CDN2A_MOUSE
ID CDN2A_MOUSE Reviewed; 168 AA.
AC P51480; A2ANM1; A2ANM2; O89088; P97510; P97937; Q6PEA2; Q78E39; Q78E57;
AC Q792X7; Q9QWH6; Q9QWH7; Q9QWH8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Cyclin-dependent kinase inhibitor 2A {ECO:0000312|MGI:MGI:104738};
DE AltName: Full=Cyclin-dependent kinase 4 inhibitor A;
DE Short=CDK4I;
DE AltName: Full=p16-INK4a;
DE Short=p16-INK4;
GN Name=Cdkn2a {ECO:0000312|MGI:MGI:104738}; Synonyms=P16ink4a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7651726;
RA Quelle D.E., Ashmun R.A., Hannon G.J., Rehberger P.A., Trono D.,
RA Richter K.H., Walker C., Beach D., Sherr C.J., Serrano M.;
RT "Cloning and characterization of murine p16INK4a and p15INK4b genes.";
RL Oncogene 11:635-645(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-18; ILE-51;
RP MET-74; TYR-75 AND ARG-90.
RC STRAIN=BALB/cJ, and DBA/2N; TISSUE=Spleen;
RX PubMed=9482902; DOI=10.1073/pnas.95.5.2429;
RA Zhang S., Ramsay E.S., Mock B.A.;
RT "Cdkn2a, the cyclin-dependent kinase inhibitor encoding p16(INK4a) and
RT p19(ARF), is a candidate for the plasmacytoma susceptibility locus,
RT Pctr1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2429-2434(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Gong Z., Li J., Fu J.;
RT "Cloning and structure analysis of murine p16INK4a.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
RC STRAIN=C57BL/6J X DBA;
RX PubMed=9178896; DOI=10.1038/sj.onc.1200969;
RA Malumbres M., de Castro I.P., Santos J., Melendez B., Mangues R.,
RA Serrano M., Pellicer A., Fernandez-Piqueras J.;
RT "Inactivation of the cyclin-dependent kinase inhibitor p15INK4b by deletion
RT and de novo methylation with independence of p16INK4a alterations in murine
RT primary T-cell lymphomas.";
RL Oncogene 14:1361-1370(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155, AND VARIANTS PRO-18; ILE-51;
RP GLN-90 AND SER-127.
RC STRAIN=BALB/cJ, C57BL/6J, CAST/EiJ, MOLF/EiJ, and RF/J;
RA Santos J., Melendez B., Perez de Castro I., Malumbres M., Serrano M.,
RA Pellicer A., Fernandez-Piqueras J.;
RT "Comparative analysis of the p16(INK4a) and p15(INK4b) DNA sequences in
RT mouse inbred strains.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-42 (ISOFORM 1), AND VARIANT PRO-18.
RC STRAIN=020, 129/J, A/J, A/Wy, AKR/J, B10.A, B10.D2(58N), BALB/cJ, C3H/21BG,
RC C3H/HeJ, C57BL/10ScNJ, C57BL/10SN, C57BL/6By, C57BL/6J, C57BR/cdJ, CBA/J,
RC DBA/2J, HS/IBG, LP/J, LS/IBG, MA/M4J, PL/J, RF/J, Sencar, SJL/J, SM/J,
RC ST/J, and SWR/J; TISSUE=Lung;
RX PubMed=9021155; DOI=10.1007/s003359900352;
RA Herzog C.R., You M.;
RT "Sequence variation and chromosomal mapping of the murine Cdkn2a tumor
RT suppressor gene.";
RL Mamm. Genome 8:65-66(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42, AND VARIANTS VAL-12; GLU-27 AND
RP LEU-73.
RX PubMed=9667743; DOI=10.1093/carcin/19.6.1045;
RA Gressani K.M., Rollins L.A., Leone-Kabler S., Cline J.M., Miller M.S.;
RT "Induction of mutations in Ki-ras and INK4a in liver tumors of mice exposed
RT in utero to 3-methylcholanthrene.";
RL Carcinogenesis 19:1045-1052(1998).
RN [10]
RP MUTAGENESIS OF CYS-64; ASP-76 AND 84-ASP-THR-85.
RX PubMed=9012842; DOI=10.1073/pnas.94.2.669;
RA Quelle D.E., Cheng M., Ashmun R.A., Sherr C.J.;
RT "Cancer-associated mutations at the INK4a locus cancel cell cycle arrest by
RT p16INK4a but not by the alternative reading frame protein p19ARF.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:669-673(1997).
CC -!- FUNCTION: Acts as a negative regulator of the proliferation of normal
CC cells by interacting strongly with CDK4 and CDK6. This inhibits their
CC ability to interact with cyclins D and to phosphorylate the
CC retinoblastoma protein.
CC -!- SUBUNIT: Heterodimer with CDK4 or CDK6. Predominamt P16 complexes
CC contained CDK6. Interacts with CDK4 (both 'T-172'-phosphorylated and
CC non-phosphorylated forms); the interaction inhibits cyclin D-CDK4
CC kinase activity. Interacts with ISCO2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Isoform 1 and isoform tumor suppressor ARF arise due to the
CC use of two alternative first exons joined to a common exon 2 at the
CC same acceptor site but in different reading frames, resulting in two
CC completely different isoforms.;
CC Name=1; Synonyms=p16INK4a;
CC IsoId=P51480-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51480-2; Sequence=VSP_015867;
CC Name=tumor suppressor ARF; Synonyms=p19ARF;
CC IsoId=Q64364-1; Sequence=External;
CC Name=smARF;
CC IsoId=Q64364-2; Sequence=External;
CC -!- PTM: Phosphorylation seems to increase interaction with CDK4.
CC {ECO:0000250}.
CC -!- POLYMORPHISM: Strain BALB/c displays a significantly reduced ability to
CC inhibit phosphorylation of the retinoblastoma protein.
CC -!- SIMILARITY: Belongs to the CDKN2 cyclin-dependent kinase inhibitor
CC family. {ECO:0000305}.
CC -!- CAUTION: The proteins described here are encoded by the gene CDKN2A,
CC but are completely unrelated in terms of sequence and function to tumor
CC suppressor ARF (AC Q64364) which is encoded by the same gene.
CC {ECO:0000305}.
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DR EMBL; L76150; AAA85453.1; -; mRNA.
DR EMBL; AF044335; AAC08962.1; -; mRNA.
DR EMBL; AF044336; AAC08963.1; -; mRNA.
DR EMBL; AF332190; AAK83159.1; -; Genomic_DNA.
DR EMBL; AK155307; BAE33180.1; -; mRNA.
DR EMBL; AL831719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U66087; AAB39600.1; -; Genomic_DNA.
DR EMBL; U66086; AAB39600.1; JOINED; Genomic_DNA.
DR EMBL; U79625; AAD00223.1; -; Genomic_DNA.
DR EMBL; U79626; AAD00224.1; -; Genomic_DNA.
DR EMBL; U79627; AAD00225.1; -; Genomic_DNA.
DR EMBL; U79628; AAD00226.1; -; Genomic_DNA.
DR EMBL; U79630; AAD00227.1; -; Genomic_DNA.
DR EMBL; U79631; AAD00228.1; -; Genomic_DNA.
DR EMBL; U79632; AAD00229.1; -; Genomic_DNA.
DR EMBL; U49279; AAC00051.1; -; Genomic_DNA.
DR EMBL; U49280; AAC00052.1; -; Genomic_DNA.
DR EMBL; AF004588; AAB61416.1; -; Genomic_DNA.
DR CCDS; CCDS38812.1; -. [P51480-1]
DR RefSeq; NP_001035744.1; NM_001040654.1. [P51480-1]
DR AlphaFoldDB; P51480; -.
DR SMR; P51480; -.
DR BioGRID; 198654; 40.
DR CORUM; P51480; -.
DR DIP; DIP-60251N; -.
DR IntAct; P51480; 1.
DR iPTMnet; P51480; -.
DR PhosphoSitePlus; P51480; -.
DR PeptideAtlas; P51480; -.
DR PRIDE; P51480; -.
DR ProteomicsDB; 281299; -. [P51480-1]
DR ProteomicsDB; 281300; -. [P51480-2]
DR DNASU; 12578; -.
DR Ensembl; ENSMUST00000060501; ENSMUSP00000061847; ENSMUSG00000044303. [P51480-1]
DR GeneID; 12578; -.
DR KEGG; mmu:12578; -.
DR UCSC; uc008toh.1; mouse. [P51480-1]
DR CTD; 1029; -.
DR MGI; MGI:104738; Cdkn2a.
DR VEuPathDB; HostDB:ENSMUSG00000044303; -.
DR GeneTree; ENSGT00940000168083; -.
DR HOGENOM; CLU_000134_37_1_1; -.
DR OMA; ANAPNRY; -.
DR TreeFam; TF352389; -.
DR BioGRID-ORCS; 12578; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Cdkn2a; mouse.
DR Proteomes; UP000000589; Chromosome 4.
DR Bgee; ENSMUSG00000044303; Expressed in yolk sac and 53 other tissues.
DR ExpressionAtlas; P51480; baseline and differential.
DR Genevisible; P51480; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISO:MGI.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:MGI.
DR GO; GO:0060057; P:apoptotic process involved in mammary gland involution; IMP:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
DR GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:0051882; P:mitochondrial depolarization; ISO:MGI.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:2000346; P:negative regulation of hepatocyte proliferation; ISO:MGI.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:2000435; P:negative regulation of protein neddylation; ISO:MGI.
DR GO; GO:1903051; P:negative regulation of proteolysis involved in protein catabolic process; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:2000111; P:positive regulation of macrophage apoptotic process; IGI:BHF-UCL.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:MGI.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IGI:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IGI:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IGI:MGI.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0090399; P:replicative senescence; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0009303; P:rRNA transcription; IGI:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell cycle; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Tumor suppressor.
FT CHAIN 1..168
FT /note="Cyclin-dependent kinase inhibitor 2A"
FT /id="PRO_0000144178"
FT REPEAT 3..32
FT /note="ANK 1"
FT REPEAT 36..64
FT /note="ANK 2"
FT REPEAT 69..98
FT /note="ANK 3"
FT REPEAT 102..131
FT /note="ANK 4"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42771"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42771"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015867"
FT VARIANT 12
FT /note="A -> V (in some liver tumors)"
FT /evidence="ECO:0000269|PubMed:9667743"
FT VARIANT 18
FT /note="H -> P (in strain: 020, BALB/c, BALB/cJ, C3H/21BG,
FT C3H/HeJ, CBA/J, MA/M4J and PL/J)"
FT /evidence="ECO:0000269|PubMed:9021155,
FT ECO:0000269|PubMed:9482902, ECO:0000269|Ref.7"
FT VARIANT 27
FT /note="G -> E (in some liver tumors)"
FT /evidence="ECO:0000269|PubMed:9667743"
FT VARIANT 51
FT /note="V -> I (in strain: BALB/c and BALB/cJ)"
FT /evidence="ECO:0000269|PubMed:9482902, ECO:0000269|Ref.7"
FT VARIANT 73
FT /note="P -> L (in some liver tumors)"
FT /evidence="ECO:0000269|PubMed:9667743"
FT VARIANT 74
FT /note="V -> M (in plasmacytoma cell lines)"
FT /evidence="ECO:0000269|PubMed:9482902"
FT VARIANT 75
FT /note="H -> Y (in plasmacytoma cell lines)"
FT /evidence="ECO:0000269|PubMed:9482902"
FT VARIANT 90
FT /note="H -> Q (in strain: BALB/cJ, C57BL/6J and MOLF/Ei)"
FT /evidence="ECO:0000269|Ref.7"
FT VARIANT 90
FT /note="H -> R (in plasmacytoma cell lines)"
FT /evidence="ECO:0000269|PubMed:9482902"
FT VARIANT 127
FT /note="C -> S (in strain: BALB/cJ, C57BL/6J and MOLF/Ei)"
FT /evidence="ECO:0000269|Ref.7"
FT MUTAGEN 64
FT /note="C->G,R: No effect on activity."
FT /evidence="ECO:0000269|PubMed:9012842"
FT MUTAGEN 76
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9012842"
FT MUTAGEN 84..85
FT /note="Missing: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9012842"
FT CONFLICT 11
FT /note="Missing (in Ref. 1; AAA85453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 17941 MW; 9A6B0F24F34D5FEC CRC64;
MESAADRLAR AAAQGRVHDV RALLEAGVSP NAPNSFGRTP IQVMMMGNVH VAALLLNYGA
DSNCEDPTTF SRPVHDAARE GFLDTLVVLH GSGARLDVRD AWGRLPLDLA QERGHQDIVR
YLRSAGCSLC SAGWSLCTAG NVAQTDGHSF SSSTPRALEL RGQSQEQS
