Q11119 (UBP14_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Deubiquitinating enzyme 14
UBA domain-containing protein 2
Ubiquitin thioesterase 14
Ubiquitin-specific-processing protease 14

Gene names

Name:	ubp14
Synonyms:	ucp2
ORF Names:	SPBC6B1.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	775 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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).
Sequence similarities	Belongs to the peptidase C19 family. Contains 2 UBA domains. Contains 2 UBP-type zinc fingers.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to cadmium ion Inferred from mutant phenotype PubMed 18684775. Source: PomBase detoxification of cadmium ion Inferred from mutant phenotype PubMed 18684775. Source: PomBase proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence orthology. Source: PomBase protein deubiquitination Inferred from direct assay PubMed 20838651. Source: PomBase
Cellular_component	nucleoplasm Inferred from direct assay PubMed 20838651. Source: PomBase
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 PubMed 20838651. Source: PomBase 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 – 775	775	Ubiquitin carboxyl-terminal hydrolase 14		PRO_0000080613
Regions
	Domain	576 – 617	42	UBA 1
	Domain	639 – 679	41	UBA 2
	Zinc finger	26 – 91	66	UBP-type 1
	Zinc finger	172 – 245	74	UBP-type 2
Sites
	Active site	309	1	Nucleophile By similarity
	Active site	730	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	456	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q11119 [UniParc]. Last modified August 1, 1999. Version 2. Checksum: EFF8942E925CF7C0	FASTA	775	86,783
	10 20 30 40 50 60 MSCPHLTETN VVIPDNSQVI YREECVRCFN SQDEEGGIDL CLTCFQSGCG ETGLKHSLVH 70 80 90 100 110 120 FEQTLHPIVV TIARQPKQKI NDEPPQKITK LEIREDSDED LYDYFYVPKC LVCNIILDIQ 130 140 150 160 170 180 DPLLSLSLEA MKNATKASNK SQLTAWENEL TTCDHIINLP ENETYVTNLD NATCSKCDLA 190 200 210 220 230 240 ENLWMCLTCG ALSCGRKQYG GGGGNGHALS HYDDTGHPLA VKLKSISPDG QADIYCYSCD 250 260 270 280 290 300 EERIDPNIKT HMLNFGIDIA KLNKTEKSLA ELQLEQNLNW DFGASEEDDA SKRLFGPGLT 310 320 330 340 350 360 GLKNLGNSCY LASTMQSLFS IKEFAIHELN LFNTYNSVCQ TPTTDLQCQL GKLADGLVSG 370 380 390 400 410 420 KFSKPSKIGL LNNPSSSILP YQDGLRPFMF KDVVGQGHSE FGTSQQQDAY EFLLYLLGKI 430 440 450 460 470 480 RKSSIAKTDI TKIFDFETEQ KLSCLSCKRV RYSSFSSQGL TLTVPRVKIG EIEGEQIYEE 490 500 510 520 530 540 VSIDQCLDAT IQPDQMEYTC EACKSKLGAT TTTAMKSFPK VLILQANRFD LQGYQVKKLS 550 560 570 580 590 600 IPIIVNEDGI YNFDRLMAKD HPNDEDYLPE KTETIEWNQS AIEQLQAMGF PLVRCQRALL 610 620 630 640 650 660 ATGNSDTETA MNWLFEHMED PEIDKPIEVS ELLPKADSSV SEENVQSLCE FGFTVAQARK 670 680 690 700 710 720 GLLESNNNIE RAVDWILNHP DESFEEPPLE GSDSSIKNEN MGSWESTNVP VNYNLKAIIS 730 740 750 760 770 HKGSSAHAGH YVAFIRKEID GKQQWVLFND EKVLQVASLE EAKTTGYVYL FERLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Fission yeast TPR gene involved in G0 transition." Okazaki K., Okayama H. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-386.
[3]	"Proteins containing the UBA domain are able to bind to multi-ubiquitin chains." Wilkinson C.R.M., Seeger M., Hartmann-Petersen R., Stone M., Wallace M., Semple C., Gordon C. Nat. Cell Biol. 3:939-943(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17049.1. D83659 Genomic DNA. Translation: BAA12032.1.
PIR	T40647.
RefSeq	NP_596085.1. NM_001021999.2.
3D structure databases
ProteinModelPortal	Q11119.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC6B1.06c-1.
Protein family/group databases
MEROPS	C19.A65.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC6B1.06c.1; SPBC6B1.06c.1:pep; SPBC6B1.06c.
GeneID	2541157.
KEGG	spo:SPBC6B1.06c.
Organism-specific databases
PomBase	SPBC6B1.06c.
Phylogenomic databases
eggNOG	COG5207.
HOGENOM	HOG000162311.
KO	K11836.
OMA	DDMVEDP.
OrthoDB	EOG470XRN.
Family and domain databases
Gene3D	3.30.40.10. 2 hits.
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. 2 hits. [Graphical view]
PIRSF	PIRSF016308. UBP. 1 hit.
SMART	SM00165. UBA. 2 hits. SM00290. ZnF_UBP. 2 hits. [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. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802270.

Entry information

Entry name

UBP14_SCHPO

Accession

Primary (citable) accession number: Q11119

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	August 1, 1999
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program