O74442 (UBP16_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ubiquitin carboxyl-terminal hydrolase 16
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 16
Ubiquitin thioesterase 16
Ubiquitin-specific-processing protease 16

Gene names

Name:	ubp16
ORF Names:	SPCC1682.12c

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	457 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein deubiquitination Inferred from direct assay PubMed 20838651. Source: PomBase ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleolus Inferred from direct assay PubMed 16823372PubMed 20838651. Source: PomBase
Molecular_function	ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay PubMed 20838651. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 457	457	Probable ubiquitin carboxyl-terminal hydrolase 16		PRO_0000248399
Sites
	Active site	134	1	Nucleophile By similarity
	Active site	388	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	61	1	Phosphoserine Ref.2
	Modified residue	64	1	Phosphothreonine Ref.2
	Modified residue	65	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O74442 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 56AADB2AA996EFF3	FASTA	457	51,582
	10 20 30 40 50 60 MSLATLQGQS LDFAVKHSLD DLLKNPVRFR PAVVSSPSVP EGTYTVLNNP KQSTVSRKSF 70 80 90 100 110 120 SAPTSPTRNK RSGSSSQEYK KSSGTRGDGA NDFVDEDPAF IPPARILFPE EKLSMEWDNI 130 140 150 160 170 180 MPNAPGLVNL GNTCFMNSVL QLMTQTPPLV QYLLSGQHSL SCRMNACVLC RMEQHVARAY 190 200 210 220 230 240 PNKGTKRASA FKPSGIQSML KVISSHFRPY RQEDAHEFMR YLVDAWQKSC LQNHKNLDHP 250 260 270 280 290 300 SRETSVVHRI FGGYLRQQIL CSVCKKPSNT YQALLDLSVD AKGSSLADSL KHFVHAEKLT 310 320 330 340 350 360 KQNKYRCENC KQLVDASKQM TIYRAPNILT IHFKRFTFNG FQSSKISKQI SYPESFNLGP 370 380 390 400 410 420 YMSDPNCSCW YELIGVLVHA GGSTRSGHYY SFCKSSNGVW LKFDDDFVSN SSIDRVLNQQ 430 440 450 AYILQYKRKS TSSSKHKLNT ENTVTKTSNK KRRKISF

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]

"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-61; THR-64 AND SER-65, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA20678.1.
PIR	T41069.
RefSeq	NP_587805.1. NM_001022798.2.
3D structure databases
HSSP	HSSP built from PDB template 2AYN based on UniProtKB P54578.
ProteinModelPortal	O74442.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC1682.12c-1.
Protein family/group databases
MEROPS	C19.A66.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1682.12c.1; SPCC1682.12c.1:pep; SPCC1682.12c.
GeneID	2538947.
KEGG	spo:SPCC1682.12c.
Organism-specific databases
PomBase	SPCC1682.12c.
Phylogenomic databases
eggNOG	COG5077.
KO	K11855.
OMA	YSHETEN.
OrthoDB	EOG4JHGQN.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20800122.

Entry information

Entry name

UBP16_SCHPO

Accession

Primary (citable) accession number: O74442

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program