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Polyamine-modulated factor 1 (PMF-1)

 PMF1_HUMAN              Reviewed;         205 AA.
Q6P1K2; A8K0C5; Q5TCJ8; Q5TCJ9; Q5TCK0; Q5TCK1; Q5TCK3; Q69YZ9;
Q6PHR4; Q6ZVE6; Q86VJ6; Q8N4T6; Q9UBQ3;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 2.
12-SEP-2018, entry version 132.
RecName: Full=Polyamine-modulated factor 1;
Short=PMF-1;
Name=PMF1 {ECO:0000312|EMBL:AAH65031.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD50081.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
[MRNA] OF 4-205 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INDUCTION,
AND VARIANTS ARG-75 AND ILE-137.
TISSUE=Lung carcinoma {ECO:0000312|EMBL:AAD50081.1};
PubMed=10419538; DOI=10.1074/jbc.274.31.22095;
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
"Cloning and characterization of human polyamine-modulated factor-1, a
transcriptional cofactor that regulates the transcription of the
spermidine/spermine N(1)-acetyltransferase gene.";
J. Biol. Chem. 274:22095-22101(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT
ARG-75.
TISSUE=Cerebellum, and Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4] {ECO:0000305, ECO:0000312|EMBL:CAH10730.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:AAH65031.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
VARIANTS ARG-75 AND ILE-137.
TISSUE=Colon {ECO:0000312|EMBL:AAH56417.1},
Skin {ECO:0000312|EMBL:AAH65031.1},
Testis {ECO:0000312|EMBL:AAH50735.1}, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-205 (ISOFORM 1).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7] {ECO:0000305}
FUNCTION, AND INTERACTION WITH NFE2L2.
PubMed=11256947; DOI=10.1042/0264-6021:3550045;
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
"Characterization of the interaction between the transcription factors
human polyamine modulated factor (PMF-1) and NF-E2-related factor 2
(Nrf-2) in the transcriptional regulation of the spermidine/spermine
N1-acetyltransferase (SSAT) gene.";
Biochem. J. 355:45-49(2001).
[8] {ECO:0000305}
INTERACTION WITH COPS7A.
PubMed=12020345; DOI=10.1042/BJ20020211;
Wang Y., Devereux W., Stewart T.M., Casero R.A. Jr.;
"Polyamine-modulated factor 1 binds to the human homologue of the 7a
subunit of the Arabidopsis COP9 signalosome: implications in gene
expression.";
Biochem. J. 366:79-86(2002).
[9] {ECO:0000305}
FUNCTION, INTERACTION WITH DSN1 AND MIS12, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15502821; DOI=10.1038/ncb1187;
Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y.,
Yanagida M.;
"A conserved Mis12 centromere complex is linked to heterochromatic HP1
and outer kinetochore protein Zwint-1.";
Nat. Cell Biol. 6:1135-1141(2004).
[10]
FUNCTION, COMPONENT OF MIS12 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=16585270; DOI=10.1083/jcb.200509158;
Kline S.L., Cheeseman I.M., Hori T., Fukagawa T., Desai A.;
"The human Mis12 complex is required for kinetochore assembly and
proper chromosome segregation.";
J. Cell Biol. 173:9-17(2006).
-!- FUNCTION: Part of the MIS12 complex which is required for normal
chromosome alignment and segregation and kinetochore formation
during mitosis. May act as a cotranscription partner of NFE2L2
involved in regulation of polyamine-induced transcription of SSAT.
{ECO:0000269|PubMed:10419538, ECO:0000269|PubMed:11256947,
ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.
-!- SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1,
NSL1 and PMF1. Interacts with COPS7A. Interacts via its coiled-
coil domain with the leucine-zipper domain of NFE2L2. The
interaction with NFE2L2 is required for the transcriptional
regulation of SSAT. {ECO:0000269|PubMed:11256947,
ECO:0000269|PubMed:12020345, ECO:0000269|PubMed:15502821}.
-!- INTERACTION:
Q9H081:MIS12; NbExp=10; IntAct=EBI-713832, EBI-1001205;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-713832, EBI-739895;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585270}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16585270}.
Note=Associated with the kinetochore.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1 {ECO:0000269|PubMed:10419538};
IsoId=Q6P1K2-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:16710414};
IsoId=Q6P1K2-2; Sequence=VSP_052137;
Note=Gene prediction based on EST data. {ECO:0000305};
Name=3 {ECO:0000269|PubMed:15489334};
IsoId=Q6P1K2-3; Sequence=VSP_052139, VSP_052140;
Note=No experimental confirmation available. {ECO:0000305};
Name=4 {ECO:0000269|PubMed:10419538};
IsoId=Q6P1K2-4; Sequence=VSP_052136;
Name=5 {ECO:0000269|PubMed:16710414};
IsoId=Q6P1K2-5; Sequence=VSP_052138;
Note=Gene prediction based on EST data. {ECO:0000305};
Name=6;
IsoId=Q6P1K2-6; Sequence=VSP_044638;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest levels of expression in heart and
skeletal muscle, with significant levels expressed in kidney and
liver. {ECO:0000269|PubMed:10419538}.
-!- INDUCTION: By polyamine analogs in analog-sensitive H157 cells.
{ECO:0000269|PubMed:10419538}.
-!- SEQUENCE CAUTION:
Sequence=AAD50081.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH10730.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH10730.1; Type=Frameshift; Positions=75; Evidence={ECO:0000305};
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EMBL; AF141309; AAD50080.1; -; Genomic_DNA.
EMBL; AF141308; AAD50080.1; JOINED; Genomic_DNA.
EMBL; AF141310; AAD50081.1; ALT_INIT; mRNA.
EMBL; AK124646; BAC85916.1; -; mRNA.
EMBL; AK289490; BAF82179.1; -; mRNA.
EMBL; AK290260; BAF82949.1; -; mRNA.
EMBL; AL135927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52989.1; -; Genomic_DNA.
EMBL; CH471121; EAW52990.1; -; Genomic_DNA.
EMBL; BC033656; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC050735; AAH50735.1; -; mRNA.
EMBL; BC056417; AAH56417.1; -; mRNA.
EMBL; BC065031; AAH65031.1; -; mRNA.
EMBL; AL080101; CAH10730.1; ALT_SEQ; mRNA.
CCDS; CCDS30886.1; -. [Q6P1K2-1]
CCDS; CCDS55648.1; -. [Q6P1K2-2]
CCDS; CCDS55649.1; -. [Q6P1K2-6]
RefSeq; NP_001186582.1; NM_001199653.1. [Q6P1K2-6]
RefSeq; NP_001186583.1; NM_001199654.1. [Q6P1K2-2]
RefSeq; NP_001186590.1; NM_001199661.1. [Q6P1K2-5]
RefSeq; NP_001186592.1; NM_001199663.1. [Q6P1K2-3]
RefSeq; NP_009152.2; NM_007221.3. [Q6P1K2-1]
UniGene; Hs.530479; -.
UniGene; Hs.654541; -.
PDB; 5LSJ; X-ray; 3.25 A; B/E=31-205.
PDB; 5LSK; X-ray; 3.50 A; B=31-205.
PDBsum; 5LSJ; -.
PDBsum; 5LSK; -.
ProteinModelPortal; Q6P1K2; -.
SMR; Q6P1K2; -.
BioGrid; 116405; 64.
BioGrid; 1529341; 1.
CORUM; Q6P1K2; -.
IntAct; Q6P1K2; 38.
MINT; Q6P1K2; -.
STRING; 9606.ENSP00000458021; -.
iPTMnet; Q6P1K2; -.
PhosphoSitePlus; Q6P1K2; -.
BioMuta; PMF1; -.
DMDM; 114152119; -.
EPD; Q6P1K2; -.
MaxQB; Q6P1K2; -.
PaxDb; Q6P1K2; -.
PeptideAtlas; Q6P1K2; -.
PRIDE; Q6P1K2; -.
ProteomicsDB; 66837; -.
ProteomicsDB; 66838; -. [Q6P1K2-2]
ProteomicsDB; 66839; -. [Q6P1K2-3]
ProteomicsDB; 66840; -. [Q6P1K2-4]
ProteomicsDB; 66841; -. [Q6P1K2-5]
DNASU; 11243; -.
Ensembl; ENST00000368273; ENSP00000357256; ENSG00000160783. [Q6P1K2-2]
Ensembl; ENST00000368277; ENSP00000357260; ENSG00000160783. [Q6P1K2-1]
Ensembl; ENST00000368279; ENSP00000357262; ENSG00000160783. [Q6P1K2-6]
GeneID; 100527963; -.
GeneID; 11243; -.
KEGG; hsa:100527963; -.
KEGG; hsa:11243; -.
UCSC; uc001fnq.4; human. [Q6P1K2-1]
CTD; 100527963; -.
CTD; 11243; -.
DisGeNET; 100527963; -.
DisGeNET; 11243; -.
EuPathDB; HostDB:ENSG00000160783.19; -.
GeneCards; PMF1; -.
HGNC; HGNC:9112; PMF1.
HPA; HPA034583; -.
HPA; HPA071854; -.
MIM; 609176; gene.
neXtProt; NX_Q6P1K2; -.
OpenTargets; ENSG00000160783; -.
OpenTargets; ENSG00000260238; -.
PharmGKB; PA33438; -.
eggNOG; ENOG410IWZA; Eukaryota.
eggNOG; ENOG4111Q9B; LUCA.
GeneTree; ENSGT00390000006469; -.
HOGENOM; HOG000012991; -.
HOVERGEN; HBG058607; -.
InParanoid; Q6P1K2; -.
KO; K11546; -.
OMA; YQLQPEV; -.
OrthoDB; EOG091G0WAU; -.
PhylomeDB; Q6P1K2; -.
TreeFam; TF333180; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
ChiTaRS; PMF1; human.
GeneWiki; Polyamine-modulated_factor_1; -.
PRO; PR:Q6P1K2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000160783; Expressed in 223 organ(s), highest expression level in muscle of leg.
ExpressionAtlas; Q6P1K2; baseline and differential.
Genevisible; Q6P1K2; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IDA:WormBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0000444; C:MIS12/MIND type complex; IDA:UniProtKB.
GO; GO:0000818; C:nuclear MIS12/MIND complex; IEA:InterPro.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; TAS:ProtInc.
GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
InterPro; IPR007128; PMF1/Nnf1.
PANTHER; PTHR15459; PTHR15459; 1.
Pfam; PF03980; Nnf1; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell cycle;
Cell division; Centromere; Chromosome; Chromosome partition;
Coiled coil; Complete proteome; Kinetochore; Mitosis; Nucleus;
Polymorphism; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 205 Polyamine-modulated factor 1.
/FTId=PRO_0000248237.
COILED 141 193 {ECO:0000255}.
VAR_SEQ 1 40 Missing (in isoform 4).
{ECO:0000303|PubMed:10419538}.
/FTId=VSP_052136.
VAR_SEQ 55 89 YQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIR -> SP
LLHWDGSAGPRLPSGGQSVKQAFSWAACRLPQGRK (in
isoform 2).
{ECO:0000303|PubMed:16710414}.
/FTId=VSP_052137.
VAR_SEQ 123 205 WRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLA
DAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREP
E -> CNGTPCGAMCRNRRPRTSSWQMPSWQGGGRWRSCSY
RSRPSSRPGRCEAQRCRVQQRCSLCVQAGGQRGSEETQALP
VSMAGSPSPLPGSPGAQEGGV (in isoform 5).
{ECO:0000303|PubMed:16710414}.
/FTId=VSP_052138.
VAR_SEQ 123 205 WRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLA
DAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREP
E -> CNGTPCGAMCRNRRPRTSSWQMPSWQGGGRWRSCSY
RSRPSSRPGRLYTENRGSWLLC (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044638.
VAR_SEQ 124 175 RPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLAD
AVLAGRRQVEE -> CEAQRCRVQQRCSLCVQAGGQRGSEE
TQALPVSMAGSPSPLPGSPGAQEGGV (in isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_052139.
VAR_SEQ 176 205 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_052140.
VARIANT 75 75 Q -> R (in dbSNP:rs1052053).
{ECO:0000269|PubMed:10419538,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_034147.
VARIANT 137 137 M -> I (in dbSNP:rs1052067).
{ECO:0000269|PubMed:10419538,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_034148.
CONFLICT 2 2 A -> G (in Ref. 6; CAH10730).
{ECO:0000305}.
TURN 32 34 {ECO:0000244|PDB:5LSJ}.
HELIX 35 51 {ECO:0000244|PDB:5LSJ}.
HELIX 56 61 {ECO:0000244|PDB:5LSJ}.
HELIX 63 66 {ECO:0000244|PDB:5LSJ}.
HELIX 70 96 {ECO:0000244|PDB:5LSJ}.
TURN 97 100 {ECO:0000244|PDB:5LSJ}.
HELIX 101 115 {ECO:0000244|PDB:5LSJ}.
HELIX 129 188 {ECO:0000244|PDB:5LSJ}.
HELIX 190 200 {ECO:0000244|PDB:5LSJ}.
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


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GWB-F276BC Anti- PMF1 (polyamine-modulated factor 1) Antibody
CSB-EL018234BO Bovine Polyamine-modulated factor 1(PMF1) ELISA kit 96T
PMFBP_RAT Rat ELISA Kit FOR Polyamine-modulated factor 1-binding protein 1 96T
CSB-EL018234MO Mouse Polyamine-modulated factor 1(PMF1) ELISA kit 96T
18-003-43428 Polyamine-modulated factor 1 - HCG1999356. isoform CRA_c Polyclonal 0.05 mg Aff Pur
YHB0868Ra Rat Polyamine-modulated factor 1-binding protein 1,PMFBP1 ELISA kit 48T
CSB-EL018234MO Mouse Polyamine-modulated factor 1(PMF1) ELISA kit SpeciesMouse 96T
CSB-EL018234BO Bovine Polyamine-modulated factor 1(PMF1) ELISA kit SpeciesBovine 96T
CSB-EL018234HU Human Polyamine-modulated factor 1(PMF1) ELISA kit SpeciesHuman 96T
E0979Ra Rat Polyamine-modulated factor 1-binding protein 1,PMFBP1 ELISA kit 48T
CSB-EL018235RA Rat Polyamine-modulated factor 1-binding protein 1(PMFBP1) ELISA kit 96T
18-003-43497 Polyamine-modulated factor 1 - HCG1999356. isoform CRA_c Polyclonal 0.05 mg Aff Pur
PMM1 PMFBP1 Gene polyamine modulated factor 1 binding protein 1
PMFBP_MOUSE Mouse ELISA Kit FOR Polyamine-modulated factor 1-binding protein 1 96T
E0980Ra Rat Polyamine-modulated factor 1-binding protein 1,PMFBP1 ELISA kit 96T
201-20-4315 PMFBP1{polyamine modulated factor 1 binding protein 1}rabbit.pAb 0.2ml
E0980Ra Rat Polyamine-modulated factor 1-binding protein 1,PMFBP1 ELISA kit 48T
YHB0868Ra Rat Polyamine-modulated factor 1-binding protein 1,PMFBP1 ELISA kit 96T


 

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