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P46414 (CDN1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase inhibitor 1B
Alternative name(s):
Cyclin-dependent kinase inhibitor p27
p27Kip1
Gene names
Name:Cdkn1b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.10 Ref.12 Ref.15

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15

Subcellular location

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. Ref.10 Ref.15

Domain

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

Post-translational modification

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. Ref.7 Ref.10 Ref.12 Ref.16

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. Ref.15

Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation.

Sequence similarities

Belongs to the CDI family.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Endosome
Nucleus
   Molecular functionProtein kinase inhibitor
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from direct assay Ref.6. Source: UniProtKB

autophagic cell death

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from direct assay Ref.1. Source: MGI

cellular response to antibiotic

Inferred from direct assay PubMed 19056892. Source: MGI

cellular response to lithium ion

Inferred from sequence orthology PubMed 19056892. Source: MGI

cellular response to organic cyclic compound

Inferred from direct assay PubMed 19056892. Source: MGI

inner ear development

Inferred from mutant phenotype PubMed 10079221. Source: MGI

mitotic cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16014817. Source: MGI

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 11751454. Source: MGI

negative regulation of cellular component movement

Inferred from direct assay PubMed 15652749. Source: MGI

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 12130539. Source: MGI

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 10079221. Source: MGI

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from mutant phenotype PubMed 16014817. Source: MGI

negative regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell death

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 12759355. Source: MGI

positive regulation of microtubule polymerization

Inferred from genetic interaction PubMed 15652749. Source: MGI

positive regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Inferred from genetic interaction PubMed 16393152. Source: MGI

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from mutant phenotype PubMed 10079221. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15652749. Source: MGI

cytosol

Inferred from direct assay PubMed 15964824. Source: MGI

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 10827137PubMed 15652749PubMed 16195383PubMed 19056892PubMed 20016102. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncyclin-dependent protein serine/threonine kinase inhibitor activity

Inferred from direct assay PubMed 12130539Ref.1. Source: MGI

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.14Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Cyclin-dependent kinase inhibitor 1B
PRO_0000190085

Regions

Motif153 – 16917Nuclear localization signal Potential

Sites

Site901Required for interaction with NUP50

Amino acid modifications

Modified residue101Phosphoserine; by UHMK1 Ref.10 Ref.12 Ref.13
Modified residue741Phosphotyrosine; by SRC By similarity
Modified residue881Phosphotyrosine; by ABL, LYN, SRC and JAK2 By similarity
Modified residue891Phosphotyrosine By similarity
Modified residue1701Phosphothreonine; by CaMK1 Ref.16
Modified residue1871Phosphothreonine; by PKB/AKT1, CDK1 and CDK2 Ref.7
Modified residue1971Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1, RPS6KA3 and PIM1 By similarity

Experimental info

Mutagenesis101S → 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. Ref.7 Ref.12
Mutagenesis901R → G: Loss of interaction with NUP50. No cyclin E-mediated degradation of phosphorylated p27KIP1. Ref.9
Mutagenesis1871T → E: Loss of cMyc-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by c-Myc. Ref.7
Mutagenesis1871T → V: Loss of cMYC-induced CDK2-mediated phosphorylation Dissociates very slowly from the cyclin E/CDK2 complex after induction by cMYC. Cell cycle arrest. Ref.7
Sequence conflict221E → D in AAA21149. Ref.1
Sequence conflict221E → D in AAA20235. Ref.2
Sequence conflict221E → D in AAH14296. Ref.5
Sequence conflict1411P → Q in AAA21149. Ref.1
Sequence conflict1411P → Q in AAA20235. Ref.2
Sequence conflict1411P → Q in AAH14296. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P46414 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: BAC30D648B9BA3D6

FASTA19722,193
        10         20         30         40         50         60 
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVNHEE LTRDLEKHCR DMEEASQRKW 

        70         80         90        100        110        120 
NFDFQNHKPL EGRYEWQEVE RGSLPEFYYR PPRPPKSACK VLAQESQDVS GSRQAVPLIG 

       130        140        150        160        170        180 
SQANSEDRHL VDQMPDSSDN PAGLAEQCPG MRKRPAAEDS SSQNKRANRT EENVSDGSPN 

       190 
AGTVEQTPKK PGLRRQT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS20642.1.
PIRI49064.
RefSeqNP_034005.2. NM_009875.4.
XP_006505529.1. XM_006505466.1.
UniGeneMm.2958.

3D structure databases

ProteinModelPortalP46414.
SMRP46414. Positions 25-93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198652. 24 interactions.
DIPDIP-445N.
IntActP46414. 7 interactions.
MINTMINT-1780106.
STRING10090.ENSMUSP00000065832.

PTM databases

PhosphoSiteP46414.

Proteomic databases

PaxDbP46414.
PRIDEP46414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003115; ENSMUSP00000003115; ENSMUSG00000003031.
ENSMUST00000067327; ENSMUSP00000065832; ENSMUSG00000003031.
GeneID12576.
KEGGmmu:12576.
UCSCuc009ela.2. mouse.

Organism-specific databases

CTD1027.
MGIMGI:104565. Cdkn1b.

Phylogenomic databases

eggNOGNOG245842.
GeneTreeENSGT00530000063588.
HOGENOMHOG000294081.
HOVERGENHBG073988.
InParanoidP46414.
KOK06624.
OMAFYFRPPR.
OrthoDBEOG7GJ6HD.
TreeFamTF101038.

Gene expression databases

CleanExMM_CDKN1B.
GenevestigatorP46414.

Family and domain databases

InterProIPR003175. CDI.
[Graphical view]
PANTHERPTHR10265. PTHR10265. 1 hit.
PfamPF02234. CDI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDKN1B. mouse.
NextBio281690.
PROP46414.
SOURCESearch...

Entry information

Entry nameCDN1B_MOUSE
AccessionPrimary (citable) accession number: P46414
Secondary accession number(s): Q8BG74
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot