Q96EP5 (DAZP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DAZ-associated protein 1

Alternative name(s):
Deleted in azoospermia-associated protein 1

Gene names

Name:

DAZAP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. 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.7
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.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.
Sequence caution	The sequence BAB71295.1 differs from that shown. Reason: Erroneous initiation.

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
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred 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

Modified residue

150

1

N6-acetyllysine Ref.7

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.9

VAR_035480

Experimental info

Sequence conflict

109

1

N → Y in AAF78364. Ref.1

Secondary structure

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407

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: CFEB42903F4D5AFB	FASTA	407	43,383
	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
	Isoform 2 [UniParc]. Checksum: F8DDAD1AFDD37C3E	FASTA	378	40,530
	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 QPDFPYGQYG LGSYSPAPPG 370 CGPHFVYSLM VRLSSDVA

References

	« Hide 'large scale' referencesShow '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. , 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]	"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].
[7]	"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.
[8]	"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.
[9]	"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. , 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.

IPI

IPI00165230.
IPI00335930.

RefSeq

NP_061832.2. NM_018959.2.
NP_733829.1. NM_170711.1.

UniGene

Hs.222510.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DGS	NMR	-	A	110-195	[»]
2DH8	NMR	-	A	1-92	[»]

ProteinModelPortal

Q96EP5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96EP5. 8 interactions.

STRING

9606.ENSP00000233078.

PTM databases

PhosphoSite

Q96EP5.

Polymorphism databases

DMDM

44887869.

2D gel databases

REPRODUCTION-2DPAGE

IPI00165230.

Proteomic databases

PaxDb

Q96EP5.

PRIDE

Q96EP5.

Protocols and materials databases

DNASU

26528.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233078; ENSP00000233078; ENSG00000071626.
ENST00000336761; ENSP00000337132; ENSG00000071626.

GeneID

26528.

KEGG

hsa:26528.

UCSC

uc002lsm.3. human.
uc002lsn.3. human.

Organism-specific databases

CTD

26528.

GeneCards

GC19P001407.

HGNC

HGNC:2683. DAZAP1.

HPA

HPA004201.
HPA004631.

MIM

607430. gene.

neXtProt

NX_Q96EP5.

PharmGKB

PA27153.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000234441.

HOVERGEN

HBG002295.

InParanoid

Q96EP5.

KO

K14411.

OMA

HNLDGRN.

OrthoDB

EOG40ZQXT.

PhylomeDB

Q96EP5.

Gene expression databases

ArrayExpress

Q96EP5.

Bgee

Q96EP5.

CleanEx

HS_DAZAP1.

Genevestigator

Q96EP5.

GermOnline

ENSG00000071626. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

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

ChiTaRS

DAZAP1. human.

EvolutionaryTrace

Q96EP5.

GenomeRNAi

26528.

NextBio

48864.

SOURCE

Search...

Entry information

Entry name

DAZP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.