YAGB_SCHPO
ID YAGB_SCHPO Reviewed; 365 AA.
AC Q09874;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Uncharacterized protein C12G12.11c;
GN ORFNames=SPAC12G12.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
CC -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14655046}.
CC -!- SIMILARITY: To yeast YGL082w. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA91506.1; -; Genomic_DNA.
DR PIR; S62542; S62542.
DR RefSeq; NP_592887.1; NM_001018287.2.
DR AlphaFoldDB; Q09874; -.
DR SMR; Q09874; -.
DR BioGRID; 279480; 2.
DR IntAct; Q09874; 1.
DR STRING; 4896.SPAC12G12.11c.1; -.
DR SwissPalm; Q09874; -.
DR MaxQB; Q09874; -.
DR PaxDb; Q09874; -.
DR EnsemblFungi; SPAC12G12.11c.1; SPAC12G12.11c.1:pep; SPAC12G12.11c.
DR GeneID; 2543045; -.
DR KEGG; spo:SPAC12G12.11c; -.
DR PomBase; SPAC12G12.11c; -.
DR VEuPathDB; FungiDB:SPAC12G12.11c; -.
DR eggNOG; KOG2427; Eukaryota.
DR HOGENOM; CLU_794910_0_0_1; -.
DR InParanoid; Q09874; -.
DR OMA; MHFGQQL; -.
DR PhylomeDB; Q09874; -.
DR PRO; PR:Q09874; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISM:PomBase.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; PTHR18063; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..365
FT /note="Uncharacterized protein C12G12.11c"
FT /id="PRO_0000116430"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 42280 MW; 74B729CACBD5C24F CRC64;
MDNVQEHDPD TQEHNNETQN HKQEDHSNSY QTRTIPFIEP LSREYQKRII LCQTVNGPCP
IIALSNALIL KSNVDRPFEL PKKRYITPDE LTEYLVEFAK AYGLCKNQQS LQDKLTSMHF
GQQLNPCLYD IEKFEYGHEI FCTFGVRLVH GWILSDDMGL SDEDLSYLRK LEYYEKVADT
FAERRSLLEM QEPLTEQQQD FLNNSTCVDK VMENRYTMQF LTNAGLKKIL ELVGPGEIVV
VFRSSHFSTM YSNPDSFAQF TLVTDSGYAR TGEDVVWETF DSQTVETGNG ELCAANFIPA
VYVLNQRKEE KKKRAKDDEQ YAKRLAKEEE ERGKKETPKK ASNTPRRNKS NTQKSRKQSE
NCLIS