ID L9KKZ7_TUPCH Unreviewed; 974 AA.
AC L9KKZ7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN ORFNames=TREES_T100014221 {ECO:0000313|EMBL:ELW61817.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW61817.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC kinases and is essential for their biological function.
CC {ECO:0000256|ARBA:ARBA00002449, ECO:0000256|RuleBase:RU311113}.
CC -!- SUBUNIT: Forms a homohexamer that can probably bind six kinase
CC subunits. {ECO:0000256|ARBA:ARBA00011253}.
CC -!- SIMILARITY: Belongs to the CKS family. {ECO:0000256|RuleBase:RU311113}.
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DR EMBL; KB320853; ELW61817.1; -; Genomic_DNA.
DR AlphaFoldDB; L9KKZ7; -.
DR STRING; 246437.L9KKZ7; -.
DR eggNOG; ENOG502QUP4; Eukaryota.
DR InParanoid; L9KKZ7; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.170.10; Cyclin-dependent kinase, regulatory subunit; 1.
DR InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR InterPro; IPR040051; SECISBP2.
DR PANTHER; PTHR13284; GH01354P; 1.
DR PANTHER; PTHR13284:SF9; SELENOCYSTEINE INSERTION SEQUENCE-BINDING PROTEIN 2; 1.
DR Pfam; PF01111; CKS; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00296; CYCLINKINASE.
DR SMART; SM01084; CKS; 1.
DR SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
DR SUPFAM; SSF55315; L30e-like; 1.
DR PROSITE; PS00944; CKS_1; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU311113};
KW Cell division {ECO:0000256|RuleBase:RU311113};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518}.
FT DOMAIN 780..877
FT /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT /evidence="ECO:0000259|Pfam:PF01248"
FT REGION 192..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 106365 MW; D82C9A0103928646 CRC64;
MAHKQIYYSD KYFDEHYEYR HVMLPRELSK QVPKTHLMSE EEWRRLGVQQ SLGWVHYMIH
EPGPELPGVS GAAWAGGSAL GARAGGRDSR TGLGLPGGIK LSADVKPFVP KLSRLNVAWK
ESSEACIFPG CAATYYSFVQ EPPGAEQKIY TEDVAFGASA FPPQYLSSGI TLHPYAFSPY
TLASVPDGGP VPGSQYSYSQ PSGYHGLQAA QPRNEHACPL RQETKALTKK KTYVEKKTCD
EPKLDSARAD GTTSSAIRSS KGSHHLPVEN SLKSDGSKRT DRKSRITAKS GSTSKPEFEF
TRLDFPELQG PEDESISEIR KHPKWGPVPS ASPGISLLGE VGKPPAVLPE TLPTGLSPAP
KNVPSTINVK TVASAADPKS VGMSSSELSS SDPSCSREKH PGHPTKKSKV SQGGDLEQNE
TSRRNKKKKE KSKPKYETLT VQEPPRIEDA EEFPNLAVAS ERRDRVDAPK FQPTQNPQSN
FKNSTKKSQI PVQLDLGGML TALEKKQHSQ HAKQSSKPVV FSVGAVPVLS KEAMSGERGH
RFSQVKTPHN PLDSSAPLMK KGKQREVPKA KKPTSLKKRL QENAASPALA SDGAPDVESG
DDDQVPEAEP TVGAVPVLSK EAMSGERGHR FSQVKTPHNP LDSSAPLMKK GKQREVPKAK
KPTSLKKPHP LFGPGLPFDG PLHEMAPGIC STCHKAAAGP RAVDELASCT PAIEDQPEEP
LGTEQQRDTG AYPLAPEHPG LPKIHSRRFR DYCSQMLSKE VDACVTDLLK ELVRFQDRMY
QKDPVKAKTK RRVVLGLREV LKHLKLKKLK CVIISPNCEK IQSKGGLDDT LHTIIAYACA
QNIPFVFALN RKALGRSLNK AVPVSVVGIF SYDGAQDQFH KMVELTMEAR QAYRSMLESA
RQELAGEPGL QAPPQPPVQG PRASSEGSAP APTGRQEPHC TEVWRERLEA YSQCALELEE
SLEASTSQMM SLNL
//
