PMF1_HUMAN
ID PMF1_HUMAN Reviewed; 205 AA.
AC Q6P1K2; A8K0C5; Q5TCJ8; Q5TCJ9; Q5TCK0; Q5TCK1; Q5TCK3; Q69YZ9; Q6PHR4;
AC Q6ZVE6; Q86VJ6; Q8N4T6; Q9UBQ3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Polyamine-modulated factor 1;
DE Short=PMF-1;
GN Name=PMF1 {ECO:0000312|EMBL:AAH65031.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD50081.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 4-205 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND VARIANTS
RP ARG-75 AND ILE-137.
RC TISSUE=Lung carcinoma {ECO:0000312|EMBL:AAD50081.1};
RX PubMed=10419538; DOI=10.1074/jbc.274.31.22095;
RA Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
RT "Cloning and characterization of human polyamine-modulated factor-1, a
RT transcriptional cofactor that regulates the transcription of the
RT spermidine/spermine N(1)-acetyltransferase gene.";
RL J. Biol. Chem. 274:22095-22101(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT
RP ARG-75.
RC TISSUE=Cerebellum, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAH10730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH65031.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP ARG-75 AND ILE-137.
RC TISSUE=Colon {ECO:0000312|EMBL:AAH56417.1},
RC Skin {ECO:0000312|EMBL:AAH65031.1}, Testis {ECO:0000312|EMBL:AAH50735.1},
RC and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-205 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NFE2L2.
RX PubMed=11256947; DOI=10.1042/0264-6021:3550045;
RA Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
RT "Characterization of the interaction between the transcription factors
RT human polyamine modulated factor (PMF-1) and NF-E2-related factor 2 (Nrf-2)
RT in the transcriptional regulation of the spermidine/spermine N1-
RT acetyltransferase (SSAT) gene.";
RL Biochem. J. 355:45-49(2001).
RN [8] {ECO:0000305}
RP INTERACTION WITH COPS7A.
RX PubMed=12020345; DOI=10.1042/bj20020211;
RA Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
RT "Polyamine-modulated factor 1 binds to the human homologue of the 7a
RT subunit of the Arabidopsis COP9 signalosome: implications in gene
RT expression.";
RL Biochem. J. 366:79-86(2002).
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DSN1 AND MIS12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15502821; DOI=10.1038/ncb1187;
RA Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.;
RT "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and
RT outer kinetochore protein Zwint-1.";
RL Nat. Cell Biol. 6:1135-1141(2004).
RN [10]
RP FUNCTION, COMPONENT OF MIS12 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16585270; DOI=10.1083/jcb.200509158;
RA Kline S.L., Cheeseman I.M., Hori T., Fukagawa T., Desai A.;
RT "The human Mis12 complex is required for kinetochore assembly and proper
RT chromosome segregation.";
RL J. Cell Biol. 173:9-17(2006).
CC -!- FUNCTION: Part of the MIS12 complex which is required for normal
CC chromosome alignment and segregation and kinetochore formation during
CC mitosis. May act as a cotranscription partner of NFE2L2 involved in
CC regulation of polyamine-induced transcription of SSAT.
CC {ECO:0000269|PubMed:10419538, ECO:0000269|PubMed:11256947,
CC ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.
CC -!- SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1
CC and PMF1. Interacts with COPS7A. Interacts via its coiled-coil domain
CC with the leucine-zipper domain of NFE2L2. The interaction with NFE2L2
CC is required for the transcriptional regulation of SSAT.
CC {ECO:0000269|PubMed:11256947, ECO:0000269|PubMed:12020345,
CC ECO:0000269|PubMed:15502821}.
CC -!- INTERACTION:
CC Q6P1K2; P46379-2: BAG6; NbExp=3; IntAct=EBI-713832, EBI-10988864;
CC Q6P1K2; Q8TD16-2: BICD2; NbExp=4; IntAct=EBI-713832, EBI-11975051;
CC Q6P1K2; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-713832, EBI-715104;
CC Q6P1K2; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-713832, EBI-743105;
CC Q6P1K2; Q9NVF7: FBXO28; NbExp=4; IntAct=EBI-713832, EBI-740282;
CC Q6P1K2; O14901: KLF11; NbExp=3; IntAct=EBI-713832, EBI-948266;
CC Q6P1K2; Q14696: MESD; NbExp=3; IntAct=EBI-713832, EBI-6165891;
CC Q6P1K2; Q9H081: MIS12; NbExp=17; IntAct=EBI-713832, EBI-1001205;
CC Q6P1K2; Q16236: NFE2L2; NbExp=2; IntAct=EBI-713832, EBI-2007911;
CC Q6P1K2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-713832, EBI-2811583;
CC Q6P1K2; Q92529: SHC3; NbExp=3; IntAct=EBI-713832, EBI-79084;
CC Q6P1K2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-713832, EBI-5235340;
CC Q6P1K2; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-713832, EBI-12018146;
CC Q6P1K2; Q99598: TSNAX; NbExp=4; IntAct=EBI-713832, EBI-742638;
CC Q6P1K2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-713832, EBI-739895;
CC Q6P1K2-3; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-12906008, EBI-744545;
CC Q6P1K2-3; P42858: HTT; NbExp=3; IntAct=EBI-12906008, EBI-466029;
CC Q6P1K2-3; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-12906008, EBI-25929070;
CC Q6P1K2-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12906008, EBI-5235340;
CC Q6P1K2-3; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-12906008, EBI-12018146;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585270}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16585270}.
CC Note=Associated with the kinetochore.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1 {ECO:0000269|PubMed:10419538};
CC IsoId=Q6P1K2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16710414};
CC IsoId=Q6P1K2-2; Sequence=VSP_052137;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q6P1K2-3; Sequence=VSP_052139, VSP_052140;
CC Name=4 {ECO:0000269|PubMed:10419538};
CC IsoId=Q6P1K2-4; Sequence=VSP_052136;
CC Name=5 {ECO:0000269|PubMed:16710414};
CC IsoId=Q6P1K2-5; Sequence=VSP_052138;
CC Name=6;
CC IsoId=Q6P1K2-6; Sequence=VSP_044638;
CC -!- TISSUE SPECIFICITY: Highest levels of expression in heart and skeletal
CC muscle, with significant levels expressed in kidney and liver.
CC {ECO:0000269|PubMed:10419538}.
CC -!- INDUCTION: By polyamine analogs in analog-sensitive H157 cells.
CC {ECO:0000269|PubMed:10419538}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50081.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10730.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10730.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF141309; AAD50080.1; -; Genomic_DNA.
DR EMBL; AF141308; AAD50080.1; JOINED; Genomic_DNA.
DR EMBL; AF141310; AAD50081.1; ALT_INIT; mRNA.
DR EMBL; AK124646; BAC85916.1; -; mRNA.
DR EMBL; AK289490; BAF82179.1; -; mRNA.
DR EMBL; AK290260; BAF82949.1; -; mRNA.
DR EMBL; AL135927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52989.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52990.1; -; Genomic_DNA.
DR EMBL; BC033656; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC050735; AAH50735.1; -; mRNA.
DR EMBL; BC056417; AAH56417.1; -; mRNA.
DR EMBL; BC065031; AAH65031.1; -; mRNA.
DR EMBL; AL080101; CAH10730.1; ALT_SEQ; mRNA.
DR CCDS; CCDS30886.1; -. [Q6P1K2-1]
DR CCDS; CCDS55648.1; -. [Q6P1K2-2]
DR CCDS; CCDS55649.1; -. [Q6P1K2-6]
DR RefSeq; NP_001186582.1; NM_001199653.1. [Q6P1K2-6]
DR RefSeq; NP_001186583.1; NM_001199654.1. [Q6P1K2-2]
DR RefSeq; NP_001186590.1; NM_001199661.1. [Q6P1K2-5]
DR RefSeq; NP_001186592.1; NM_001199663.1. [Q6P1K2-3]
DR RefSeq; NP_009152.2; NM_007221.3. [Q6P1K2-1]
DR PDB; 5LSJ; X-ray; 3.25 A; B/E=31-205.
DR PDB; 5LSK; X-ray; 3.50 A; B=31-205.
DR PDBsum; 5LSJ; -.
DR PDBsum; 5LSK; -.
DR AlphaFoldDB; Q6P1K2; -.
DR SMR; Q6P1K2; -.
DR BioGRID; 116405; 117.
DR BioGRID; 1529341; 15.
DR ComplexPortal; CPX-5643; Kinetochore MIS12 complex.
DR CORUM; Q6P1K2; -.
DR IntAct; Q6P1K2; 69.
DR MINT; Q6P1K2; -.
DR STRING; 9606.ENSP00000357259; -.
DR GlyGen; Q6P1K2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P1K2; -.
DR PhosphoSitePlus; Q6P1K2; -.
DR SwissPalm; Q6P1K2; -.
DR BioMuta; PMF1; -.
DR DMDM; 114152119; -.
DR EPD; Q6P1K2; -.
DR jPOST; Q6P1K2; -.
DR MassIVE; Q6P1K2; -.
DR MaxQB; Q6P1K2; -.
DR PaxDb; Q6P1K2; -.
DR PeptideAtlas; Q6P1K2; -.
DR PRIDE; Q6P1K2; -.
DR ProteomicsDB; 64966; -.
DR ProteomicsDB; 66837; -. [Q6P1K2-1]
DR ProteomicsDB; 66838; -. [Q6P1K2-2]
DR ProteomicsDB; 66839; -. [Q6P1K2-3]
DR ProteomicsDB; 66840; -. [Q6P1K2-4]
DR ProteomicsDB; 66841; -. [Q6P1K2-5]
DR Antibodypedia; 4085; 173 antibodies from 26 providers.
DR DNASU; 11243; -.
DR Ensembl; ENST00000368273.8; ENSP00000357256.4; ENSG00000160783.19. [Q6P1K2-2]
DR Ensembl; ENST00000368277.3; ENSP00000357260.3; ENSG00000160783.19. [Q6P1K2-1]
DR Ensembl; ENST00000368279.7; ENSP00000357262.3; ENSG00000160783.19. [Q6P1K2-6]
DR GeneID; 100527963; -.
DR GeneID; 11243; -.
DR KEGG; hsa:100527963; -.
DR KEGG; hsa:11243; -.
DR MANE-Select; ENST00000368277.3; ENSP00000357260.3; NM_007221.4; NP_009152.2.
DR UCSC; uc001fnq.4; human. [Q6P1K2-1]
DR CTD; 100527963; -.
DR CTD; 11243; -.
DR DisGeNET; 100527963; -.
DR DisGeNET; 11243; -.
DR GeneCards; PMF1; -.
DR HGNC; HGNC:9112; PMF1.
DR HPA; ENSG00000160783; Low tissue specificity.
DR MIM; 609176; gene.
DR neXtProt; NX_Q6P1K2; -.
DR OpenTargets; ENSG00000160783; -.
DR OpenTargets; ENSG00000260238; -.
DR PharmGKB; PA33438; -.
DR VEuPathDB; HostDB:ENSG00000160783; -.
DR eggNOG; ENOG502T3RE; Eukaryota.
DR GeneTree; ENSGT00940000162656; -.
DR HOGENOM; CLU_106985_0_0_1; -.
DR InParanoid; Q6P1K2; -.
DR OMA; IHLAHLM; -.
DR OrthoDB; 1614035at2759; -.
DR PhylomeDB; Q6P1K2; -.
DR TreeFam; TF333180; -.
DR PathwayCommons; Q6P1K2; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q6P1K2; -.
DR SIGNOR; Q6P1K2; -.
DR BioGRID-ORCS; 100527963; 338 hits in 969 CRISPR screens.
DR BioGRID-ORCS; 11243; 716 hits in 1043 CRISPR screens.
DR ChiTaRS; PMF1; human.
DR GeneWiki; Polyamine-modulated_factor_1; -.
DR Pharos; Q6P1K2; Tbio.
DR PRO; PR:Q6P1K2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6P1K2; protein.
DR Bgee; ENSG00000160783; Expressed in hindlimb stylopod muscle and 202 other tissues.
DR ExpressionAtlas; Q6P1K2; baseline and differential.
DR Genevisible; Q6P1K2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0000444; C:MIS12/MIND type complex; IDA: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; IDA:HPA.
DR GO; GO:0005667; C:transcription regulator complex; TAS:ProtInc.
DR GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR007128; PMF1/Nnf1.
DR PANTHER; PTHR15459; PTHR15459; 1.
DR Pfam; PF03980; Nnf1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; Chromosome partition; Coiled coil; Kinetochore;
KW Mitosis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..205
FT /note="Polyamine-modulated factor 1"
FT /id="PRO_0000248237"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..193
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10419538"
FT /id="VSP_052136"
FT VAR_SEQ 55..89
FT /note="YQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIR -> SPLLHWDGSAGPR
FT LPSGGQSVKQAFSWAACRLPQGRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16710414"
FT /id="VSP_052137"
FT VAR_SEQ 123..205
FT /note="WRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVE
FT ELQLQVQAQQQAWQALHREQRELVAVLREPE -> CNGTPCGAMCRNRRPRTSSWQMPS
FT WQGGGRWRSCSYRSRPSSRPGRCEAQRCRVQQRCSLCVQAGGQRGSEETQALPVSMAGS
FT PSPLPGSPGAQEGGV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16710414"
FT /id="VSP_052138"
FT VAR_SEQ 123..205
FT /note="WRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVE
FT ELQLQVQAQQQAWQALHREQRELVAVLREPE -> CNGTPCGAMCRNRRPRTSSWQMPS
FT WQGGGRWRSCSYRSRPSSRPGRLYTENRGSWLLC (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044638"
FT VAR_SEQ 124..175
FT /note="RPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVEE
FT -> CEAQRCRVQQRCSLCVQAGGQRGSEETQALPVSMAGSPSPLPGSPGAQEGGV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052139"
FT VAR_SEQ 176..205
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052140"
FT VARIANT 75
FT /note="Q -> R (in dbSNP:rs1052053)"
FT /evidence="ECO:0000269|PubMed:10419538,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_034147"
FT VARIANT 137
FT /note="M -> I (in dbSNP:rs1052067)"
FT /evidence="ECO:0000269|PubMed:10419538,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034148"
FT CONFLICT 2
FT /note="A -> G (in Ref. 6; CAH10730)"
FT /evidence="ECO:0000305"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 70..96
FT /evidence="ECO:0007829|PDB:5LSJ"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 129..188
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:5LSJ"
SQ SEQUENCE 205 AA; 23339 MW; DAE3A0BF43F14820 CRC64;
MAEASSANLG SGCEEKRHEG SSSESVPPGT TISRVKLLDT MVDTFLQKLV AAGSYQRFTD
CYKCFYQLQP AMTQQIYDKF IAQLQTSIRE EISDIKEEGN LEAVLNALDK IVEEGKVRKE
PAWRPSGIPE KDLHSVMAPY FLQQRDTLRR HVQKQEAENQ QLADAVLAGR RQVEELQLQV
QAQQQAWQAL HREQRELVAV LREPE
