ID   CDNB_HUMAN     STANDARD;      PRT;   198 AA.
AC   P46527; Q16307;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   01-OCT-2000 (Rel. 40, Last annotation update)
DE   CYCLIN-DEPENDENT KINASE INHIBITOR 1B (CYCLIN-DEPENDENT KINASE
DE   INHIBITOR P27) (P27KIP1).
GN   CDKN1B OR KIP1.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 28-79 AND 104-152.
RC   TISSUE=Kidney;
RX   MEDLINE=94306518; PubMed=8033212;
RA   Polyak K., Lee M.-H., Erdjument-Bromage H., Koff A., Roberts J.M.,
RA   Tempst P., Massague J.;
RT   "Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a
RT   potential mediator of extracellular antimitogenic signals.";
RL   Cell 78:59-66(1994).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=95188144; PubMed=7882309;
RA   Pietenpol J.A., Bohlander S.K., Sato Y., Papadopoulos N., Liu B.,
RA   Friedman C., Trask B.J., Roberts J.M., Kinzler K.W., Rowley J.D.;
RT   "Assignment of the human p27Kip1 gene to 12p13 and its analysis in
RT   leukemias.";
RL   Cancer Res. 55:1206-1210(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-106 IN CDK2/CG2A COMPLEX.
RX   MEDLINE=96300318; PubMed=8684460;
RA   Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
RT   "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor
RT   bound to the cyclin A-Cdk2 complex.";
RL   Nature 382:325-331(1996).
CC   -!- FUNCTION: INVOLVED IN G1 ARREST. MAY MEDIATE TGF BETA-INDUCED G1
CC       ARREST. BINDS TO AND INHIBITS COMPLEXES FORMED BY CYCLIN E-CDK2,
CC       CYCLIN A-CDK2, AND CYCLIN D1-CDK4.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- TISSUE SPECIFICITY: EXPRESSED IN ALL TISSUES TESTED. HIGHEST
CC       LEVELS IN SKELETAL MUSCLE, LOWEST IN LIVER AND KIDNEY.
CC   -!- DOMAIN: A PEPTIDE SEQUENCE CONTAINING ONLY AA 28-79 RETAINS
CC       SUBSTANTIAL KIP1 CYCLIN A/CDK2 INHIBITORY ACTIVITY.
CC   -!- SIMILARITY: THE N-TERMINAL OF CIP1 AND KIP ARE SIMILAR.
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DR   EMBL; U10906; AAA20240.1; -.
DR   EMBL; S76988; AAD14244.1; -.
DR   EMBL; S76986; AAD14244.1; JOINED.
DR   PDB; 1JSU; 29-JUL-97.
DR   SWISS-2DPAGE; P46527; HUMAN.
DR   MIM; 600778; -.
KW   Cell cycle; Nuclear protein; 3D-structure.
FT   DOMAIN      153    169       NUCLEAR LOCALIZATION SIGNAL (POTENTIAL).
FT   CONFLICT     22     22       E -> D (IN REF. 2).
FT   CONFLICT    109    109       V -> G (IN REF. 2).
SQ   SEQUENCE   198 AA;  22073 MW;  1118D58901CDF3FC CRC64;
     MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVDHEE LTRDLEKHCR DMEEASQRKW
     NFDFQNHKPL EGKYEWQEVE KGSLPEFYYR PPRPPKGACK VPAQESQDVS GSRPAAPLIG
     APANSEDTHL VDPKTDPSDS QTGLAEQCAG IRKRPATDDS STQNKRANRT EENVSDGSPN
     AGSVEQTPKK PGLRRRQT
//