PMF1_MOUSE
ID PMF1_MOUSE Reviewed; 202 AA.
AC Q9CPV5; Q3UCB8; Q8K237; Q924B3; Q9D6E2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Polyamine-modulated factor 1;
DE Short=PMF-1;
GN Name=Pmf1 {ECO:0000312|MGI:MGI:1914287};
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] {ECO:0000305, ECO:0000312|EMBL:AAK84829.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP INTERACTION WITH NFE2L2, AND INDUCTION.
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:AAK84829.1}, and
RC Liver {ECO:0000312|EMBL:AAK84830.1};
RX PubMed=11583586; DOI=10.1042/0264-6021:3590387;
RA Wang Y., Devereux W., Woster P.M., Casero R.A. Jr.;
RT "Cloning and characterization of the mouse polyamine-modulated factor-1
RT (mPMF-1) gene: an alternatively spliced homologue of the human
RT transcription factor.";
RL Biochem. J. 359:387-392(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB27447.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAE40160.1}, and
RC C57BL/6J {ECO:0000312|EMBL:BAB27447.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE29695.1},
RC Embryo {ECO:0000312|EMBL:BAB27447.1}, and
RC Hippocampus {ECO:0000312|EMBL:BAB28994.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH37139.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH34333.1},
RC FVB/N {ECO:0000312|EMBL:AAH37139.1}, and
RC NMRI {ECO:0000312|EMBL:AAH49223.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH37139.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Part of the MIS12 complex which is required for normal
CC chromosome alignment and segregation and for kinetochore formation
CC during mitosis (By similarity). May act as a cotranscription partner of
CC NFE2L2 involved in regulation of polyamine-induced transcription of
CC SSAT. {ECO:0000250, ECO:0000269|PubMed:11583586}.
CC -!- SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1
CC and PMF1. Interacts with COPS7A (By similarity). Interacts via its
CC coiled-coil domain with the leucine-zipper domain of NFE2L2. The
CC interaction with NFE2L2 is required for the transcriptional regulation
CC of SSAT. {ECO:0000250, ECO:0000269|PubMed:11583586}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Note=Associated with the kinetochore.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11583586}; Synonyms=PMF-1L
CC {ECO:0000269|PubMed:11583586};
CC IsoId=Q9CPV5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11583586}; Synonyms=PMF-1S
CC {ECO:0000269|PubMed:11583586};
CC IsoId=Q9CPV5-2; Sequence=VSP_052141;
CC -!- INDUCTION: By polyamine analogs in M1 myeloid leukemia cells.
CC {ECO:0000269|PubMed:11583586}.
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DR EMBL; AF348509; AAK84828.1; -; mRNA.
DR EMBL; AF348510; AAK84829.1; -; mRNA.
DR EMBL; AF348512; AAK84830.1; -; Genomic_DNA.
DR EMBL; AF348511; AAK84830.1; JOINED; Genomic_DNA.
DR EMBL; AK011174; BAB27447.1; -; mRNA.
DR EMBL; AK012113; BAB28041.1; -; mRNA.
DR EMBL; AK013787; BAB28994.1; -; mRNA.
DR EMBL; AK150603; BAE29695.1; -; mRNA.
DR EMBL; AK168200; BAE40160.1; -; mRNA.
DR EMBL; BC034333; AAH34333.1; -; mRNA.
DR EMBL; BC037139; AAH37139.1; -; mRNA.
DR EMBL; BC049223; AAH49223.1; -; mRNA.
DR CCDS; CCDS38481.1; -. [Q9CPV5-1]
DR CCDS; CCDS79942.1; -. [Q9CPV5-2]
DR RefSeq; NP_001297534.1; NM_001310605.1. [Q9CPV5-2]
DR RefSeq; NP_080204.1; NM_025928.4. [Q9CPV5-1]
DR AlphaFoldDB; Q9CPV5; -.
DR SMR; Q9CPV5; -.
DR ComplexPortal; CPX-5701; Kinetochore MIS12 complex.
DR IntAct; Q9CPV5; 1.
DR MINT; Q9CPV5; -.
DR STRING; 10090.ENSMUSP00000062420; -.
DR iPTMnet; Q9CPV5; -.
DR PhosphoSitePlus; Q9CPV5; -.
DR REPRODUCTION-2DPAGE; IPI00623557; -.
DR EPD; Q9CPV5; -.
DR jPOST; Q9CPV5; -.
DR MaxQB; Q9CPV5; -.
DR PaxDb; Q9CPV5; -.
DR PeptideAtlas; Q9CPV5; -.
DR PRIDE; Q9CPV5; -.
DR ProteomicsDB; 289697; -. [Q9CPV5-1]
DR ProteomicsDB; 289698; -. [Q9CPV5-2]
DR Antibodypedia; 4085; 173 antibodies from 26 providers.
DR DNASU; 67037; -.
DR Ensembl; ENSMUST00000056370; ENSMUSP00000062420; ENSMUSG00000028066. [Q9CPV5-1]
DR Ensembl; ENSMUST00000193338; ENSMUSP00000141696; ENSMUSG00000028066. [Q9CPV5-2]
DR GeneID; 67037; -.
DR KEGG; mmu:67037; -.
DR UCSC; uc008pva.1; mouse. [Q9CPV5-1]
DR UCSC; uc008pvb.1; mouse. [Q9CPV5-2]
DR CTD; 11243; -.
DR MGI; MGI:1914287; Pmf1.
DR VEuPathDB; HostDB:ENSMUSG00000028066; -.
DR eggNOG; ENOG502S3AR; Eukaryota.
DR GeneTree; ENSGT00940000162656; -.
DR HOGENOM; CLU_1906070_0_0_1; -.
DR InParanoid; Q9CPV5; -.
DR OMA; IHLAHLM; -.
DR OrthoDB; 1614035at2759; -.
DR PhylomeDB; Q9CPV5; -.
DR TreeFam; TF333180; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 67037; 29 hits in 75 CRISPR screens.
DR ChiTaRS; Pmf1; mouse.
DR PRO; PR:Q9CPV5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CPV5; protein.
DR Bgee; ENSMUSG00000028066; Expressed in yolk sac and 159 other tissues.
DR ExpressionAtlas; Q9CPV5; baseline and differential.
DR Genevisible; Q9CPV5; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0000444; C:MIS12/MIND type complex; ISS:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0000818; C:nuclear MIS12/MIND complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR InterPro; IPR007128; PMF1/Nnf1.
DR PANTHER; PTHR15459; PTHR15459; 1.
DR Pfam; PF03980; Nnf1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Coiled coil; Kinetochore; Mitosis;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..202
FT /note="Polyamine-modulated factor 1"
FT /id="PRO_0000248238"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..194
FT /evidence="ECO:0000255"
FT VAR_SEQ 51..120
FT /note="SYERFTTCYKHFHQLNPEVTQRIYDKFVAQLQTSIREEISEIKEEGNLEAVL
FT NSLDKIIEEGRERGEPAW -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11583586"
FT /id="VSP_052141"
FT CONFLICT 34
FT /note="L -> H (in Ref. 2; BAB28994)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="Y -> F (in Ref. 3; AAH34333)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="I -> K (in Ref. 2; BAE29695)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="R -> H (in Ref. 3; AAH34333)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 23121 MW; F2474291AF9C1EAE CRC64;
MAEVSRDSEA AERGPEGSSP EAVPGDATIP RVKLLDAIVD TFLQKLVADR SYERFTTCYK
HFHQLNPEVT QRIYDKFVAQ LQTSIREEIS EIKEEGNLEA VLNSLDKIIE EGRERGEPAW
RPSGIPEKDL CSVMAPYFLK QQDTLCHQVR KQEAKNQELA DAVLAGRRQV EELQQQVRAL
QQTWQALHRE QRELLSVLRA PE
