Ubiquitin carboxyl-terminal hydrolase 14 - Arabidopsis thaliana (Mouse-ear cress)

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Q8L6Y1 (UBP14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 14
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 14
Short name=AtUBP14
TITAN-6 protein
Ubiquitin thioesterase 14
Ubiquitin-specific-processing protease 14

Gene names

Name:	UBP14
Synonyms:	TTN6
Ordered Locus Names:	At3g20630, At3g20625
ORF Names:	F3H11_1, K10D20.17, K10D20.26

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	797 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Involved in seed and embryo development. Ref.6 Ref.7
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Tissue specificity	Constitutively and ubiquitously expressed (at protein level). Ref.6
Sequence similarities	Belongs to the peptidase C19 family. Contains 2 UBA domains. Contains 1 UBP-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	embryo development ending in seed dormancy Inferred from mutant phenotype Ref.6 Ref.7. Source: TAIR protein deubiquitination Inferred from direct assay Ref.6. Source: TAIR root hair elongation Inferred from mutant phenotype PubMed 19969521. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	omega peptidase activity Inferred from electronic annotation. Source: InterPro ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay Ref.6 PubMed 19969521. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 797

797

Ubiquitin carboxyl-terminal hydrolase 14

PRO_0000080697

Regions

Domain

613 – 654

UBA 1

Domain

670 – 710

UBA 2

Zinc finger

178 – 252

UBP-type

Sites

Active site

317

Nucleophile By similarity

Active site

758

Proton acceptor By similarity

Experimental info

Sequence conflict

601

G → A in AAG42755. Ref.1

Secondary structure

797

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q8L6Y1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: B827C513A6D5C4E2
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FASTA

797

88,374

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine." Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D. Plant Physiol. 124:1828-1843(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.
[2]	"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." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." 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. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"The ubiquitin-specific protease UBP14 is essential for early embryo development in Arabidopsis thaliana." Doelling J.H., Yan N., Kurepa J., Walker J., Vierstra R.D. Plant J. 27:393-405(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]	"Diversity of TITAN functions in Arabidopsis seed development." Tzafrir I., McElver J.A., Liu C.-M., Yang L.J., Wu J.Q., Martinez A., Patton D.A., Meinke D.W. Plant Physiol. 128:38-51(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Solution structure of RSGI RUH-011, a UBA domain from Arabidopsis cDNA." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 594-665.
[9]	"Solution structure of RSGI RUH-023, a UBA domain from Arabidopsis cDNA." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 651-710.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF302664 mRNA. Translation: AAG42755.1.
AP000410, AP002034 Genomic DNA. Translation: BAB01171.1.
CP002686 Genomic DNA. Translation: AEE76405.1.
AY140096 mRNA. Translation: AAM98237.1.
AK226894 mRNA. Translation: BAE98971.1.

IPI

IPI00525815.

RefSeq

NP_566666.2. NM_112954.3.

UniGene

At.16942.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VEK	NMR	-	A	594-664	[»]
1WIV	NMR	-	A	651-710	[»]

ProteinModelPortal

Q8L6Y1.

SMR

Q8L6Y1. Positions 2-796.

ModBase

Search...

Protein family/group databases

MEROPS

C19.084.

Proteomic databases

PaxDb

Q8L6Y1.

PRIDE

Q8L6Y1.

Protocols and materials databases

DNASU

821610.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G20630.1; AT3G20630.1; AT3G20630.

GeneID

821610.

KEGG

ath:AT3G20630.

Organism-specific databases

TAIR

At3g20630.

Phylogenomic databases

eggNOG

COG5207.

HOGENOM

HOG000162311.

InParanoid

Q8L6Y1.

K11836.

OMA

DDMVEDP.

PhylomeDB

Q8L6Y1.

ProtClustDB

CLSN2690557.

Gene expression databases

Genevestigator

Q8L6Y1.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR016652. Ubiquitinyl_hydrolase.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]

Pfam

PF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]

PIRSF

PIRSF016308. UBP. 1 hit.

SMART

SM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS50030. UBA. 2 hits.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8L6Y1.

Entry information

Entry name

UBP14_ARATH

Accession

Primary (citable) accession number: Q8L6Y1
Secondary accession number(s): Q0WV77, Q9FPT0, Q9LJT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents