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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.
12-SEP-2018, entry version 203.
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:
P00520:Abl1 (xeno); NbExp=2; IntAct=EBI-519280, EBI-914519;
Q8N9N5-2:BANP; NbExp=3; IntAct=EBI-519280, EBI-11524452;
P20248:CCNA2; NbExp=15; IntAct=EBI-519280, EBI-457097;
P14635:CCNB1; NbExp=2; IntAct=EBI-519280, EBI-495332;
P24385:CCND1; NbExp=3; IntAct=EBI-519280, EBI-375001;
P30279:CCND2; NbExp=5; IntAct=EBI-519280, EBI-748789;
P24864:CCNE1; NbExp=8; IntAct=EBI-519280, EBI-519526;
O96020:CCNE2; NbExp=3; IntAct=EBI-519280, EBI-375033;
P24941:CDK2; NbExp=23; IntAct=EBI-519280, EBI-375096;
P11802:CDK4; NbExp=6; IntAct=EBI-519280, EBI-295644;
Q00535:CDK5; NbExp=7; IntAct=EBI-519280, EBI-1041567;
O15111:CHUK; NbExp=4; IntAct=EBI-519280, EBI-81249;
Q92905:COPS5; NbExp=3; IntAct=EBI-519280, EBI-594661;
Q13616:CUL1; NbExp=2; IntAct=EBI-519280, EBI-359390;
Q62120:Jak2 (xeno); NbExp=7; IntAct=EBI-519280, EBI-646604;
O00505:KPNA3; NbExp=4; IntAct=EBI-519280, EBI-358297;
O15131:KPNA5; NbExp=6; IntAct=EBI-519280, EBI-540602;
P07948:LYN; NbExp=2; IntAct=EBI-519280, EBI-79452;
P33993:MCM7; NbExp=2; IntAct=EBI-519280, EBI-355924;
P11309:PIM1; NbExp=2; IntAct=EBI-519280, EBI-696621;
P61586:RHOA; NbExp=3; IntAct=EBI-519280, EBI-446668;
Q15418:RPS6KA1; NbExp=2; IntAct=EBI-519280, EBI-963034;
Q9UQR0-1:SCML2; NbExp=2; IntAct=EBI-519280, EBI-16087037;
Q13309:SKP2; NbExp=4; IntAct=EBI-519280, EBI-456291;
P16949:STMN1; NbExp=3; IntAct=EBI-519280, EBI-445909;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-519280, EBI-741515;
Q12933:TRAF2; NbExp=5; IntAct=EBI-519280, EBI-355744;
-!- 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.
UniGene; Hs.238990; -.
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.
PDBsum; 1H27; -.
PDBsum; 1JSU; -.
PDBsum; 2AST; -.
PDBsum; 5UQ3; -.
DisProt; DP00018; -.
ProteinModelPortal; P46527; -.
SMR; P46527; -.
BioGrid; 107461; 88.
CORUM; P46527; -.
DIP; DIP-33341N; -.
IntAct; P46527; 68.
MINT; P46527; -.
STRING; 9606.ENSP00000228872; -.
MoonDB; P46527; Predicted.
iPTMnet; P46527; -.
PhosphoSitePlus; P46527; -.
BioMuta; CDKN1B; -.
SWISS-2DPAGE; P46527; -.
EPD; P46527; -.
PaxDb; P46527; -.
PeptideAtlas; P46527; -.
PRIDE; P46527; -.
ProteomicsDB; 55741; -.
TopDownProteomics; P46527; -.
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; CAB003691; -.
HPA; CAB021888; -.
HPA; HPA059086; -.
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; ENSGT00530000063588; -.
HOGENOM; HOG000294081; -.
HOVERGEN; HBG073988; -.
InParanoid; P46527; -.
KO; K06624; -.
OMA; YPKPSAC; -.
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.
SIGNOR; P46527; -.
ChiTaRS; CDKN1B; human.
EvolutionaryTrace; P46527; -.
GeneWiki; CDKN1B; -.
GenomeRNAi; 1027; -.
PMAP-CutDB; P46527; -.
PRO; PR:P46527; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111276; Expressed in 243 organ(s), highest expression level in pigmented layer of retina.
CleanEx; HS_CDKN1B; -.
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.
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; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0030332; F:cyclin binding; IPI:CAFA.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; EXP:Reactome.
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:0005072; F:transforming growth factor beta receptor, cytoplasmic mediator activity; TAS:ProtInc.
GO; GO:0048102; P:autophagic cell death; IDA:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; IMP:HGNC.
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: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: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 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 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:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
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.
InterPro; IPR003175; CDI.
InterPro; IPR029843; CDKN1B.
PANTHER; PTHR10265; PTHR10265; 1.
PANTHER; PTHR10265:SF9; PTHR10265:SF9; 1.
Pfam; PF02234; CDI; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Complete proteome; Cytoplasm;
Direct protein sequencing; Endosome; Nucleus; Phosphoprotein;
Polymorphism; Protein kinase inhibitor; Reference proteome;
Tumor suppressor; Ubl conjugation.
CHAIN 1 198 Cyclin-dependent kinase inhibitor 1B.
/FTId=PRO_0000190084.
REGION 51 91 Interaction with CDK2.
{ECO:0000269|PubMed:28666995}.
MOTIF 153 169 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 10 10 Phosphoserine; by UHMK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10831586,
ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:14504289}.
MOD_RES 74 74 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:17254967}.
MOD_RES 88 88 Phosphotyrosine; by ABL, LYN, SRC and
JAK2. {ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:17254966,
ECO:0000269|PubMed:17254967,
ECO:0000269|PubMed:21423214}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000269|PubMed:16195327}.
MOD_RES 157 157 Phosphothreonine; by CaMK1, PKB/AKT1 and
PIM1. {ECO:0000269|PubMed:12244301,
ECO:0000269|PubMed:12244303,
ECO:0000269|PubMed:18593906,
ECO:0000269|PubMed:23707388}.
MOD_RES 170 170 Phosphothreonine.
{ECO:0000250|UniProtKB:P46414}.
MOD_RES 187 187 Phosphothreonine; by PKB/AKT1, CDK1 and
CDK2. {ECO:0000269|PubMed:10323868,
ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:23478441}.
MOD_RES 198 198 Phosphothreonine; by CaMK1, PKB/AKT1,
RPS6KA1, RPS6KA3 and PIM1.
{ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:14504289,
ECO:0000269|PubMed:15280662,
ECO:0000269|PubMed:18593906,
ECO:0000269|PubMed:23707388}.
VARIANT 15 15 R -> W (in dbSNP:rs2066828).
{ECO:0000269|Ref.4}.
/FTId=VAR_011871.
VARIANT 69 69 P -> L (found in a patient with multiple
endocrine tumors; germline mutation;
reduced expression levels; shows impaired
binding to CDK2; dbSNP:rs777354267).
{ECO:0000269|PubMed:20824794}.
/FTId=VAR_064429.
VARIANT 109 109 V -> G (in dbSNP:rs2066827).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
/FTId=VAR_011872.
MUTAGEN 10 10 S->A: Loss of phosphorylation by UHMK1.
No translocation to the cytoplasm.
Greater cell cycle arrest.
{ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:15280662}.
MUTAGEN 10 10 S->D: Exported to the cytoplasm. Inhibits
cell cycle arrest.
{ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:15280662}.
MUTAGEN 10 10 S->E: Increased stability in vivo and in
vitro. {ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:15280662}.
MUTAGEN 74 74 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.
{ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:19075005}.
MUTAGEN 88 88 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.
{ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:17254966,
ECO:0000269|PubMed:19075005}.
MUTAGEN 89 89 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.
{ECO:0000269|PubMed:16195327,
ECO:0000269|PubMed:17254966,
ECO:0000269|PubMed:19075005}.
MUTAGEN 157 157 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. {ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12244301,
ECO:0000269|PubMed:12244303,
ECO:0000269|PubMed:14504289,
ECO:0000269|PubMed:15280662}.
MUTAGEN 161 161 S->A: No change in PKB/AKT1-mediated
phosphorylation.
{ECO:0000269|PubMed:12244301}.
MUTAGEN 162 162 T->A: No change in PKB/AKT1-mediated
phosphorylation.
{ECO:0000269|PubMed:12244301}.
MUTAGEN 185 185 E->A,D,Q: Strongly reduced ubiquitination
by a TRIM21-containing SCF(SKP2) complex.
{ECO:0000269|PubMed:16209941}.
MUTAGEN 187 187 T->A,D: No change in PKB/AKT1- nor UHMK1-
mediated phosphorylation.
{ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:15280662,
ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:16880511}.
MUTAGEN 187 187 T->A: Abolishes phosphorylation-dependent
ubiquitination.
{ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:15280662,
ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:16880511}.
MUTAGEN 198 198 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.
{ECO:0000269|PubMed:12042314,
ECO:0000269|PubMed:14504289,
ECO:0000269|PubMed:15280662}.
CONFLICT 22 22 E -> D (in Ref. 2; AAD14244).
{ECO:0000305}.
HELIX 38 49 {ECO:0000244|PDB:1JSU}.
TURN 50 53 {ECO:0000244|PDB:1JSU}.
HELIX 54 60 {ECO:0000244|PDB:1JSU}.
TURN 64 67 {ECO:0000244|PDB:1JSU}.
STRAND 71 74 {ECO:0000244|PDB:1JSU}.
STRAND 77 80 {ECO:0000244|PDB:1JSU}.
HELIX 86 89 {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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