P46527 (CDN1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 147. History...
Names and origin
|Protein names||Recommended name:|
Cyclin-dependent kinase inhibitor 1B
Cyclin-dependent kinase inhibitor p27
|Organism||Homo sapiens (Human) [Reference proteome]|
|Taxonomic identifier||9606 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo|
|Sequence length||198 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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 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. Ref.7 Ref.11 Ref.17 Ref.22 Ref.26
Forms a ternary compex with CCNE1/CDK2/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. 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 with UHMK1; the interaction leads to cytoplasmic mislocation, phosphorylation of CDKN1B and inhibition of cell cycle arrest. Interacts also with CDK1. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 Ref.26
Nucleus. Cytoplasm. Endosome By similarity. 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney.
Maximal levels in quiescence cells and early G1. Levels decrease after mitogen stimulation as cells progress toward S-phase. Ref.26
A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity.
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, 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 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26
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. Ref.6 Ref.18 Ref.25
Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation By similarity.
|Involvement in 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.
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.
Belongs to the CDI family.
|Abl1||P00520||2||EBI-519280,EBI-914519||From a different organism.|
|Jak2||Q62120||7||EBI-519280,EBI-646604||From a different organism.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 198||198||Cyclin-dependent kinase inhibitor 1B||PRO_0000190084|
|Motif||153 – 169||17||Nuclear localization signal Potential|
Amino acid modifications
|Modified residue||10||1||Phosphoserine; by UHMK1 Ref.7 Ref.8 Ref.9 Ref.12|
|Modified residue||74||1||Phosphotyrosine; by SRC|
|Modified residue||88||1||Phosphotyrosine; by ABL, LYN, SRC and JAK2 Ref.16 Ref.26|
|Modified residue||89||1||Phosphotyrosine Ref.16|
|Modified residue||157||1||Phosphothreonine; by PKB/AKT1 and PIM1 Ref.10 Ref.11 Ref.21|
|Modified residue||187||1||Phosphothreonine; by PKB/AKT1 and CDK2 Ref.6 Ref.9 Ref.25|
|Modified residue||198||1||Phosphothreonine; by PKB/AKT1, RPS6KA1, RPS6KA3 and PIM1 Ref.9 Ref.12 Ref.14 Ref.21|
|Natural variant||15||1||R → W. Ref.4|
Corresponds to variant rs2066828 [ dbSNP | Ensembl ].
|Natural variant||69||1||P → L Found in a patient with multiple endocrine tumors; germline mutation; reduced expression levels; shows impaired binding to CDK2. Ref.27||VAR_064429|
|Natural variant||109||1||V → G. Ref.3 Ref.4 Ref.5|
Corresponds to variant rs2066827 [ dbSNP | Ensembl ].
|Mutagenesis||10||1||S → A: Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest. Ref.8 Ref.9 Ref.14|
|Mutagenesis||10||1||S → D: Exported to the cytoplasm. Inhibits cell cycle arrest. Ref.8 Ref.9 Ref.14|
|Mutagenesis||10||1||S → E: Increased stability in vivo and in vitro. Ref.8 Ref.9 Ref.14|
|Mutagenesis||74||1||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. Ref.16 Ref.22|
|Mutagenesis||88||1||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. Ref.16 Ref.22 Ref.26|
|Mutagenesis||89||1||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. Ref.16 Ref.22 Ref.26|
|Mutagenesis||157||1||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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14|
|Mutagenesis||161||1||S → A: No change in PKB/AKT1-mediated phosphorylation. Ref.11|
|Mutagenesis||162||1||T → A: No change in PKB/AKT1-mediated phosphorylation. Ref.11|
|Mutagenesis||185||1||E → A, D or Q: Strongly reduced ubiquitination by a TRIM21-containing SCF(SKP2) complex. Ref.25|
|Mutagenesis||187||1||T → A or D: No change in PKB/AKT1- nor UHMK1-mediated phosphorylation. Ref.8 Ref.9 Ref.14 Ref.18 Ref.25|
|Mutagenesis||187||1||T → A: Abolishes phosphorylation-dependent ubiquitination. Ref.8 Ref.9 Ref.14 Ref.18 Ref.25|
|Mutagenesis||198||1||T → A or 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. Ref.9 Ref.12 Ref.14|
|Sequence conflict||22||1||E → D in AAD14244. Ref.2|
Helix Strand Turn
|Helix||38 – 49||12|
|Turn||50 – 53||4|
|Helix||54 – 60||7|
|Turn||64 – 67||4|
|Beta strand||71 – 74||4|
|Beta strand||77 – 80||4|
|Helix||86 – 89||4|
|||"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], PROTEIN SEQUENCE OF 28-79 AND 104-152.
|||"Assignment of the human p27Kip1 gene to 12p13 and its analysis in leukemias."|
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.
Cancer Res. 55:1206-1210(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
|||"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."|
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-109.
|||NIEHS SNPs program|
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-15 AND GLY-109.
|||"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], VARIANT GLY-109.
|||"Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation."|
Montagnoli A., Fiore F., Eytan E., Carrano A.C., Draetta G.F., Hershko A., Pagano M.
Genes Dev. 13:1181-1189(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, PHOSPHORYLATION AT THR-187.
|||"Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability."|
Ishida N., Kitagawa M., Hatakeyama S., Nakayama K.
J. Biol. Chem. 275:25146-25154(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-10, FUNCTION.
|||"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, PHOSPHORYLATION AT SER-10, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-10 AND THR-187.
|||"Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."|
Fujita N., Sato S., Katayama K., Tsuruo T.
J. Biol. Chem. 277:28706-28713(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-10; THR-187 AND THR-198, INTERACTION WITH AKT1 AND YWHAQ, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-10; THR-157; THR-187 AND THR-198.
|||"Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer."|
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.
Nat. Med. 8:1136-1144(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-157, SUBCELLULAR LOCATION, ASSOCIATION WITH BREAST CANCER, MUTAGENESIS OF THR-157.
|||"PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization."|
Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J., Arteaga C.L.
Nat. Med. 8:1145-1152(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-157, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF THR-157; SER-161 AND THR-162.
|||"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization."|
Fujita N., Sato S., Tsuruo T.
J. Biol. Chem. 278:49254-49260(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-10 AND THR-198, INTERACTION WITH YWHAE; YWHAH; SFN; YWHAQ; RPS6KA1 AND RPS6KA3, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-157 AND THR-198.
|||"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.
|||"Akt-dependent T198 phosphorylation of cyclin-dependent kinase inhibitor p27kip1 in breast cancer."|
Motti M.L., De Marco C., Califano D., Fusco A., Viglietto G.
Cell Cycle 3:1074-1080(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-198, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-10; THR-157; THR-187 AND THR-198.
|||"Cdc2-cyclin E complexes regulate the G1/S phase transition."|
Aleem E., Kiyokawa H., Kaldis P.
Nat. Cell Biol. 7:831-836(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK1.
|||"Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27Kip1 in the acute promyelocytic leukemia cell line NB4."|
Kardinal C., Dangers M., Kardinal A., Koch A., Brandt D.T., Tamura T., Welte K.
Blood 107:1133-1140(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-88 AND TYR-89, DEPHOSPHORYLATION, INTERACTION WITH GRB2; CDK2 AND CDK4, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-74; TYR-88 AND TYR-89.
|||"Regulated activating Thr172 phosphorylation of cyclin-dependent kinase 4(CDK4): its relationship with cyclins and CDK 'inhibitors'."|
Bockstaele L., Kooken H., Libert F., Paternot S., Dumont J.E., de Launoit Y., Roger P.P., Coulonval K.
Mol. Cell. Biol. 26:5070-5085(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK4, FUNCTION.
|||"Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein."|
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.
Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, MUTAGENESIS OF THR-187.
|||"Germ-line mutations in p27(Kip1) cause a multiple endocrine neoplasia syndrome in rats and humans."|
Pellegata N.S., Quintanilla-Martinez L., Siggelkow H., Samson E., Bink K., Hoefler H., Fend F., Graw J., Atkinson M.J.
Proc. Natl. Acad. Sci. U.S.A. 103:15558-15563(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH MEN4.
|||"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."|
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
|||"Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."|
Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIM1, PHOSPHORYLATION AT THR-157 AND THR-198.
|||"p27Kip1 inhibits cyclin D-cyclin-dependent kinase 4 by two independent modes."|
Ray A., James M.K., Larochelle S., Fisher R.P., Blain S.W.
Mol. Cell. Biol. 29:986-999(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK4, PHOSPHORYLATION, FUNCTION, MUTAGENESIS OF TYR-74; TYR-88 AND TYR-89.
|||"Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor signaling to cell cycle control."|
Jakel H., Weinl C., Hengst L.
Oncogene 30:3502-3512(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY JAK2 AT TYR-88.
|||"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."|
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
Nature 382:325-331(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-106 OF COMPLEX WITH CDK2 AND CG2A.
|||"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase."|
Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P.
Mol. Cell 20:9-19(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, UBIQUITINATION.
|||"Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases."|
Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.-M., Waddell M.B., Jaekel H., Kullmann M., Kriwacki R.W., Hengst L.
Cell 128:269-280(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 22-104, PHOSPHORYLATION AT TYR-88, FUNCTION, INDUCTION, INTERACTION WITH LYN, MASS SPECTROMETRY, MUTAGENESIS OF TYR-88 AND TYR-89.
|||"A novel germline CDKN1B mutation causing multiple endocrine tumors: clinical, genetic and functional characterization."|
Molatore S., Marinoni I., Lee M., Pulz E., Ambrosio M.R., degli Uberti E.C., Zatelli M.C., Pellegata N.S.
Hum. Mutat. 31:E1825-E1835(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-69, CHARACTERIZATION OF VARIANT LEU-69.
|+||Additional computationally mapped references.|
|U10906 mRNA. Translation: AAA20240.1.|
S76988, S76986 Genomic DNA. Translation: AAD14244.1.
BT019553 mRNA. Translation: AAV38360.1.
BT019554 mRNA. Translation: AAV38361.1.
AF480891 Genomic DNA. Translation: AAL78041.1.
BC001971 mRNA. Translation: AAH01971.1.
|RefSeq||NP_004055.1. NM_004064.3. |
3D structure databases
Protein-protein interaction databases
|IntAct||P46527. 40 interactions.|
2D gel databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENST00000228872; ENSP00000228872; ENSG00000111276. |
|UCSC||uc001rat.2. human. |
|HGNC||HGNC:1785. CDKN1B. |
|MIM||600778. gene. |
|Orphanet||652. Multiple endocrine neoplasia type 1. |
276152. Multiple endocrine neoplasia type 4.
Enzyme and pathway databases
|Pathway_Interaction_DB||pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. |
hnf3apathway. FOXA1 transcription factor network.
foxopathway. FoxO family signaling.
avb3_integrin_pathway. Integrins in angiogenesis.
telomerasepathway. Regulation of Telomerase.
|Reactome||REACT_111102. Signal Transduction. |
REACT_115566. Cell Cycle.
REACT_383. DNA Replication.
REACT_6900. Immune System.
Gene expression databases
|GermOnline||ENSG00000111276. Homo sapiens. |
Family and domain databases
|InterPro||IPR003175. CDI. |
|PANTHER||PTHR10265. PTHR10265. 1 hit. |
|Pfam||PF02234. CDI. 1 hit. |
|ChiTaRS||CDKN1B. human. |
|Accession||Primary (citable) accession number: P46527|
Secondary accession number(s): Q16307, Q5U0H2, Q9BUS6
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
|Disclaimer||Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.|
|Human chromosome 12|
Human chromosome 12: entries, gene names and cross-references to MIM
|Human entries with polymorphisms or disease mutations|
List of human entries with polymorphisms or disease mutations
|Human polymorphisms and disease mutations|
Index of human polymorphisms and disease mutations
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Index of Protein Data Bank (PDB) cross-references
Index of protein domains and families