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UniProtKB/Swiss-Prot entry Q96EP5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DAZP1_HUMAN
Primary accession number Q96EP5
Secondary accession numbers Q96MJ3 Q9NRR9
Integrated into Swiss-Prot on March 1, 2004
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 70)
Name and origin of the protein
Protein name DAZ-associated protein 1
Synonym Deleted in azoospermia-associated protein 1
Gene name
Name: DAZAP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY, AND INTERACTION WITH DAZ AND DAZL.
TISSUE=Testis;
DOI=10.1006/geno.2000.6169; PubMed=10857750 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 1-27; 136-150 AND 195-209, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-390 (ISOFORM 2).
TISSUE=Prostate;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[6]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[7]
STRUCTURE BY NMR OF 1-198.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the N-terminal and of the second RNA binding domain in DAZ-associated protein 1.";
Submitted (SEP-2006) to the PDB data bank.
[8]
VARIANT [LARGE SCALE ANALYSIS] THR-381.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: RNA-binding protein, which may be required during spermatogenesis.
  • SUBUNIT: Interacts with DAZ and DAZL.
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity). 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).
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ96EP5-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ96EP5-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_009441.
  • TISSUE SPECIFICITY: 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.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF181719; AAF78364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012062; AAH12062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK056850; BAB71295.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00165230; -.
IPI00335930; -.
RefSeq NP_061832.2; -.
NP_733829.1; -.
UniGene Hs.222510
3D structure databases
PDB
2DGS; NMR; -; A=110-195.[ExPASy / RCSB / EBI]
2DH8; NMR; -; A=1-92.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2DGS; -.
2DH8; -.
ModBase Q96EP5.
PTM databases
PhosphoSite Q96EP5; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00165230; -.
Organism-specific databases
GeneCards GC19P001361; -.
H-InvDB HIX0014584; -.
HGNC HGNC:2683; DAZAP1.
GenAtlas DAZAP1.
HPA HPA004201; -.
HPA004631; -.
MIM 607430; gene. [NCBI / EBI]
PharmGKB PA27153; -.
Gene expression databases
ArrayExpress Q96EP5; -.
Bgee Q96EP5; -.
CleanEx HS_DAZAP1; -.
GermOnline ENSG00000071626; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (traceable author statement from ProtInc).
GO:0030154; Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0007275; Biological process: multicellular organismal development (inferred from electronic annotation from UniProtKB-KW).
GO:0007283; Biological process: spermatogenesis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
Pfam PF00076; RRM_1; 2.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 2.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q96EP5; -.
Genome annotation databases
Ensembl ENSG00000071626; Homo sapiens. [Contig view]
GeneID 26528; -.
KEGG hsa:26528; -.
Phylogenomic databases
HOGENOM Q96EP5; -.
HOVERGEN Q96EP5; -.
OMA Q96EP5; GFAPATT.
Other
NextBio 48864; -.
SOURCE DAZAP1; Homo sapiens.
ProtoNet Q96EP5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Repeat; RNA-binding; Spermatogenesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   407  407     DAZ-associated protein 1. PRO_0000081565
DOMAIN   10    97  88     RRM 1. 
DOMAIN   113   190  78     RRM 2. 
COMPBIAS   222   385  164     Pro-rich. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   204   204        Phosphoserine. 
VAR_SEQ   350   407        AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGS GFGRGQNHNVQGFHPYRR -> GLGSYSPAPPGCGPHFVYSLMVRLSSDVA (in isoform 2). VSP_009441
VARIANT   381   381  1     S -> T (in a breast cancer sample; somatic mutation). VAR_035480 
CONFLICT   109   109        N -> Y (in Ref. 1; AAF78364). 
STRAND   6    12  7      
HELIX   23    31  9      
STRAND   36    43  8      
STRAND   45    47  3      
STRAND   50    60  11      
HELIX   63    70  8      
STRAND   72    75  4      
STRAND   78    81  4      
STRAND   114   119  6      
HELIX   126   133  8      
STRAND   134   137  4      
STRAND   139   144  6      
TURN   148   150  3      
STRAND   155   163  9      
HELIX   164   173  10      
STRAND   177   180  4      
STRAND   184   187  4      
Sequence information
Length: 407 AA [This is the length of the unprocessed precursor] Molecular weight: 43383 Da [This is the MW of the unprocessed precursor] CRC64: CFEB42903F4D5AFB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNNSGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS RGFGFVKFKD 

        70         80         90        100        110        120 
PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG WQKGPRSDNS KSNKIFVGGI 

       130        140        150        160        170        180 
PHNCGETELR EYFKKFGVVT EVVMIYDAEK QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG 

       190        200        210        220        230        240 
KKVEVKRAEP RDSKSQAPGQ PGASQWGSRV VPNAANGWAG QPPPTWQQGY GPQGMWVPAG 

       250        260        270        280        290        300 
QAIGGYGPPP AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP 

       310        320        330        340        350        360 
PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYA GYGQDLSGFG 

       370        380        390        400 
QGFSDPSQQP PSYGGPSVPG SGGPPAGGSG FGRGQNHNVQ GFHPYRR 

Q96EP5 in FASTA format

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