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Q96EP5

- DAZP1_HUMAN

UniProt

Q96EP5 - DAZP1_HUMAN

Protein

DAZ-associated protein 1

Gene

DAZAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    RNA-binding protein, which may be required during spermatogenesis.

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. RNA binding Source: ProtInc
    4. RNA stem-loop binding Source: Ensembl

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cell proliferation Source: Ensembl
    3. maternal placenta development Source: Ensembl
    4. spermatogenesis Source: ProtInc

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Spermatogenesis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DAZ-associated protein 1
    Alternative name(s):
    Deleted in azoospermia-associated protein 1
    Gene namesi
    Name:DAZAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2683. DAZAP1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Predominantly cytoplasmic By similarity. Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27153.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407DAZ-associated protein 1PRO_0000081565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei150 – 1501N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation at Lys-150 is predominantly observed in the nuclear fraction, and may regulate nucleocytoplasmic transport.4 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96EP5.
    PaxDbiQ96EP5.
    PRIDEiQ96EP5.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00165230.

    PTM databases

    PhosphoSiteiQ96EP5.

    Expressioni

    Tissue specificityi

    Mainly expressed in testis. Expressed to a lower level in thymus. Weakly or not expressed in heart, liver, brain, placenta, lung, skeletal muscle, kidney and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ96EP5.
    BgeeiQ96EP5.
    CleanExiHS_DAZAP1.
    GenevestigatoriQ96EP5.

    Organism-specific databases

    HPAiHPA004201.
    HPA004631.

    Interactioni

    Subunit structurei

    Interacts with DAZ and DAZL.1 Publication

    Protein-protein interaction databases

    BioGridi117730. 29 interactions.
    IntActiQ96EP5. 9 interactions.
    MINTiMINT-3052538.
    STRINGi9606.ENSP00000233078.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Helixi23 – 319
    Beta strandi36 – 438
    Beta strandi45 – 473
    Beta strandi50 – 6011
    Helixi63 – 708
    Beta strandi72 – 754
    Beta strandi78 – 814
    Beta strandi114 – 1196
    Helixi126 – 1338
    Beta strandi134 – 1374
    Beta strandi139 – 1446
    Turni148 – 1503
    Beta strandi155 – 1639
    Helixi164 – 17310
    Beta strandi177 – 1804
    Beta strandi184 – 1874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DGSNMR-A110-195[»]
    2DH8NMR-A1-92[»]
    ProteinModelPortaliQ96EP5.
    SMRiQ96EP5. Positions 6-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96EP5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 9788RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini113 – 19078RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi222 – 385164Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000234441.
    HOVERGENiHBG002295.
    InParanoidiQ96EP5.
    KOiK14411.
    OMAiDFPYSQY.
    OrthoDBiEOG715Q6V.
    PhylomeDBiQ96EP5.
    TreeFamiTF314808.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96EP5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNNSGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS    50
    RGFGFVKFKD PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG 100
    WQKGPRSDNS KSNKIFVGGI PHNCGETELR EYFKKFGVVT EVVMIYDAEK 150
    QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG KKVEVKRAEP RDSKSQAPGQ 200
    PGASQWGSRV VPNAANGWAG QPPPTWQQGY GPQGMWVPAG QAIGGYGPPP 250
    AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP 300
    PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYA 350
    GYGQDLSGFG QGFSDPSQQP PSYGGPSVPG SGGPPAGGSG FGRGQNHNVQ 400
    GFHPYRR 407
    Length:407
    Mass (Da):43,383
    Last modified:December 1, 2001 - v1
    Checksum:iCFEB42903F4D5AFB
    GO
    Isoform 2 (identifier: Q96EP5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         350-407: AGYGQDLSGF...NVQGFHPYRR → GLGSYSPAPPGCGPHFVYSLMVRLSSDVA

    Note: No experimental confirmation available.

    Show »
    Length:378
    Mass (Da):40,530
    Checksum:iF8DDAD1AFDD37C3E
    GO

    Sequence cautioni

    The sequence BAB71295.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091N → Y in AAF78364. (PubMed:10857750)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti381 – 3811S → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035480

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei350 – 40758AGYGQ…HPYRR → GLGSYSPAPPGCGPHFVYSL MVRLSSDVA in isoform 2. 1 PublicationVSP_009441Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF181719 mRNA. Translation: AAF78364.1.
    BC012062 mRNA. Translation: AAH12062.1.
    AK056850 mRNA. Translation: BAB71295.1. Different initiation.
    CCDSiCCDS12065.1. [Q96EP5-1]
    CCDS12066.1. [Q96EP5-2]
    RefSeqiNP_061832.2. NM_018959.3. [Q96EP5-1]
    NP_733829.1. NM_170711.2. [Q96EP5-2]
    UniGeneiHs.222510.

    Genome annotation databases

    EnsembliENST00000233078; ENSP00000233078; ENSG00000071626. [Q96EP5-1]
    ENST00000336761; ENSP00000337132; ENSG00000071626. [Q96EP5-2]
    GeneIDi26528.
    KEGGihsa:26528.
    UCSCiuc002lsm.3. human. [Q96EP5-2]
    uc002lsn.3. human. [Q96EP5-1]

    Polymorphism databases

    DMDMi44887869.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF181719 mRNA. Translation: AAF78364.1 .
    BC012062 mRNA. Translation: AAH12062.1 .
    AK056850 mRNA. Translation: BAB71295.1 . Different initiation.
    CCDSi CCDS12065.1. [Q96EP5-1 ]
    CCDS12066.1. [Q96EP5-2 ]
    RefSeqi NP_061832.2. NM_018959.3. [Q96EP5-1 ]
    NP_733829.1. NM_170711.2. [Q96EP5-2 ]
    UniGenei Hs.222510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DGS NMR - A 110-195 [» ]
    2DH8 NMR - A 1-92 [» ]
    ProteinModelPortali Q96EP5.
    SMRi Q96EP5. Positions 6-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117730. 29 interactions.
    IntActi Q96EP5. 9 interactions.
    MINTi MINT-3052538.
    STRINGi 9606.ENSP00000233078.

    PTM databases

    PhosphoSitei Q96EP5.

    Polymorphism databases

    DMDMi 44887869.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00165230.

    Proteomic databases

    MaxQBi Q96EP5.
    PaxDbi Q96EP5.
    PRIDEi Q96EP5.

    Protocols and materials databases

    DNASUi 26528.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233078 ; ENSP00000233078 ; ENSG00000071626 . [Q96EP5-1 ]
    ENST00000336761 ; ENSP00000337132 ; ENSG00000071626 . [Q96EP5-2 ]
    GeneIDi 26528.
    KEGGi hsa:26528.
    UCSCi uc002lsm.3. human. [Q96EP5-2 ]
    uc002lsn.3. human. [Q96EP5-1 ]

    Organism-specific databases

    CTDi 26528.
    GeneCardsi GC19P001407.
    HGNCi HGNC:2683. DAZAP1.
    HPAi HPA004201.
    HPA004631.
    MIMi 607430. gene.
    neXtProti NX_Q96EP5.
    PharmGKBi PA27153.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000234441.
    HOVERGENi HBG002295.
    InParanoidi Q96EP5.
    KOi K14411.
    OMAi DFPYSQY.
    OrthoDBi EOG715Q6V.
    PhylomeDBi Q96EP5.
    TreeFami TF314808.

    Miscellaneous databases

    ChiTaRSi DAZAP1. human.
    EvolutionaryTracei Q96EP5.
    GeneWikii DAZ_associated_protein_1.
    GenomeRNAii 26528.
    NextBioi 48864.
    PROi Q96EP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96EP5.
    Bgeei Q96EP5.
    CleanExi HS_DAZAP1.
    Genevestigatori Q96EP5.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1."
      Tsui S., Dai T., Roettger S., Schempp W., Salido E.C., Yen P.H.
      Genomics 65:266-273(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY, INTERACTION WITH DAZ AND DAZL.
      Tissue: Testis.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    3. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-27; 136-150 AND 195-209, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-390 (ISOFORM 2).
      Tissue: Prostate.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Acetylation of Prrp K150 regulates the subcellular localization."
      Sasaki K., Suzuki A., Kagatsume S., Ono M., Matsuzawa K., Taguchi Y., Kurihara Y.
      Gene 491:13-19(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-150, SUBCELLULAR LOCATION.
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structure of the N-terminal and of the second RNA binding domain in DAZ-associated protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-198.
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-381.

    Entry informationi

    Entry nameiDAZP1_HUMAN
    AccessioniPrimary (citable) accession number: Q96EP5
    Secondary accession number(s): Q96MJ3, Q9NRR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3