Reviewed, UniProtKB/Swiss-Prot Q11119 (UBP14_SCHPO)

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 14
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 14
    Ubiquitin-specific-processing protease 14
    Deubiquitinating enzyme 14
    UBA domain-containing protein 2

Gene names

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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

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

General annotation (Comments)

Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
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
Gene Ontology (GO)
Biological process	proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW polyubiquitin binding Traceable author statement. Source: GeneDB_SPombe ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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	By similarity
	Active site	721	1	By similarity
	Active site	730	1	By similarity
Amino acid modifications
	Modified residue	456	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q11119-1 [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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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: 11584278] [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: 18257517] [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.
3D structure databases
SMR	Q11119. Positions 1-72, 146-261, 297-774.
ModBase	Search...
Protein-protein interaction databases
STRING	Q11119.
Protein family/group databases
MEROPS	C19.083.
Genome annotation databases
GeneID	2541157.
GenomeReviews	Gene locus ubp14 in contig CU329671_GR.
KEGG	spo:SPBC6B1.06c.
NMPDR	fig|4896.1.peg.1951.
Organism-specific databases
GeneDB_Spombe	SPBC6B1.06c.
Phylogenomic databases
eggNOG	fuNOG04424.
HOGENOM	HBG746888.
OMA	WSTALQA.
OrthoDB	EOG9322F9.
PhylomeDB	Q11119.
Enzyme and pathway databases
BRENDA	3.1.2.15. 653.
Gene expression databases
ArrayExpress	Q11119.
Family and domain databases
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. 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]
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...

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:	January 19, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)