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Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)

 CDN1B_HUMAN             Reviewed;         198 AA.
P46527; Q16307; Q5U0H2; Q9BUS6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
17-JUN-2020, entry version 217.
RecName: Full=Cyclin-dependent kinase inhibitor 1B;
AltName: Full=Cyclin-dependent kinase inhibitor p27 {ECO:0000303|PubMed:28666995};
AltName: Full=p27Kip1 {ECO:0000303|PubMed:8033212};
Name=CDKN1B; Synonyms=KIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-79 AND 104-152.
TISSUE=Kidney;
PubMed=8033212; DOI=10.1016/0092-8674(94)90572-x;
Polyak K., Lee M.-H., Erdjument-Bromage H., Koff A., Roberts J.M.,
Tempst P., Massague J.;
"Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential
mediator of extracellular antimitogenic signals.";
Cell 78:59-66(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7882309;
Pietenpol J.A., Bohlander S.K., Sato Y., Papadopoulos N., Liu B.,
Friedman C., Trask B.J., Roberts J.M., Kinzler K.W., Rowley J.D.;
"Assignment of the human p27Kip1 gene to 12p13 and its analysis in
leukemias.";
Cancer Res. 55:1206-1210(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-109.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-15 AND GLY-109.
NIEHS SNPs program;
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-109.
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
UBIQUITINATION, AND PHOSPHORYLATION AT THR-187.
PubMed=10323868; DOI=10.1101/gad.13.9.1181;
Montagnoli A., Fiore F., Eytan E., Carrano A.C., Draetta G.F., Hershko A.,
Pagano M.;
"Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and
trimeric complex formation.";
Genes Dev. 13:1181-1189(1999).
[7]
PHOSPHORYLATION AT SER-10, AND FUNCTION.
PubMed=10831586; DOI=10.1074/jbc.m001144200;
Ishida N., Kitagawa M., Hatakeyama S., Nakayama K.;
"Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1),
increases its protein stability.";
J. Biol. Chem. 275:25146-25154(2000).
[8]
INTERACTION WITH UHMK1, PHOSPHORYLATION AT SER-10, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF SER-10 AND THR-187.
PubMed=12093740; DOI=10.1093/emboj/cdf343;
Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J.,
Nabel E.G.;
"A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and
regulates cell cycle progression.";
EMBO J. 21:3390-3401(2002).
[9]
PHOSPHORYLATION AT SER-10; THR-187 AND THR-198, INTERACTION WITH AKT1 AND
YWHAQ, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-10; THR-157; THR-187
AND THR-198.
PubMed=12042314; DOI=10.1074/jbc.m203668200;
Fujita N., Sato S., Katayama K., Tsuruo T.;
"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and
cytoplasmic localization.";
J. Biol. Chem. 277:28706-28713(2002).
[10]
PHOSPHORYLATION AT THR-157, SUBCELLULAR LOCATION, ASSOCIATION WITH BREAST
CANCER, AND MUTAGENESIS OF THR-157.
PubMed=12244303; DOI=10.1038/nm762;
Viglietto G., Motti M.L., Bruni P., Melillo R.M., D'Alessio A.,
Califano D., Vinci F., Chiappetta G., Tsichlis P., Bellacosa A., Fusco A.,
Santoro M.;
"Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase
inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer.";
Nat. Med. 8:1136-1144(2002).
[11]
PHOSPHORYLATION AT THR-157, INTERACTION WITH AKT1, SUBCELLULAR LOCATION,
FUNCTION, AND MUTAGENESIS OF THR-157; SER-161 AND THR-162.
PubMed=12244301; DOI=10.1038/nm759;
Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J.,
Arteaga C.L.;
"PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at
threonine 157 and modulation of its cellular localization.";
Nat. Med. 8:1145-1152(2002).
[12]
PHOSPHORYLATION AT SER-10 AND THR-198, INTERACTION WITH YWHAE; YWHAH; SFN;
YWHAQ; RPS6KA1 AND RPS6KA3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
THR-157 AND THR-198.
PubMed=14504289; DOI=10.1074/jbc.m306614200;
Fujita N., Sato S., Tsuruo T.;
"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6
kinases promotes its binding to 14-3-3 and cytoplasmic localization.";
J. Biol. Chem. 278:49254-49260(2003).
[13]
INTERACTION WITH SPDYA.
PubMed=12972555; DOI=10.1091/mbc.e02-12-0820;
Porter L.A., Kong-Beltran M., Donoghue D.J.;
"Spy1 interacts with p27Kip1 to allow G1/S progression.";
Mol. Biol. Cell 14:3664-3674(2003).
[14]
PHOSPHORYLATION AT THR-198, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
SER-10; THR-157; THR-187 AND THR-198.
PubMed=15280662;
Motti M.L., De Marco C., Califano D., Fusco A., Viglietto G.;
"Akt-dependent T198 phosphorylation of cyclin-dependent kinase inhibitor
p27kip1 in breast cancer.";
Cell Cycle 3:1074-1080(2004).
[15]
INTERACTION WITH CDK1.
PubMed=16007079; DOI=10.1038/ncb1284;
Aleem E., Kiyokawa H., Kaldis P.;
"Cdc2-cyclin E complexes regulate the G1/S phase transition.";
Nat. Cell Biol. 7:831-836(2005).
[16]
PHOSPHORYLATION AT TYR-88 AND TYR-89, DEPHOSPHORYLATION, INTERACTION WITH
GRB2; CDK2 AND CDK4, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-74;
TYR-88 AND TYR-89.
PubMed=16195327; DOI=10.1182/blood-2005-05-1771;
Kardinal C., Dangers M., Kardinal A., Koch A., Brandt D.T., Tamura T.,
Welte K.;
"Tyrosine phosphorylation modulates binding preference to cyclin-dependent
kinases and subcellular localization of p27Kip1 in the acute promyelocytic
leukemia cell line NB4.";
Blood 107:1133-1140(2006).
[17]
INTERACTION WITH CDK4, AND FUNCTION.
PubMed=16782892; DOI=10.1128/mcb.02006-05;
Bockstaele L., Kooken H., Libert F., Paternot S., Dumont J.E.,
de Launoit Y., Roger P.P., Coulonval K.;
"Regulated activating Thr172 phosphorylation of cyclin-dependent kinase
4(CDK4): its relationship with cyclins and CDK 'inhibitors'.";
Mol. Cell. Biol. 26:5070-5085(2006).
[18]
UBIQUITINATION, AND MUTAGENESIS OF THR-187.
PubMed=16880511; DOI=10.1128/mcb.01630-05;
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
Krek W.;
"Regulation of p27 degradation and S-phase progression by Ro52 RING finger
protein.";
Mol. Cell. Biol. 26:5994-6004(2006).
[19]
INVOLVEMENT IN MEN4.
PubMed=17030811; DOI=10.1073/pnas.0603877103;
Pellegata N.S., Quintanilla-Martinez L., Siggelkow H., Samson E., Bink K.,
Hoefler H., Fend F., Graw J., Atkinson M.J.;
"Germ-line mutations in p27(Kip1) cause a multiple endocrine neoplasia
syndrome in rats and humans.";
Proc. Natl. Acad. Sci. U.S.A. 103:15558-15563(2006).
[20]
PHOSPHORYLATION AT TYR-74 AND TYR-88 BY SRC.
PubMed=17254967; DOI=10.1016/j.cell.2006.11.049;
Chu I., Sun J., Arnaout A., Kahn H., Hanna W., Narod S., Sun P., Tan C.K.,
Hengst L., Slingerland J.;
"p27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2.";
Cell 128:281-294(2007).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[22]
INTERACTION WITH PIM1, AND PHOSPHORYLATION AT THR-157 AND THR-198.
PubMed=18593906; DOI=10.1158/0008-5472.can-08-0634;
Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.;
"Pim kinases promote cell cycle progression by phosphorylating and down-
regulating p27Kip1 at the transcriptional and posttranscriptional levels.";
Cancer Res. 68:5076-5085(2008).
[23]
INTERACTION WITH CDK4, PHOSPHORYLATION, FUNCTION, AND MUTAGENESIS OF
TYR-74; TYR-88 AND TYR-89.
PubMed=19075005; DOI=10.1128/mcb.00898-08;
Ray A., James M.K., Larochelle S., Fisher R.P., Blain S.W.;
"p27Kip1 inhibits cyclin D-cyclin-dependent kinase 4 by two independent
modes.";
Mol. Cell. Biol. 29:986-999(2009).
[24]
DEPHOSPHORYLATION BY PPM1H AT THR-187.
PubMed=22586611; DOI=10.1158/2159-8290.cd-11-0062;
Lee-Hoeflich S.T., Pham T.Q., Dowbenko D., Munroe X., Lee J., Li L.,
Zhou W., Haverty P.M., Pujara K., Stinson J., Chan S.M.,
Eastham-Anderson J., Pandita A., Seshagiri S., Hoeflich K.P.,
Turashvili G., Gelmon K.A., Aparicio S.A., Davis D.P., Sliwkowski M.X.,
Stern H.M.;
"PPM1H is a p27 phosphatase implicated in trastuzumab resistance.";
Cancer Discov. 1:326-337(2011).
[25]
PHOSPHORYLATION AT TYR-88 BY JAK2.
PubMed=21423214; DOI=10.1038/onc.2011.68;
Jakel H., Weinl C., Hengst L.;
"Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor
signaling to cell cycle control.";
Oncogene 30:3502-3512(2011).
[26]
PHOSPHORYLATION AT THR-157 AND THR-198 BY CAMK1.
PubMed=23707388; DOI=10.1016/j.cellsig.2013.05.012;
Mallampalli R.K., Kaercher L., Snavely C., Pulijala R., Chen B.B., Coon T.,
Zhao J., Agassandian M.;
"Fbxl12 triggers G1 arrest by mediating degradation of calmodulin kinase
I.";
Cell. Signal. 25:2047-2059(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION AT THR-187 BY CDK1 AND CDK2.
PubMed=23478441; DOI=10.1016/j.molcel.2013.02.004;
Rossi M., Duan S., Jeong Y.T., Horn M., Saraf A., Florens L.,
Washburn M.P., Antebi A., Pagano M.;
"Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the
SCF(Fbxo11) ubiquitin ligase.";
Mol. Cell 49:1159-1166(2013).
[29]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-106 IN COMPLEX WITH CCNA2 AND
CDK2.
PubMed=8684460; DOI=10.1038/382325a0;
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound
to the cyclin A-Cdk2 complex.";
Nature 382:325-331(1996).
[30]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 181-190 IN COMPLEX WITH SKP1; SKP2
AND CKS1B, PHOSPHORYLATION AT THR-187, MUTAGENESIS OF GLU-185 AND THR-187,
AND UBIQUITINATION.
PubMed=16209941; DOI=10.1016/j.molcel.2005.09.003;
Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M.,
Pavletich N.P.;
"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the
SCF(Skp2) ubiquitin ligase.";
Mol. Cell 20:9-19(2005).
[31]
STRUCTURE BY NMR OF 22-104, PHOSPHORYLATION AT TYR-88, FUNCTION, INDUCTION,
INTERACTION WITH LYN, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
OF TYR-88 AND TYR-89.
PubMed=17254966; DOI=10.1016/j.cell.2006.11.047;
Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.-M., Waddell M.B.,
Jaekel H., Kullmann M., Kriwacki R.W., Hengst L.;
"Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by
oncogenic tyrosine kinases.";
Cell 128:269-280(2007).
[32] {ECO:0000244|PDB:5UQ3}
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN COMPLEX WITH CDK2 AND SPDYA,
FUNCTION, AND SUBUNIT.
PubMed=28666995; DOI=10.15252/embj.201796905;
McGrath D.A., Fifield B.A., Marceau A.H., Tripathi S., Porter L.A.,
Rubin S.M.;
"Structural basis of divergent cyclin-dependent kinase activation by
Spy1/RINGO proteins.";
EMBO J. 36:2251-2262(2017).
[33]
VARIANT LEU-69, AND CHARACTERIZATION OF VARIANT LEU-69.
PubMed=20824794; DOI=10.1002/humu.21354;
Molatore S., Marinoni I., Lee M., Pulz E., Ambrosio M.R.,
degli Uberti E.C., Zatelli M.C., Pellegata N.S.;
"A novel germline CDKN1B mutation causing multiple endocrine tumors:
clinical, genetic and functional characterization.";
Hum. Mutat. 31:E1825-E1835(2010).
-!- FUNCTION: Important regulator of cell cycle progression. Inhibits the
kinase activity of CDK2 bound to cyclin A, but has little inhibitory
activity on CDK2 bound to SPDYA (PubMed:28666995). Involved in G1
arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes.
Forms a complex with cyclin type D-CDK4 complexes and is involved in
the assembly, stability, and modulation of CCND1-CDK4 complex
activation. Acts either as an inhibitor or an activator of cyclin type
D-CDK4 complexes depending on its phosphorylation state and/or
stoichometry. {ECO:0000269|PubMed:10831586,
ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:16782892,
ECO:0000269|PubMed:17254966, ECO:0000269|PubMed:19075005,
ECO:0000269|PubMed:28666995}.
-!- SUBUNIT: Forms a ternary complex composed of CCNE1, CDK2 and CDKN1B.
Interacts directly with CCNE1; the interaction is inhibited by CDK2-
dependent phosphorylation on Thr-187. Interacts with COPS5, subunit of
the COP9 signalosome complex; the interaction leads to CDKN1B
degradation. Interacts with NUP50; the interaction leads to nuclear
import and degradation of phosphorylated CDKN1B. Interacts with CCND1
and SNX6 (By similarity). Interacts (Thr-198-phosphorylated form) with
14-3-3 proteins, binds strongly YWHAQ, weakly YWHAE and YWHAH, but not
YWHAB nor YWHAZ; the interaction with YWHAQ results in translocation to
the cytoplasm (PubMed:14504289). Interacts with AKT1 and LYN; the
interactions lead to cytoplasmic mislocation, phosphorylation of CDKN1B
and inhibition of cell cycle arrest (PubMed:12042314, PubMed:12244301,
PubMed:17254966). Forms a ternary complex with CCNA2 and CDK2; CDKN1B
inhibits the kinase activity of CDK2 through conformational
rearrangements. Interacts (unphosphorylated form) with CDK2. Forms a
complex with CDK2 and SPDYA, but does not directly interact with SPDYA
(PubMed:12972555, PubMed:28666995). Forms a ternary complex composed of
cyclin D, CDK4 and CDKN1B. Interacts (phosphorylated on Tyr-88 and Tyr-
89) with CDK4; the interaction is required for cyclin D and CDK4
complex assembly, induces nuclear translocation and activates the CDK4
kinase activity. Interacts with GRB2 (PubMed:16195327). Interacts with
PIM1 (PubMed:18593906). Identified in a complex with SKP1, SKP2 and
CKS1B (PubMed:16209941). Interacts with UHMK1; the interaction leads to
cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of
cell cycle arrest (PubMed:12093740). Interacts also with CDK1
(PubMed:16007079). Dephosphorylated on Thr-187 by PPM1H, leading to
CDKN1B stability (PubMed:22586611). {ECO:0000250,
ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:12972555,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:16007079,
ECO:0000269|PubMed:16195327, ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:16782892, ECO:0000269|PubMed:17254966,
ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:19075005,
ECO:0000269|PubMed:22586611, ECO:0000269|PubMed:28666995,
ECO:0000269|PubMed:8684460}.
-!- INTERACTION:
P46527; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-519280, EBI-11524452;
P46527; P78396: CCNA1; NbExp=5; IntAct=EBI-519280, EBI-375065;
P46527; P20248: CCNA2; NbExp=17; IntAct=EBI-519280, EBI-457097;
P46527; P14635: CCNB1; NbExp=2; IntAct=EBI-519280, EBI-495332;
P46527; P24385: CCND1; NbExp=4; IntAct=EBI-519280, EBI-375001;
P46527; P30279: CCND2; NbExp=6; IntAct=EBI-519280, EBI-748789;
P46527; P24864: CCNE1; NbExp=8; IntAct=EBI-519280, EBI-519526;
P46527; O96020: CCNE2; NbExp=3; IntAct=EBI-519280, EBI-375033;
P46527; P24941: CDK2; NbExp=25; IntAct=EBI-519280, EBI-375096;
P46527; P11802: CDK4; NbExp=7; IntAct=EBI-519280, EBI-295644;
P46527; Q00535: CDK5; NbExp=8; IntAct=EBI-519280, EBI-1041567;
P46527; Q00534: CDK6; NbExp=2; IntAct=EBI-519280, EBI-295663;
P46527; O15111: CHUK; NbExp=4; IntAct=EBI-519280, EBI-81249;
P46527; Q92905: COPS5; NbExp=3; IntAct=EBI-519280, EBI-594661;
P46527; Q13616: CUL1; NbExp=2; IntAct=EBI-519280, EBI-359390;
P46527; O00505: KPNA3; NbExp=4; IntAct=EBI-519280, EBI-358297;
P46527; O15131: KPNA5; NbExp=6; IntAct=EBI-519280, EBI-540602;
P46527; P07948: LYN; NbExp=2; IntAct=EBI-519280, EBI-79452;
P46527; P33993: MCM7; NbExp=2; IntAct=EBI-519280, EBI-355924;
P46527; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-519280, EBI-11522433;
P46527; P11309-1: PIM1; NbExp=2; IntAct=EBI-519280, EBI-1018629;
P46527; P61586: RHOA; NbExp=3; IntAct=EBI-519280, EBI-446668;
P46527; Q15418: RPS6KA1; NbExp=2; IntAct=EBI-519280, EBI-963034;
P46527; Q9UQR0-1: SCML2; NbExp=2; IntAct=EBI-519280, EBI-16087037;
P46527; Q13309: SKP2; NbExp=4; IntAct=EBI-519280, EBI-456291;
P46527; Q5MJ70: SPDYA; NbExp=3; IntAct=EBI-519280, EBI-7125479;
P46527; P16949: STMN1; NbExp=3; IntAct=EBI-519280, EBI-445909;
P46527; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-519280, EBI-741515;
P46527; Q12933: TRAF2; NbExp=6; IntAct=EBI-519280, EBI-355744;
P46527; P00520: Abl1; Xeno; NbExp=2; IntAct=EBI-519280, EBI-914519;
P46527; Q62120: Jak2; Xeno; NbExp=7; IntAct=EBI-519280, EBI-646604;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endosome {ECO:0000250}.
Note=Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated
phosphorylation on Thr-198, binds 14-3-3, translocates to the cytoplasm
and promotes cell cycle progression. Mitogen-activated UHMK1
phosphorylation on Ser-10 also results in translocation to the
cytoplasm and cell cycle progression. Phosphorylation on Ser-10
facilitates nuclear export. Translocates to the nucleus on
phosphorylation of Tyr-88 and Tyr-89. Colocalizes at the endosome with
SNX6; this leads to lysosomal degradation (By similarity).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highest levels in
skeletal muscle, lowest in liver and kidney.
-!- INDUCTION: Maximal levels in quiescence cells and early G(1). Levels
decrease after mitogen stimulation as cells progress toward S-phase.
{ECO:0000269|PubMed:17254966}.
-!- DOMAIN: A peptide sequence containing only AA 28-79 retains substantial
Kip1 cyclin A/CDK2 inhibitory activity.
-!- PTM: Phosphorylated; phosphorylation occurs on serine, threonine and
tyrosine residues. Phosphorylation on Ser-10 is the major site of
phosphorylation in resting cells, takes place at the G(0)-G(1) phase
and leads to protein stability. Phosphorylation on other sites is
greatly enhanced by mitogens, growth factors, cMYC and in certain
cancer cell lines. The phosphorylated form found in the cytoplasm is
inactivate. Phosphorylation on Thr-198 is required for interaction with
14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to
protein ubiquitination and proteasomal degradation. Tyrosine
phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can
be suppressed by LY294002, an inhibitor of the catalytic subunit of
PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding
CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine
residues by G-CSF. {ECO:0000269|PubMed:10323868,
ECO:0000269|PubMed:10831586, ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:14504289,
ECO:0000269|PubMed:15280662, ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:16209941, ECO:0000269|PubMed:17254966,
ECO:0000269|PubMed:17254967, ECO:0000269|PubMed:18593906,
ECO:0000269|PubMed:21423214, ECO:0000269|PubMed:23478441,
ECO:0000269|PubMed:23707388}.
-!- PTM: Ubiquitinated; in the cytoplasm by the KPC complex (composed of
RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The
latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a
TRIM21-containing SCF(SKP2)-like complex; leads to its degradation.
{ECO:0000269|PubMed:10323868, ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:16209941, ECO:0000269|PubMed:23478441}.
-!- PTM: Subject to degradation in the lysosome. Interaction with SNX6
promotes lysosomal degradation (By similarity). {ECO:0000250}.
-!- DISEASE: Multiple endocrine neoplasia 4 (MEN4) [MIM:610755]: Multiple
endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of
the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of
both MEN1 and MEN2. {ECO:0000269|PubMed:17030811}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Decreased levels of p27Kip1, mainly due to proteasomal
degradation, are found in various epithelial tumors originating from
lung, breast, colon, ovary, esophagus, thyroid and prostate.
-!- SIMILARITY: Belongs to the CDI family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDKN1BID116.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdkn1b/";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; U10906; AAA20240.1; -; mRNA.
EMBL; S76988; AAD14244.1; -; Genomic_DNA.
EMBL; S76986; AAD14244.1; JOINED; Genomic_DNA.
EMBL; BT019553; AAV38360.1; -; mRNA.
EMBL; BT019554; AAV38361.1; -; mRNA.
EMBL; AF480891; AAL78041.1; -; Genomic_DNA.
EMBL; BC001971; AAH01971.1; -; mRNA.
CCDS; CCDS8653.1; -.
RefSeq; NP_004055.1; NM_004064.4.
PDB; 1H27; X-ray; 2.20 A; E=25-35.
PDB; 1JSU; X-ray; 2.30 A; C=23-106.
PDB; 2AST; X-ray; 2.30 A; D=181-190.
PDB; 5UQ3; X-ray; 3.60 A; C=1-198.
PDB; 6ATH; X-ray; 1.82 A; C=22-85.
PDB; 6P8E; X-ray; 2.30 A; C=25-93.
PDB; 6P8F; X-ray; 2.89 A; C=25-106.
PDB; 6P8G; X-ray; 2.80 A; C=25-93.
PDBsum; 1H27; -.
PDBsum; 1JSU; -.
PDBsum; 2AST; -.
PDBsum; 5UQ3; -.
PDBsum; 6ATH; -.
PDBsum; 6P8E; -.
PDBsum; 6P8F; -.
PDBsum; 6P8G; -.
SMR; P46527; -.
BioGRID; 107461; 98.
CORUM; P46527; -.
DIP; DIP-33341N; -.
IntAct; P46527; 72.
MINT; P46527; -.
STRING; 9606.ENSP00000228872; -.
ChEMBL; CHEMBL3758070; -.
MoonDB; P46527; Predicted.
iPTMnet; P46527; -.
PhosphoSitePlus; P46527; -.
BioMuta; CDKN1B; -.
SWISS-2DPAGE; P46527; -.
CPTAC; CPTAC-1237; -.
CPTAC; CPTAC-1238; -.
EPD; P46527; -.
jPOST; P46527; -.
MassIVE; P46527; -.
PaxDb; P46527; -.
PeptideAtlas; P46527; -.
PRIDE; P46527; -.
ProteomicsDB; 55741; -.
TopDownProteomics; P46527; -.
Antibodypedia; 3295; 2570 antibodies.
DNASU; 1027; -.
Ensembl; ENST00000228872; ENSP00000228872; ENSG00000111276.
GeneID; 1027; -.
KEGG; hsa:1027; -.
CTD; 1027; -.
DisGeNET; 1027; -.
EuPathDB; HostDB:ENSG00000111276.10; -.
GeneCards; CDKN1B; -.
HGNC; HGNC:1785; CDKN1B.
HPA; ENSG00000111276; Low tissue specificity.
MalaCards; CDKN1B; -.
MIM; 600778; gene.
MIM; 610755; phenotype.
neXtProt; NX_P46527; -.
OpenTargets; ENSG00000111276; -.
Orphanet; 652; Multiple endocrine neoplasia type 1.
Orphanet; 276152; Multiple endocrine neoplasia type 4.
PharmGKB; PA105; -.
eggNOG; KOG4743; Eukaryota.
eggNOG; ENOG410XXN5; LUCA.
GeneTree; ENSGT00940000159852; -.
HOGENOM; CLU_077692_2_0_1; -.
InParanoid; P46527; -.
KO; K06624; -.
OMA; EGRYEWQ; -.
OrthoDB; 1595421at2759; -.
PhylomeDB; P46527; -.
TreeFam; TF101038; -.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-8849470; PTK6 Regulates Cell Cycle.
Reactome; R-HSA-9617828; FOXO-mediated transcription of cell cycle genes.
Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
SIGNOR; P46527; -.
BioGRID-ORCS; 1027; 5 hits in 793 CRISPR screens.
ChiTaRS; CDKN1B; human.
EvolutionaryTrace; P46527; -.
GeneWiki; CDKN1B; -.
GenomeRNAi; 1027; -.
Pharos; P46527; Tbio.
PRO; PR:P46527; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; P46527; protein.
Bgee; ENSG00000111276; Expressed in pigmented layer of retina and 242 other tissues.
ExpressionAtlas; P46527; baseline and differential.
Genevisible; P46527; HS.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
GO; GO:0030332; F:cyclin binding; IPI:CAFA.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
GO; GO:0004860; F:protein kinase inhibitor activity; IMP:CAFA.
GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
GO; GO:0044877; F:protein-containing complex binding; IPI:CAFA.
GO; GO:0048102; P:autophagic cell death; IDA:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; IMP:HGNC-UCL.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:1905179; P:negative regulation of cardiac muscle tissue regeneration; ISS:BHF-UCL.
GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
GO; GO:0051271; P:negative regulation of cellular component movement; IEA:Ensembl.
GO; GO:1904030; P:negative regulation of cyclin-dependent protein kinase activity; IMP:CAFA.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0033673; P:negative regulation of kinase activity; IDA:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0042326; P:negative regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0045787; P:positive regulation of cell cycle; TAS:Reactome.
GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:GO_Central.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:GO_Central.
GO; GO:0007096; P:regulation of exit from mitosis; IEA:Ensembl.
GO; GO:1902746; P:regulation of lens fiber cell differentiation; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DisProt; DP00018; -.
IDEAL; IID00049; -.
InterPro; IPR003175; CDI.
InterPro; IPR029843; CDKN1B.
PANTHER; PTHR10265:SF9; PTHR10265:SF9; 1.
Pfam; PF02234; CDI; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cytoplasm; Direct protein sequencing; Endosome;
Nucleus; Phosphoprotein; Polymorphism; Protein kinase inhibitor;
Reference proteome; Tumor suppressor; Ubl conjugation.
CHAIN 1..198
/note="Cyclin-dependent kinase inhibitor 1B"
/id="PRO_0000190084"
REGION 51..91
/note="Interaction with CDK2"
/evidence="ECO:0000269|PubMed:28666995"
MOTIF 153..169
/note="Nuclear localization signal"
/evidence="ECO:0000255"
MOD_RES 10
/note="Phosphoserine; by UHMK1"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10831586, ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:14504289"
MOD_RES 74
/note="Phosphotyrosine; by SRC"
/evidence="ECO:0000269|PubMed:17254967"
MOD_RES 88
/note="Phosphotyrosine; by ABL, LYN, SRC and JAK2"
/evidence="ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:17254966, ECO:0000269|PubMed:17254967,
ECO:0000269|PubMed:21423214"
MOD_RES 89
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:16195327"
MOD_RES 157
/note="Phosphothreonine; by CaMK1, PKB/AKT1 and PIM1"
/evidence="ECO:0000269|PubMed:12244301,
ECO:0000269|PubMed:12244303, ECO:0000269|PubMed:18593906,
ECO:0000269|PubMed:23707388"
MOD_RES 170
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P46414"
MOD_RES 187
/note="Phosphothreonine; by PKB/AKT1, CDK1 and CDK2"
/evidence="ECO:0000269|PubMed:10323868,
ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:23478441"
MOD_RES 198
/note="Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1,
RPS6KA3 and PIM1"
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15280662,
ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:23707388"
VARIANT 15
/note="R -> W (in dbSNP:rs2066828)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_011871"
VARIANT 69
/note="P -> L (found in a patient with multiple endocrine
tumors; germline mutation; reduced expression levels; shows
impaired binding to CDK2; dbSNP:rs777354267)"
/evidence="ECO:0000269|PubMed:20824794"
/id="VAR_064429"
VARIANT 109
/note="V -> G (in dbSNP:rs2066827)"
/evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
ECO:0000269|Ref.4"
/id="VAR_011872"
MUTAGEN 10
/note="S->A: Loss of phosphorylation by UHMK1. No
translocation to the cytoplasm. Greater cell cycle arrest."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15280662"
MUTAGEN 10
/note="S->D: Exported to the cytoplasm. Inhibits cell cycle
arrest."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15280662"
MUTAGEN 10
/note="S->E: Increased stability in vivo and in vitro."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15280662"
MUTAGEN 74
/note="Y->F: No change in binding CDK4 and no inhibition of
CDK4 activity. Translocates to nucleus. No effect on in
vitro phosphorylation of CDK4 by CCNH-CDK7."
/evidence="ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:19075005"
MUTAGEN 88
/note="Y->F: Abolishes LYN-mediated phosphorylation,
reduces CDK2-mediated phosphorylation on T-187, has greater
cell cycle arrest into S-phase, no effect on binding CDK2
complexes, reduced CDK4 binding and inhibits CDK4 enzyme
activity. No nuclear translocation. No effect on in vitro
phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes
CDK4 binding; when associated with F-89."
/evidence="ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:17254966, ECO:0000269|PubMed:19075005"
MUTAGEN 89
/note="Y->F: No effect on binding CDK2 complexes, reduced
CDK4 binding and greatly inhibits CDK4 enzyme activity. No
nuclear translocation. Inhibits in vitro phosphorylation of
CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when
associated with F-88."
/evidence="ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:17254966, ECO:0000269|PubMed:19075005"
MUTAGEN 157
/note="T->A: Greatly reduced PKB/AKT1-mediated
phosphorylation. Nuclear location. Inhibits cyclin E/CDK2
cell cycle progression. No effect on binding AKT1.
Completely abolishes PKB/AKT1-mediated phosphorylation and
no cytoplasmic translocation; when associated with A-198."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12244301, ECO:0000269|PubMed:12244303,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15280662"
MUTAGEN 161
/note="S->A: No change in PKB/AKT1-mediated
phosphorylation."
/evidence="ECO:0000269|PubMed:12244301"
MUTAGEN 162
/note="T->A: No change in PKB/AKT1-mediated
phosphorylation."
/evidence="ECO:0000269|PubMed:12244301"
MUTAGEN 185
/note="E->A,D,Q: Strongly reduced ubiquitination by a
TRIM21-containing SCF(SKP2) complex."
/evidence="ECO:0000269|PubMed:16209941"
MUTAGEN 187
/note="T->A,D: No change in PKB/AKT1- nor UHMK1-mediated
phosphorylation."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15280662,
ECO:0000269|PubMed:16209941, ECO:0000269|PubMed:16880511"
MUTAGEN 187
/note="T->A: Abolishes phosphorylation-dependent
ubiquitination."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15280662,
ECO:0000269|PubMed:16209941, ECO:0000269|PubMed:16880511"
MUTAGEN 198
/note="T->A,D: Abolishes PKB/AKT1-mediated phosphorylation.
46% cytoplasmic location. Greatly reduced binding to YWHAQ.
Equally reduced binding; when associated with A-10 and A-
187. No nuclear import; when associated with A-157.
Completely abolishes PKB/AKT1-mediated phosphorylation and
no cytoplasmic translocation; when associated with A-157."
/evidence="ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:15280662"
CONFLICT 22
/note="E -> D (in Ref. 2; AAD14244)"
/evidence="ECO:0000305"
HELIX 38..47
/evidence="ECO:0000244|PDB:6ATH"
TURN 50..53
/evidence="ECO:0000244|PDB:1JSU"
HELIX 55..60
/evidence="ECO:0000244|PDB:6ATH"
TURN 64..67
/evidence="ECO:0000244|PDB:6ATH"
STRAND 71..78
/evidence="ECO:0000244|PDB:6ATH"
HELIX 86..89
/evidence="ECO:0000244|PDB:1JSU"
SEQUENCE 198 AA; 22073 MW; 1118D58901CDF3FC CRC64;
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVDHEE LTRDLEKHCR DMEEASQRKW
NFDFQNHKPL EGKYEWQEVE KGSLPEFYYR PPRPPKGACK VPAQESQDVS GSRPAAPLIG
APANSEDTHL VDPKTDPSDS QTGLAEQCAG IRKRPATDDS STQNKRANRT EENVSDGSPN
AGSVEQTPKK PGLRRRQT


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1619: Amino sugar and nucleotide sugar metabolism
WP1033: ACE Inhibitor Pathway
WP710: DNA damage response (only ATM dependent)
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2361: Gastric cancer network 1
WP1625: Base excision repair
WP1676: Non-homologous end-joining
WP396: ACE Inhibitor Pathway
WP557: ACE Inhibitor Pathway
WP1701: Starch and sucrose metabolism
WP1946: Cori Cycle
WP656: p53 signal pathway
WP1403: AMPK signaling
WP915: ACE Inhibitor Pathway
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1672: Mismatch repair
WP32: Translation Factors
WP554: ACE Inhibitor Pathway
WP1681: Pantothenate and CoA biosynthesis
WP1844: MAP kinase cascade
WP655: p53 pathway
WP801: ACE Inhibitor Pathway
WP215: noncanonical wnt pathway

Related Genes :
[CDKN1B KIP1] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[Cdkn1b] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[CDKN1B KIP1] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[CDKN1B] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) (Fragment)
[CDKN1B KIP1] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[CDKN1B KIP1] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[CDKN1A CIP1 WAF1] Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (p21)
[LAMTOR1 C11orf59 PDRO PP7157] Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18) (Protein associated with DRMs and endosomes) (p27Kip1-releasing factor from RhoA) (p27RF-Rho)
[CDK2 CDKN2] Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2) (p33 protein kinase)
[CDKN1A CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1] Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein 6) (MDA-6) (p21)
[CDK4] Cyclin-dependent kinase 4 (EC 2.7.11.22) (Cell division protein kinase 4) (PSK-J3)
[Cdkn1a Cip1 Waf1] Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein) (p21)
[CDKN2A CDKN2 MTS1] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (Multiple tumor suppressor 1) (MTS-1) (p16-INK4a) (p16-INK4) (p16INK4A)
[CDKN1C KIP2] Cyclin-dependent kinase inhibitor 1C (Cyclin-dependent kinase inhibitor p57) (p57Kip2)
[Cdkn2a P16ink4a] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16-INK4)
[Cdkn2a P16ink4a] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16) (p16-INK4)
[CCND1 BCL1 PRAD1] G1/S-specific cyclin-D1 (B-cell lymphoma 1 protein) (BCL-1) (BCL-1 oncogene) (PRAD1 oncogene)
[CDKN3 CDI1 CIP2 KAP] Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase)
[CCNA2 CCN1 CCNA] Cyclin-A2 (Cyclin-A) (Cyclin A)
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)
[CDKN2A CDKN2 MLM] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p14ARF)
[KRP1 ICK1 At2g23430 F26B6.8] Cyclin-dependent kinase inhibitor 1 (Inhibitor/interactor of CDK protein 1) (KIP-related protein 1)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Rps6ka3 Mapkapk1b Rps6ka-rs1 Rsk2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[cdk1-b cdc2 cdc2x1.2] Cyclin-dependent kinase 1-B (CDK1-B) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 2) (Cell division control protein 2-B) (Cell division protein kinase 1) (p34 protein kinase 2)
[CDKN2B MTS2] Cyclin-dependent kinase 4 inhibitor B (Multiple tumor suppressor 2) (MTS-2) (p14-INK4b) (p15-INK4b) (p15INK4B)
[Cdkn2b Ink4] Cyclin-dependent kinase 4 inhibitor B (p14-INK4b) (p15-INK4b)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

Bibliography :
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