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ADN2_SCHPO
ID   ADN2_SCHPO              Reviewed;         743 AA.
AC   O94619;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Adhesion defective protein 2;
DE   AltName: Full=LisH domain-containing protein adn2;
GN   Name=adn2; ORFNames=SPBC1289.10c;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=19542312; DOI=10.1128/ec.00078-09;
RA   Dodgson J., Avula H., Hoe K.L., Kim D.U., Park H.O., Hayles J.,
RA   Armstrong J.;
RT   "Functional genomics of adhesion, invasion, and mycelial formation in
RT   Schizosaccharomyces pombe.";
RL   Eukaryot. Cell 8:1298-1306(2009).
CC   -!- FUNCTION: Probable transcriptional regulator involved in cell adhesion.
CC       {ECO:0000269|PubMed:19542312}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FLO8 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB38690.1; -; Genomic_DNA.
DR   PIR; T39361; T39361.
DR   RefSeq; NP_596834.1; NM_001023855.2.
DR   AlphaFoldDB; O94619; -.
DR   BioGRID; 276726; 52.
DR   STRING; 4896.SPBC1289.10c.1; -.
DR   iPTMnet; O94619; -.
DR   MaxQB; O94619; -.
DR   PaxDb; O94619; -.
DR   PRIDE; O94619; -.
DR   EnsemblFungi; SPBC1289.10c.1; SPBC1289.10c.1:pep; SPBC1289.10c.
DR   GeneID; 2540193; -.
DR   KEGG; spo:SPBC1289.10c; -.
DR   PomBase; SPBC1289.10c; adn2.
DR   VEuPathDB; FungiDB:SPBC1289.10c; -.
DR   eggNOG; ENOG502R28W; Eukaryota.
DR   HOGENOM; CLU_376492_0_0_1; -.
DR   InParanoid; O94619; -.
DR   OMA; FLIEWWN; -.
DR   PhylomeDB; O94619; -.
DR   PRO; PR:O94619; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; ISO:PomBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:PomBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:PomBase.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:PomBase.
DR   InterPro; IPR006594; LisH.
DR   Pfam; PF08513; LisH; 1.
DR   SMART; SM00667; LisH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..743
FT                   /note="Adhesion defective protein 2"
FT                   /id="PRO_0000303959"
FT   DOMAIN          38..70
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   743 AA;  81159 MW;  B55B4B71A85B4398 CRC64;
     MADPGLRSGV GLPSQQGQKH DLQKDQKQPH VNNADRTTQS LLNSYIYDYL IKKDYCEAAR
     AFGREAQVQT LVRSQEETNS LAKRHKRMSP VAVKHEGISN NESSDENMNV NNGNLDSFSS
     SSAPPPPPIL PIDSAGGFLI EWWNVFWDIY NARRGQGSEP AKAYMSHISN LRKKSRLNLQ
     EIQKNSLHTG NTSHPYANAS FPHDPANAMG QQIDSSQFHQ GAGGLNDRNQ HLMRQAMLNN
     QSRETFPPTA AQLQQLKQLH YRQLQSVQQQ QKQHQQKKTP QSGSTPQMQN TTSQPTTHDT
     HPPKQQGPIS DFRSIPSSPK TEGAPSNAQF RPSLPATPNG SVPQSNPLYD TTGLNGGQYP
     VVQNSAQPLL HEINFASNRN PHLKQGGAVP SSTLPQQQKS LDKPKPAQQP STGQFSGNQM
     NQYGFSNSPY SQNMLYNFNG NANPSRLNPA LKNYMEELKL LEQQNKKRLL LVSQEKERKG
     YTSASPDRPL SQTITESSVA KTKSTTPKST DTPTEATTSP VKVSTKNSNT TENLNGINES
     NMPMLQNGLP LRTSGDHPSN YSNLIENSST SDTNNADNGM DVMGNWQLQQ THSSRPTPNA
     SSPLDVRSKQ KPSSANSNAP TPAPTVNTTN PESSTNEATS VGPALEPSQG ANVHKSDSEL
     DNQNQSGKSN PDTSATPSAP TESTTVATKS SDNQLLDVGN STDIDAALLN DFDFDKFLKD
     TSTGDDLWFG LFNLPDNEDS TAA
 
 
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