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Prefoldin subunit 5 (Myc modulator 1) (c-Myc-binding protein Mm-1)

 PFD5_HUMAN              Reviewed;         154 AA.
Q99471; A8K9A8; Q54AA8; Q9C083; Q9C084;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
18-JUL-2018, entry version 166.
RecName: Full=Prefoldin subunit 5;
AltName: Full=Myc modulator 1;
AltName: Full=c-Myc-binding protein Mm-1;
Name=PFDN5; Synonyms=MM1, PFD5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9792694; DOI=10.1074/jbc.273.45.29794;
Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.;
"MM-1, a novel c-Myc-associating protein that represses
transcriptional activity of c-Myc.";
J. Biol. Chem. 273:29794-29800(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Blood, and Fibroblast;
PubMed=11567024; DOI=10.1074/jbc.M106127200;
Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H.,
Iguchi-Ariga S.M.M., Nagashima K., Ariga H.;
"MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor
in leukemia/lymphoma and tongue cancer.";
J. Biol. Chem. 276:45137-45144(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
AND ALTERNATIVE SPLICING.
TISSUE=B-cell, and Placenta;
PubMed=16173081; DOI=10.1002/jcb.20619;
Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M.,
Ariga H.;
"Distinct localizations and repression activities of MM-1 isoforms
toward c-Myc.";
J. Cell. Biochem. 97:145-155(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thymus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[9]
FUNCTION.
PubMed=9630229; DOI=10.1016/S0092-8674(00)81446-4;
Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
Klein H.L., Cowan N.J.;
"Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
chaperonin.";
Cell 93:863-873(1998).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
transfers target proteins to it. Binds to nascent polypeptide
chain and promotes folding in an environment in which there are
many competing pathways for nonnative proteins. Represses the
transcriptional activity of MYC. {ECO:0000269|PubMed:9630229}.
-!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
type subunits. Binds to MYC; interacts with its N-terminal domain.
-!- INTERACTION:
Q13137:CALCOCO2; NbExp=4; IntAct=EBI-357275, EBI-739580;
O76003:GLRX3; NbExp=3; IntAct=EBI-357275, EBI-374781;
Q9UKT9:IKZF3; NbExp=5; IntAct=EBI-357275, EBI-747204;
Q96MT4:LINC01600; NbExp=4; IntAct=EBI-357275, EBI-12804988;
Q9UHV9:PFDN2; NbExp=3; IntAct=EBI-357275, EBI-359873;
P61289:PSME3; NbExp=5; IntAct=EBI-357275, EBI-355546;
P61758:VBP1; NbExp=4; IntAct=EBI-357275, EBI-357430;
Q9DUN1:vIRF-3 (xeno); NbExp=8; IntAct=EBI-357275, EBI-1647907;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=MM1-alpha;
IsoId=Q99471-1; Sequence=Displayed;
Name=2; Synonyms=MM1-beta;
IsoId=Q99471-2; Sequence=VSP_043104;
Note=Does not repress transcription activity of MYC.;
Name=3; Synonyms=MM1-gamma;
IsoId=Q99471-3; Sequence=VSP_043103;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal
muscle and moderately in other tissues.
-!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA14006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D89667; BAA14006.1; ALT_INIT; mRNA.
EMBL; AB055802; BAB32643.1; -; Genomic_DNA.
EMBL; AB055803; BAB32644.1; -; mRNA.
EMBL; AB055804; BAB32645.1; -; mRNA.
EMBL; AB055805; BAB32646.1; -; mRNA.
EMBL; BT007195; AAP35859.1; -; mRNA.
EMBL; AK292623; BAF85312.1; -; mRNA.
EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96683.1; -; Genomic_DNA.
EMBL; CH471054; EAW96685.1; -; Genomic_DNA.
EMBL; BC003373; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC062671; AAH62671.1; -; mRNA.
CCDS; CCDS8853.1; -. [Q99471-1]
CCDS; CCDS8854.1; -. [Q99471-3]
RefSeq; NP_002615.2; NM_002624.3. [Q99471-1]
RefSeq; NP_665904.1; NM_145897.2. [Q99471-3]
UniGene; Hs.655327; -.
ProteinModelPortal; Q99471; -.
SMR; Q99471; -.
BioGrid; 111226; 80.
CORUM; Q99471; -.
DIP; DIP-28155N; -.
IntAct; Q99471; 150.
MINT; Q99471; -.
STRING; 9606.ENSP00000334188; -.
iPTMnet; Q99471; -.
PhosphoSitePlus; Q99471; -.
BioMuta; PFDN5; -.
DMDM; 12231038; -.
OGP; Q99471; -.
EPD; Q99471; -.
MaxQB; Q99471; -.
PaxDb; Q99471; -.
PeptideAtlas; Q99471; -.
PRIDE; Q99471; -.
ProteomicsDB; 78287; -.
ProteomicsDB; 78288; -. [Q99471-2]
ProteomicsDB; 78289; -. [Q99471-3]
TopDownProteomics; Q99471-1; -. [Q99471-1]
TopDownProteomics; Q99471-3; -. [Q99471-3]
DNASU; 5204; -.
Ensembl; ENST00000243040; ENSP00000243040; ENSG00000123349. [Q99471-2]
Ensembl; ENST00000334478; ENSP00000334188; ENSG00000123349. [Q99471-1]
Ensembl; ENST00000351500; ENSP00000266964; ENSG00000123349. [Q99471-3]
Ensembl; ENST00000551018; ENSP00000447942; ENSG00000123349. [Q99471-1]
GeneID; 5204; -.
KEGG; hsa:5204; -.
UCSC; uc001scl.5; human. [Q99471-1]
CTD; 5204; -.
DisGeNET; 5204; -.
EuPathDB; HostDB:ENSG00000123349.13; -.
GeneCards; PFDN5; -.
HGNC; HGNC:8869; PFDN5.
HPA; HPA008587; -.
MIM; 604899; gene.
neXtProt; NX_Q99471; -.
OpenTargets; ENSG00000123349; -.
PharmGKB; PA33210; -.
eggNOG; KOG3048; Eukaryota.
eggNOG; COG1730; LUCA.
GeneTree; ENSGT00390000008783; -.
HOGENOM; HOG000207562; -.
HOVERGEN; HBG004539; -.
InParanoid; Q99471; -.
KO; K04797; -.
OMA; FQPDWEN; -.
OrthoDB; EOG091G0TVG; -.
PhylomeDB; Q99471; -.
TreeFam; TF106509; -.
Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
ChiTaRS; PFDN5; human.
GeneWiki; PFDN5; -.
GenomeRNAi; 5204; -.
PRO; PR:Q99471; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123349; -.
CleanEx; HS_PFDN5; -.
ExpressionAtlas; Q99471; baseline and differential.
Genevisible; Q99471; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0016272; C:prefoldin complex; IBA:GO_Central.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
Gene3D; 1.10.287.370; -; 1.
HAMAP; MF_00308; PfdA; 1.
InterPro; IPR011599; PFD_alpha_archaea.
InterPro; IPR009053; Prefoldin.
InterPro; IPR004127; Prefoldin_subunit_alpha.
Pfam; PF02996; Prefoldin; 1.
TIGRFAMs; TIGR00293; TIGR00293; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chaperone; Complete proteome;
Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 154 Prefoldin subunit 5.
/FTId=PRO_0000153661.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 25 69 Missing (in isoform 3).
{ECO:0000303|PubMed:16173081}.
/FTId=VSP_043103.
VAR_SEQ 59 154 GKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDA
KDFFKRKIDFLTKQMEKIQPALQEKHAMKQAVMEMMSQKIQ
QLTALGAAQATAKA -> DVCPWEAA (in isoform
2). {ECO:0000303|PubMed:16173081}.
/FTId=VSP_043104.
SEQUENCE 154 AA; 17328 MW; 0DA1F3644548CB14 CRC64;
MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK
ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA
LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA


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Genprice Inc, Invoices and accounting
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