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Database: UniProt
Entry: G1NZH2_MYOLU
LinkDB: G1NZH2_MYOLU
Original site: G1NZH2_MYOLU 
ID   G1NZH2_MYOLU            Unreviewed;       198 AA.
AC   G1NZH2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 1B {ECO:0000256|ARBA:ARBA00014547};
DE   AltName: Full=Cyclin-dependent kinase inhibitor p27 {ECO:0000256|ARBA:ARBA00031925};
DE   AltName: Full=p27Kip1 {ECO:0000256|ARBA:ARBA00031903};
GN   Name=CDKN1B {ECO:0000313|Ensembl:ENSMLUP00000002864.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000002864.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000002864.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000002864.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Endosome {ECO:0000256|ARBA:ARBA00004177}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CDI family. {ECO:0000256|ARBA:ARBA00006726}.
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DR   EMBL; AAPE02007148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006084318.1; XM_006084256.2.
DR   AlphaFoldDB; G1NZH2; -.
DR   STRING; 59463.ENSMLUP00000002864; -.
DR   Ensembl; ENSMLUT00000003150.2; ENSMLUP00000002864.2; ENSMLUG00000003161.2.
DR   GeneID; 102429961; -.
DR   KEGG; mlf:102429961; -.
DR   CTD; 1027; -.
DR   eggNOG; KOG4743; Eukaryota.
DR   GeneTree; ENSGT00940000159852; -.
DR   HOGENOM; CLU_077692_2_0_1; -.
DR   InParanoid; G1NZH2; -.
DR   OMA; THLRDQK; -.
DR   OrthoDB; 4144394at2759; -.
DR   TreeFam; TF101038; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0048102; P:autophagic cell death; IEA:Ensembl.
DR   GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
DR   GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR   GO; GO:1905179; P:negative regulation of cardiac muscle tissue regeneration; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR   GO; GO:0042326; P:negative regulation of phosphorylation; IEA:Ensembl.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0051168; P:nuclear export; IEA:Ensembl.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IEA:Ensembl.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:1902746; P:regulation of lens fiber cell differentiation; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   Gene3D; 4.10.365.10; p27; 1.
DR   InterPro; IPR003175; CDI_dom.
DR   InterPro; IPR044898; CDI_dom_sf.
DR   PANTHER; PTHR10265; CYCLIN-DEPENDENT KINASE INHIBITOR 1; 1.
DR   PANTHER; PTHR10265:SF9; CYCLIN-DEPENDENT KINASE INHIBITOR 1B; 1.
DR   Pfam; PF02234; CDI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein kinase inhibitor {ECO:0000256|ARBA:ARBA00023013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          31..79
FT                   /note="Cyclin-dependent kinase inhibitor"
FT                   /evidence="ECO:0000259|Pfam:PF02234"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  22096 MW;  A1569AE92EB7CEB1 CRC64;
     MSTVRVSNGS PSLERMDARQ AEYPKPSACR NLFGPVDHEE LTRDLEKHCR DMEEASQRKW
     NFDFKNHKPL EGRYEWQEVE KASLPEFYYR APRPPKGACK VPAQESQDVS GSRQAVPLVG
     SQANSEDTHL AEQKTDASDS QPGLAEPCAG MRKRPAADDA SSQNKRTNRT DENVSDGSPN
     AGSVEQTPKK PGLRKRQT
//
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