Full text data of PDAP1
PDAP1
(HASPP28)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
28 kDa heat- and acid-stable phosphoprotein (PDGF-associated protein; PAP; PDGFA-associated protein 1; PAP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
28 kDa heat- and acid-stable phosphoprotein (PDGF-associated protein; PAP; PDGFA-associated protein 1; PAP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q13442
ID HAP28_HUMAN Reviewed; 181 AA.
AC Q13442; D6W5S5; Q92906;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=28 kDa heat- and acid-stable phosphoprotein;
DE AltName: Full=PDGF-associated protein;
DE Short=PAP;
DE AltName: Full=PDGFA-associated protein 1;
DE Short=PAP1;
GN Name=PDAP1; Synonyms=HASPP28;
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].
RC TISSUE=Neuroretina;
RX PubMed=8780057;
RA Fischer W.H., Schubert D.;
RT "Characterization of a novel platelet-derived growth factor-associated
RT protein.";
RL J. Neurochem. 66:2213-2216(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
RA Huang F.L.;
RT "5' flanking sequence of HASPP28.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-57; SER-60;
RP SER-63 AND SER-176, AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63,
RP AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-63 AND SER-176,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-57; SER-60;
RP SER-63 AND SER-176, AND 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND MASS
RP 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).
CC -!- FUNCTION: Enhances PDGFA-stimulated cell growth in fibroblasts,
CC but inhibits the mitogenic effect of PDGFB (By similarity).
CC -!- SIMILARITY: Belongs to the PDAP1 family.
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; U41745; AAC50462.1; -; mRNA.
DR EMBL; AC004922; AAF03506.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76675.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76676.1; -; Genomic_DNA.
DR EMBL; BC000684; AAH00684.1; -; mRNA.
DR EMBL; BC007873; AAH07873.1; -; mRNA.
DR EMBL; U65960; AAB07135.1; -; Genomic_DNA.
DR RefSeq; NP_055706.1; NM_014891.6.
DR UniGene; Hs.632296; -.
DR ProteinModelPortal; Q13442; -.
DR IntAct; Q13442; 6.
DR MINT; MINT-5002803; -.
DR STRING; 9606.ENSP00000222968; -.
DR DrugBank; DB00102; Becaplermin.
DR PhosphoSite; Q13442; -.
DR DMDM; 2498464; -.
DR PaxDb; Q13442; -.
DR PeptideAtlas; Q13442; -.
DR PRIDE; Q13442; -.
DR DNASU; 11333; -.
DR Ensembl; ENST00000350498; ENSP00000222968; ENSG00000106244.
DR GeneID; 11333; -.
DR KEGG; hsa:11333; -.
DR UCSC; uc003uqe.3; human.
DR CTD; 11333; -.
DR GeneCards; GC07M098989; -.
DR HGNC; HGNC:14634; PDAP1.
DR HPA; CAB021103; -.
DR MIM; 607075; gene.
DR neXtProt; NX_Q13442; -.
DR PharmGKB; PA33102; -.
DR eggNOG; NOG313368; -.
DR HOGENOM; HOG000241539; -.
DR HOVERGEN; HBG000319; -.
DR InParanoid; Q13442; -.
DR OMA; ENPNRIG; -.
DR OrthoDB; EOG7WX0C5; -.
DR PhylomeDB; Q13442; -.
DR ChiTaRS; PDAP1; human.
DR GeneWiki; PDAP1; -.
DR GenomeRNAi; 11333; -.
DR NextBio; 43057; -.
DR PMAP-CutDB; Q13442; -.
DR PRO; PR:Q13442; -.
DR ArrayExpress; Q13442; -.
DR Bgee; Q13442; -.
DR CleanEx; HS_PDAP1; -.
DR Genevestigator; Q13442; -.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR019380; Casein_kinase_sb_PP28.
DR Pfam; PF10252; PP28; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Reference proteome.
FT CHAIN 1 181 28 kDa heat- and acid-stable
FT phosphoprotein.
FT /FTId=PRO_0000083897.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 60 60 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT MOD_RES 70 70 Phosphotyrosine (By similarity).
FT MOD_RES 132 132 N6-acetyllysine.
FT MOD_RES 176 176 Phosphoserine.
FT CONFLICT 1 1 M -> MI (in Ref. 5; AAB07135).
FT CONFLICT 13 13 R -> W (in Ref. 5; AAB07135).
FT CONFLICT 25 25 A -> T (in Ref. 5; AAB07135).
FT CONFLICT 29 29 A -> S (in Ref. 5; AAB07135).
FT CONFLICT 67 67 E -> D (in Ref. 5; AAB07135).
FT CONFLICT 80 80 L -> F (in Ref. 5; AAB07135).
FT CONFLICT 126 126 K -> R (in Ref. 5; AAB07135).
SQ SEQUENCE 181 AA; 20630 MW; F97914C7920ABAB3 CRC64;
MPKGGRKGGH KGRARQYTSP EEIDAQLQAE KQKAREEEEQ KEGGDGAAGD PKKEKKSLDS
DESEDEEDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD LDGPKELSRR EREEIEKQKA
KERYMKMHLA GKTEQAKADL ARLAIIRKQR EEAARKKEEE RKAKDDATLS GKRMQSLSLN
K
//
ID HAP28_HUMAN Reviewed; 181 AA.
AC Q13442; D6W5S5; Q92906;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=28 kDa heat- and acid-stable phosphoprotein;
DE AltName: Full=PDGF-associated protein;
DE Short=PAP;
DE AltName: Full=PDGFA-associated protein 1;
DE Short=PAP1;
GN Name=PDAP1; Synonyms=HASPP28;
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].
RC TISSUE=Neuroretina;
RX PubMed=8780057;
RA Fischer W.H., Schubert D.;
RT "Characterization of a novel platelet-derived growth factor-associated
RT protein.";
RL J. Neurochem. 66:2213-2216(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
RA Huang F.L.;
RT "5' flanking sequence of HASPP28.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-57; SER-60;
RP SER-63 AND SER-176, AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63,
RP AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-63 AND SER-176,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-57; SER-60;
RP SER-63 AND SER-176, AND 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND MASS
RP 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).
CC -!- FUNCTION: Enhances PDGFA-stimulated cell growth in fibroblasts,
CC but inhibits the mitogenic effect of PDGFB (By similarity).
CC -!- SIMILARITY: Belongs to the PDAP1 family.
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; U41745; AAC50462.1; -; mRNA.
DR EMBL; AC004922; AAF03506.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76675.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76676.1; -; Genomic_DNA.
DR EMBL; BC000684; AAH00684.1; -; mRNA.
DR EMBL; BC007873; AAH07873.1; -; mRNA.
DR EMBL; U65960; AAB07135.1; -; Genomic_DNA.
DR RefSeq; NP_055706.1; NM_014891.6.
DR UniGene; Hs.632296; -.
DR ProteinModelPortal; Q13442; -.
DR IntAct; Q13442; 6.
DR MINT; MINT-5002803; -.
DR STRING; 9606.ENSP00000222968; -.
DR DrugBank; DB00102; Becaplermin.
DR PhosphoSite; Q13442; -.
DR DMDM; 2498464; -.
DR PaxDb; Q13442; -.
DR PeptideAtlas; Q13442; -.
DR PRIDE; Q13442; -.
DR DNASU; 11333; -.
DR Ensembl; ENST00000350498; ENSP00000222968; ENSG00000106244.
DR GeneID; 11333; -.
DR KEGG; hsa:11333; -.
DR UCSC; uc003uqe.3; human.
DR CTD; 11333; -.
DR GeneCards; GC07M098989; -.
DR HGNC; HGNC:14634; PDAP1.
DR HPA; CAB021103; -.
DR MIM; 607075; gene.
DR neXtProt; NX_Q13442; -.
DR PharmGKB; PA33102; -.
DR eggNOG; NOG313368; -.
DR HOGENOM; HOG000241539; -.
DR HOVERGEN; HBG000319; -.
DR InParanoid; Q13442; -.
DR OMA; ENPNRIG; -.
DR OrthoDB; EOG7WX0C5; -.
DR PhylomeDB; Q13442; -.
DR ChiTaRS; PDAP1; human.
DR GeneWiki; PDAP1; -.
DR GenomeRNAi; 11333; -.
DR NextBio; 43057; -.
DR PMAP-CutDB; Q13442; -.
DR PRO; PR:Q13442; -.
DR ArrayExpress; Q13442; -.
DR Bgee; Q13442; -.
DR CleanEx; HS_PDAP1; -.
DR Genevestigator; Q13442; -.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR019380; Casein_kinase_sb_PP28.
DR Pfam; PF10252; PP28; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Reference proteome.
FT CHAIN 1 181 28 kDa heat- and acid-stable
FT phosphoprotein.
FT /FTId=PRO_0000083897.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 60 60 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT MOD_RES 70 70 Phosphotyrosine (By similarity).
FT MOD_RES 132 132 N6-acetyllysine.
FT MOD_RES 176 176 Phosphoserine.
FT CONFLICT 1 1 M -> MI (in Ref. 5; AAB07135).
FT CONFLICT 13 13 R -> W (in Ref. 5; AAB07135).
FT CONFLICT 25 25 A -> T (in Ref. 5; AAB07135).
FT CONFLICT 29 29 A -> S (in Ref. 5; AAB07135).
FT CONFLICT 67 67 E -> D (in Ref. 5; AAB07135).
FT CONFLICT 80 80 L -> F (in Ref. 5; AAB07135).
FT CONFLICT 126 126 K -> R (in Ref. 5; AAB07135).
SQ SEQUENCE 181 AA; 20630 MW; F97914C7920ABAB3 CRC64;
MPKGGRKGGH KGRARQYTSP EEIDAQLQAE KQKAREEEEQ KEGGDGAAGD PKKEKKSLDS
DESEDEEDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD LDGPKELSRR EREEIEKQKA
KERYMKMHLA GKTEQAKADL ARLAIIRKQR EEAARKKEEE RKAKDDATLS GKRMQSLSLN
K
//
MIM
607075
*RECORD*
*FIELD* NO
607075
*FIELD* TI
*607075 PDGFA-ASSOCIATED PROTEIN 1; PDAP1
;;PAP1; PAP
*FIELD* TX
CLONING
By screening a retina cDNA library with rat PAP sequence as probe,
read moreFischer and Schubert (1996) cloned the human homolog, designated PDAP1,
encoding a deduced 181-amino acid protein. The authors found no obvious
secretion signal peptide. Northern blot analysis of newborn rat tissues
detected expression in all tissues tested except liver; abundant
expression was found in brain.
GENE FUNCTION
Fischer and Schubert (1996) found that PDAP1 enhanced PDGFA
(173430)-stimulated cell growth in mouse fibroblasts, but inhibited the
mitogenic effect of PDGFB (190040). It had no effect on the action of
any other growth hormone tested. Solid-phase binding studies showed that
the binding between PDGFA and PDAP1 is a low affinity/high capacity
interaction.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PDAP1
gene to chromosome 7 (TMAP RH41780).
*FIELD* RF
1. Fischer, W. H.; Schubert, D.: Characterization of a novel platelet-derived
growth factor-associated protein. J. Neurochem. 66: 2213-2216, 1996.
*FIELD* CD
Patricia A. Hartz: 6/27/2002
*FIELD* ED
carol: 06/27/2002
carol: 6/27/2002
*RECORD*
*FIELD* NO
607075
*FIELD* TI
*607075 PDGFA-ASSOCIATED PROTEIN 1; PDAP1
;;PAP1; PAP
*FIELD* TX
CLONING
By screening a retina cDNA library with rat PAP sequence as probe,
read moreFischer and Schubert (1996) cloned the human homolog, designated PDAP1,
encoding a deduced 181-amino acid protein. The authors found no obvious
secretion signal peptide. Northern blot analysis of newborn rat tissues
detected expression in all tissues tested except liver; abundant
expression was found in brain.
GENE FUNCTION
Fischer and Schubert (1996) found that PDAP1 enhanced PDGFA
(173430)-stimulated cell growth in mouse fibroblasts, but inhibited the
mitogenic effect of PDGFB (190040). It had no effect on the action of
any other growth hormone tested. Solid-phase binding studies showed that
the binding between PDGFA and PDAP1 is a low affinity/high capacity
interaction.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PDAP1
gene to chromosome 7 (TMAP RH41780).
*FIELD* RF
1. Fischer, W. H.; Schubert, D.: Characterization of a novel platelet-derived
growth factor-associated protein. J. Neurochem. 66: 2213-2216, 1996.
*FIELD* CD
Patricia A. Hartz: 6/27/2002
*FIELD* ED
carol: 06/27/2002
carol: 6/27/2002