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P46414

- CDN1B_MOUSE

UniProt

P46414 - CDN1B_MOUSE

Protein

Cyclin-dependent kinase inhibitor 1B

Gene

Cdkn1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Important regulator of cell cycle progression. 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 cyclin D-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.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei90 – 901Required for interaction with NUP50

    GO - Molecular functioni

    1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: MGI
    2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: Ensembl
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. autophagic cell death Source: Ensembl
    2. cell cycle arrest Source: MGI
    3. cellular response to antibiotic Source: MGI
    4. cellular response to lithium ion Source: MGI
    5. cellular response to organic cyclic compound Source: MGI
    6. G1/S transition of mitotic cell cycle Source: UniProtKB
    7. inner ear development Source: MGI
    8. mitotic cell cycle arrest Source: Ensembl
    9. negative regulation of apoptotic process Source: MGI
    10. negative regulation of cell growth Source: Ensembl
    11. negative regulation of cell proliferation Source: MGI
    12. negative regulation of cellular component movement Source: MGI
    13. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: MGI
    14. negative regulation of epithelial cell proliferation Source: MGI
    15. negative regulation of epithelial cell proliferation involved in prostate gland development Source: MGI
    16. negative regulation of mitotic cell cycle Source: Ensembl
    17. negative regulation of transcription, DNA-templated Source: Ensembl
    18. positive regulation of cell death Source: Ensembl
    19. positive regulation of cell proliferation Source: MGI
    20. positive regulation of microtubule polymerization Source: MGI
    21. positive regulation of protein catabolic process Source: Ensembl
    22. potassium ion transport Source: MGI
    23. response to amino acid Source: Ensembl
    24. response to cadmium ion Source: Ensembl
    25. response to drug Source: Ensembl
    26. response to estradiol Source: Ensembl
    27. response to glucose Source: Ensembl
    28. response to hypoxia Source: Ensembl
    29. response to peptide hormone Source: Ensembl
    30. sensory perception of sound Source: MGI

    Keywords - Molecular functioni

    Protein kinase inhibitor

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_220918. AKT phosphorylates targets in the cytosol.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase inhibitor 1B
    Alternative name(s):
    Cyclin-dependent kinase inhibitor p27
    p27Kip1
    Gene namesi
    Name:Cdkn1b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:104565. Cdkn1b.

    Subcellular locationi

    Nucleus. Cytoplasm. Endosome
    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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. endosome Source: UniProtKB-SubCell
    4. nucleus Source: MGI
    5. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101S → 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. 2 Publications
    Mutagenesisi90 – 901R → G: Loss of interaction with NUP50. No cyclin E-mediated degradation of phosphorylated p27KIP1. 1 Publication
    Mutagenesisi187 – 1871T → E: Loss of cMyc-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by c-Myc. 1 Publication
    Mutagenesisi187 – 1871T → V: Loss of cMYC-induced CDK2-mediated phosphorylation Dissociates very slowly from the cyclin E/CDK2 complex after induction by cMYC. Cell cycle arrest. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 197197Cyclin-dependent kinase inhibitor 1BPRO_0000190085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine; by UHMK13 Publications
    Modified residuei74 – 741Phosphotyrosine; by SRCBy similarity
    Modified residuei88 – 881Phosphotyrosine; by ABL, LYN, SRC and JAK2By similarity
    Modified residuei89 – 891PhosphotyrosineBy similarity
    Modified residuei170 – 1701Phosphothreonine; by CaMK11 Publication
    Modified residuei187 – 1871Phosphothreonine; by PKB/AKT1, CDK1 and CDK21 Publication
    Modified residuei197 – 1971Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1, RPS6KA3 and PIM1By similarity

    Post-translational modificationi

    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)-G1 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.By similarity
    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.By similarity
    Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP46414.
    PRIDEiP46414.

    PTM databases

    PhosphoSiteiP46414.

    Expressioni

    Gene expression databases

    CleanExiMM_CDKN1B.
    GenevestigatoriP46414.

    Interactioni

    Subunit structurei

    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. Interacts (unphosphorylated form) with CDK2. Forms a ternary complex, cyclin D/CDK4/CDKN1B. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction is required for cyclin D/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 also with CDK1 By similarity. Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated CDKN1B. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to CDKN1B degradation. Interacts with SPDYA in the SPDYA/CDK2/CDKN1B complex. Interacts with UHMK1; the interaction leads to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest. Forms a ternary complex with CCNE1/CDK2/CDKN1B. Interacts directly with CCNE1; the interaction is inhibited by CDK2-dependent phosphorylation on Thr-187. Interacts with CCND1 and SNX6.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Mcm7Q618812EBI-1005742,EBI-457180
    Stmn1P542272EBI-1005742,EBI-1006438

    Protein-protein interaction databases

    BioGridi198652. 24 interactions.
    DIPiDIP-445N.
    IntActiP46414. 7 interactions.
    MINTiMINT-1780106.
    STRINGi10090.ENSMUSP00000065832.

    Structurei

    3D structure databases

    ProteinModelPortaliP46414.
    SMRiP46414. Positions 25-93.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi153 – 16917Nuclear localization signalSequence AnalysisAdd
    BLAST

    Domaini

    A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity.By similarity

    Sequence similaritiesi

    Belongs to the CDI family.Curated

    Phylogenomic databases

    eggNOGiNOG245842.
    GeneTreeiENSGT00530000063588.
    HOGENOMiHOG000294081.
    HOVERGENiHBG073988.
    InParanoidiP46414.
    KOiK06624.
    OMAiFYFRPPR.
    OrthoDBiEOG7GJ6HD.
    TreeFamiTF101038.

    Family and domain databases

    InterProiIPR003175. CDI.
    [Graphical view]
    PANTHERiPTHR10265. PTHR10265. 1 hit.
    PfamiPF02234. CDI. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46414-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVNHEE LTRDLEKHCR    50
    DMEEASQRKW NFDFQNHKPL EGRYEWQEVE RGSLPEFYYR PPRPPKSACK 100
    VLAQESQDVS GSRQAVPLIG SQANSEDRHL VDQMPDSSDN PAGLAEQCPG 150
    MRKRPAAEDS SSQNKRANRT EENVSDGSPN AGTVEQTPKK PGLRRQT 197
    Length:197
    Mass (Da):22,193
    Last modified:October 3, 2012 - v2
    Checksum:iBAC30D648B9BA3D6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221E → D in AAA21149. (PubMed:8033213)Curated
    Sequence conflicti22 – 221E → D in AAA20235. (PubMed:8033212)Curated
    Sequence conflicti22 – 221E → D in AAH14296. (PubMed:15489334)Curated
    Sequence conflicti141 – 1411P → Q in AAA21149. (PubMed:8033213)Curated
    Sequence conflicti141 – 1411P → Q in AAA20235. (PubMed:8033212)Curated
    Sequence conflicti141 – 1411P → Q in AAH14296. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10440 mRNA. Translation: AAA21149.1.
    U09968 mRNA. Translation: AAA20235.1.
    AK046676 mRNA. Translation: BAC32833.1.
    AK047669 mRNA. Translation: BAC33119.1.
    AK050240 mRNA. Translation: BAC34141.1.
    AC122193 Genomic DNA. No translation available.
    BC014296 mRNA. Translation: AAH14296.1.
    CCDSiCCDS20642.1.
    PIRiI49064.
    RefSeqiNP_034005.2. NM_009875.4.
    XP_006505529.1. XM_006505466.1.
    UniGeneiMm.2958.

    Genome annotation databases

    EnsembliENSMUST00000003115; ENSMUSP00000003115; ENSMUSG00000003031.
    ENSMUST00000067327; ENSMUSP00000065832; ENSMUSG00000003031.
    GeneIDi12576.
    KEGGimmu:12576.
    UCSCiuc009ela.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10440 mRNA. Translation: AAA21149.1 .
    U09968 mRNA. Translation: AAA20235.1 .
    AK046676 mRNA. Translation: BAC32833.1 .
    AK047669 mRNA. Translation: BAC33119.1 .
    AK050240 mRNA. Translation: BAC34141.1 .
    AC122193 Genomic DNA. No translation available.
    BC014296 mRNA. Translation: AAH14296.1 .
    CCDSi CCDS20642.1.
    PIRi I49064.
    RefSeqi NP_034005.2. NM_009875.4.
    XP_006505529.1. XM_006505466.1.
    UniGenei Mm.2958.

    3D structure databases

    ProteinModelPortali P46414.
    SMRi P46414. Positions 25-93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198652. 24 interactions.
    DIPi DIP-445N.
    IntActi P46414. 7 interactions.
    MINTi MINT-1780106.
    STRINGi 10090.ENSMUSP00000065832.

    PTM databases

    PhosphoSitei P46414.

    Proteomic databases

    PaxDbi P46414.
    PRIDEi P46414.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003115 ; ENSMUSP00000003115 ; ENSMUSG00000003031 .
    ENSMUST00000067327 ; ENSMUSP00000065832 ; ENSMUSG00000003031 .
    GeneIDi 12576.
    KEGGi mmu:12576.
    UCSCi uc009ela.2. mouse.

    Organism-specific databases

    CTDi 1027.
    MGIi MGI:104565. Cdkn1b.

    Phylogenomic databases

    eggNOGi NOG245842.
    GeneTreei ENSGT00530000063588.
    HOGENOMi HOG000294081.
    HOVERGENi HBG073988.
    InParanoidi P46414.
    KOi K06624.
    OMAi FYFRPPR.
    OrthoDBi EOG7GJ6HD.
    TreeFami TF101038.

    Enzyme and pathway databases

    Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_220918. AKT phosphorylates targets in the cytosol.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    ChiTaRSi CDKN1B. mouse.
    NextBioi 281690.
    PROi P46414.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CDKN1B.
    Genevestigatori P46414.

    Family and domain databases

    InterProi IPR003175. CDI.
    [Graphical view ]
    PANTHERi PTHR10265. PTHR10265. 1 hit.
    Pfami PF02234. CDI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21."
      Toyoshima H., Hunter T.
      Cell 78:67-74(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals."
      Polyak K., Lee M.-H., Erdjument-Bromage H., Koff A., Roberts J.M., Tempst P., Massague J.
      Cell 78:59-66(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    3. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Adipose tissue, Corpus striatum and Liver.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Salivary gland.
    6. "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."
      Poon R.Y., Toyoshima H., Hunter T.
      Mol. Biol. Cell 6:1197-1213(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCND1 IN THE CCND1-CDK4-CDKN1B COMPLEX.
    7. "Cdk2-dependent phosphorylation of p27 facilitates its Myc-induced release from cyclin E/cdk2 complexes."
      Mueller D., Bouchard C., Rudolph B., Steiner P., Stuckmann I., Saffrich R., Ansorge W., Huttner W., Eilers M.
      Oncogene 15:2561-2576(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-187, INTERACTION WITH CCNE1 IN CCNE1/ CDK2/CDKN1B COMPLEX, FUNCTION, MUTAGENESIS OF SER-10 AND THR-187.
    8. "Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1."
      Tomoda K., Kubota Y., Kato J.-Y.
      Nature 398:160-165(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPS5.
    9. "Cyclin E-mediated elimination of p27 requires its interaction with the nuclear pore-associated protein mNPAP60."
      Mueller D., Thieke K., Buergin A., Dickmanns A., Eilers M.
      EMBO J. 19:2168-2180(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUP50, MUTAGENESIS OF ARG-90.
      Strain: BALB/c.
    10. "A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression."
      Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J., Nabel E.G.
      EMBO J. 21:3390-3401(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UHMK1, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-10.
    11. "Spy1 interacts with p27Kip1 to allow G1/S progression."
      Porter L.A., Kong-Beltran M., Donoghue D.J.
      Mol. Biol. Cell 14:3664-3674(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPDYA.
    12. "Role of serine 10 phosphorylation in p27 stabilization revealed by analysis of p27 knock-in mice harboring a serine 10 mutation."
      Kotake Y., Nakayama K., Ishida N., Nakayama K.I.
      J. Biol. Chem. 280:1095-1102(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-10, FUNCTION, MUTAGENESIS OF SER-10.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. "Lysine 269 is essential for cyclin D1 ubiquitylation by the SCF(Fbx4/alphaB-crystallin) ligase and subsequent proteasome-dependent degradation."
      Barbash O., Egan E., Pontano L.L., Kosak J., Diehl J.A.
      Oncogene 28:4317-4325(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCND1.
    15. "Tumor suppressor p27(Kip1) undergoes endolysosomal degradation through its interaction with sorting nexin 6."
      Fuster J.J., Gonzalez J.M., Edo M.D., Viana R., Boya P., Cervera J., Verges M., Rivera J., Andres V.
      FASEB J. 24:2998-3009(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEGRADATION IN THE LYSOSOME, INTERACTION WITH SNX6.
    16. "Fbxl12 triggers G1 arrest by mediating degradation of calmodulin kinase I."
      Mallampalli R.K., Kaercher L., Snavely C., Pulijala R., Chen B.B., Coon T., Zhao J., Agassandian M.
      Cell. Signal. 25:2047-2059(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-170 AND THR-197 BY CAMK1.

    Entry informationi

    Entry nameiCDN1B_MOUSE
    AccessioniPrimary (citable) accession number: P46414
    Secondary accession number(s): Q8BG74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3