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

 CDN1B_MOUSE             Reviewed;         197 AA.
P46414; Q8BG74;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
17-JUN-2020, entry version 167.
RecName: Full=Cyclin-dependent kinase inhibitor 1B;
AltName: Full=Cyclin-dependent kinase inhibitor p27 {ECO:0000303|PubMed:8033213};
AltName: Full=p27Kip1 {ECO:0000303|PubMed:8033212};
Name=Cdkn1b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=8033213; DOI=10.1016/0092-8674(94)90573-8;
Toyoshima H., Hunter T.;
"p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is
related to p21.";
Cell 78:67-74(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Adipose tissue, Corpus striatum, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Salivary gland;
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]
INTERACTION WITH CCND1 IN THE CCND1-CDK4-CDKN1B COMPLEX.
PubMed=8534916; DOI=10.1091/mbc.6.9.1197;
Poon R.Y., Toyoshima H., Hunter T.;
"Redistribution of the CDK inhibitor p27 between different cyclin.CDK
complexes in the mouse fibroblast cell cycle and in cells arrested with
lovastatin or ultraviolet irradiation.";
Mol. Biol. Cell 6:1197-1213(1995).
[7]
PHOSPHORYLATION AT THR-187, INTERACTION WITH CCNE1 IN CCNE1/ CDK2/CDKN1B
COMPLEX, FUNCTION, AND MUTAGENESIS OF SER-10 AND THR-187.
PubMed=9399644; DOI=10.1038/sj.onc.1201440;
Mueller D., Bouchard C., Rudolph B., Steiner P., Stuckmann I., Saffrich R.,
Ansorge W., Huttner W., Eilers M.;
"Cdk2-dependent phosphorylation of p27 facilitates its Myc-induced release
from cyclin E/cdk2 complexes.";
Oncogene 15:2561-2576(1997).
[8]
INTERACTION WITH COPS5.
PubMed=10086358; DOI=10.1038/18230;
Tomoda K., Kubota Y., Kato J.-Y.;
"Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated
by Jab1.";
Nature 398:160-165(1999).
[9]
INTERACTION WITH NUP50, AND MUTAGENESIS OF ARG-90.
STRAIN=BALB/cJ;
PubMed=10811608; DOI=10.1093/emboj/19.10.2168;
Mueller D., Thieke K., Buergin A., Dickmanns A., Eilers M.;
"Cyclin E-mediated elimination of p27 requires its interaction with the
nuclear pore-associated protein mNPAP60.";
EMBO J. 19:2168-2180(2000).
[10]
INTERACTION WITH UHMK1, FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION
AT SER-10.
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).
[11]
INTERACTION WITH SPDYA, AND FUNCTION.
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).
[12]
PHOSPHORYLATION AT SER-10, FUNCTION, AND MUTAGENESIS OF SER-10.
PubMed=15528185; DOI=10.1074/jbc.m406117200;
Kotake Y., Nakayama K., Ishida N., Nakayama K.I.;
"Role of serine 10 phosphorylation in p27 stabilization revealed by
analysis of p27 knock-in mice harboring a serine 10 mutation.";
J. Biol. Chem. 280:1095-1102(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[14]
INTERACTION WITH CCND1.
PubMed=19767775; DOI=10.1038/onc.2009.287;
Barbash O., Egan E., Pontano L.L., Kosak J., Diehl J.A.;
"Lysine 269 is essential for cyclin D1 ubiquitylation by the
SCF(Fbx4/alphaB-crystallin) ligase and subsequent proteasome-dependent
degradation.";
Oncogene 28:4317-4325(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION, SUBCELLULAR LOCATION, DEGRADATION IN THE LYSOSOME, AND
INTERACTION WITH SNX6.
PubMed=20228253; DOI=10.1096/fj.09-138255;
Fuster J.J., Gonzalez J.M., Edo M.D., Viana R., Boya P., Cervera J.,
Verges M., Rivera J., Andres V.;
"Tumor suppressor p27(Kip1) undergoes endolysosomal degradation through its
interaction with sorting nexin 6.";
FASEB J. 24:2998-3009(2010).
[17]
PHOSPHORYLATION AT THR-170 AND THR-197 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).
-!- FUNCTION: Important regulator of cell cycle progression
(PubMed:8033213, PubMed:12972555). Inhibits the kinase activity of CDK2
bound to cyclin A, but has little inhibitory activity on CDK2 bound to
SPDYA (By similarity). Involved in G1 arrest. Potent inhibitor of
cyclin E- and cyclin A-CDK2 complexes (PubMed:8033213). 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:0000250|UniProtKB:P46527, ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:12972555, ECO:0000269|PubMed:15528185,
ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:8033213,
ECO:0000269|PubMed:9399644}.
-!- 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-197-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. Interacts with AKT1 and LYN; the interactions lead to
cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of
cell cycle arrest. 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.
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. Interacts with PIM1. Identified in a complex with SKP1, SKP2
and CKS1B. Interacts with UHMK1; the interaction leads to cytoplasmic
mislocation, phosphorylation of CDKN1B and inhibition of cell cycle
arrest. Interacts also with CDK1. Dephosphorylated on Thr-187 by PPM1H,
leading to CDKN1B stability (By similarity).
{ECO:0000250|UniProtKB:P46527, ECO:0000269|PubMed:10086358,
ECO:0000269|PubMed:10811608, ECO:0000269|PubMed:12093740,
ECO:0000269|PubMed:12972555, ECO:0000269|PubMed:19767775,
ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:8534916,
ECO:0000269|PubMed:9399644}.
-!- INTERACTION:
P46414; P30285: Cdk4; NbExp=2; IntAct=EBI-1005742, EBI-847225;
P46414; Q61881: Mcm7; NbExp=2; IntAct=EBI-1005742, EBI-457180;
P46414; P54227: Stmn1; NbExp=2; IntAct=EBI-1005742, EBI-1006438;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endosome
{ECO:0000269|PubMed:20228253}. Note=Nuclear and cytoplasmic in
quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-197, 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 (By similarity).
Colocalizes at the endosome with SNX6; this leads to lysosomal
degradation (PubMed:20228253). {ECO:0000250,
ECO:0000269|PubMed:20228253}.
-!- DOMAIN: A peptide sequence containing only AA 28-79 retains substantial
Kip1 cyclin A/CDK2 inhibitory activity. {ECO:0000250}.
-!- 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, MYC and in certain cancer
cell lines. The phosphorylated form found in the cytoplasm is
inactivate. Phosphorylation on Thr-197 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 (By similarity). Dephosphorylated on Thr-187 by
PPM1H, leading to CDKN1B stability (By similarity).
{ECO:0000250|UniProtKB:P46527}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- PTM: Subject to degradation in the lysosome. Interaction with SNX6
promotes lysosomal degradation.
-!- SIMILARITY: Belongs to the CDI family. {ECO:0000305}.
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EMBL; U10440; AAA21149.1; -; mRNA.
EMBL; U09968; AAA20235.1; -; mRNA.
EMBL; AK046676; BAC32833.1; -; mRNA.
EMBL; AK047669; BAC33119.1; -; mRNA.
EMBL; AK050240; BAC34141.1; -; mRNA.
EMBL; AC122193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014296; AAH14296.1; -; mRNA.
CCDS; CCDS20642.1; -.
PIR; I49064; I49064.
RefSeq; NP_034005.2; NM_009875.4.
SMR; P46414; -.
BioGRID; 198652; 23.
DIP; DIP-445N; -.
IntAct; P46414; 9.
MINT; P46414; -.
STRING; 10090.ENSMUSP00000003115; -.
iPTMnet; P46414; -.
PhosphoSitePlus; P46414; -.
EPD; P46414; -.
jPOST; P46414; -.
PaxDb; P46414; -.
PeptideAtlas; P46414; -.
PRIDE; P46414; -.
Antibodypedia; 3295; 2570 antibodies.
Ensembl; ENSMUST00000003115; ENSMUSP00000003115; ENSMUSG00000003031.
Ensembl; ENSMUST00000067327; ENSMUSP00000065832; ENSMUSG00000003031.
Ensembl; ENSMUST00000204807; ENSMUSP00000145056; ENSMUSG00000003031.
GeneID; 12576; -.
KEGG; mmu:12576; -.
UCSC; uc009ela.2; mouse.
CTD; 1027; -.
MGI; MGI:104565; Cdkn1b.
eggNOG; KOG4743; Eukaryota.
eggNOG; ENOG410XXN5; LUCA.
GeneTree; ENSGT00940000159852; -.
HOGENOM; CLU_077692_2_0_1; -.
InParanoid; P46414; -.
KO; K06624; -.
OMA; EGRYEWQ; -.
OrthoDB; 1595421at2759; -.
TreeFam; TF101038; -.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-MMU-8849470; PTK6 Regulates Cell Cycle.
Reactome; R-MMU-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
BioGRID-ORCS; 12576; 1 hit in 12 CRISPR screens.
ChiTaRS; Cdkn1b; mouse.
PRO; PR:P46414; -.
Proteomes; UP000000589; Chromosome 6.
RNAct; P46414; protein.
Bgee; ENSMUSG00000003031; Expressed in cerebellar vermis and 291 other tissues.
Genevisible; P46414; MM.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0030332; F:cyclin binding; IDA:BHF-UCL.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:MGI.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004860; F:protein kinase inhibitor activity; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0048102; P:autophagic cell death; ISO:MGI.
GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
GO; GO:0008219; P:cell death; ISO:MGI.
GO; GO:0071236; P:cellular response to antibiotic; IDA:MGI.
GO; GO:0071285; P:cellular response to lithium ion; ISO:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0007507; P:heart development; IMP:BHF-UCL.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0071850; P:mitotic cell cycle arrest; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:1905179; P:negative regulation of cardiac muscle tissue regeneration; IMP:BHF-UCL.
GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
GO; GO:0051271; P:negative regulation of cellular component movement; IDA:MGI.
GO; GO:1904030; P:negative regulation of cyclin-dependent protein kinase activity; ISO:MGI.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0033673; P:negative regulation of kinase activity; ISO:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0042326; P:negative regulation of phosphorylation; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; ISO:MGI.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:0001890; P:placenta development; IGI:MGI.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IGI:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0006813; P:potassium ion transport; IGI:MGI.
GO; GO:0007096; P:regulation of exit from mitosis; IGI:MGI.
GO; GO:1902746; P:regulation of lens fiber cell differentiation; IGI:MGI.
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; IMP:MGI.
InterPro; IPR003175; CDI.
InterPro; IPR029843; CDKN1B.
PANTHER; PTHR10265:SF9; PTHR10265:SF9; 1.
Pfam; PF02234; CDI; 1.
1: Evidence at protein level;
Cell cycle; Cytoplasm; Endosome; Nucleus; Phosphoprotein;
Protein kinase inhibitor; Reference proteome; Ubl conjugation.
CHAIN 1..197
/note="Cyclin-dependent kinase inhibitor 1B"
/id="PRO_0000190085"
REGION 51..91
/note="Interaction with CDK2"
/evidence="ECO:0000250|UniProtKB:P46527"
MOTIF 153..169
/note="Nuclear localization signal"
/evidence="ECO:0000255"
SITE 90
/note="Required for interaction with NUP50"
MOD_RES 10
/note="Phosphoserine; by UHMK1"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:15528185"
MOD_RES 74
/note="Phosphotyrosine; by SRC"
/evidence="ECO:0000250|UniProtKB:P46527"
MOD_RES 88
/note="Phosphotyrosine; by ABL, LYN, SRC and JAK2"
/evidence="ECO:0000250|UniProtKB:P46527"
MOD_RES 89
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P46527"
MOD_RES 170
/note="Phosphothreonine; by CaMK1"
/evidence="ECO:0000269|PubMed:23707388"
MOD_RES 187
/note="Phosphothreonine; by PKB/AKT1, CDK1 and CDK2"
/evidence="ECO:0000269|PubMed:9399644"
MOD_RES 197
/note="Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1,
RPS6KA3 and PIM1"
/evidence="ECO:0000250|UniProtKB:P46527"
MUTAGEN 10
/note="S->A: Loss of phosphorylation in G(0) phase. No
change in cMYC-induced CDK2-mediated phosphorylation. Rapid
dissociation from the cyclin E/CDK2 complex after induction
by cMYC. Loss of protein stability in G(0) phase. No change
in protein stability at S-phase."
/evidence="ECO:0000269|PubMed:15528185,
ECO:0000269|PubMed:9399644"
MUTAGEN 90
/note="R->G: Loss of interaction with NUP50. No cyclin E-
mediated degradation of phosphorylated p27KIP1."
/evidence="ECO:0000269|PubMed:10811608"
MUTAGEN 187
/note="T->E: Loss of cMyc-induced CDK2-mediated
phosphorylation. Rapid dissociation from the cyclin E/CDK2
complex after induction by c-Myc."
/evidence="ECO:0000269|PubMed:9399644"
MUTAGEN 187
/note="T->V: Loss of cMYC-induced CDK2-mediated
phosphorylation Dissociates very slowly from the cyclin
E/CDK2 complex after induction by cMYC. Cell cycle arrest."
/evidence="ECO:0000269|PubMed:9399644"
CONFLICT 22
/note="E -> D (in Ref. 1; AAA21149, 2; AAA20235 and 5;
AAH14296)"
/evidence="ECO:0000305"
CONFLICT 141
/note="P -> Q (in Ref. 1; AAA21149, 2; AAA20235 and 5;
AAH14296)"
/evidence="ECO:0000305"
SEQUENCE 197 AA; 22193 MW; BAC30D648B9BA3D6 CRC64;
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVNHEE LTRDLEKHCR DMEEASQRKW
NFDFQNHKPL EGRYEWQEVE RGSLPEFYYR PPRPPKSACK VLAQESQDVS GSRQAVPLIG
SQANSEDRHL VDQMPDSSDN PAGLAEQCPG MRKRPAAEDS SSQNKRANRT EENVSDGSPN
AGTVEQTPKK PGLRRQT


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1619: Amino sugar and nucleotide sugar metabolism
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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
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WP1844: MAP kinase cascade
WP655: p53 pathway
WP801: ACE Inhibitor Pathway
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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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