Full text data of DAZAP1
DAZAP1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
DAZ-associated protein 1 (Deleted in azoospermia-associated protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DAZ-associated protein 1 (Deleted in azoospermia-associated protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96EP5
ID DAZP1_HUMAN Reviewed; 407 AA.
AC Q96EP5; Q96MJ3; Q9NRR9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=DAZ-associated protein 1;
DE AltName: Full=Deleted in azoospermia-associated protein 1;
GN Name=DAZAP1;
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] (ISOFORM 1), RNA-BINDING, TISSUE
RP SPECIFICITY, AND INTERACTION WITH DAZ AND DAZL.
RC TISSUE=Testis;
RX PubMed=10857750; DOI=10.1006/geno.2000.6169;
RA Tsui S., Dai T., Roettger S., Schempp W., Salido E.C., Yen P.H.;
RT "Identification of two novel proteins that interact with germ-cell-
RT specific RNA-binding proteins DAZ and DAZL1.";
RL Genomics 65:266-273(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [3]
RP PROTEIN SEQUENCE OF 1-27; 136-150 AND 195-209, ACETYLATION AT MET-1,
RP AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-390 (ISOFORM 2).
RC TISSUE=Prostate;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [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).
RN [8]
RP ACETYLATION AT LYS-150, AND SUBCELLULAR LOCATION.
RX PubMed=22001406; DOI=10.1016/j.gene.2011.09.022;
RA Sasaki K., Suzuki A., Kagatsume S., Ono M., Matsuzawa K., Taguchi Y.,
RA Kurihara Y.;
RT "Acetylation of Prrp K150 regulates the subcellular localization.";
RL Gene 491:13-19(2012).
RN [9]
RP STRUCTURE BY NMR OF 1-198.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal and of the second RNA binding
RT domain in DAZ-associated protein 1.";
RL Submitted (SEP-2006) to the PDB data bank.
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] THR-381.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: RNA-binding protein, which may be required during
CC spermatogenesis.
CC -!- SUBUNIT: Interacts with DAZ and DAZL.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic (By similarity). Nuclear at some stages of
CC spermatozoides development. In midpachytene spermatocytes, it is
CC localized in both the cytoplasm and the nuclei and is clearly
CC excluded from the sex vesicles. In round spermatids, it localizes
CC mainly in the nuclei, whereas in elongated spermatids, it
CC localizes to the cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96EP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96EP5-2; Sequence=VSP_009441;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis. Expressed to a
CC lower level in thymus. Weakly or not expressed in heart, liver,
CC brain, placenta, lung, skeletal muscle, kidney and pancreas.
CC -!- PTM: Acetylation at Lys-150 is predominantly observed in the
CC nuclear fraction, and may regulate nucleocytoplasmic transport.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71295.1; Type=Erroneous initiation;
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; AF181719; AAF78364.1; -; mRNA.
DR EMBL; BC012062; AAH12062.1; -; mRNA.
DR EMBL; AK056850; BAB71295.1; ALT_INIT; mRNA.
DR RefSeq; NP_061832.2; NM_018959.3.
DR RefSeq; NP_733829.1; NM_170711.2.
DR RefSeq; XP_005259590.1; XM_005259533.1.
DR UniGene; Hs.222510; -.
DR PDB; 2DGS; NMR; -; A=110-195.
DR PDB; 2DH8; NMR; -; A=1-92.
DR PDBsum; 2DGS; -.
DR PDBsum; 2DH8; -.
DR ProteinModelPortal; Q96EP5; -.
DR SMR; Q96EP5; 6-198.
DR IntAct; Q96EP5; 9.
DR MINT; MINT-3052538; -.
DR STRING; 9606.ENSP00000233078; -.
DR PhosphoSite; Q96EP5; -.
DR DMDM; 44887869; -.
DR REPRODUCTION-2DPAGE; IPI00165230; -.
DR PaxDb; Q96EP5; -.
DR PRIDE; Q96EP5; -.
DR DNASU; 26528; -.
DR Ensembl; ENST00000233078; ENSP00000233078; ENSG00000071626.
DR Ensembl; ENST00000336761; ENSP00000337132; ENSG00000071626.
DR GeneID; 26528; -.
DR KEGG; hsa:26528; -.
DR UCSC; uc002lsn.3; human.
DR CTD; 26528; -.
DR GeneCards; GC19P001407; -.
DR HGNC; HGNC:2683; DAZAP1.
DR HPA; HPA004201; -.
DR HPA; HPA004631; -.
DR MIM; 607430; gene.
DR neXtProt; NX_Q96EP5; -.
DR PharmGKB; PA27153; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000234441; -.
DR HOVERGEN; HBG002295; -.
DR InParanoid; Q96EP5; -.
DR KO; K14411; -.
DR OMA; DFPYSQY; -.
DR OrthoDB; EOG715Q6V; -.
DR PhylomeDB; Q96EP5; -.
DR ChiTaRS; DAZAP1; human.
DR EvolutionaryTrace; Q96EP5; -.
DR GeneWiki; DAZ_associated_protein_1; -.
DR GenomeRNAi; 26528; -.
DR NextBio; 48864; -.
DR PRO; PR:Q96EP5; -.
DR ArrayExpress; Q96EP5; -.
DR Bgee; Q96EP5; -.
DR CleanEx; HS_DAZAP1; -.
DR Genevestigator; Q96EP5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Nucleus; Polymorphism; Reference proteome;
KW Repeat; RNA-binding; Spermatogenesis.
FT CHAIN 1 407 DAZ-associated protein 1.
FT /FTId=PRO_0000081565.
FT DOMAIN 10 97 RRM 1.
FT DOMAIN 113 190 RRM 2.
FT COMPBIAS 222 385 Pro-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 150 150 N6-acetyllysine.
FT VAR_SEQ 350 407 AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSG
FT FGRGQNHNVQGFHPYRR -> GLGSYSPAPPGCGPHFVYSL
FT MVRLSSDVA (in isoform 2).
FT /FTId=VSP_009441.
FT VARIANT 381 381 S -> T (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035480.
FT CONFLICT 109 109 N -> Y (in Ref. 1; AAF78364).
FT STRAND 6 12
FT HELIX 23 31
FT STRAND 36 43
FT STRAND 45 47
FT STRAND 50 60
FT HELIX 63 70
FT STRAND 72 75
FT STRAND 78 81
FT STRAND 114 119
FT HELIX 126 133
FT STRAND 134 137
FT STRAND 139 144
FT TURN 148 150
FT STRAND 155 163
FT HELIX 164 173
FT STRAND 177 180
FT STRAND 184 187
SQ SEQUENCE 407 AA; 43383 MW; CFEB42903F4D5AFB CRC64;
MNNSGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS RGFGFVKFKD
PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG WQKGPRSDNS KSNKIFVGGI
PHNCGETELR EYFKKFGVVT EVVMIYDAEK QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG
KKVEVKRAEP RDSKSQAPGQ PGASQWGSRV VPNAANGWAG QPPPTWQQGY GPQGMWVPAG
QAIGGYGPPP AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP
PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYA GYGQDLSGFG
QGFSDPSQQP PSYGGPSVPG SGGPPAGGSG FGRGQNHNVQ GFHPYRR
//
ID DAZP1_HUMAN Reviewed; 407 AA.
AC Q96EP5; Q96MJ3; Q9NRR9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=DAZ-associated protein 1;
DE AltName: Full=Deleted in azoospermia-associated protein 1;
GN Name=DAZAP1;
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] (ISOFORM 1), RNA-BINDING, TISSUE
RP SPECIFICITY, AND INTERACTION WITH DAZ AND DAZL.
RC TISSUE=Testis;
RX PubMed=10857750; DOI=10.1006/geno.2000.6169;
RA Tsui S., Dai T., Roettger S., Schempp W., Salido E.C., Yen P.H.;
RT "Identification of two novel proteins that interact with germ-cell-
RT specific RNA-binding proteins DAZ and DAZL1.";
RL Genomics 65:266-273(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [3]
RP PROTEIN SEQUENCE OF 1-27; 136-150 AND 195-209, ACETYLATION AT MET-1,
RP AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-390 (ISOFORM 2).
RC TISSUE=Prostate;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [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).
RN [8]
RP ACETYLATION AT LYS-150, AND SUBCELLULAR LOCATION.
RX PubMed=22001406; DOI=10.1016/j.gene.2011.09.022;
RA Sasaki K., Suzuki A., Kagatsume S., Ono M., Matsuzawa K., Taguchi Y.,
RA Kurihara Y.;
RT "Acetylation of Prrp K150 regulates the subcellular localization.";
RL Gene 491:13-19(2012).
RN [9]
RP STRUCTURE BY NMR OF 1-198.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal and of the second RNA binding
RT domain in DAZ-associated protein 1.";
RL Submitted (SEP-2006) to the PDB data bank.
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] THR-381.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: RNA-binding protein, which may be required during
CC spermatogenesis.
CC -!- SUBUNIT: Interacts with DAZ and DAZL.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic (By similarity). Nuclear at some stages of
CC spermatozoides development. In midpachytene spermatocytes, it is
CC localized in both the cytoplasm and the nuclei and is clearly
CC excluded from the sex vesicles. In round spermatids, it localizes
CC mainly in the nuclei, whereas in elongated spermatids, it
CC localizes to the cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96EP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96EP5-2; Sequence=VSP_009441;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis. Expressed to a
CC lower level in thymus. Weakly or not expressed in heart, liver,
CC brain, placenta, lung, skeletal muscle, kidney and pancreas.
CC -!- PTM: Acetylation at Lys-150 is predominantly observed in the
CC nuclear fraction, and may regulate nucleocytoplasmic transport.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71295.1; Type=Erroneous initiation;
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; AF181719; AAF78364.1; -; mRNA.
DR EMBL; BC012062; AAH12062.1; -; mRNA.
DR EMBL; AK056850; BAB71295.1; ALT_INIT; mRNA.
DR RefSeq; NP_061832.2; NM_018959.3.
DR RefSeq; NP_733829.1; NM_170711.2.
DR RefSeq; XP_005259590.1; XM_005259533.1.
DR UniGene; Hs.222510; -.
DR PDB; 2DGS; NMR; -; A=110-195.
DR PDB; 2DH8; NMR; -; A=1-92.
DR PDBsum; 2DGS; -.
DR PDBsum; 2DH8; -.
DR ProteinModelPortal; Q96EP5; -.
DR SMR; Q96EP5; 6-198.
DR IntAct; Q96EP5; 9.
DR MINT; MINT-3052538; -.
DR STRING; 9606.ENSP00000233078; -.
DR PhosphoSite; Q96EP5; -.
DR DMDM; 44887869; -.
DR REPRODUCTION-2DPAGE; IPI00165230; -.
DR PaxDb; Q96EP5; -.
DR PRIDE; Q96EP5; -.
DR DNASU; 26528; -.
DR Ensembl; ENST00000233078; ENSP00000233078; ENSG00000071626.
DR Ensembl; ENST00000336761; ENSP00000337132; ENSG00000071626.
DR GeneID; 26528; -.
DR KEGG; hsa:26528; -.
DR UCSC; uc002lsn.3; human.
DR CTD; 26528; -.
DR GeneCards; GC19P001407; -.
DR HGNC; HGNC:2683; DAZAP1.
DR HPA; HPA004201; -.
DR HPA; HPA004631; -.
DR MIM; 607430; gene.
DR neXtProt; NX_Q96EP5; -.
DR PharmGKB; PA27153; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000234441; -.
DR HOVERGEN; HBG002295; -.
DR InParanoid; Q96EP5; -.
DR KO; K14411; -.
DR OMA; DFPYSQY; -.
DR OrthoDB; EOG715Q6V; -.
DR PhylomeDB; Q96EP5; -.
DR ChiTaRS; DAZAP1; human.
DR EvolutionaryTrace; Q96EP5; -.
DR GeneWiki; DAZ_associated_protein_1; -.
DR GenomeRNAi; 26528; -.
DR NextBio; 48864; -.
DR PRO; PR:Q96EP5; -.
DR ArrayExpress; Q96EP5; -.
DR Bgee; Q96EP5; -.
DR CleanEx; HS_DAZAP1; -.
DR Genevestigator; Q96EP5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Nucleus; Polymorphism; Reference proteome;
KW Repeat; RNA-binding; Spermatogenesis.
FT CHAIN 1 407 DAZ-associated protein 1.
FT /FTId=PRO_0000081565.
FT DOMAIN 10 97 RRM 1.
FT DOMAIN 113 190 RRM 2.
FT COMPBIAS 222 385 Pro-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 150 150 N6-acetyllysine.
FT VAR_SEQ 350 407 AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSG
FT FGRGQNHNVQGFHPYRR -> GLGSYSPAPPGCGPHFVYSL
FT MVRLSSDVA (in isoform 2).
FT /FTId=VSP_009441.
FT VARIANT 381 381 S -> T (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035480.
FT CONFLICT 109 109 N -> Y (in Ref. 1; AAF78364).
FT STRAND 6 12
FT HELIX 23 31
FT STRAND 36 43
FT STRAND 45 47
FT STRAND 50 60
FT HELIX 63 70
FT STRAND 72 75
FT STRAND 78 81
FT STRAND 114 119
FT HELIX 126 133
FT STRAND 134 137
FT STRAND 139 144
FT TURN 148 150
FT STRAND 155 163
FT HELIX 164 173
FT STRAND 177 180
FT STRAND 184 187
SQ SEQUENCE 407 AA; 43383 MW; CFEB42903F4D5AFB CRC64;
MNNSGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS RGFGFVKFKD
PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG WQKGPRSDNS KSNKIFVGGI
PHNCGETELR EYFKKFGVVT EVVMIYDAEK QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG
KKVEVKRAEP RDSKSQAPGQ PGASQWGSRV VPNAANGWAG QPPPTWQQGY GPQGMWVPAG
QAIGGYGPPP AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP
PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYA GYGQDLSGFG
QGFSDPSQQP PSYGGPSVPG SGGPPAGGSG FGRGQNHNVQ GFHPYRR
//
MIM
607430
*RECORD*
*FIELD* NO
607430
*FIELD* TI
*607430 DAZ-ASSOCIATED PROTEIN 1; DAZAP1
*FIELD* TX
CLONING
Using a yeast 2-hybrid screen of a human testis cDNA library with the
read morecoding region of DAZ (400003) as bait, Tsui et al. (2000) cloned cDNAs
encoding DAZAP1 and DAZAP2 (607431). DAZAP1 is an RNA-binding protein of
407 amino acids. It contains 2 RNP motifs in the N terminus and has a
proline-rich C terminus. The protein shares high sequence homology in
the RNP regions with hnRNP A/B proteins (see 600124), but differs from
these proteins in the C terminus. Northern blot analysis detected
expression of 2 DAZAP1 transcripts of 2.75 and 2.4 kb that were most
abundant in the testis and to a lesser degree in the thymus. All other
tissues expressed low levels of the transcript. RT-PCR of RNA samples
from testicular biopsies of 4 infertile men detected expression of
DAZAP1 only in samples with normal spermatogenesis, suggesting that
DAZAP1 is expressed mainly in the germ cells.
GENE FUNCTION
Using GST-fusion binding analysis, Tsui et al. (2000) determined that
both DAZAP1 and DAZAP2 interact with DAZ and DAZL (601486). Deletion
constructs indicated that DAZ and DAZL bind to DAZAP1/DAZAP2 mainly
through the DAZ repeat region.
MAPPING
By FISH, Tsui et al. (2000) mapped the DAZAP1 gene to chromosome
19p13.3.
*FIELD* RF
1. Tsui, S.; Dai, T.; Roettger, S.; Schempp, W.; Salido, E. C.; Yen,
P. H.: Identification of two novel proteins that interact with germ-cell-specific
RNA-binding proteins DAZ and DAZL1. Genomics 65: 266-273, 2000.
*FIELD* CD
Carol A. Bocchini: 12/18/2002
*FIELD* ED
cwells: 12/20/2002
mgross: 12/20/2002
carol: 12/18/2002
*RECORD*
*FIELD* NO
607430
*FIELD* TI
*607430 DAZ-ASSOCIATED PROTEIN 1; DAZAP1
*FIELD* TX
CLONING
Using a yeast 2-hybrid screen of a human testis cDNA library with the
read morecoding region of DAZ (400003) as bait, Tsui et al. (2000) cloned cDNAs
encoding DAZAP1 and DAZAP2 (607431). DAZAP1 is an RNA-binding protein of
407 amino acids. It contains 2 RNP motifs in the N terminus and has a
proline-rich C terminus. The protein shares high sequence homology in
the RNP regions with hnRNP A/B proteins (see 600124), but differs from
these proteins in the C terminus. Northern blot analysis detected
expression of 2 DAZAP1 transcripts of 2.75 and 2.4 kb that were most
abundant in the testis and to a lesser degree in the thymus. All other
tissues expressed low levels of the transcript. RT-PCR of RNA samples
from testicular biopsies of 4 infertile men detected expression of
DAZAP1 only in samples with normal spermatogenesis, suggesting that
DAZAP1 is expressed mainly in the germ cells.
GENE FUNCTION
Using GST-fusion binding analysis, Tsui et al. (2000) determined that
both DAZAP1 and DAZAP2 interact with DAZ and DAZL (601486). Deletion
constructs indicated that DAZ and DAZL bind to DAZAP1/DAZAP2 mainly
through the DAZ repeat region.
MAPPING
By FISH, Tsui et al. (2000) mapped the DAZAP1 gene to chromosome
19p13.3.
*FIELD* RF
1. Tsui, S.; Dai, T.; Roettger, S.; Schempp, W.; Salido, E. C.; Yen,
P. H.: Identification of two novel proteins that interact with germ-cell-specific
RNA-binding proteins DAZ and DAZL1. Genomics 65: 266-273, 2000.
*FIELD* CD
Carol A. Bocchini: 12/18/2002
*FIELD* ED
cwells: 12/20/2002
mgross: 12/20/2002
carol: 12/18/2002