Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DAZ-associated protein 1

Gene

DAZAP1

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

Functioni

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

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • RNA stem-loop binding Source: Ensembl

GO - Biological processi

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 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27153.

Polymorphism and mutation databases

DMDMi44887869.

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

BgeeiQ96EP5.
CleanExiHS_DAZAP1.
ExpressionAtlasiQ96EP5. baseline and differential.
GenevisibleiQ96EP5. HS.

Organism-specific databases

HPAiHPA004201.
HPA004631.

Interactioni

Subunit structurei

Interacts with DAZ and DAZL.1 Publication

Protein-protein interaction databases

BioGridi117730. 30 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 – 127Combined sources
Helixi23 – 319Combined sources
Beta strandi36 – 438Combined sources
Beta strandi45 – 473Combined sources
Beta strandi50 – 6011Combined sources
Helixi63 – 708Combined sources
Beta strandi72 – 754Combined sources
Beta strandi78 – 814Combined sources
Beta strandi114 – 1196Combined sources
Helixi126 – 1338Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi139 – 1446Combined sources
Turni148 – 1503Combined sources
Beta strandi155 – 1639Combined sources
Helixi164 – 17310Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi184 – 1874Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiQ96EP5.
KOiK14411.
OMAiYSQYAGY.
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. AlignAdd to basket

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

        10         20         30         40         50
MNNSGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS
60 70 80 90 100
RGFGFVKFKD PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG
110 120 130 140 150
WQKGPRSDNS KSNKIFVGGI PHNCGETELR EYFKKFGVVT EVVMIYDAEK
160 170 180 190 200
QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG KKVEVKRAEP RDSKSQAPGQ
210 220 230 240 250
PGASQWGSRV VPNAANGWAG QPPPTWQQGY GPQGMWVPAG QAIGGYGPPP
260 270 280 290 300
AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP
310 320 330 340 350
PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYA
360 370 380 390 400
GYGQDLSGFG QGFSDPSQQP PSYGGPSVPG SGGPPAGGSG FGRGQNHNVQ

GFHPYRR
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi117730. 30 interactions.
IntActiQ96EP5. 9 interactions.
MINTiMINT-3052538.
STRINGi9606.ENSP00000233078.

PTM databases

PhosphoSiteiQ96EP5.

Polymorphism and mutation databases

DMDMi44887869.

2D gel databases

REPRODUCTION-2DPAGEIPI00165230.

Proteomic databases

MaxQBiQ96EP5.
PaxDbiQ96EP5.
PRIDEiQ96EP5.

Protocols and materials databases

DNASUi26528.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi26528.
GeneCardsiGC19P001407.
HGNCiHGNC:2683. DAZAP1.
HPAiHPA004201.
HPA004631.
MIMi607430. gene.
neXtProtiNX_Q96EP5.
PharmGKBiPA27153.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiQ96EP5.
KOiK14411.
OMAiYSQYAGY.
OrthoDBiEOG715Q6V.
PhylomeDBiQ96EP5.
TreeFamiTF314808.

Miscellaneous databases

ChiTaRSiDAZAP1. human.
EvolutionaryTraceiQ96EP5.
GeneWikiiDAZ_associated_protein_1.
GenomeRNAii26528.
NextBioi48864.
PROiQ96EP5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96EP5.
CleanExiHS_DAZAP1.
ExpressionAtlasiQ96EP5. baseline and differential.
GenevisibleiQ96EP5. HS.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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.
  12. 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: June 24, 2015
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.