[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-79 AND 104-152. TISSUE=Kidney; DOI=10.1016/0092-8674(94)90572-X; PubMed=8033212 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7882309 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Assignment of the human p27Kip1 gene to 12p13 and its analysis in leukemias."; Cancer Res. 55:1206-1210(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-109. 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.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-15 AND GLY-109. NIEHS SNPs program; Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-109. TISSUE=Cervix; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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]	UBIQUITINATION, AND PHOSPHORYLATION. PubMed=10323868 [NCBI, ExPASy, EBI, Israel, Japan] Montagnoli A., Fiore F., Eytan E., Carrano A.C., Draetta G.F., Hershko A., Pagano M.; "Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation."; Genes Dev. 13:1181-1189(1999).
[7]	PHOSPHORYLATION AT SER-10, AND FUNCTION. DOI=10.1074/jbc.M001144200; PubMed=10831586 [NCBI, ExPASy, EBI, Israel, Japan] Ishida N., Kitagawa M., Hatakeyama S., Nakayama K.; "Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability."; J. Biol. Chem. 275:25146-25154(2000).
[8]	INTERACTION WITH UHMK1, PHOSPHORYLATION AT SER-10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-10 AND THR-187. DOI=10.1093/emboj/cdf343; PubMed=12093740 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	PHOSPHORYLATION AT SER-10; THR-187 AND THR-198, INTERACTION WITH AKT1 AND YWHAQ, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-10; THR-157; THR-187 AND THR-198. DOI=10.1074/jbc.M203668200; PubMed=12042314 [NCBI, ExPASy, EBI, Israel, Japan] Fujita N., Sato S., Katayama K., Tsuruo T.; "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."; J. Biol. Chem. 277:28706-28713(2002).
[10]	PHOSPHORYLATION AT THR-157, SUBCELLULAR LOCATION, ASSOCIATED WITH BREAST CANCER, AND MUTAGENESIS OF THR-157. DOI=10.1038/nm762; PubMed=12244303 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer."; Nat. Med. 8:1136-1144(2002).
[11]	PHOSPHORYLATION AT THR-157, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF THR-157; SER-161 AND THR-162. DOI=10.1038/nm759; PubMed=12244301 [NCBI, ExPASy, EBI, Israel, Japan] Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J., Arteaga C.L.; "PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization."; Nat. Med. 8:1145-1152(2002).
[12]	PHOSPHORYLATION AT SER-10 AND THR-198, INTERACTION WITH YWHAE; YWHAH; SFN; YWHAQ; RPS6KA4 AND RPS6KA5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-157 AND THR-198. DOI=10.1074/jbc.M306614200; PubMed=14504289 [NCBI, ExPASy, EBI, Israel, Japan] Fujita N., Sato S., Tsuruo T.; "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization."; J. Biol. Chem. 278:49254-49260(2003).
[13]	INTERACTION WITH SPDYA. DOI=10.1091/mbc.E02-12-0820; PubMed=12972555 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	PHOSPHORYLATION AT THR-198, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-10; THR-157; THR-187 AND THR-198. PubMed=15280662 [NCBI, ExPASy, EBI, Israel, Japan] Motti M.L., De Marco C., Califano D., Fusco A., Viglietto G.; "Akt-dependent T198 phosphorylation of cyclin-dependent kinase inhibitor p27kip1 in breast cancer."; Cell Cycle 3:1074-1080(2004).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[16]	PHOSPHORYLATION AT TYR-88 AND TYR-89, DEPHOSPHORYLATION, INTERACTION WITH GRB2; CDK2 AND CDK4, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-74; TYR-88 AND TYR-89. DOI=10.1182/blood-2005-05-1771; PubMed=16195327 [NCBI, ExPASy, EBI, Israel, Japan] Kardinal C., Dangers M., Kardinal A., Koch A., Brandt D.T., Tamura T., Welte K.; "Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27Kip1 in the acute promyelocytic leukemia cell line NB4."; Blood 107:1133-1140(2006).
[17]	ASSOCIATION WITH MEN4. DOI=10.1073/pnas.0603877103; PubMed=17030811 [NCBI, ExPASy, EBI, Israel, Japan] Pellegata N.S., Quintanilla-Martinez L., Siggelkow H., Samson E., Bink K., Hoefler H., Fend F., Graw J., Atkinson M.J.; "Germ-line mutations in p27(Kip1) cause a multiple endocrine neoplasia syndrome in rats and humans."; Proc. Natl. Acad. Sci. U.S.A. 103:15558-15563(2006).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[19]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-106 OF COMPLEX WITH CDK2 AND CG2A. DOI=10.1038/382325a0; PubMed=8684460 [NCBI, ExPASy, EBI, Israel, Japan] Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.; "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."; Nature 382:325-331(1996).
[20]	STRUCTURE BY NMR OF 22-104, PHOSPHORYLATION AT TYR-88, FUNCTION, INDUCTION, INTERACTION WITH LYN, MASS SPECTROMETRY, AND MUTAGENESIS OF TYR-88 AND TYR-89. DOI=10.1016/j.cell.2006.11.047; PubMed=17254966 [NCBI, ExPASy, EBI, Israel, Japan] Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.-M., Waddell M.B., Jaekel H., Kullmann M., Kriwacki R.W., Hengst L.; "Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases."; Cell 128:269-280(2007).

Comments

FUNCTION: Important regulator of cell cycle progrssion. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Positive regulator of cyclin D-dependent kinases such as CDK4. Regulated by phosphorylation and degradation events.
SUBUNIT: Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated p27kip1. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to p27KIP degradation. Interacts with SPDYA in the SPDYA/CDK2/p27kip1 complex. 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, LYN and UHMK1; the interactions lead to cytoplasmic mislocation, phosphorylation of p27kip1 and inhibition of cell cycle arrest. Interacts (unphosphorylated form) with CDK2. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction induces nuclear translocation. Interacts with GRB2.
INTERACTION:
P00520:Abl1 (xeno); NbExp=1; IntAct=EBI-519280, EBI-914519;
P20248:CCNA2; NbExp=4; IntAct=EBI-519280, EBI-457097;
P14635:CCNB1; NbExp=1; IntAct=EBI-519280, EBI-495332;
P24385:CCND1; NbExp=2; IntAct=EBI-519280, EBI-375001;
P24864:CCNE1; NbExp=2; IntAct=EBI-519280, EBI-519526;
O96020:CCNE2; NbExp=1; IntAct=EBI-519280, EBI-375033;
P24941:CDK2; NbExp=6; IntAct=EBI-519280, EBI-375096;
P11802:CDK4; NbExp=2; IntAct=EBI-519280, EBI-295644;
Q00535:CDK5; NbExp=2; IntAct=EBI-519280, EBI-1041567;
Q92905:COPS5; NbExp=1; IntAct=EBI-519280, EBI-594661;
O00505:KPNA3; NbExp=1; IntAct=EBI-519280, EBI-358297;
O15131:KPNA5; NbExp=3; IntAct=EBI-519280, EBI-540602;
P07948:LYN; NbExp=2; IntAct=EBI-519280, EBI-79452;
P12931:SRC; NbExp=1; IntAct=EBI-519280, EBI-621482;
P16949:STMN1; NbExp=1; IntAct=EBI-519280, EBI-445909;
P09936:UCHL1; NbExp=1; IntAct=EBI-519280, EBI-714860;
P07947:YES1; NbExp=1; IntAct=EBI-519280, EBI-515331;
P31946:YWHAB; NbExp=1; IntAct=EBI-519280, EBI-359815;
P62258:YWHAE; NbExp=1; IntAct=EBI-519280, EBI-356498;
P61981:YWHAG; NbExp=1; IntAct=EBI-519280, EBI-359832;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. 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.
TISSUE SPECIFICITY: Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney.
INDUCTION: Maximal levels in quiescence cells and early G(1). Levels decrease after mitogen stimulation as cells progress toward S-phase.
DOMAIN: A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity.
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, 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.
PTM: Ubiquitinated; in the cytoplasm by the KPC1/KPC2 complex and, in the nucleus, by SCF/SKP2. The latter requires prior phosphorylation on Thr-187.
DISEASE: Defects in CDKN1B are the cause of multiple endocrine neoplasia type 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.
MISCELLANEOUS: Decreased levels of p27Kip1, mainly due to proteosomal degradation, are found in various epithelial tumors originating from lung, breast, colon, ovary, esophagus, thyroid and prostate.
SIMILARITY: Belongs to the CDI family.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CDKN1BID116.html";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdkn1b/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U10906; AAA20240.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S76988; AAD14244.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S76986; AAD14244.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019553; AAV38360.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019554; AAV38361.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF480891; AAL78041.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001971; AAH01971.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00006991; -.

NP_004055.1; -.

3D structure databases

PDB

1H27; X-ray; 2.20 A; E=25-35.	[ExPASy / RCSB / EBI]
1JSU; X-ray; 2.30 A; C=23-106.	[ExPASy / RCSB / EBI]
2AST; X-ray; 2.30 A; D=181-190.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1H27; -.
1JSU; -.
2AST; -.

DisProt

DP00018; -.

ModBase

P46527.

Protein-protein interaction databases

IntAct

P46527; 35.

PTM databases

PhosphoSite

P46527; -.

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_11061; Signalling by NGF.

2D gel databases

SWISS-2DPAGE

P46527; -.

Organism-specific databases

GC12P012761; -.

HIX0010441; -.

HGNC:1785; CDKN1B.

CAB003691; -.

600778; gene. [NCBI / EBI]
610755; phenotype. [NCBI / EBI]

PharmGKB

PA105; -.

Gene expression databases

P46527; -.

P46527; -.

HS_CDKN1B; -.

ENSG00000111276; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0004861;	Molecular function: cyclin-dependent protein kinase inhibitor activity (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005072;	Molecular function: transforming growth factor beta receptor, cytoplasmic mediator activity (traceable author statement from ProtInc).
GO:0048102;	Biological process: autophagic cell death (inferred from direct assay from UniProtKB).
GO:0007050;	Biological process: cell cycle arrest (inferred from mutant phenotype from HGNC).
GO:0000082;	Biological process: G1/S transition of mitotic cell cycle (inferred from direct assay from UniProtKB).
GO:0006917;	Biological process: induction of apoptosis (inferred from direct assay from UniProtKB).
GO:0030308;	Biological process: negative regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0008285;	Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0042326;	Biological process: negative regulation of phosphorylation (inferred from direct assay from UniProtKB).
GO:0000079;	Biological process: regulation of cyclin-dependent protein kinase activity (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR003175; CDI.
IPR015456; Cyclin_inhib_p27.
Graphical view of domain structure.

PANTHER

PTHR10265; CDI; 1.
PTHR10265:SF4; p27_Kip1; 1.

Pfam

PF02234; CDI; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

P46527; -.

Genome annotation databases

Ensembl

ENSG00000111276; Homo sapiens. [Contig view]

GeneID

1027; -.

KEGG

hsa:1027; -.

Phylogenomic databases

HOGENOM

P46527; -.

HOVERGEN

P46527; -.

OMA

P46527; VNHEELT.

Other

NextBio

4315; -.

PMAP-CutDB

P46527; -.

SOURCE

CDKN1B; Homo sapiens.

ProtoNet

P46527.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell cycle; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Protein kinase inhibitor; Proto-oncogene; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 198`	`198`	`Cyclin-dependent kinase inhibitor 1B.`	`PRO_0000190084`
`MOTIF`	`153 169`	`17`	`Nuclear localization signal (Potential).`
`MOD_RES`	`10 10`		`Phosphoserine; by UHMK1.`
`MOD_RES`	`74 74`		`Phosphotyrosine; by SRC.`
`MOD_RES`	`88 88`		`Phosphotyrosine; by ABL, LYN and SRC.`
`MOD_RES`	`89 89`		`Phosphotyrosine.`
`MOD_RES`	`140 140`		`Phosphoserine.`
`MOD_RES`	`157 157`		`Phosphothreonine; by PKB/AKT1.`
`MOD_RES`	`187 187`		`Phosphothreonine; by PKB/AKT1 and CDK2.`
`MOD_RES`	`198 198`		`Phosphothreonine; by PKB/AKT1; RPS6KA4 and RPS6KA5.`
`VARIANT`	`15 15`	`1`	`R -> W (in dbSNP:rs2066828 [NCBI]).`	`VAR_011871`
`VARIANT`	`109 109`	`1`	`V -> G (in dbSNP:rs2066827 [NCBI]).`	`VAR_011872`
`MUTAGEN`	`10 10`		`S->A: Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest.`
`MUTAGEN`	`10 10`		`S->D: Exported to the cytoplasm. Inhibits cell cycle arrest.`
`MUTAGEN`	`10 10`		`S->E: Increased stability in vivo and in vitro.`
`MUTAGEN`	`74 74`		`Y->F: No change in binding CDK4. Translocates to nucleus.`
`MUTAGEN`	`88 88`		`Y->F: Abolishes LYN-mediated phosphorylation. Reduced CDK2 phosphorylation on T-187. Greater cell cycle arrest into S-phase. No effect on binding CDK2 complexes. Reduction of CDK4 binding. No nuclear translocation. Completely abolishes CDK4 binding; when associated with F-89.`
`MUTAGEN`	`89 89`		`Y->F: No effect on binding CDK2 complexes. Reduction of CDK4 binding. No nuclear translocation. Completely abolishes CDK4 binding; when associated with F-88.`
`MUTAGEN`	`157 157`		`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.`
`MUTAGEN`	`161 161`		`S->A: No change in PKB/AKT1-mediated phosphorylation.`
`MUTAGEN`	`162 162`		`T->A: No change in PKB/AKT1-mediated phosphorylation.`
`MUTAGEN`	`187 187`		`T->A,D: No change in PKB/AKT1- nor UHMK1-mediated phosphorylation.`
`MUTAGEN`	`198 198`		`T->A,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.`
`CONFLICT`	`22 22`		`E -> D (in Ref. 2; AAD14244).`
`HELIX`	`38 49`	`12`
`TURN`	`50 53`	`4`
`HELIX`	`54 60`	`7`
`TURN`	`64 67`	`4`
`STRAND`	`71 74`	`4`
`STRAND`	`77 80`	`4`
`HELIX`	`86 89`	`4`

Sequence information

Length: 198 AA [This is the length of the unprocessed precursor]

Molecular weight: 22073 Da [This is the MW of the unprocessed precursor]

CRC64: 1118D58901CDF3FC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVDHEE LTRDLEKHCR DMEEASQRKW 

        70         80         90        100        110        120 
NFDFQNHKPL EGKYEWQEVE KGSLPEFYYR PPRPPKGACK VPAQESQDVS GSRPAAPLIG 

       130        140        150        160        170        180 
APANSEDTHL VDPKTDPSDS QTGLAEQCAG IRKRPATDDS STQNKRANRT EENVSDGSPN 

       190 
AGSVEQTPKK PGLRRRQT

P46527 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools