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CSK2B_NEUCR
ID   CSK2B_NEUCR             Reviewed;         333 AA.
AC   Q8TG12; Q7S6V4;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Casein kinase II subunit beta-1;
DE            Short=CK II beta-1;
GN   Name=ckb-1; Synonyms=ckb1; ORFNames=NCU05485;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11959847; DOI=10.1101/gad.965102;
RA   Yang Y., Cheng P., Liu Y.;
RT   "Regulation of the Neurospora circadian clock by casein kinase II.";
RL   Genes Dev. 16:994-1006(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Regulatory subunit of casein kinase II/CK2 (By similarity).
CC       As part of the kinase complex regulates the basal catalytic activity of
CC       the alpha subunit a constitutively active serine/threonine-protein
CC       kinase that phosphorylates a large number of substrates containing
CC       acidic residues C-terminal to the phosphorylated serine or threonine
CC       (By similarity). {ECO:0000250|UniProtKB:P67870}.
CC   -!- SUBUNIT: Tetramer composed of two alpha chains, one beta chain and one
CC       beta' chain. {ECO:0000250|UniProtKB:P43639}.
CC   -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}.
CC   -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AF494377; AAM14625.1; -; mRNA.
DR   EMBL; CM002241; EAA31211.1; -; Genomic_DNA.
DR   RefSeq; XP_960447.1; XM_955354.3.
DR   AlphaFoldDB; Q8TG12; -.
DR   SMR; Q8TG12; -.
DR   STRING; 5141.EFNCRP00000005501; -.
DR   EnsemblFungi; EAA31211; EAA31211; NCU05485.
DR   GeneID; 3876626; -.
DR   KEGG; ncr:NCU05485; -.
DR   VEuPathDB; FungiDB:NCU05485; -.
DR   HOGENOM; CLU_034027_1_1_1; -.
DR   InParanoid; Q8TG12; -.
DR   OMA; YTILDYQ; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0032545; C:CURI complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0034456; C:UTP-C complex; IBA:GO_Central.
DR   GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:EnsemblFungi.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:EnsemblFungi.
DR   GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IEA:EnsemblFungi.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IEA:EnsemblFungi.
DR   GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IBA:GO_Central.
DR   Gene3D; 1.10.1820.10; -; 1.
DR   InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR   InterPro; IPR035991; Casein_kinase_II_beta-like.
DR   InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR   PANTHER; PTHR11740; PTHR11740; 1.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; SSF57798; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..333
FT                   /note="Casein kinase II subunit beta-1"
FT                   /id="PRO_0000068253"
FT   REGION          58..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..78
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   333 AA;  37107 MW;  1744C2D1F7E1D67C CRC64;
     MSSSSGVPES WIASFCSLLG HEYFAEVSEE FIEDDFNLTG LQTQVAMYKE ALEMILDVEP
     EDDDDEEEED EEDEEDMSGG DGINKPHGER RHHSRIASDL SVIESSAEML YGLIHQRFIC
     SRAGIQQMSE KYELGHFGIC PRTNCNQTRT LPVGLSDTPG EDTVKLFCPS CLDVYVPPNS
     RFQTVDGAFF GRTFGALFLM TFPEYDLTKT GAESVSNLTR SGSDDTTVIN GMYARNIAPG
     LGRGKIYQPK IYGFKVSEIA RSGPRMQWLR SKPDDLSVLD EARRYAEQQG SDDEDESMGV
     SSRTASRRRG PPRRQKQNGS PMAIEQNGAE SEL
 
 
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