEDVAR KALKASGGDI EKATDWVFNN PNASVSDMDV 

       730        740        750        760        770        780 
SSSNSAQTPA QSGLPDGGGK YKLFGIVSHM GTSVHCGHYV AHILKEGRWV IFNDDKVGIS 

       790 
TDPPKDMGYV YFFQRLD 

Q8L6Y1 in FASTA format

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