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Q9P7V9

- UBP9_SCHPO

UniProt

Q9P7V9 - UBP9_SCHPO

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Protein

Probable ubiquitin carboxyl-terminal hydrolase 9

Gene
ubp9, SPBC1703.12
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Ubiquitin C-terminal hydrolase involved in regulating actin dynamics and/or endocytosis at cell tips and septa.1 Publication

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Nucleophile By similarity
Active sitei375 – 3751Proton acceptor By similarity

GO - Molecular functioni

  1. protein binding Source: PomBase
  2. ubiquitin-specific protease activity Source: PomBase

GO - Biological processi

  1. cellular protein localization Source: PomBase
  2. endocytosis Source: PomBase
  3. protein deubiquitination Source: PomBase
  4. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.A62.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ubp9
ORF Names:SPBC1703.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC1703.12.

Subcellular locationi

Nucleus. Cytoplasm. Cell septum. Cell tip 1 Publication

GO - Cellular componenti

  1. cell division site Source: PomBase
  2. cell septum Source: UniProtKB-SubCell
  3. cell tip Source: PomBase
  4. cytoplasm Source: PomBase
  5. cytosol Source: PomBase
  6. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Probable ubiquitin carboxyl-terminal hydrolase 9PRO_0000080610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei505 – 5051Phosphoserine1 Publication
Modified residuei549 – 5491Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P7V9.

Interactioni

Subunit structurei

Interacts with bun107 and bun62.1 Publication

Protein-protein interaction databases

BioGridi276657. 6 interactions.
MINTiMINT-4706427.
STRINGi4896.SPBC1703.12-1.

Structurei

3D structure databases

ProteinModelPortaliQ9P7V9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 424384USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5077.
KOiK11872.
OMAiCENITSR.
OrthoDBiEOG7TF7JV.
PhylomeDBiQ9P7V9.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P7V9-1 [UniParc]FASTAAdd to Basket

« Hide

MSLLRWMGMN SPGSTDRRKS TWEAELPKPS IRPETLTDRF YGLTNYGNTC    50
YVSSVLVSLY HLKPFRDSLN SYPLPSAPPN FKSVCTKTNH PESSSSRHSK 100
KKSMENRKSS LYGSNGINSC GCVDISNVGS ESGTKHQIVV GESNCSAYGM 150
KENIYTCLKD LYCSVSCCDC RYGICSPERF IQVLRRDNEA FRSTQQQDAH 200
EFFNFLLNSV TETLDEYYGN HSDVMHPKWV HSLFEGTLTS ETKCLTCENI 250
TSRDESFLDL SIDIENHTSV TSCLRSFSAS EMLSSKNKFH CDVCKSLQEA 300
EKRMKIKKLP KILSLHLKRF KYNETQEGHD KLFYTIVFTN EMRLFTTTED 350
AENAERMYYL SSVIVHVGGG PHRGHYVSIV RTKTYGWVLF DDENVTPVNE 400
NYLQRFFGDQ PGQATAYVLF YTAADEEDDD VSEVDTKESI KPMSIPSQLK 450
QESVEVSNLS STPRSNSTIT YPDMDPMVAS FSSQYSHKTL DRDINSRSYF 500
DREPSLDAER FHSRSVDASP KAVRRESRSF FPSLTRKRSK FFGSSQSNSP 550
KDSPLRDTHK SSDEHSESKH SHTLPWQFSR SRSKR 585
Length:585
Mass (Da):66,788
Last modified:October 1, 2000 - v1
Checksum:iDA4C7951C62E38B9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB66456.1.
PIRiT50325.
RefSeqiNP_596207.1. NM_001022126.2.

Genome annotation databases

EnsemblFungiiSPBC1703.12.1; SPBC1703.12.1:pep; SPBC1703.12.
GeneIDi2540120.
KEGGispo:SPBC1703.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB66456.1 .
PIRi T50325.
RefSeqi NP_596207.1. NM_001022126.2.

3D structure databases

ProteinModelPortali Q9P7V9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 276657. 6 interactions.
MINTi MINT-4706427.
STRINGi 4896.SPBC1703.12-1.

Protein family/group databases

MEROPSi C19.A62.

Proteomic databases

MaxQBi Q9P7V9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC1703.12.1 ; SPBC1703.12.1:pep ; SPBC1703.12 .
GeneIDi 2540120.
KEGGi spo:SPBC1703.12.

Organism-specific databases

PomBasei SPBC1703.12.

Phylogenomic databases

eggNOGi COG5077.
KOi K11872.
OMAi CENITSR.
OrthoDBi EOG7TF7JV.
PhylomeDBi Q9P7V9.

Miscellaneous databases

NextBioi 20801256.
PROi Q9P7V9.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-549, IDENTIFICATION BY 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. 8:708-716(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BUN107 AND BUN62.

Entry informationi

Entry nameiUBP9_SCHPO
AccessioniPrimary (citable) accession number: Q9P7V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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