DAZP1_HUMAN
ID DAZP1_HUMAN Reviewed; 407 AA.
AC Q96EP5; Q96MJ3; Q9NRR9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY,
RP 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-specific
RT 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 project:
RT 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, AND
RP IDENTIFICATION BY 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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., Buerckstuemmer T.,
RA 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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-253, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
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 domain
RT in DAZ-associated protein 1.";
RL Submitted (SEP-2006) to the PDB data bank.
RN [14]
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal 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. {ECO:0000269|PubMed:10857750}.
CC -!- INTERACTION:
CC Q96EP5; Q9NQZ3: DAZ1; NbExp=3; IntAct=EBI-2133162, EBI-997955;
CC Q96EP5; P09012: SNRPA; NbExp=3; IntAct=EBI-2133162, EBI-607085;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22001406}. Nucleus
CC {ECO:0000269|PubMed:22001406}. Note=Predominantly cytoplasmic (By
CC similarity). Nuclear at some stages of spermatozoides development. In
CC midpachytene spermatocytes, it is localized in both the cytoplasm and
CC the nuclei and is clearly excluded from the sex vesicles. In round
CC spermatids, it localizes mainly in the nuclei, whereas in elongated
CC spermatids, it localizes to the cytoplasm (By similarity).
CC {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Mainly expressed in testis. Expressed to a lower
CC level in thymus. Weakly or not expressed in heart, liver, brain,
CC placenta, lung, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:10857750}.
CC -!- PTM: Acetylation at Lys-150 is predominantly observed in the nuclear
CC fraction, and may regulate nucleocytoplasmic transport.
CC {ECO:0000269|PubMed:22001406, ECO:0000269|Ref.3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71295.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF181719; AAF78364.1; -; mRNA.
DR EMBL; BC012062; AAH12062.1; -; mRNA.
DR EMBL; AK056850; BAB71295.1; ALT_INIT; mRNA.
DR CCDS; CCDS12065.1; -. [Q96EP5-1]
DR CCDS; CCDS12066.1; -. [Q96EP5-2]
DR RefSeq; NP_061832.2; NM_018959.3. [Q96EP5-1]
DR RefSeq; NP_733829.1; NM_170711.2. [Q96EP5-2]
DR PDB; 2DGS; NMR; -; A=110-195.
DR PDB; 2DH8; NMR; -; A=1-92.
DR PDBsum; 2DGS; -.
DR PDBsum; 2DH8; -.
DR AlphaFoldDB; Q96EP5; -.
DR SMR; Q96EP5; -.
DR BioGRID; 117730; 135.
DR IntAct; Q96EP5; 30.
DR MINT; Q96EP5; -.
DR STRING; 9606.ENSP00000233078; -.
DR GlyGen; Q96EP5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96EP5; -.
DR MetOSite; Q96EP5; -.
DR PhosphoSitePlus; Q96EP5; -.
DR SwissPalm; Q96EP5; -.
DR BioMuta; DAZAP1; -.
DR DMDM; 44887869; -.
DR REPRODUCTION-2DPAGE; IPI00165230; -.
DR EPD; Q96EP5; -.
DR jPOST; Q96EP5; -.
DR MassIVE; Q96EP5; -.
DR MaxQB; Q96EP5; -.
DR PaxDb; Q96EP5; -.
DR PeptideAtlas; Q96EP5; -.
DR PRIDE; Q96EP5; -.
DR ProteomicsDB; 76437; -. [Q96EP5-1]
DR ProteomicsDB; 76438; -. [Q96EP5-2]
DR Antibodypedia; 1414; 198 antibodies from 26 providers.
DR DNASU; 26528; -.
DR Ensembl; ENST00000233078.9; ENSP00000233078.4; ENSG00000071626.17. [Q96EP5-1]
DR Ensembl; ENST00000336761.10; ENSP00000337132.5; ENSG00000071626.17. [Q96EP5-2]
DR GeneID; 26528; -.
DR KEGG; hsa:26528; -.
DR MANE-Select; ENST00000233078.9; ENSP00000233078.4; NM_018959.4; NP_061832.2.
DR UCSC; uc002lsm.5; human. [Q96EP5-1]
DR CTD; 26528; -.
DR DisGeNET; 26528; -.
DR GeneCards; DAZAP1; -.
DR HGNC; HGNC:2683; DAZAP1.
DR HPA; ENSG00000071626; Low tissue specificity.
DR MIM; 607430; gene.
DR neXtProt; NX_Q96EP5; -.
DR OpenTargets; ENSG00000071626; -.
DR PharmGKB; PA27153; -.
DR VEuPathDB; HostDB:ENSG00000071626; -.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000156757; -.
DR InParanoid; Q96EP5; -.
DR OMA; FVMFRKA; -.
DR OrthoDB; 1565323at2759; -.
DR PhylomeDB; Q96EP5; -.
DR TreeFam; TF314808; -.
DR PathwayCommons; Q96EP5; -.
DR SignaLink; Q96EP5; -.
DR SIGNOR; Q96EP5; -.
DR BioGRID-ORCS; 26528; 99 hits in 1083 CRISPR screens.
DR ChiTaRS; DAZAP1; human.
DR EvolutionaryTrace; Q96EP5; -.
DR GeneWiki; DAZ_associated_protein_1; -.
DR GenomeRNAi; 26528; -.
DR Pharos; Q96EP5; Tbio.
DR PRO; PR:Q96EP5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96EP5; protein.
DR Bgee; ENSG00000071626; Expressed in left testis and 191 other tissues.
DR ExpressionAtlas; Q96EP5; baseline and differential.
DR Genevisible; Q96EP5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IMP:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0034046; F:poly(G) binding; IMP:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR CDD; cd12574; RRM1_DAZAP1; 1.
DR CDD; cd12327; RRM2_DAZAP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034134; DAZAP1_RRM1.
DR InterPro; IPR034131; DAZAP1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Methylation; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Spermatogenesis.
FT CHAIN 1..407
FT /note="DAZ-associated protein 1"
FT /id="PRO_0000081565"
FT DOMAIN 10..97
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 113..190
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 74..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22001406"
FT MOD_RES 253
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 350..407
FT /note="AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQG
FT FHPYRR -> GLGSYSPAPPGCGPHFVYSLMVRLSSDVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009441"
FT VARIANT 381
FT /note="S -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035480"
FT CONFLICT 109
FT /note="N -> Y (in Ref. 1; AAF78364)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:2DH8"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:2DH8"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2DH8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2DH8"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:2DH8"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:2DH8"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2DH8"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2DH8"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:2DGS"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:2DGS"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2DGS"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2DGS"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2DGS"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:2DGS"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:2DGS"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:2DGS"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2DGS"
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
