ID   DAZP2_RAT               Reviewed;         168 AA.
AC   P60486; A0A0H2UHD1;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   12-OCT-2022, sequence version 2.
DT   04-NOV-2026, entry version 98.
DE   RecName: Full=DAZ-associated protein 2 {ECO:0000250|UniProtKB:Q15038};
DE   AltName: Full=Deleted in azoospermia-associated protein 2;
DE   AltName: Full=Proline-rich transcript in brain protein {ECO:0000250|UniProtKB:Q15038};
GN   Name=Dazap2 {ECO:0000250|UniProtKB:Q15038};
GN   Synonyms=Prtb {ECO:0000250|UniProtKB:Q15038};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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).
CC   -!- FUNCTION: In unstressed cells, promotes SIAH1-mediated
CC       polyubiquitination and degradation of the serine/threonine-protein
CC       kinase HIPK2, probably by acting as a loading factor that potentiates
CC       complex formation between HIPK2 and ubiquitin ligase SIAH1 (By
CC       similarity). In response to DNA damage, localizes to the nucleus
CC       following phosphorylation by HIPK2 and modulates the expression of a
CC       subset of TP53/p53 target genes by binding to TP53 at target gene
CC       promoters (By similarity). This limits the expression of a number of
CC       cell death-mediating TP53 target genes, reducing DNA damage-induced
CC       cell death (By similarity). Enhances the binding of transcription
CC       factor TCF7L2/TCF4, a Wnt signaling pathway effector, to the promoters
CC       of target genes (By similarity). Plays a role in stress granule
CC       formation (By similarity). {ECO:0000250|UniProtKB:Q15038,
CC       ECO:0000250|UniProtKB:Q9DCP9}.
CC   -!- SUBUNIT: Interacts with SOX6. Interacts with DAZ1 and DAZL. Interacts
CC       with IL17RB. May interact with FAM168B. Interacts with INCA1. Interacts
CC       with EIF4G1 and EIF4G2 (By similarity). Interacts (via PPAY motif) with
CC       NEDD4 (via WW domains) (By similarity). Interacts with transcription
CC       factor TCF4; the interaction results in localization of DAZAP2 to the
CC       nucleus (By similarity). Interacts with transcription factors TCF7 and
CC       TCF7L1 (By similarity). Interacts with transcription factor LEF1 (By
CC       similarity). Interacts with serine/threonine-protein kinase HIPK2; the
CC       interaction results in phosphorylation of DAZAP2 which causes
CC       localization of DAZAP2 to the nucleus, reduces interaction of DAZAP2
CC       with HIPK2 and prevents DAZAP2-dependent degradation of HIPK2 (By
CC       similarity). Interacts with ubiquitin ligase SIAH1; the interaction is
CC       decreased following phosphorylation of DAZAP2 by HIPK2 (By similarity).
CC       Interacts with TP53; the interaction is triggered by DNA damage (By
CC       similarity). {ECO:0000250|UniProtKB:Q15038,
CC       ECO:0000250|UniProtKB:Q9DCP9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15038}. Nucleus
CC       {ECO:0000250|UniProtKB:Q15038}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q15038}. Nucleus, nuclear body
CC       {ECO:0000250|UniProtKB:Q15038}. Cytoplasm, Stress granule
CC       {ECO:0000250|UniProtKB:Q15038}. Note=Predominantly nuclear in
CC       macrophages, stimulation of IL17RB with its ligand IL17E induces
CC       accumulation in the cytoplasm (By similarity). Predominantly
CC       cytoplasmic when unphosphorylated and localizes to the nucleus
CC       following phosphorylation by HIPK2 (By similarity). Localizes to stress
CC       granules under cellular stress conditions (By similarity).
CC       {ECO:0000250|UniProtKB:Q15038}.
CC   -!- PTM: Ubiquitinated by SMURF2, leading to proteasomal degradation.
CC       Ubiquitinated by NEDD4, leading to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:Q15038}.
CC   -!- PTM: Following DNA damage, phosphorylated by HIPK2 which promotes
CC       DAZAP2 localization to the nucleus, reduces interaction of DAZAP2 with
CC       HIPK2 and SIAH1, and prevents DAZAP2-dependent ubiquitination of HIPK2
CC       by E3 ubiquitin-protein ligase SIAH1 and subsequent HIPK2 proteasomal
CC       degradation. {ECO:0000250|UniProtKB:Q15038}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH62052.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH474035; EDL86931.1; -; Genomic_DNA.
DR   EMBL; CH474035; EDL86932.1; -; Genomic_DNA.
DR   EMBL; BC062052; AAH62052.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001382601.1; NM_001395672.1.
DR   RefSeq; XP_038934862.1; XM_039078934.2.
DR   STRING; 10116.ENSRNOP00000006239; -.
DR   PhosphoSitePlus; P60486; -.
DR   PaxDb; 10116-ENSRNOP00000006239; -.
DR   Ensembl; ENSRNOT00000006239.9; ENSRNOP00000006239.6; ENSRNOG00000004628.9.
DR   Ensembl; ENSRNOT00055045976; ENSRNOP00055037705; ENSRNOG00055026630.
DR   Ensembl; ENSRNOT00060026115; ENSRNOP00060020908; ENSRNOG00060015232.
DR   Ensembl; ENSRNOT00065035264; ENSRNOP00065028376; ENSRNOG00065020794.
DR   GeneID; 300235; -.
DR   KEGG; rno:300235; -.
DR   CTD; 9802; -.
DR   AGR; RGD:1307407; -.
DR   RGD; 1307407; Dazap2.
DR   eggNOG; ENOG502QTNQ; Eukaryota.
DR   GeneTree; ENSGT00390000000685; -.
DR   HOGENOM; CLU_135110_0_0_1; -.
DR   InParanoid; P60486; -.
DR   OMA; AAGCQVQ; -.
DR   OrthoDB; 6514304at2759; -.
DR   PhylomeDB; P60486; -.
DR   PRO; PR:P60486; -.
DR   Bgee; ENSRNOG00000004628; Expressed in spleen and 19 other cell types or tissues.
DR   InterPro; IPR022730; DAZ_assoc-2.
DR   PANTHER; PTHR31638; DAZ-ASSOCIATED PROTEIN 2; 1.
DR   PANTHER; PTHR31638:SF3; DAZ-ASSOCIATED PROTEIN 2; 1.
DR   Pfam; PF11029; DAZAP2; 1.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:RGD.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:RGD.
DR   GO; GO:0120283; F:protein serine/threonine kinase binding; ISS:UniProtKB.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR   GO; GO:0050699; F:WW domain binding; ISO:RGD.
DR   GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR   GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR   Proteomes; UP000002494; Chromosome 7.
DR   AlphaFoldDB; P60486; -.
DR   FunCoup; P60486; 755.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..168
FT                   /note="DAZ-associated protein 2"
FT                   /id="PRO_0000079790"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           39..42
FT                   /note="PPAY"
FT                   /evidence="ECO:0000250|UniProtKB:Q15038"
FT   COMPBIAS        1..13
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15038"
SQ   SEQUENCE   168 AA;  17292 MW;  49F76AA286040315 CRC64;
     MNSKGQYPTQ PTYPVQPPGN PVYPQTLHLP QAPPYTDAPP AYSELYRPSF VHPGAATVPT
     MSAAFPGASL YLPMAQSVAV GPLGSTIPMA YYPVGPIYPP GSAVLVEGGY DAGARFGAGA
     TTGSIPPPPP GCPPNAAQLA VMQGANVLVT QRKGNFFMGG SDGGYTIW
//