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Q96EP5

- DAZP1_HUMAN

UniProt

Q96EP5 - DAZP1_HUMAN

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Protein

DAZ-associated protein 1

Gene
DAZAP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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. Nucleus
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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

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.2 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.

Miscellaneous databases

EvolutionaryTraceiQ96EP5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 9788RRM 1Add
BLAST
Domaini113 – 19078RRM 2Add
BLAST

Compositional bias

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

Sequence similaritiesi

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.

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. VSP_009441Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091N → Y in AAF78364. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 117 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

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