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Protein

DAZ-associated protein 2

Gene

DAZAP2

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

Functioni

GO - Molecular functioni

  • WW domain binding Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
DAZ-associated protein 2
Alternative name(s):
Deleted in azoospermia-associated protein 2
Gene namesi
Name:DAZAP2
Synonyms:KIAA0058
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2684. DAZAP2.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Predominantly nuclear in macrophages, stimulation of IL17RB with its ligand IL17E induces accumulation in the cytoplasm.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27154.

Polymorphism and mutation databases

BioMutaiDAZAP2.
DMDMi44887865.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168DAZ-associated protein 2PRO_0000079788Add
BLAST

Post-translational modificationi

Ubiquitinated by SMURF2, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ15038.
PRIDEiQ15038.

PTM databases

PhosphoSiteiQ15038.

Expressioni

Tissue specificityi

Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. Down-regulated in multiple myeloma.1 Publication

Gene expression databases

BgeeiQ15038.
CleanExiHS_DAZAP2.
ExpressionAtlasiQ15038. baseline and differential.
GenevisibleiQ15038. HS.

Interactioni

Subunit structurei

Interacts with SOX6 (By similarity). Interacts with DAZ and DAZL. Interacts with IL17RB. May interact with FAM168B.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARID5AC9J1Q03EBI-724310,EBI-10176351
ATXN1P542532EBI-724310,EBI-930964
BAG3O958174EBI-724310,EBI-747185
BATF2Q8N1L93EBI-724310,EBI-742695
C1orf94Q6P1W54EBI-724310,EBI-946029
CALCOCO2Q131374EBI-724310,EBI-739580
DAB1O755533EBI-724310,EBI-7875264
DCUN1D1Q96GG94EBI-724310,EBI-740086
EPN1Q9Y6I33EBI-724310,EBI-713198
EXD3Q9NX533EBI-724310,EBI-750745
FAM168AQ925673EBI-724310,EBI-7957930
HGSO149644EBI-724310,EBI-740220
HIP1O002913EBI-724310,EBI-473886
KRTAP19-5Q3LI723EBI-724310,EBI-1048945
KRTAP8-1Q8IUC23EBI-724310,EBI-10261141
NEDD4LQ96PU53EBI-724310,EBI-717962
OPTNQ96CV93EBI-724310,EBI-748974
OTULINQ96BN83EBI-724310,EBI-750730
PEF1Q9UBV83EBI-724310,EBI-724639
PLEKHB2Q96CS73EBI-724310,EBI-373552
PLSCR1O151624EBI-724310,EBI-740019
POGZQ7Z3K33EBI-724310,EBI-1389308
POLIQ9UNA43EBI-724310,EBI-741774
PRR20CP864794EBI-724310,EBI-10172814
RABGEF1Q9UJ413EBI-724310,EBI-913954
RBFOX2O432514EBI-724310,EBI-746056
RBPMSQ930626EBI-724310,EBI-740322
RHOXF2Q9BQY46EBI-724310,EBI-372094
RNF115Q9Y4L54EBI-724310,EBI-2129242
RNF208Q9H0X64EBI-724310,EBI-751555
ROR2A1L4F53EBI-724310,EBI-10172778
RPS27AP629794EBI-724310,EBI-357375
SMAP2Q8WU793EBI-724310,EBI-2822515
STAM2O758864EBI-724310,EBI-373258
TAX1BP1Q86VP13EBI-724310,EBI-529518
TEX37Q96LM63EBI-724310,EBI-743976
TNIP3Q96KP63EBI-724310,EBI-2509913
TOLLIPQ6FIE93EBI-724310,EBI-10249783
TOLLIPQ9H0E26EBI-724310,EBI-74615
UBAC1Q9BSL14EBI-724310,EBI-749370
UBASH3AP570754EBI-724310,EBI-2105393
UBASH3BQ8TF423EBI-724310,EBI-1380492
UBBQ5U5U63EBI-724310,EBI-1642104
UBCQ96C324EBI-724310,EBI-745483
UBE2D4Q9Y2X83EBI-724310,EBI-745527
UBE2E2Q96LR53EBI-724310,EBI-2129763
USP5P459743EBI-724310,EBI-741277
VHLLQ6RSH73EBI-724310,EBI-10254232
VPS37CA5D8V63EBI-724310,EBI-2559305
ZFAND2BQ8WV996EBI-724310,EBI-747823

Protein-protein interaction databases

BioGridi115143. 97 interactions.
IntActiQ15038. 90 interactions.
MINTiMINT-1179995.
STRINGi9606.ENSP00000448051.

Structurei

3D structure databases

ProteinModelPortaliQ15038.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 134127Pro-richAdd
BLAST

Phylogenomic databases

eggNOGiNOG286791.
GeneTreeiENSGT00390000000685.
HOGENOMiHOG000007683.
HOVERGENiHBG051300.
InParanoidiQ15038.
OMAiAYSEIYQ.
OrthoDBiEOG77HDG0.
PhylomeDBiQ15038.
TreeFamiTF329672.

Family and domain databases

InterProiIPR022730. DAZ_assoc-2.
[Graphical view]
PfamiPF11029. DAZAP2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15038-1) [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
MNSKGQYPTQ PTYPVQPPGN PVYPQTLHLP QAPPYTDAPP AYSELYRPSF
60 70 80 90 100
VHPGAATVPT MSAAFPGASL YLPMAQSVAV GPLGSTIPMA YYPVGPIYPP
110 120 130 140 150
GSTVLVEGGY DAGARFGAGA TAGNIPPPPP GCPPNAAQLA VMQGANVLVT
160
QRKGNFFMGG SDGGYTIW
Length:168
Mass (Da):17,319
Last modified:November 1, 1996 - v1
Checksum:i49F1B6D281E24AAC
GO
Isoform 2 (identifier: Q15038-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-168: PPPPGCPPNAAQLAVMQGANVLVTQRKGNFFMGGSDGGYTIW → VKEDQDHDREQGEEDNGDNNLERRGKM

Note: No experimental confirmation available.
Show »
Length:153
Mass (Da):16,187
Checksum:iFAF1904AF43CA4E4
GO
Isoform 6 (identifier: Q15038-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-86: Missing.

Note: No experimental confirmation available.
Show »
Length:146
Mass (Da):15,173
Checksum:i3EA0DB83FB16A1A8
GO
Isoform 3 (identifier: Q15038-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-76: Missing.

Show »
Length:136
Mass (Da):13,987
Checksum:i46E379CE7F8A3A04
GO
Isoform 4 (identifier: Q15038-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-126: Missing.

Note: No experimental confirmation available.
Show »
Length:86
Mass (Da):9,167
Checksum:i5A99269B0CBA9174
GO
Isoform 5 (identifier: Q15038-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-168: GSTVLVEGGY...GGSDGGYTIW → ASTSWMPSQC...RNHVMVAVPP

Note: No experimental confirmation available.
Show »
Length:207
Mass (Da):22,823
Checksum:i24B6E3CC46C33150
GO

Sequence cautioni

The sequence BAA06545.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291L → P in BAG64775 (PubMed:14702039).Curated
Sequence conflicti47 – 471R → S in AAR11454 (PubMed:17935665).Curated
Sequence conflicti90 – 901A → V in BU662353 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021S → A.
Corresponds to variant rs57917280 [ dbSNP | Ensembl ].
VAR_061639

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei45 – 12682Missing in isoform 4. 1 PublicationVSP_045678Add
BLAST
Alternative sequencei45 – 7632Missing in isoform 3. 1 PublicationVSP_045679Add
BLAST
Alternative sequencei65 – 8622Missing in isoform 6. CuratedVSP_055181Add
BLAST
Alternative sequencei101 – 16868GSTVL…GYTIW → ASTSWMPSQCCSACSHAGSQ RPRNSAEGELLHGWFRWWLH HLVRNQGHLCAGKDITYLQH FSQCNCFSHINLKLQFRHML LGCLSGAQTFRHFSNLIRNH VMVAVPP in isoform 5. 1 PublicationVSP_046764Add
BLAST
Alternative sequencei127 – 16842PPPPG…GYTIW → VKEDQDHDREQGEEDNGDNN LERRGKM in isoform 2. 1 PublicationVSP_042773Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY430097 mRNA. Translation: AAR11454.1.
BU662353 mRNA. No translation available.
D31767 mRNA. Translation: BAA06545.2. Different initiation.
BX441137 mRNA. No translation available.
AK095963 mRNA. No translation available.
AK290119 mRNA. Translation: BAF82808.1.
AK293330 mRNA. Translation: BAG56846.1.
AK303828 mRNA. Translation: BAG64775.1.
AC046135 Genomic DNA. No translation available.
AC139768 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58181.1.
BC002334 mRNA. Translation: AAH02334.1.
BC007900 mRNA. Translation: AAH07900.1.
CCDSiCCDS44884.1. [Q15038-2]
CCDS44885.1. [Q15038-5]
CCDS44886.1. [Q15038-6]
CCDS44887.1. [Q15038-3]
CCDS44888.1. [Q15038-4]
CCDS8809.1. [Q15038-1]
RefSeqiNP_001129736.1. NM_001136264.1. [Q15038-6]
NP_001129738.1. NM_001136266.1. [Q15038-5]
NP_001129739.1. NM_001136267.1. [Q15038-3]
NP_001129740.1. NM_001136268.1. [Q15038-4]
NP_001129741.1. NM_001136269.1. [Q15038-2]
NP_055579.1. NM_014764.3. [Q15038-1]
UniGeneiHs.369761.

Genome annotation databases

EnsembliENST00000412716; ENSP00000394699; ENSG00000183283. [Q15038-1]
ENST00000425012; ENSP00000408251; ENSG00000183283. [Q15038-2]
ENST00000439799; ENSP00000398804; ENSG00000183283. [Q15038-4]
ENST00000449723; ENSP00000412812; ENSG00000183283. [Q15038-6]
ENST00000549555; ENSP00000448051; ENSG00000183283. [Q15038-5]
ENST00000549732; ENSP00000446554; ENSG00000183283. [Q15038-3]
GeneIDi9802.
KEGGihsa:9802.
UCSCiuc001ryb.3. human. [Q15038-1]
uc010snf.1. human. [Q15038-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY430097 mRNA. Translation: AAR11454.1.
BU662353 mRNA. No translation available.
D31767 mRNA. Translation: BAA06545.2. Different initiation.
BX441137 mRNA. No translation available.
AK095963 mRNA. No translation available.
AK290119 mRNA. Translation: BAF82808.1.
AK293330 mRNA. Translation: BAG56846.1.
AK303828 mRNA. Translation: BAG64775.1.
AC046135 Genomic DNA. No translation available.
AC139768 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58181.1.
BC002334 mRNA. Translation: AAH02334.1.
BC007900 mRNA. Translation: AAH07900.1.
CCDSiCCDS44884.1. [Q15038-2]
CCDS44885.1. [Q15038-5]
CCDS44886.1. [Q15038-6]
CCDS44887.1. [Q15038-3]
CCDS44888.1. [Q15038-4]
CCDS8809.1. [Q15038-1]
RefSeqiNP_001129736.1. NM_001136264.1. [Q15038-6]
NP_001129738.1. NM_001136266.1. [Q15038-5]
NP_001129739.1. NM_001136267.1. [Q15038-3]
NP_001129740.1. NM_001136268.1. [Q15038-4]
NP_001129741.1. NM_001136269.1. [Q15038-2]
NP_055579.1. NM_014764.3. [Q15038-1]
UniGeneiHs.369761.

3D structure databases

ProteinModelPortaliQ15038.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115143. 97 interactions.
IntActiQ15038. 90 interactions.
MINTiMINT-1179995.
STRINGi9606.ENSP00000448051.

PTM databases

PhosphoSiteiQ15038.

Polymorphism and mutation databases

BioMutaiDAZAP2.
DMDMi44887865.

Proteomic databases

MaxQBiQ15038.
PRIDEiQ15038.

Protocols and materials databases

DNASUi9802.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000412716; ENSP00000394699; ENSG00000183283. [Q15038-1]
ENST00000425012; ENSP00000408251; ENSG00000183283. [Q15038-2]
ENST00000439799; ENSP00000398804; ENSG00000183283. [Q15038-4]
ENST00000449723; ENSP00000412812; ENSG00000183283. [Q15038-6]
ENST00000549555; ENSP00000448051; ENSG00000183283. [Q15038-5]
ENST00000549732; ENSP00000446554; ENSG00000183283. [Q15038-3]
GeneIDi9802.
KEGGihsa:9802.
UCSCiuc001ryb.3. human. [Q15038-1]
uc010snf.1. human. [Q15038-2]

Organism-specific databases

CTDi9802.
GeneCardsiGC12P051634.
HGNCiHGNC:2684. DAZAP2.
MIMi607431. gene.
neXtProtiNX_Q15038.
PharmGKBiPA27154.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG286791.
GeneTreeiENSGT00390000000685.
HOGENOMiHOG000007683.
HOVERGENiHBG051300.
InParanoidiQ15038.
OMAiAYSEIYQ.
OrthoDBiEOG77HDG0.
PhylomeDBiQ15038.
TreeFamiTF329672.

Miscellaneous databases

ChiTaRSiDAZAP2. human.
GeneWikiiDAZAP2.
GenomeRNAii9802.
NextBioi36908.
PROiQ15038.
SOURCEiSearch...

Gene expression databases

BgeeiQ15038.
CleanExiHS_DAZAP2.
ExpressionAtlasiQ15038. baseline and differential.
GenevisibleiQ15038. HS.

Family and domain databases

InterProiIPR022730. DAZ_assoc-2.
[Graphical view]
PfamiPF11029. DAZAP2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular features and expression of DAZAP2 in human multiple myeloma."
    Shi Y.-W., Shen R., Ren W., Tang L.J., Tan D.-R., Hu W.-X.
    Chin. Med. J. 120:1659-1665(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Bone marrow.
  2. "Gene expression in human erythroid precursor cells."
    Gubin A.N., Lee Y.T., Bouffard G.G., Miller J.L.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Erythroblast.
  3. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Fetal brain.
  5. "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] (ISOFORMS 1; 2 AND 5).
    Tissue: Lung, Mammary gland and Thalamus.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: B-cell and Brain.
  9. "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: TISSUE SPECIFICITY, INTERACTION WITH DAZ AND DAZL.
    Tissue: Testis.
  10. "Characterizing the neurite outgrowth inhibitory effect of Mani."
    Mishra M., Lee S., Lin M.K., Yamashita T., Heese K.
    FEBS Lett. 586:3018-3023(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM168B.
  11. "Smurf2 regulates IL17RB by proteasomal degradation of its novel binding partner DAZAP2."
    Popova A., Kzhyshkowska J., Nurgazieva D., Goerdt S., Gratchev A.
    Immunobiology 217:321-328(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY SMURF2, SUBCELLULAR LOCATION, INTERACTION WITH IL17RB.

Entry informationi

Entry nameiDAZP2_HUMAN
AccessioniPrimary (citable) accession number: Q15038
Secondary accession number(s): A8K254
, B4DDT5, B4E1G3, C9JA96, C9JP84, E9PB45, F8VU62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 118 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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.