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Protein Page:
p27Kip1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
p27Kip1 a cell-cycle regulatory protein that Interacts with cyclin-CDK2 and -CDK4, inhibiting cell cycle progression at G1. May mediate TGF beta-induced g1 arrest. Its degradation is triggered by its CDK dependent phosphorylation and subsequent ubiquitination by SCF complexes, is required for the cellular transition from quiescence to the proliferative state. Note: This description may include information from UniProtKB.
Protein type: Inhibitor protein; Protein kinase, regulatory subunit; Cell cycle regulation
Cellular Component: nucleoplasm; protein complex; cytoplasm; cytosol; nucleus; endosome
Molecular Function: cyclin-dependent protein kinase inhibitor activity; protein binding; chaperone binding; protein complex binding; caspase activator activity; Hsp70 protein binding; protein phosphatase binding; transforming growth factor beta receptor, cytoplasmic mediator activity
Biological Process: response to peptide hormone stimulus; negative regulation of kinase activity; nerve growth factor receptor signaling pathway; positive regulation of microtubule polymerization; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; response to estradiol stimulus; negative regulation of cell proliferation; sensory perception of sound; positive regulation of cell proliferation; response to glucose stimulus; negative regulation of mitotic cell cycle; cell cycle arrest; inner ear development; potassium ion transport; response to drug; caspase activation; epidermal growth factor receptor signaling pathway; phosphoinositide-mediated signaling; fibroblast growth factor receptor signaling pathway; negative regulation of cyclin-dependent protein kinase activity; negative regulation of cell motility; response to amino acid stimulus; response to cadmium ion; response to hypoxia; autophagic cell death; positive regulation of protein catabolic process; innate immune response; negative regulation of phosphorylation; mitotic cell cycle; regulation of cyclin-dependent protein kinase activity; negative regulation of cell growth; negative regulation of transcription, DNA-dependent; negative regulation of apoptosis; G1/S transition of mitotic cell cycle
Reference #:  P46527 (UniProtKB)
Alt. Names/Synonyms: CDKN1B; CDKN4; CDN1B; Cyclin-dependent kinase inhibitor 1B; cyclin-dependent kinase inhibitor 1B (p27, Kip1); Cyclin-dependent kinase inhibitor p27; KIP1; MEN1B; MEN4; p27Kip1
Gene Symbols: CDKN1B
Molecular weight: 22,073 Da
Basal Isoelectric point: 6.54  Predict pI for various phosphorylation states
CST Pathways:  ErbB/HER Signaling  |  G1/S Checkpoint  |  Growth And Differentiation Control by MAPKs  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

p27Kip1

Protein Structure Not Found.


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Sites Implicated In
apoptosis, inhibited: S10‑p, T157‑p
cell adhesion, induced: S10‑p
cell cycle regulation: S10‑p, Y74‑p, Y88‑p, Y89‑p, T157‑p, T187‑p, T198‑p
cell growth, altered: T157‑p, T198‑p
cell motility, induced: S10‑p
cytoskeletal reorganization: S10‑p, T157‑p
transcription, altered: S10‑p
activity, inhibited: Y88‑p, Y89‑p
intracellular localization: S10‑p, Y88‑p, Y89‑p, T157‑p, T198‑p
molecular association, regulation: S10‑p, Y74‑p, Y88‑p, Y89‑p, T157‑p, T187‑p, T198‑p
phosphorylation: S10‑p, T157‑p
protein conformation: S83‑p, T187‑p
protein degradation: S10‑p, Y74‑p, Y88‑p, T157‑p, T187‑p, T198‑p
protein stabilization: S10‑p, T187‑p, T198‑p
ubiquitination: T187‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S7 _MSNVRVSNGsPSLE
39 17 S10-p NVRVSNGsPSLErMD
1 2 S12 RVSNGsPSLErMDAR
0 1 R15-m1 NGsPSLErMDARQAE
1 0 T42 PVDHEELTRDLEKHC
7 0 Y74-p HKPLEGKyEWQEVEk
0 1 K81-ac yEWQEVEkGsLPEFy
2 0 S83-p WQEVEkGsLPEFyyR
9 0 Y88-p kGsLPEFyyRPPRPP
6 0 Y89-p GsLPEFyyRPPRPPK
0 9 S106 CKVPAQESQDVSGSR
1 0 K134-ub DTHLVDPkTDPSDsQ
0 2 S140-p PkTDPSDsQTGLAEQ
1 0 K153-ub EQCAGIRkrPAtDDS
0 1 R154-m2 QCAGIRkrPAtDDSS
19 1 T157-p GIRkrPAtDDSSTQN
1 0 K165-ub DDSSTQNkRANRTEE
2 0 T170 QNkRANRTEENVSDG
1 0 S175 NRTEENVSDGsPNAG
5 3 S178-p EENVSDGsPNAGsVE
1 1 S183-p DGsPNAGsVEQtPKK
40 0 T187-p NAGsVEQtPKKPGLR
20 6 T198-p PGLRRRQt_______
  mouse

 
S7-p _MSNVRVsNGsPsLE
S10-p NVRVsNGsPsLERMD
S12-p RVsNGsPsLERMDAR
R15 NGsPsLERMDARQAE
T42-p PVNHEELtRDLEKHC
Y74 HKPLEGRYEWQEVER
R81 YEWQEVERGsLPEFy
S83-p WQEVERGsLPEFyYR
Y88-p RGsLPEFyYRPPRPP
Y89 GsLPEFyYRPPRPPK
S106-p CKVLAQEsQDVSGSR
M134 DRHLVDQMPDSSDNP
N140 QMPDSSDNPAGLAEQ
K153 EQCPGMRKRPAaEDS
R154 QCPGMRKRPAaEDSS
A157-p GMRKRPAaEDSSSQN
K165 EDSSSQNKRANRtEE
T170-p QNKRANRtEENVsDG
S175-p NRtEENVsDGsPNAG
S178-p EENVsDGsPNAGtVE
T183-p DGsPNAGtVEQtPKK
T187-p NAGtVEQtPKKPGLR
T197-p KPGLRRQt_______
  rat

 
S7 _MSNVRVSNGsPSLE
S10-p NVRVSNGsPSLERMD
S12 RVSNGsPSLERMDAR
R15 NGsPSLERMDARQTE
T42 PVNHEELTRDLEKHC
Y74 HKPLEGRYEWQEVER
R81 YEWQEVERGSLPEFY
S83 WQEVERGSLPEFYYR
Y88 RGSLPEFYYRPPRPP
Y89 GSLPEFYYRPPRPPK
S106 CKVPAQESLDVSGSR
M134 DRHLVDQMPDSSDSP
S140 QMPDSSDSPAGLAEQ
K153 EQCPGMRKRPAAEDS
R154 QCPGMRKRPAAEDSS
A157 GMRKRPAAEDSSSQN
K165 EDSSSQNKRANRTEE
T170 QNKRANRTEENVSDG
S175 NRTEENVSDGsPNAG
S178-p EENVSDGsPNAGTVE
T183 DGsPNAGTVEQTPKK
T187 NAGTVEQTPKKPGLR
T197 KPGLRRQT_______
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