O42726 (UBP2_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 2
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2

Gene names

Name:	UBP2
Ordered Locus Names:	KLLA0E02376g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces › Kluyveromyces lactis

Protein attributes

Sequence length	1220 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin By similarity.
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity 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 – 1220	1220	Ubiquitin carboxyl-terminal hydrolase 2		PRO_0000080587
Sites
	Active site	707	1	Nucleophile By similarity
	Active site	1153	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	646 – 650	5	KWSHG → EMESR in AAB94074. Ref.1
	Sequence conflict	1009 – 1022	14	KSIEP…ETLYM → QVYRAATFRRKRCTW in AAB94074. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O42726 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: 7362B30C368B4A47	FASTA	1,220	141,120
	10 20 30 40 50 60 MMASQEPALE LNGEQRDSVS ETAEVLRSKS LESFSDLVDD GKTLLYGDIS KSFPFKTCDR 70 80 90 100 110 120 ILDDIRISPW FLKKFGSSVM KQPMLQYSRE RQQLQPWNLV HLIDQVNLRS RYDYDSMTCP 130 140 150 160 170 180 GKNTISVMFA LLVDPNFTPN DFDDIDKFPE YFFHLKITVK RRSYLENFNR HVGITHYHVL 190 200 210 220 230 240 EPESLHPFDK RDIFIMEEKD CRLVDQSIFV SADTNKLILV EIIKPEFNSE NLAEYRTAKI 250 260 270 280 290 300 EERYKNACQE FDLLNPDDIP SQAECLKTLF MIFKNPLQRK SANSEFKIIS RDSVALNSQI 310 320 330 340 350 360 NTDWLTTMFD FSLQKTAVED NVQSGEEYKP PDLVDYITDF KVRGIREAYT RKSMEVVLIG 370 380 390 400 410 420 KQSMLLENEL GTEKKTVAKC FSNQHFSASH TWWFNILNHQ HIEPFPYDIN YHFINLSVAF 430 440 450 460 470 480 KYIDKDIIKN YETQIALDQE NISHYFDALQ YVTNAKGSYQ LIAYCGKQDV VGYEDLNNAL 490 500 510 520 530 540 QVFGLDPTDI DASLLDANTM IEYYNSHLLR SSDNQRKDLR NALRVLGKYL GSQKMLFLVE 550 560 570 580 590 600 YEPYYNVQQA YTLLKVDETV DDDIIQTAYT INIADAPGLK KDYDRAIFTI ALDRRSIFLL 610 620 630 640 650 660 NVLTDECPEF AQYYNCTDIS YDEALNIIEI DMNASDDVIL EVFQKKWSHG IMTGPDYLLK 670 680 690 700 710 720 LKMALQNIGF TRNSKLINHF LDTGIVDVSC LPVATWPAGI NNVGNTCYLN SLLQFFFTIK 730 740 750 760 770 780 PLRDFILNYD DDSAKLLDAS EYHSRRRIGG REVSKQEELR SVQFVYHLRD LFNDMIHTNS 790 800 810 820 830 840 RCVTPTKELV YLAFAPSNVE VEFGDDTVAQ KELIDLTTDV VEDPTDTTRH LASCDDDIIM 850 860 870 880 890 900 CQSPVALPEH KTSSEAGTQQ YSVQVAKISA DQLENTLEIG RQQDVTECIG NVLAQLEIAS 910 920 930 940 950 960 EPLSLEDDLE QNDLVKQLFY GRIKQDLIPV NDEASVRTKY ERFLSLLVNT GDHPKDIYDA 970 980 990 1000 1010 1020 LDFYFQNDYL NLEEYGDVKR TVSISELPAV LQIQIQRVYY DREKFMPFKS IEPLPFGETL 1030 1040 1050 1060 1070 1080 YMDRYMATED PKLLAEIQQN AELKQKLQDL KQRQRKLLSQ NEIGLTLKSS LIETKKFLQS 1090 1100 1110 1120 1130 1140 GTLKAHDIDA DNIPSSIAYI DILINNIDEE LKSLFNKITD LETTISQQFS EFKHIGYSLF 1150 1160 1170 1180 1190 1200 AVFIHRGEAS YGHYWVYIKD HTKNGIWRKY NDDSVTEVPQ SEVFNFTEGN TATPYFLVYV 1210 1220 REGQEQETIE PLKRILQQQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of KIUBP2, a ubiquitin hydrolase gene of Kluyveromyces lactis that can suppress a ts-mutation in CBF2, a gene encoding a centromeric protein of Saccharomyces cerevisiae." Winkler A.A., Korstanje R., Zonneveld B.J.M., Hooykaas P.J.J., Steensma H.Y. Curr. Genet. 38:17-22(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-539 / JBD100.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF022776 Genomic DNA. Translation: AAB94074.1. CR382125 Genomic DNA. Translation: CAG99142.1.
PIR	T30529.
RefSeq	XP_454055.1. XM_454055.1.
3D structure databases
ProteinModelPortal	O42726.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.O42726.
Protein family/group databases
MEROPS	C19.003.
Proteomic databases
PRIDE	O42726.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2894270.
KEGG	kla:KLLA0E02377g.
Phylogenomic databases
eggNOG	NOG275561.
HOGENOM	HOG000094458.
KO	K11849.
OMA	IFRKYND.
OrthoDB	EOG498Z7X.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR025305. UCH_repeat_domain. [Graphical view]
Pfam	PF13446. RPT. 2 hits. 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...

Entry information

Entry name

UBP2_KLULA

Accession

Primary (citable) accession number: O42726
Secondary accession number(s): Q6CPT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	September 27, 2004
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program