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Q9P7V9 (UBP9_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable ubiquitin carboxyl-terminal hydrolase 9
EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 9
Ubiquitin thioesterase 9
Ubiquitin-specific-processing protease 9
Gene names
Name:ubp9
ORF Names:SPBC1703.12
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin C-terminal hydrolase involved in regulating actin dynamics and/or endocytosis at cell tips and septa. Ref.3

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).

Subunit structure

Interacts with bun107 and bun62. Ref.3

Subcellular location

Nucleus. Cytoplasm. Cell septum. Cell tip Ref.3.

Sequence similarities

Belongs to the peptidase C19 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Probable ubiquitin carboxyl-terminal hydrolase 9
PRO_0000080610

Sites

Active site501Nucleophile By similarity
Active site3751Proton acceptor By similarity

Amino acid modifications

Modified residue5051Phosphoserine Ref.2
Modified residue5491Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9P7V9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DA4C7951C62E38B9

FASTA58566,788
        10         20         30         40         50         60 
MSLLRWMGMN SPGSTDRRKS TWEAELPKPS IRPETLTDRF YGLTNYGNTC YVSSVLVSLY 

        70         80         90        100        110        120 
HLKPFRDSLN SYPLPSAPPN FKSVCTKTNH PESSSSRHSK KKSMENRKSS LYGSNGINSC 

       130        140        150        160        170        180 
GCVDISNVGS ESGTKHQIVV GESNCSAYGM KENIYTCLKD LYCSVSCCDC RYGICSPERF 

       190        200        210        220        230        240 
IQVLRRDNEA FRSTQQQDAH EFFNFLLNSV TETLDEYYGN HSDVMHPKWV HSLFEGTLTS 

       250        260        270        280        290        300 
ETKCLTCENI TSRDESFLDL SIDIENHTSV TSCLRSFSAS EMLSSKNKFH CDVCKSLQEA 

       310        320        330        340        350        360 
EKRMKIKKLP KILSLHLKRF KYNETQEGHD KLFYTIVFTN EMRLFTTTED AENAERMYYL 

       370        380        390        400        410        420 
SSVIVHVGGG PHRGHYVSIV RTKTYGWVLF DDENVTPVNE NYLQRFFGDQ PGQATAYVLF 

       430        440        450        460        470        480 
YTAADEEDDD VSEVDTKESI KPMSIPSQLK QESVEVSNLS STPRSNSTIT YPDMDPMVAS 

       490        500        510        520        530        540 
FSSQYSHKTL DRDINSRSYF DREPSLDAER FHSRSVDASP KAVRRESRSF FPSLTRKRSK 

       550        560        570        580 
FFGSSQSNSP KDSPLRDTHK SSDEHSESKH SHTLPWQFSR SRSKR

« Hide

References

« Hide '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. expand/collapse author list , 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-505 AND SER-549, MASS SPECTROMETRY.
[3]"A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity."
Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E., Roberts-Galbraith R.H., Gould K.L.
PLoS Biol. 8:0-0(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BUN107 AND BUN62.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAB66456.1.
PIRT50325.
RefSeqNP_596207.1. NM_001022126.2.

3D structure databases

ProteinModelPortalQ9P7V9.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBC1703.12-1.

Protein family/group databases

MEROPSC19.A62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1703.12.1; SPBC1703.12.1:pep; SPBC1703.12.
GeneID2540120.
KEGGspo:SPBC1703.12.

Organism-specific databases

PomBaseSPBC1703.12.

Phylogenomic databases

eggNOGCOG5077.
KOK11872.
OMAASAFHEL.
OrthoDBEOG43XZCS.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. False negative.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801256.

Entry information

Entry nameUBP9_SCHPO
AccessionPrimary (citable) accession number: Q9P7V9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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