Full text data of PFDN2
PFDN2
(PFD2)
[Confidence: low (only semi-automatic identification from reviews)]
Prefoldin subunit 2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prefoldin subunit 2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UHV9
ID PFD2_HUMAN Reviewed; 154 AA.
AC Q9UHV9; Q9P0P7; Q9UN05;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Prefoldin subunit 2;
GN Name=PFDN2; Synonyms=PFD2; ORFNames=HSPC231;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Xu Y., Yu Y., Fang C., Zhang H., Ying H., Yan J., Chang Y.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=9630229; DOI=10.1016/S0092-8674(00)81446-4;
RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
RA Klein H.L., Cowan N.J.;
RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
RT chaperonin.";
RL Cell 93:863-873(1998).
RN [6]
RP INTERACTION WITH URI1, AND SUBCELLULAR LOCATION.
RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
RA Aebersold R., Hess D., Krek W.;
RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
RT activates a negative feedback program that counters S6K1 survival
RT signaling.";
RL Mol. Cell 28:28-40(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide
CC chain and promotes folding in an environment in which there are
CC many competing pathways for nonnative proteins.
CC -!- SUBUNIT: Binds to c-Myc; interacts with its N-terminal domain (By
CC similarity). Heterohexamer of two PFD-alpha type and four PFD-beta
CC type subunits. Interacts with URI1; the interaction is
CC phosphorylation-dependent and occurs in a growth-dependent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36151.1; Type=Frameshift; Positions=8, 23, 28, 34;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF117237; AAF17218.1; -; mRNA.
DR EMBL; AF165883; AAD47084.1; -; mRNA.
DR EMBL; AF151065; AAF36151.1; ALT_FRAME; mRNA.
DR EMBL; BC012464; AAH12464.1; -; mRNA.
DR EMBL; BC047042; AAH47042.1; -; mRNA.
DR RefSeq; NP_036526.2; NM_012394.3.
DR UniGene; Hs.492516; -.
DR ProteinModelPortal; Q9UHV9; -.
DR SMR; Q9UHV9; 22-123.
DR DIP; DIP-27557N; -.
DR IntAct; Q9UHV9; 15.
DR MINT; MINT-1132228; -.
DR STRING; 9606.ENSP00000356989; -.
DR PhosphoSite; Q9UHV9; -.
DR DMDM; 12643887; -.
DR PaxDb; Q9UHV9; -.
DR PeptideAtlas; Q9UHV9; -.
DR PRIDE; Q9UHV9; -.
DR DNASU; 5202; -.
DR Ensembl; ENST00000368010; ENSP00000356989; ENSG00000143256.
DR GeneID; 5202; -.
DR KEGG; hsa:5202; -.
DR UCSC; uc001fxu.3; human.
DR CTD; 5202; -.
DR GeneCards; GC01M161070; -.
DR HGNC; HGNC:8867; PFDN2.
DR HPA; HPA028700; -.
DR MIM; 613466; gene.
DR neXtProt; NX_Q9UHV9; -.
DR PharmGKB; PA33208; -.
DR eggNOG; NOG331971; -.
DR HOGENOM; HOG000211843; -.
DR HOVERGEN; HBG008172; -.
DR InParanoid; Q9UHV9; -.
DR KO; K09549; -.
DR OMA; VDPSRKC; -.
DR OrthoDB; EOG74XS8Z; -.
DR PhylomeDB; Q9UHV9; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GeneWiki; PFDN2; -.
DR GenomeRNAi; 5202; -.
DR NextBio; 20118; -.
DR PRO; PR:Q9UHV9; -.
DR ArrayExpress; Q9UHV9; -.
DR Bgee; Q9UHV9; -.
DR CleanEx; HS_PFDN2; -.
DR Genevestigator; Q9UHV9; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016272; C:prefoldin complex; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR InterPro; IPR027235; PFD2.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR13303; PTHR13303; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR SUPFAM; SSF46579; SSF46579; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Cytoplasm; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1 154 Prefoldin subunit 2.
FT /FTId=PRO_0000124835.
FT CONFLICT 14 22 SGAGKGAVS -> TPRRGRGRCP (in Ref. 2;
FT AAD47084).
FT CONFLICT 15 15 Missing (in Ref. 3; AAF36151).
FT CONFLICT 29 34 GFNRLR -> SFNAF (in Ref. 3; AAF36151).
SQ SEQUENCE 154 AA; 16648 MW; 2FC68A7425412198 CRC64;
MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE
KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS
//
ID PFD2_HUMAN Reviewed; 154 AA.
AC Q9UHV9; Q9P0P7; Q9UN05;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Prefoldin subunit 2;
GN Name=PFDN2; Synonyms=PFD2; ORFNames=HSPC231;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Xu Y., Yu Y., Fang C., Zhang H., Ying H., Yan J., Chang Y.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=9630229; DOI=10.1016/S0092-8674(00)81446-4;
RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
RA Klein H.L., Cowan N.J.;
RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
RT chaperonin.";
RL Cell 93:863-873(1998).
RN [6]
RP INTERACTION WITH URI1, AND SUBCELLULAR LOCATION.
RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
RA Aebersold R., Hess D., Krek W.;
RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
RT activates a negative feedback program that counters S6K1 survival
RT signaling.";
RL Mol. Cell 28:28-40(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide
CC chain and promotes folding in an environment in which there are
CC many competing pathways for nonnative proteins.
CC -!- SUBUNIT: Binds to c-Myc; interacts with its N-terminal domain (By
CC similarity). Heterohexamer of two PFD-alpha type and four PFD-beta
CC type subunits. Interacts with URI1; the interaction is
CC phosphorylation-dependent and occurs in a growth-dependent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36151.1; Type=Frameshift; Positions=8, 23, 28, 34;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF117237; AAF17218.1; -; mRNA.
DR EMBL; AF165883; AAD47084.1; -; mRNA.
DR EMBL; AF151065; AAF36151.1; ALT_FRAME; mRNA.
DR EMBL; BC012464; AAH12464.1; -; mRNA.
DR EMBL; BC047042; AAH47042.1; -; mRNA.
DR RefSeq; NP_036526.2; NM_012394.3.
DR UniGene; Hs.492516; -.
DR ProteinModelPortal; Q9UHV9; -.
DR SMR; Q9UHV9; 22-123.
DR DIP; DIP-27557N; -.
DR IntAct; Q9UHV9; 15.
DR MINT; MINT-1132228; -.
DR STRING; 9606.ENSP00000356989; -.
DR PhosphoSite; Q9UHV9; -.
DR DMDM; 12643887; -.
DR PaxDb; Q9UHV9; -.
DR PeptideAtlas; Q9UHV9; -.
DR PRIDE; Q9UHV9; -.
DR DNASU; 5202; -.
DR Ensembl; ENST00000368010; ENSP00000356989; ENSG00000143256.
DR GeneID; 5202; -.
DR KEGG; hsa:5202; -.
DR UCSC; uc001fxu.3; human.
DR CTD; 5202; -.
DR GeneCards; GC01M161070; -.
DR HGNC; HGNC:8867; PFDN2.
DR HPA; HPA028700; -.
DR MIM; 613466; gene.
DR neXtProt; NX_Q9UHV9; -.
DR PharmGKB; PA33208; -.
DR eggNOG; NOG331971; -.
DR HOGENOM; HOG000211843; -.
DR HOVERGEN; HBG008172; -.
DR InParanoid; Q9UHV9; -.
DR KO; K09549; -.
DR OMA; VDPSRKC; -.
DR OrthoDB; EOG74XS8Z; -.
DR PhylomeDB; Q9UHV9; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GeneWiki; PFDN2; -.
DR GenomeRNAi; 5202; -.
DR NextBio; 20118; -.
DR PRO; PR:Q9UHV9; -.
DR ArrayExpress; Q9UHV9; -.
DR Bgee; Q9UHV9; -.
DR CleanEx; HS_PFDN2; -.
DR Genevestigator; Q9UHV9; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016272; C:prefoldin complex; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR InterPro; IPR027235; PFD2.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR13303; PTHR13303; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR SUPFAM; SSF46579; SSF46579; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Cytoplasm; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1 154 Prefoldin subunit 2.
FT /FTId=PRO_0000124835.
FT CONFLICT 14 22 SGAGKGAVS -> TPRRGRGRCP (in Ref. 2;
FT AAD47084).
FT CONFLICT 15 15 Missing (in Ref. 3; AAF36151).
FT CONFLICT 29 34 GFNRLR -> SFNAF (in Ref. 3; AAF36151).
SQ SEQUENCE 154 AA; 16648 MW; 2FC68A7425412198 CRC64;
MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE
KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS
//
MIM
613466
*RECORD*
*FIELD* NO
613466
*FIELD* TI
*613466 PREFOLDIN 2; PFDN2
*FIELD* TX
CLONING
Vainberg et al. (1998) purified the prefoldin heterohexameric chaperone
read morefrom bovine testis and, by database analysis, identified mouse and S.
cerevisiae Pfdn2. The deduced mouse protein contains 154 amino acids.
GENE FUNCTION
Hutchins et al. (2010) showed that mouse Pfdn2 associated with the
centralspindlin complex (see KIF23, 605064) in transfected HeLa cells.
This complex is believed to have a role in spindle assembly and
cytokinesis.
MAPPING
Hartz (2010) mapped the PFDN2 gene to chromosome 1q23.3 based on an
alignment of the PFDN2 sequence (GenBank GENBANK AF165883) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 6/29/2010.
2. Hutchins, J. R. A.; Toyoda, Y.; Hegemann, B.; Poser, I.; Heriche,
J.-K.; Sykora, M. M.; Augsburg, M.; Hudecz, O.; Buschhorn, B. A.;
Bulkescher, J.; Conrad, C.; Comartin, D.; and 18 others: Systematic
analysis of human protein complexes identifies chromosome segregation
proteins. Science 328: 593-599, 2010.
3. 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.
*FIELD* CD
Patricia A. Hartz: 6/29/2010
*FIELD* ED
carol: 06/29/2010
*RECORD*
*FIELD* NO
613466
*FIELD* TI
*613466 PREFOLDIN 2; PFDN2
*FIELD* TX
CLONING
Vainberg et al. (1998) purified the prefoldin heterohexameric chaperone
read morefrom bovine testis and, by database analysis, identified mouse and S.
cerevisiae Pfdn2. The deduced mouse protein contains 154 amino acids.
GENE FUNCTION
Hutchins et al. (2010) showed that mouse Pfdn2 associated with the
centralspindlin complex (see KIF23, 605064) in transfected HeLa cells.
This complex is believed to have a role in spindle assembly and
cytokinesis.
MAPPING
Hartz (2010) mapped the PFDN2 gene to chromosome 1q23.3 based on an
alignment of the PFDN2 sequence (GenBank GENBANK AF165883) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 6/29/2010.
2. Hutchins, J. R. A.; Toyoda, Y.; Hegemann, B.; Poser, I.; Heriche,
J.-K.; Sykora, M. M.; Augsburg, M.; Hudecz, O.; Buschhorn, B. A.;
Bulkescher, J.; Conrad, C.; Comartin, D.; and 18 others: Systematic
analysis of human protein complexes identifies chromosome segregation
proteins. Science 328: 593-599, 2010.
3. 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.
*FIELD* CD
Patricia A. Hartz: 6/29/2010
*FIELD* ED
carol: 06/29/2010