Full text data of PDCL3
PDCL3
(PhLP2A, VIAF1)
[Confidence: low (only semi-automatic identification from reviews)]
Phosducin-like protein 3 (HTPHLP; PhPL3; Viral IAP-associated factor 1; VIAF-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosducin-like protein 3 (HTPHLP; PhPL3; Viral IAP-associated factor 1; VIAF-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H2J4
ID PDCL3_HUMAN Reviewed; 239 AA.
AC Q9H2J4; B2RA00; Q53S68;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Phosducin-like protein 3;
DE AltName: Full=HTPHLP;
DE AltName: Full=PhPL3;
DE AltName: Full=Viral IAP-associated factor 1;
DE Short=VIAF-1;
GN Name=PDCL3; Synonyms=PhLP2A, VIAF1;
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 [MRNA], FUNCTION, INTERACTION WITH VIRAL IAP,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC TISSUE=B-cell;
RX PubMed=15371430; DOI=10.1074/jbc.M409623200;
RA Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E.,
RA Rumble J.M., Balliu B., Duckett C.S.;
RT "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor
RT that modulates caspase activation.";
RL J. Biol. Chem. 279:51091-51099(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH KDR/VEGFR2.
RX PubMed=23792958; DOI=10.1074/jbc.M113.473173;
RA Srinivasan S., Meyer R.D., Lugo R., Rahimi N.;
RT "Identification of PDCL3 as a novel chaperone protein involved in the
RT generation of functional VEGF receptor 2.";
RL J. Biol. Chem. 288:23171-23181(2013).
CC -!- FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor
CC KDR/VEGFR2, controlling its abundance and inhibiting its
CC ubiquitination and degradation. Modulates the activation of
CC caspases during apoptosis. Is a substrate for Orgyia pseudotsugata
CC multicapsid polyhedrosis virus (OpMNPV) IAP-mediated
CC ubiquitination.
CC -!- SUBUNIT: Interacts (via thioredoxin fold region) with KDR/VEGFR2
CC (via juxtamembrane domain). Interacts with OpMNPV IAP3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC spleen, thymus, prostate, testis, ovary, small intestine and
CC colon.
CC -!- SIMILARITY: Belongs to the phosducin family.
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DR EMBL; AF110511; AAG21887.1; -; mRNA.
DR EMBL; AF267853; AAG44722.1; -; mRNA.
DR EMBL; AK313985; BAG36697.1; -; mRNA.
DR EMBL; AC068538; AAX93227.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01838.1; -; Genomic_DNA.
DR EMBL; BC001021; AAH01021.1; -; mRNA.
DR RefSeq; NP_076970.1; NM_024065.4.
DR UniGene; Hs.469459; -.
DR ProteinModelPortal; Q9H2J4; -.
DR SMR; Q9H2J4; 20-207.
DR IntAct; Q9H2J4; 3.
DR STRING; 9606.ENSP00000264254; -.
DR BindingDB; Q9H2J4; -.
DR PhosphoSite; Q9H2J4; -.
DR DMDM; 50401164; -.
DR PaxDb; Q9H2J4; -.
DR PeptideAtlas; Q9H2J4; -.
DR PRIDE; Q9H2J4; -.
DR DNASU; 79031; -.
DR Ensembl; ENST00000264254; ENSP00000264254; ENSG00000115539.
DR GeneID; 79031; -.
DR KEGG; hsa:79031; -.
DR UCSC; uc002tao.2; human.
DR CTD; 79031; -.
DR GeneCards; GC02P101179; -.
DR HGNC; HGNC:28860; PDCL3.
DR HPA; HPA018469; -.
DR HPA; HPA027094; -.
DR MIM; 611678; gene.
DR neXtProt; NX_Q9H2J4; -.
DR PharmGKB; PA134979849; -.
DR eggNOG; NOG294106; -.
DR HOGENOM; HOG000184445; -.
DR HOVERGEN; HBG108238; -.
DR OMA; PLCSLIN; -.
DR PhylomeDB; Q9H2J4; -.
DR GenomeRNAi; 79031; -.
DR NextBio; 67743; -.
DR PRO; PR:Q9H2J4; -.
DR ArrayExpress; Q9H2J4; -.
DR Bgee; Q9H2J4; -.
DR CleanEx; HS_PDCL3; -.
DR Genevestigator; Q9H2J4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR006442; Antitoxin_Phd/YefM.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01552; phd_fam; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Apoptosis; Complete proteome; Cytoplasm;
KW Host-virus interaction; Phosphoprotein; Reference proteome.
FT CHAIN 1 239 Phosducin-like protein 3.
FT /FTId=PRO_0000163758.
FT REGION 91 239 Thioredoxin fold (By similarity).
FT MOD_RES 234 234 Phosphoserine.
FT MOD_RES 236 236 Phosphoserine.
SQ SEQUENCE 239 AA; 27614 MW; D54900B9EEE3A1FB CRC64;
MQDPNADTEW NDILRKKGIL PPKESLKELE EEAEEEQRIL QQSVVKTYED MTLEELEDHE
DEFNEEDERA IEMYRRRRLA EWKATKLKNK FGEVLEISGK DYVQEVTKAG EGLWVILHLY
KQGIPLCALI NQHLSGLARK FPDVKFIKAI STTCIPNYPD RNLPTIFVYL EGDIKAQFIG
PLVFGGMNLT RDELEWKLSE SGAIMTDLEE NPKKPIEDVL LSSVRRSVLM KRDSDSEGD
//
ID PDCL3_HUMAN Reviewed; 239 AA.
AC Q9H2J4; B2RA00; Q53S68;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Phosducin-like protein 3;
DE AltName: Full=HTPHLP;
DE AltName: Full=PhPL3;
DE AltName: Full=Viral IAP-associated factor 1;
DE Short=VIAF-1;
GN Name=PDCL3; Synonyms=PhLP2A, VIAF1;
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 [MRNA], FUNCTION, INTERACTION WITH VIRAL IAP,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC TISSUE=B-cell;
RX PubMed=15371430; DOI=10.1074/jbc.M409623200;
RA Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E.,
RA Rumble J.M., Balliu B., Duckett C.S.;
RT "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor
RT that modulates caspase activation.";
RL J. Biol. Chem. 279:51091-51099(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH KDR/VEGFR2.
RX PubMed=23792958; DOI=10.1074/jbc.M113.473173;
RA Srinivasan S., Meyer R.D., Lugo R., Rahimi N.;
RT "Identification of PDCL3 as a novel chaperone protein involved in the
RT generation of functional VEGF receptor 2.";
RL J. Biol. Chem. 288:23171-23181(2013).
CC -!- FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor
CC KDR/VEGFR2, controlling its abundance and inhibiting its
CC ubiquitination and degradation. Modulates the activation of
CC caspases during apoptosis. Is a substrate for Orgyia pseudotsugata
CC multicapsid polyhedrosis virus (OpMNPV) IAP-mediated
CC ubiquitination.
CC -!- SUBUNIT: Interacts (via thioredoxin fold region) with KDR/VEGFR2
CC (via juxtamembrane domain). Interacts with OpMNPV IAP3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC spleen, thymus, prostate, testis, ovary, small intestine and
CC colon.
CC -!- SIMILARITY: Belongs to the phosducin family.
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DR EMBL; AF110511; AAG21887.1; -; mRNA.
DR EMBL; AF267853; AAG44722.1; -; mRNA.
DR EMBL; AK313985; BAG36697.1; -; mRNA.
DR EMBL; AC068538; AAX93227.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01838.1; -; Genomic_DNA.
DR EMBL; BC001021; AAH01021.1; -; mRNA.
DR RefSeq; NP_076970.1; NM_024065.4.
DR UniGene; Hs.469459; -.
DR ProteinModelPortal; Q9H2J4; -.
DR SMR; Q9H2J4; 20-207.
DR IntAct; Q9H2J4; 3.
DR STRING; 9606.ENSP00000264254; -.
DR BindingDB; Q9H2J4; -.
DR PhosphoSite; Q9H2J4; -.
DR DMDM; 50401164; -.
DR PaxDb; Q9H2J4; -.
DR PeptideAtlas; Q9H2J4; -.
DR PRIDE; Q9H2J4; -.
DR DNASU; 79031; -.
DR Ensembl; ENST00000264254; ENSP00000264254; ENSG00000115539.
DR GeneID; 79031; -.
DR KEGG; hsa:79031; -.
DR UCSC; uc002tao.2; human.
DR CTD; 79031; -.
DR GeneCards; GC02P101179; -.
DR HGNC; HGNC:28860; PDCL3.
DR HPA; HPA018469; -.
DR HPA; HPA027094; -.
DR MIM; 611678; gene.
DR neXtProt; NX_Q9H2J4; -.
DR PharmGKB; PA134979849; -.
DR eggNOG; NOG294106; -.
DR HOGENOM; HOG000184445; -.
DR HOVERGEN; HBG108238; -.
DR OMA; PLCSLIN; -.
DR PhylomeDB; Q9H2J4; -.
DR GenomeRNAi; 79031; -.
DR NextBio; 67743; -.
DR PRO; PR:Q9H2J4; -.
DR ArrayExpress; Q9H2J4; -.
DR Bgee; Q9H2J4; -.
DR CleanEx; HS_PDCL3; -.
DR Genevestigator; Q9H2J4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR006442; Antitoxin_Phd/YefM.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01552; phd_fam; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Apoptosis; Complete proteome; Cytoplasm;
KW Host-virus interaction; Phosphoprotein; Reference proteome.
FT CHAIN 1 239 Phosducin-like protein 3.
FT /FTId=PRO_0000163758.
FT REGION 91 239 Thioredoxin fold (By similarity).
FT MOD_RES 234 234 Phosphoserine.
FT MOD_RES 236 236 Phosphoserine.
SQ SEQUENCE 239 AA; 27614 MW; D54900B9EEE3A1FB CRC64;
MQDPNADTEW NDILRKKGIL PPKESLKELE EEAEEEQRIL QQSVVKTYED MTLEELEDHE
DEFNEEDERA IEMYRRRRLA EWKATKLKNK FGEVLEISGK DYVQEVTKAG EGLWVILHLY
KQGIPLCALI NQHLSGLARK FPDVKFIKAI STTCIPNYPD RNLPTIFVYL EGDIKAQFIG
PLVFGGMNLT RDELEWKLSE SGAIMTDLEE NPKKPIEDVL LSSVRRSVLM KRDSDSEGD
//
MIM
611678
*RECORD*
*FIELD* NO
611678
*FIELD* TI
*611678 PHOSDUCIN-LIKE 3; PDCL3
;;VIRAL IAP-ASSOCIATED FACTOR; VIAF;;
PHLP2A
*FIELD* TX
read more
CLONING
Inhibitor of apoptosis proteins (IAPs) are involved in suppression of
apoptosis, signal transduction, cell cycle control, and gene regulation.
Using baculovirus Op-IAP as bait in a yeast 2-hybrid screen of a B-cell
cDNA library, followed by searching EST databases, Wilkinson et al.
(2004) obtained a full-length cDNA encoding PDCL3, which they designated
VIAF. The deduced 239-amino acid protein has a calculated molecular mass
of 28 kD. Northern blot analysis detected variable expression of a
1.2-kb transcript in all tissues examined. Epitope-tagged and endogenous
VIAF showed cytoplasmic expression. Database analysis revealed
conservation of VIAF in eukaryotes.
Stirling et al. (2007) stated that PDCL3, which they called PHLP2A,
contains an N-terminal helical domain, a central thioredoxin (TXN;
187700)-like fold, and a charged C-terminal domain.
GENE FUNCTION
By yeast 2-hybrid analysis and in vitro protein interaction assays,
Wilkinson et al. (2004) showed that VIAF interacted with baculovirus
Op-IAP and that the C-terminal 128 amino acids of VIAF were sufficient
for the interaction. VIAF overexpression did not alter the ability of
Op-IAP to prevent BAX (600040)-mediated apoptosis. However, suppression
of VIAF by RNA interference in human embryonic kidney cells inhibited
processing of caspase-3 (CASP3; 600636) following induction of the
apoptotic program by BAX. VIAF was a substrate for Op-IAP-mediated
ubiquitination, suggesting that VIAF may be regulated by IAP proteins in
a ubiquitination-dependent manner. Wilkinson et al. (2004) concluded
that VIAF modulates the activation of caspases during apoptosis.
Stirling et al. (2007) showed that, similar to its yeast ortholog, Plp2,
human PHLP2A coprecipitated with the chaperonin containing TCP1 (186980)
complex (CCT; see 605139). Excess human PHLP2A inhibited folding of
actin (see 102610) into its native conformation and caused accumulation
of nonnative actin in both CCT and prefoldin (see 604897) complexes. In
vitro-translated actin and beta-tubulin (TUBB; 191130) precipitated with
PHLP2A, which required the presence of endogenous CCT in the
reticulocyte lysate. Stirling et al. (2007) concluded that PHLP2A
modulates the folding of CCT substrates.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PDCL3
gene to chromosome 2 (TMAP SGC-57056).
*FIELD* RF
1. Stirling, P. C.; Srayko, M.; Takhar, K. S.; Pozniakovsky, A.; Hyman,
A. A.; Leroux, M. R.: Functional interaction between phosducin-like
protein 2 and cytosolic chaperonin is essential for cytoskeletal protein
function and cell cycle progression. Molec. Biol. Cell 18: 2336-2345,
2007.
2. Wilkinson, J. C.; Richter, B. W. M.; Wilkinson, A. S.; Burstein,
E.; Rumble, J. M.; Balliu, B.; Duckett, C. S.: VIAF, a conserved
inhibitor of apoptosis (IAP)-interacting factor that modulates caspase
activation. J. Biol. Chem. 279: 51091-51099, 2004.
*FIELD* CN
Patricia A. Hartz - updated: 01/29/2009
*FIELD* CD
Patricia A. Hartz: 12/14/2007
*FIELD* ED
mgross: 01/29/2009
mgross: 12/14/2007
*RECORD*
*FIELD* NO
611678
*FIELD* TI
*611678 PHOSDUCIN-LIKE 3; PDCL3
;;VIRAL IAP-ASSOCIATED FACTOR; VIAF;;
PHLP2A
*FIELD* TX
read more
CLONING
Inhibitor of apoptosis proteins (IAPs) are involved in suppression of
apoptosis, signal transduction, cell cycle control, and gene regulation.
Using baculovirus Op-IAP as bait in a yeast 2-hybrid screen of a B-cell
cDNA library, followed by searching EST databases, Wilkinson et al.
(2004) obtained a full-length cDNA encoding PDCL3, which they designated
VIAF. The deduced 239-amino acid protein has a calculated molecular mass
of 28 kD. Northern blot analysis detected variable expression of a
1.2-kb transcript in all tissues examined. Epitope-tagged and endogenous
VIAF showed cytoplasmic expression. Database analysis revealed
conservation of VIAF in eukaryotes.
Stirling et al. (2007) stated that PDCL3, which they called PHLP2A,
contains an N-terminal helical domain, a central thioredoxin (TXN;
187700)-like fold, and a charged C-terminal domain.
GENE FUNCTION
By yeast 2-hybrid analysis and in vitro protein interaction assays,
Wilkinson et al. (2004) showed that VIAF interacted with baculovirus
Op-IAP and that the C-terminal 128 amino acids of VIAF were sufficient
for the interaction. VIAF overexpression did not alter the ability of
Op-IAP to prevent BAX (600040)-mediated apoptosis. However, suppression
of VIAF by RNA interference in human embryonic kidney cells inhibited
processing of caspase-3 (CASP3; 600636) following induction of the
apoptotic program by BAX. VIAF was a substrate for Op-IAP-mediated
ubiquitination, suggesting that VIAF may be regulated by IAP proteins in
a ubiquitination-dependent manner. Wilkinson et al. (2004) concluded
that VIAF modulates the activation of caspases during apoptosis.
Stirling et al. (2007) showed that, similar to its yeast ortholog, Plp2,
human PHLP2A coprecipitated with the chaperonin containing TCP1 (186980)
complex (CCT; see 605139). Excess human PHLP2A inhibited folding of
actin (see 102610) into its native conformation and caused accumulation
of nonnative actin in both CCT and prefoldin (see 604897) complexes. In
vitro-translated actin and beta-tubulin (TUBB; 191130) precipitated with
PHLP2A, which required the presence of endogenous CCT in the
reticulocyte lysate. Stirling et al. (2007) concluded that PHLP2A
modulates the folding of CCT substrates.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PDCL3
gene to chromosome 2 (TMAP SGC-57056).
*FIELD* RF
1. Stirling, P. C.; Srayko, M.; Takhar, K. S.; Pozniakovsky, A.; Hyman,
A. A.; Leroux, M. R.: Functional interaction between phosducin-like
protein 2 and cytosolic chaperonin is essential for cytoskeletal protein
function and cell cycle progression. Molec. Biol. Cell 18: 2336-2345,
2007.
2. Wilkinson, J. C.; Richter, B. W. M.; Wilkinson, A. S.; Burstein,
E.; Rumble, J. M.; Balliu, B.; Duckett, C. S.: VIAF, a conserved
inhibitor of apoptosis (IAP)-interacting factor that modulates caspase
activation. J. Biol. Chem. 279: 51091-51099, 2004.
*FIELD* CN
Patricia A. Hartz - updated: 01/29/2009
*FIELD* CD
Patricia A. Hartz: 12/14/2007
*FIELD* ED
mgross: 01/29/2009
mgross: 12/14/2007