Reviewed,
UniProtKB/Swiss-Prot Q96EP5 (DAZP1_HUMAN)
Last modified
March 2, 2010.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DAZ-associated protein 1 Alternative name(s): Deleted in azoospermia-associated protein 1 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 407 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | RNA-binding protein, which may be required during spermatogenesis. |
| Subunit structure | Interacts with DAZ and DAZL. Ref.1 |
| 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. |
| 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. Ref.1 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5 |
| Sequence similarities | Contains 2 RRM (RNA recognition motif) domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Differentiation Spermatogenesis |
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Repeat |
| Ligand | RNA-binding |
| Molecular function | Developmental protein |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal developmentInferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | cytoplasm Inferred from direct assay. Source: HPA nucleusInferred from direct assay. Source: HPA |
| Molecular function | RNA binding Ref.1 Traceable author statement. Source: ProtInc nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q96EP5-1) 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. | ||||||
| Isoform 2 (identifier: Q96EP5-2) The sequence of this isoform differs from the canonical sequence as follows: 350-407: AGYGQDLSGF...NVQGFHPYRR → GLGSYSPAPPGCGPHFVYSLMVRLSSDVA | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 407 | 407 | DAZ-associated protein 1 | PRO_0000081565 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Domain | 10 – 97 | 88 | RRM 1 | ||||||||||||||||||||||||||||||||||||||
| Domain | 113 – 190 | 78 | RRM 2 | ||||||||||||||||||||||||||||||||||||||
| Compositional bias | 222 – 385 | 164 | Pro-rich | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.3 Ref.7 | ||||||||||||||||||||||||||||||||||||||
| Modified residue | 103 | 1 | N6-acetyllysine Ref.8 | ||||||||||||||||||||||||||||||||||||||
| Modified residue | 204 | 1 | Phosphoserine Ref.5 | ||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 350 – 407 | 58 | AGYGQ…HPYRR → GLGSYSPAPPGCGPHFVYSL MVRLSSDVA in isoform 2. | VSP_009441 | |||||||||||||||||||||||||||||||||||||
| Natural variant | 381 | 1 | S → T in a breast cancer sample; somatic mutation. Ref.10 | VAR_035480 | |||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 109 | 1 | N → Y in AAF78364. Ref.1 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 6 – 12 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 23 – 31 | 9 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 36 – 43 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 45 – 47 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 50 – 60 | 11 | |||||||||||||||||||||||||||||||||||||||
| Helix | 63 – 70 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 72 – 75 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 81 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 114 – 119 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 126 – 133 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 137 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 139 – 144 | 6 | |||||||||||||||||||||||||||||||||||||||
| Turn | 148 – 150 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 155 – 163 | 9 | |||||||||||||||||||||||||||||||||||||||
| Helix | 164 – 173 | 10 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 177 – 180 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 184 – 187 | 4 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 10857750] [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: 15489334] [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, 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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-390 (ISOFORM 2). Tissue: Prostate. |
| [5] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, MASS SPECTROMETRY. |
| [6] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [7] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. |
| [8] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, MASS SPECTROMETRY. |
| [9] | "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. |
| [10] | "The consensus coding sequences of human breast and colorectal cancers." 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. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-381. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF181719 mRNA. Translation: AAF78364.1. BC012062 mRNA. Translation: AAH12062.1. AK056850 mRNA. Translation: BAB71295.1. Different initiation. | ||||||||||||||||||
| IPI | IPI00165230. IPI00335930. | ||||||||||||||||||
| RefSeq | NP_061832.2. NP_733829.1. | ||||||||||||||||||
| UniGene | Hs.222510 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| SMR | Q96EP5. Positions 8-192. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | Q96EP5. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q96EP5. | ||||||||||||||||||
2-D gel databases | |||||||||||||||||||
| REPRODUCTION-2DPAGE | IPI00165230. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q96EP5. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000233078; ENSP00000233078; ENSG00000071626; Homo sapiens. [Genome view] | ||||||||||||||||||
| GeneID | 26528. | ||||||||||||||||||
| KEGG | hsa:26528. | ||||||||||||||||||
| UCSC | uc002lsl.1. human. uc002lsm.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 26528. | ||||||||||||||||||
| GeneCards | GC19P001361. | ||||||||||||||||||
| H-InvDB | HIX0014584. | ||||||||||||||||||
| HGNC | HGNC:2683. DAZAP1. | ||||||||||||||||||
| HPA | HPA004201. HPA004631. | ||||||||||||||||||
| MIM | 607430. gene. | ||||||||||||||||||
| PharmGKB | PA27153. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | HBG756718. | ||||||||||||||||||
| HOVERGEN | HBG002295. | ||||||||||||||||||
| InParanoid | Q96EP5. | ||||||||||||||||||
| OMA | GFAPATT. | ||||||||||||||||||
| OrthoDB | EOG9WM7F3. | ||||||||||||||||||
| PhylomeDB | Q96EP5. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q96EP5. | ||||||||||||||||||
| Bgee | Q96EP5. | ||||||||||||||||||
| CleanEx | HS_DAZAP1. | ||||||||||||||||||
| Genevestigator | Q96EP5. | ||||||||||||||||||
| GermOnline | ENSG00000071626. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits. | ||||||||||||||||||
| Pfam | PF00076. RRM_1. 2 hits. [Graphical view] | ||||||||||||||||||
| SMART | SM00360. RRM. 2 hits. [Graphical view] | ||||||||||||||||||
| PROSITE | PS50102. RRM. 2 hits. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 48864. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | DAZP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96EP5 Secondary accession number(s): Q96MJ3, Q9NRR9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 19 Human chromosome 19: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


