NAB2_SCHPO
ID NAB2_SCHPO Reviewed; 307 AA.
AC O13713;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nuclear polyadenylated RNA-binding protein nab2;
GN Name=nab2; ORFNames=SPAC14C4.06c;
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).
CC -!- FUNCTION: Binds to polyadenylated RNA and single-stranded DNA. It may
CC be involved not only in RNA processing but also in transcription
CC regulation. Believed to associate directly with nascent RNA polymerase
CC II transcripts and remain associated during subsequent nuclear RNA
CC processing reactions (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NAB2 family. {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; CAB11199.1; -; Genomic_DNA.
DR PIR; T37691; T37691.
DR RefSeq; NP_594911.1; NM_001020343.2.
DR AlphaFoldDB; O13713; -.
DR SMR; O13713; -.
DR BioGRID; 277968; 59.
DR STRING; 4896.SPAC14C4.06c.1; -.
DR iPTMnet; O13713; -.
DR SwissPalm; O13713; -.
DR MaxQB; O13713; -.
DR PaxDb; O13713; -.
DR PRIDE; O13713; -.
DR EnsemblFungi; SPAC14C4.06c.1; SPAC14C4.06c.1:pep; SPAC14C4.06c.
DR GeneID; 2541466; -.
DR KEGG; spo:SPAC14C4.06c; -.
DR PomBase; SPAC14C4.06c; nab2.
DR VEuPathDB; FungiDB:SPAC14C4.06c; -.
DR eggNOG; KOG3702; Eukaryota.
DR HOGENOM; CLU_081064_0_0_1; -.
DR InParanoid; O13713; -.
DR OMA; DEEIPLC; -.
DR PhylomeDB; O13713; -.
DR PRO; PR:O13713; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IDA:PomBase.
DR GO; GO:0036002; F:pre-mRNA binding; IPI:PomBase.
DR GO; GO:1902373; P:negative regulation of mRNA catabolic process; IGI:PomBase.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR GO; GO:0043144; P:sno(s)RNA processing; IMP:PomBase.
DR Gene3D; 1.10.340.40; -; 1.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR043094; Nab2/ZC3H14_N_sf.
DR PANTHER; PTHR14738; PTHR14738; 2.
PE 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..307
FT /note="Nuclear polyadenylated RNA-binding protein nab2"
FT /id="PRO_0000352808"
FT ZN_FING 178..202
FT /note="C3H1-type 1"
FT ZN_FING 217..232
FT /note="C3H1-type 2"
FT ZN_FING 254..268
FT /note="C3H1-type 3"
FT REGION 102..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 33929 MW; 7DC0907D588F05DE CRC64;
MTTLLETPGY SEKLHDSIEK KLSEYGWGEE AASLADFVLV MLSNGKTQTE INEELVDLIG
SDFDTSFSLW LFNQIEELEK SKNASVESVS KIDEIDFIEK ESTDKSQQSF SVPETSIQPQ
SSQTPNITSL REEKELPTGR VGQKLKLTSQ KQRFNPMAAS FNYSKSVMPA AKRALTQTQE
VPLCKYADKC SRANCIFAHP TPAAAPGEGM VLSSEMCASG KECKAADCVK GHPSPATVTT
LPPFMSMSTI PIPCKYKPCL NPACRFIHPT KSRNMTWRPP SKTEETSLSE RSFAVNESEE
QLHVPSV
