O60079 (UBP12_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ubiquitin carboxyl-terminal hydrolase 12
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 12
Ubiquitin thiolesterase 12
Ubiquitin-specific-processing protease 12

Gene names

Name:	ubp12
ORF Names:	SPCC1494.05c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	979 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 1 DUSP domain.

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. Source: GeneDB_Spombe ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 979	979	Probable ubiquitin carboxyl-terminal hydrolase 12		PRO_0000080612
Regions
	Domain	51 – 152	102	DUSP
Sites
	Active site	320	1	Nucleophile By similarity
	Active site	935	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	19	1	Phosphoserine Ref.2
	Modified residue	37	1	Phosphoserine Ref.2
	Modified residue	39	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O60079 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: A705444BCDB437D2	FASTA	979	111,967
	10 20 30 40 50 60 MDSLSESSTS SYHGKRPRSL SEESQSSSNM DDISQKSISL GDASEISKNL PSIAEQKQLI 70 80 90 100 110 120 GELVNNQPEL ELGQVDNYIL SYSWYERLCS YLAEDGPFPG PVDQEDIADL ETGTLKPDLQ 130 140 150 160 170 180 EEIDFTIISR DVWDLLVRWY GLKGPEFPRE TVNLGSESHP HLVVEVYPPI FSLTLLSTNA 190 200 210 220 230 240 VDANESHKPK KISLSSKSTL EDLLEGVKYT LSLPSDQFRL WRVDTDQPLH RTIDPSSFIK 250 260 270 280 290 300 INSKEIIDFL EKSKTLVELG MDSSCSLVAE CMINETWPVD RALRLQFLIQ QRNNQSSNEE 310 320 330 340 350 360 QKQEKRVPGT CGLSNLGNTC YMNSALQCLT HTRELRDFFT SDEWKNQVNE SNPLGMGGQV 370 380 390 400 410 420 ASIFASLIKS LYSPEHSSFA PRQFKATIGK FNHSFLGYGQ QDSQEFLAFL LDGLHEDLNR 430 440 450 460 470 480 IYQKPYTSKP DLYEVDEEKI KNTAEECWRL HKLRNDSLIV DLFQGMYRST LVCPVCNTVS 490 500 510 520 530 540 ITFDPFMDLT LPLPVKQVWS HTVTFIPADT NLTPLAIEVV LESKAATIED LVKYVAEKSG 550 560 570 580 590 600 CSDYRKILVT ETYKGRFYRF LTQLSKSLLM EISEEDEIYL YELERPYEDG SDDILVPVYH 610 620 630 640 650 660 ISDDSTNSAN SYMSSRDFGH PFVLQLSDNE VTDASFISEK LKLKYQQFTT LKNLKNIDSL 670 680 690 700 710 720 ESLELGHEDE QVQKGPLDVD MDHSQTPLFE MRVFHDRFEK IPTGWNMSVS NLPLLTERDK 730 740 750 760 770 780 KDLESTVDPL DAHSIEEEDD SEFKDVAPGS YPEPSKSNEN TKLTAKENDR LLIQGDLLVC 790 800 810 820 830 840 EWPEKSYQFV FSVAPSSPQM GRSLWLESKT ILSDKKDDSE DSRTITLNDC LDEFEKTEQL 850 860 870 880 890 900 GEEDPWYCPT CKEFRQASKQ MEIWRCPEIL IFHLKRFSSE RRFRDKIDDL VEFPIDNLDM 910 920 930 940 950 960 SMRTGSYKLS EKENPKLIYE LYAVDNHYGG LGGGHYTAFA KNPDNGQFYC FDDSRVTPVC 970 PEETVTSAAY LLFYRRKTS

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: 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: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-37 AND SER-39, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA19303.1.
PIR	T41006.
RefSeq	NP_588530.1. NM_001023518.1.
3D structure databases
ProteinModelPortal	O60079.
ModBase	Search...
Protein-protein interaction databases
STRING	O60079.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1494.05c.1; SPCC1494.05c.1:pep; SPCC1494.05c.
GeneID	2538990.
GenomeReviews	Gene locus ubp12 in contig CU329672_GR.
KEGG	spo:SPCC1494.05c.
NMPDR	fig|4896.1.peg.868.
Organism-specific databases
GeneDB_Spombe	SPCC1494.05c.
Phylogenomic databases
eggNOG	fuNOG05241.
GeneTree	EFGT00050000000212.
OMA	CKEFRQA.
OrthoDB	EOG4FR40X.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000429-MONOMER.
Gene expression databases
ArrayExpress	O60079.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
KO	K11835.
Pfam	PF06337. DUSP. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 1 hit. [Graphical view]
PROSITE	PS51283. DUSP. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP12_SCHPO

Accession

Primary (citable) accession number: O60079

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program