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SAP62_SCHPO
ID   SAP62_SCHPO             Reviewed;         217 AA.
AC   Q9P7L8;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Pre-mRNA-splicing factor sap62;
DE   AltName: Full=Spliceosome-associated protein 62;
GN   Name=sap62; ORFNames=SPBC21C3.05;
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   IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
RN   [3]
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: Involved in mRNA splicing where it associates with cdc5 and
CC       the other cwf proteins as part of the spliceosome.
CC   -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC       spliceosome sub-complex reminiscent of a late-stage spliceosome
CC       composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC       cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC       cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC       cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC       cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC       prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC       smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:16823372}. Cytoplasm
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SF3A2 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB76041.1; -; Genomic_DNA.
DR   PIR; T50349; T50349.
DR   RefSeq; NP_596585.1; NM_001022505.2.
DR   AlphaFoldDB; Q9P7L8; -.
DR   SMR; Q9P7L8; -.
DR   BioGRID; 277148; 23.
DR   IntAct; Q9P7L8; 1.
DR   STRING; 4896.SPBC21C3.05.1; -.
DR   MaxQB; Q9P7L8; -.
DR   PaxDb; Q9P7L8; -.
DR   EnsemblFungi; SPBC21C3.05.1; SPBC21C3.05.1:pep; SPBC21C3.05.
DR   GeneID; 2540622; -.
DR   KEGG; spo:SPBC21C3.05; -.
DR   PomBase; SPBC21C3.05; sap62.
DR   VEuPathDB; FungiDB:SPBC21C3.05; -.
DR   eggNOG; KOG0227; Eukaryota.
DR   HOGENOM; CLU_050757_1_0_1; -.
DR   InParanoid; Q9P7L8; -.
DR   OMA; EPYEIIG; -.
DR   PhylomeDB; Q9P7L8; -.
DR   PRO; PR:Q9P7L8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005686; C:U2 snRNP; IDA:PomBase.
DR   GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISS:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000245; P:spliceosomal complex assembly; ISS:PomBase.
DR   InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR031781; SF3A2_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   Pfam; PF16835; SF3A2; 1.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..217
FT                   /note="Pre-mRNA-splicing factor sap62"
FT                   /id="PRO_0000353820"
FT   ZN_FING         54..84
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
SQ   SEQUENCE   217 AA;  24987 MW;  06395BE71B775DAD CRC64;
     MDYQNRAGVR FGGGGVAGYQ ETNAARRERL RKLALETIDL SKDPYLMKNH LGTFECRLCL
     TTHANENSYL THTQGKKHQT NLARRQALEN KKSQENAPQV LLGISQSHVQ VKKSVVKIGR
     PGYKVSKIRE AESGKFGLRF QIKYPDIEVN AKPRYRIMSA YEQRVEAPDR KFQYLVVAAE
     PYESIAFKID RAPGKFWSYW DAPTYTIQFF YNLTKIS
 
 
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