Q9UTT1 (UBP21_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 21
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 21
Ubiquitin thioesterase 21
Ubiquitin-specific-processing protease 21

Gene names

Name:	ubp21
Synonyms:	ubp15, ubpd
ORF Names:	SPBC713.02c

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	1129 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in regulating the steady-state levels of proteins including prp4. Ref.1
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).
Subcellular location	Nucleus Ref.1.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 MATH domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to stress Inferred from expression pattern PubMed 12529438. Source: PomBase endocytosis Inferred from mutant phenotype PubMed 20838651. Source: PomBase protein deubiquitination Inferred from direct assay PubMed 20838651. Source: PomBase ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cell division site Inferred from direct assay PubMed 20838651. Source: PomBase cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay Ref.1PubMed 16823372PubMed 20838651. Source: PomBase transport vesicle Inferred from direct assay PubMed 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 – 1129	1129	Ubiquitin carboxyl-terminal hydrolase 21		PRO_0000080614
Regions
	Domain	51 – 204	154	MATH
Sites
	Active site	239	1	Nucleophile By similarity
	Active site	481	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	42	1	H → D in AAF01440. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UTT1 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 536681DD9E78EBF8	FASTA	1,129	130,832
	10 20 30 40 50 60 MVLSNVDAEE VNMDSSMELE ESSQEPLRAD NYEEIYNSLV HHEPDLEEAA HASYSWVVKN 70 80 90 100 110 120 FSTLEDKTYS PLFKAGHTTW RIVLFPKGCN QTEYASVFLE YLPQCKVEAI RKYEAELAAG 130 140 150 160 170 180 KTPTIDPEIV NDETYSCCAQ FALSLSNVQD PTVMQINTSH HRFRSEVKDW GFTRFVDLRK 190 200 210 220 230 240 IAVPTPEFPV PFLENDEICI SVTVRVLQDP TGVLWHSFVN YNSKKETGYV GLKNQGATCY 250 260 270 280 290 300 MNSLLQSLFF TNIFRKTVYK IPTDNDDSRD SVAYALQRVF YNLEKQREPV STTELTRSFG 310 320 330 340 350 360 WNSFDSFMQH DIQEFNRVLQ DNLEKKMKGT EVENALNDIF VGKMKSYVKC IDVNYESSRV 370 380 390 400 410 420 EDFWDIQLNV KGMDTLEDSF RDAIQVETLT GDNKYYAEGH GLQDAHKGII FESLPNVLQL 430 440 450 460 470 480 QLKRFDYDML RDMMVKINDR HEFPLEIDLE PYLSETADKS ESHVYVLHGV LVHGGDLHGG 490 500 510 520 530 540 HYYALIKPEK DSNWFKFDDD RVTRATIKEV LEDNYGGEPA GRAKGYNGNP FKRFMNAYML 550 560 570 580 590 600 VYFRKSRLDH ILSPVTAEDV PFHVRNTLDE EHRVVERKLL EREEQQIYRR VRVLTTDGFK 610 620 630 640 650 660 KYHGFDMTDF SASDDDPVLI TTKIKRNANI WDLQKHLAGL LNRDTSGIRI WLMTNRQNRT 670 680 690 700 710 720 VRVDLPLDKK TILVDQICDM HIRKDMDMRV YVEFLSEHNQ LLADFGATDD NDFDTYIFLK 730 740 750 760 770 780 IFDYETQQIS GLADLHVSKN SPISSLSEWI REHLKWSSDV PITYYEEIKT GMVDVLDPNA 790 800 810 820 830 840 SFEKSEIQVG DIICFEKKLV HDSSSDTSHP YKSALDLYDF MAHRVVITFE PRYSDDTNNG 850 860 870 880 890 900 VFDLVLTTHT NYTDMARAVA NKLNVDPNYL QFTMAHLPSR TPRSVIRNPS KFTLQNAIPS 910 920 930 940 950 960 TYSHNQNVVM FYEVLDITLS ELERKQLIRV HFLSNGISHE TQMEFYVDKE GTVEDILRQV 970 980 990 1000 1010 1020 TQKVPLNAED ASRLRLYEVY NHRILKSHLP TDGIYDLNEF STAYVEVTPK EEQMQLKTDD 1030 1040 1050 1060 1070 1080 AVSIVVQHFF KDLSRLHDIP FYFVLLRGET LKDLKKRLQK RLGYNDTQFS KVKLAVLQAQ 1090 1100 1110 1120 SFGKPYYLTD DDEVLYGELE PQSHILGLDH PPANGSAQYH GMDQAIRMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The deubiquitinating enzyme Ubp21p of fission yeast stabilizes a mutant form of protein kinase Prp4p." Richert K., Schmidt H., Gross T., Kaeufer N.F. Mol. Genet. Genomics 267:88-95(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION. Strain: 972 / ATCC 24843.
[2]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF187961 Genomic DNA. Translation: AAF01440.1. CU329671 Genomic DNA. Translation: CAC22603.1.
RefSeq	NP_595341.1. NM_001021249.2.
3D structure databases
ProteinModelPortal	Q9UTT1.
SMR	Q9UTT1. Positions 224-575.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UTT1. 1 interaction.
STRING	4896.SPBC713.02c-1.
Protein family/group databases
MEROPS	C19.A59.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC713.02c.1; SPBC713.02c.1:pep; SPBC713.02c.
GeneID	2541131.
KEGG	spo:SPBC713.02c.
Organism-specific databases
PomBase	SPBC713.02c.
Phylogenomic databases
eggNOG	COG5077.
HOGENOM	HOG000160240.
KO	K11838.
OMA	RLFVKSS.
OrthoDB	EOG4ZW8K5.
Family and domain databases
InterPro	IPR002083. MATH. IPR024729. Pept_C19_dom. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR008974. TRAF-like. [Graphical view]
Pfam	PF00917. MATH. 1 hit. PF00443. UCH. 1 hit. PF12436. USP7. 1 hit. [Graphical view]
SMART	SM00061. MATH. 1 hit. [Graphical view]
SUPFAM	SSF49599. Traf_like. 1 hit.
PROSITE	PS50144. MATH. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802244.

Entry information

Entry name

UBP21_SCHPO

Accession

Primary (citable) accession number: Q9UTT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program