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Q96EP5 (DAZP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DAZ-associated protein 1
Alternative name(s):
Deleted in azoospermia-associated protein 1
Gene names
Name:DAZAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.8

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

Acetylation at Lys-150 is predominantly observed in the nuclear fraction, and may regulate nucleocytoplasmic transport. Ref.3 Ref.8

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407DAZ-associated protein 1
PRO_0000081565

Regions

Domain10 – 9788RRM 1
Domain113 – 19078RRM 2
Compositional bias222 – 385164Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.3 Ref.6
Modified residue1501N6-acetyllysine Ref.8

Natural variations

Alternative sequence350 – 40758AGYGQ…HPYRR → GLGSYSPAPPGCGPHFVYSL MVRLSSDVA in isoform 2.
VSP_009441
Natural variant3811S → T in a breast cancer sample; somatic mutation. Ref.11
VAR_035480

Experimental info

Sequence conflict1091N → Y in AAF78364. Ref.1

Secondary structure

................................. 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CFEB42903F4D5AFB

FASTA40743,383
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F8DDAD1AFDD37C3E
Show »

FASTA37840,530

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] [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, 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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [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.
RefSeqNP_061832.2. NM_018959.3.
NP_733829.1. NM_170711.2.
XP_005259590.1. XM_005259533.1.
UniGeneHs.222510.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGSNMR-A110-195[»]
2DH8NMR-A1-92[»]
ProteinModelPortalQ96EP5.
SMRQ96EP5. Positions 6-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117730. 21 interactions.
IntActQ96EP5. 9 interactions.
MINTMINT-3052538.
STRING9606.ENSP00000233078.

PTM databases

PhosphoSiteQ96EP5.

Polymorphism databases

DMDM44887869.

2D gel databases

REPRODUCTION-2DPAGEIPI00165230.

Proteomic databases

PaxDbQ96EP5.
PRIDEQ96EP5.

Protocols and materials databases

DNASU26528.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233078; ENSP00000233078; ENSG00000071626. [Q96EP5-1]
ENST00000336761; ENSP00000337132; ENSG00000071626. [Q96EP5-2]
GeneID26528.
KEGGhsa:26528.
UCSCuc002lsm.3. human. [Q96EP5-2]
uc002lsn.3. human. [Q96EP5-1]

Organism-specific databases

CTD26528.
GeneCardsGC19P001407.
HGNCHGNC:2683. DAZAP1.
HPAHPA004201.
HPA004631.
MIM607430. gene.
neXtProtNX_Q96EP5.
PharmGKBPA27153.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000234441.
HOVERGENHBG002295.
InParanoidQ96EP5.
KOK14411.
OMADFPYSQY.
OrthoDBEOG715Q6V.
PhylomeDBQ96EP5.
TreeFamTF314808.

Gene expression databases

ArrayExpressQ96EP5.
BgeeQ96EP5.
CleanExHS_DAZAP1.
GenevestigatorQ96EP5.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAZAP1. human.
EvolutionaryTraceQ96EP5.
GeneWikiDAZ_associated_protein_1.
GenomeRNAi26528.
NextBio48864.
PROQ96EP5.
SOURCESearch...

Entry information

Entry nameDAZP1_HUMAN
AccessionPrimary (citable) accession number: Q96EP5
Secondary accession number(s): Q96MJ3, Q9NRR9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM