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Q92784

- DPF3_HUMAN

UniProt

Q92784 - DPF3_HUMAN

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Protein

Zinc finger protein DPF3

Gene

DPF3

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

Functioni

Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri198 – 22124C2H2-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri259 – 31961PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri316 – 36651PHD-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. nervous system development Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Repressor

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein DPF3
Alternative name(s):
BRG1-associated factor 45C
Short name:
BAF45C
Zinc finger protein cer-d4
Gene namesi
Name:DPF3
Synonyms:BAF45C, CERD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:17427. DPF3.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nBAF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi358 – 3581W → E: Abolishes binding to acetylated histones H3 and H4. 1 Publication
Mutagenesisi360 – 3601C → R: Abolishes binding to acetylated histones H3 and H4; when associated with R-363. 1 Publication
Mutagenesisi363 – 3631C → R: Abolishes binding to acetylated histones H3 and H4; when associated with R-360. 1 Publication

Organism-specific databases

PharmGKBiPA134888535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Zinc finger protein DPF3PRO_0000168154Add
BLAST

Proteomic databases

MaxQBiQ92784.
PaxDbiQ92784.
PRIDEiQ92784.

PTM databases

PhosphoSiteiQ92784.

Expressioni

Gene expression databases

BgeeiQ92784.
CleanExiHS_DPF3.
ExpressionAtlasiQ92784. baseline and differential.
GenevestigatoriQ92784.

Interactioni

Subunit structurei

Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Interacts with acetylated histones H3 and H4. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity).By similarity

Protein-protein interaction databases

BioGridi113779. 26 interactions.
DIPiDIP-59245N.
STRINGi9606.ENSP00000381791.

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi263 – 2653Combined sources
Turni273 – 2753Combined sources
Beta strandi285 – 2873Combined sources
Turni293 – 2975Combined sources
Helixi300 – 3089Combined sources
Helixi314 – 3163Combined sources
Turni320 – 3223Combined sources
Turni326 – 3305Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi340 – 3423Combined sources
Turni343 – 3453Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi355 – 3573Combined sources
Helixi361 – 3699Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWJNMR-A261-372[»]
2KWKNMR-A261-372[»]
2KWNNMR-A261-372[»]
2KWONMR-A261-372[»]
ProteinModelPortaliQ92784.
SMRiQ92784. Positions 192-223, 260-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92784.

Family & Domainsi

Domaini

The PHD-type zinc fingers mediate the binding to acetylated histones.2 Publications

Sequence similaritiesi

Belongs to the requiem/DPF family.Curated
Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri198 – 22124C2H2-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri259 – 31961PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri316 – 36651PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG271547.
GeneTreeiENSGT00530000063194.
HOGENOMiHOG000217918.
HOVERGENiHBG004475.
InParanoidiQ92784.
OMAiCLQFTTN.
PhylomeDBiQ92784.
TreeFamiTF318971.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025750. Requiem/DPF_N_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF14051. Requiem_N. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92784-1) [UniParc]FASTAAdd to Basket

Also known as: DPF3b

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
MATVIHNPLK ALGDQFYKEA IEHCRSYNSR LCAERSVRLP FLDSQTGVAQ
60 70 80 90 100
NNCYIWMEKR HRGPGLAPGQ LYTYPARCWR KKRRLHPPED PKLRLLEIKP
110 120 130 140 150
EVELPLKKDG FTSESTTLEA LLRGEGVEKK VDAREEESIQ EIQRVLENDE
160 170 180 190 200
NVEEGNEEED LEEDIPKRKN RTRGRARGSA GGRRRHDAAS QEDHDKPYVC
210 220 230 240 250
DICGKRYKNR PGLSYHYAHT HLASEEGDEA QDQETRSPPN HRNENHRPQK
260 270 280 290 300
GPDGTVIPNN YCDFCLGGSN MNKKSGRPEE LVSCADCGRS GHPTCLQFTL
310 320 330 340 350
NMTEAVKTYK WQCIECKSCI LCGTSENDDQ LLFCDDCDRG YHMYCLNPPV
360 370
AEPPEGSWSC HLCWELLKEK ASAFGCQA
Length:378
Mass (Da):43,084
Last modified:November 25, 2008 - v3
Checksum:i7E6A6FD07A0E4668
GO
Isoform 2 (identifier: Q92784-2) [UniParc]FASTAAdd to Basket

Also known as: DPF3a

The sequence of this isoform differs from the canonical sequence as follows:
     291-378: GHPTCLQFTL...EKASAFGCQA → AHLGGEGRKE...SPTADKKGSC

Note: Lacks PHD-type zinc fingers and does not bind to acetylated histones H3 and H4.

Show »
Length:357
Mass (Da):40,244
Checksum:i50914AC52A9AD3FB
GO
Isoform 3 (identifier: Q92784-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MATVIHNPLKA → MFYGRINGRN...LENLFHMCTR
     291-378: GHPTCLQFTL...EKASAFGCQA → AHLGGEGRKE...SPTADKKGSC

Note: No experimental confirmation available.

Show »
Length:412
Mass (Da):46,401
Checksum:iBB778F504DF34AD9
GO
Isoform 4 (identifier: Q92784-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-378: RGSAGGRRRH...EKASAFGCQA → RCPLPSLHCFLPSLCRDRC

Show »
Length:195
Mass (Da):22,667
Checksum:i48875102247B766B
GO
Isoform 5 (identifier: Q92784-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MATVIHNPLKA → MGFTDLEEPISGCPGGPWALG
     291-378: GHPTCLQFTL...EKASAFGCQA → AHLGGEGRKE...SPTADKKGSC

Show »
Length:367
Mass (Da):41,184
Checksum:i6038156FCCD069B2
GO

Sequence cautioni

Isoform 4 : The sequence BAB14838.1 differs from that shown. Reason: Frameshift at position 187. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121L → V in AAC50686. (PubMed:8812431)Curated
Sequence conflicti24 – 241C → S in AAC50686. (PubMed:8812431)Curated
Sequence conflicti32 – 321C → S in BAB14838. (PubMed:14702039)Curated
Sequence conflicti170 – 1701N → D in BAB14838. (PubMed:14702039)Curated
Sequence conflicti207 – 2071Y → H in BAC86753. (PubMed:14702039)Curated
Sequence conflicti216 – 2161H → Y in BAC86753. (PubMed:14702039)Curated
Isoform 5 (identifier: Q92784-5)
Sequence conflicti358 – 3581S → P in BAH11762. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771R → H.1 Publication
Corresponds to variant rs17855717 [ dbSNP | Ensembl ].
VAR_047771
Isoform 2 (identifier: Q92784-2)
Natural varianti326 – 3261H → R in dbSNP: rs17855716.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111MATVIHNPLKA → MFYGRINGRNFAASSLPVAF AATPLMLFLPNPQLICSFPI SSRNHITGLMPPGKLKLENL FHMCTR in isoform 3. 1 PublicationVSP_035882Add
BLAST
Alternative sequencei1 – 1111MATVIHNPLKA → MGFTDLEEPISGCPGGPWAL G in isoform 5. 1 PublicationVSP_055748Add
BLAST
Alternative sequencei177 – 378202RGSAG…FGCQA → RCPLPSLHCFLPSLCRDRC in isoform 4. 1 PublicationVSP_035883Add
BLAST
Alternative sequencei291 – 37888GHPTC…FGCQA → AHLGGEGRKEKEAAAAARTT EDLFGSTSESDTSTFHGFDE DDLEEPRSCRGRRSGRGSPT ADKKGSC in isoform 2, isoform 3 and isoform 5. 3 PublicationsVSP_035884Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY803021 mRNA. Translation: AAX20019.1.
AK024141 mRNA. Translation: BAB14838.1. Frameshift.
AK126933 mRNA. Translation: BAC86753.1.
AK294425 mRNA. Translation: BAH11762.1.
AC004828 Genomic DNA. No translation available.
AC006360 Genomic DNA. No translation available.
AL392024 Genomic DNA. No translation available.
AC007160 Genomic DNA. No translation available.
BC060801 mRNA. Translation: AAH60801.1.
U43919 Genomic DNA. Translation: AAC50686.1.
CCDSiCCDS45133.1. [Q92784-2]
CCDS61495.1. [Q92784-5]
CCDS61496.1. [Q92784-3]
CCDS61497.1. [Q92784-1]
RefSeqiNP_001267471.1. NM_001280542.1. [Q92784-1]
NP_001267472.1. NM_001280543.1. [Q92784-5]
NP_001267473.1. NM_001280544.1.
NP_036206.3. NM_012074.4. [Q92784-2]
UniGeneiHs.162868.

Genome annotation databases

EnsembliENST00000381216; ENSP00000370614; ENSG00000205683. [Q92784-2]
ENST00000541685; ENSP00000441640; ENSG00000205683. [Q92784-2]
ENST00000546183; ENSP00000444662; ENSG00000205683. [Q92784-5]
ENST00000556509; ENSP00000450518; ENSG00000205683. [Q92784-1]
ENST00000614862; ENSP00000481992; ENSG00000205683. [Q92784-5]
GeneIDi8110.
KEGGihsa:8110.
UCSCiuc001xnc.2. human. [Q92784-1]
uc010ari.1. human. [Q92784-2]

Polymorphism databases

DMDMi215274167.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY803021 mRNA. Translation: AAX20019.1 .
AK024141 mRNA. Translation: BAB14838.1 . Frameshift.
AK126933 mRNA. Translation: BAC86753.1 .
AK294425 mRNA. Translation: BAH11762.1 .
AC004828 Genomic DNA. No translation available.
AC006360 Genomic DNA. No translation available.
AL392024 Genomic DNA. No translation available.
AC007160 Genomic DNA. No translation available.
BC060801 mRNA. Translation: AAH60801.1 .
U43919 Genomic DNA. Translation: AAC50686.1 .
CCDSi CCDS45133.1. [Q92784-2 ]
CCDS61495.1. [Q92784-5 ]
CCDS61496.1. [Q92784-3 ]
CCDS61497.1. [Q92784-1 ]
RefSeqi NP_001267471.1. NM_001280542.1. [Q92784-1 ]
NP_001267472.1. NM_001280543.1. [Q92784-5 ]
NP_001267473.1. NM_001280544.1.
NP_036206.3. NM_012074.4. [Q92784-2 ]
UniGenei Hs.162868.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KWJ NMR - A 261-372 [» ]
2KWK NMR - A 261-372 [» ]
2KWN NMR - A 261-372 [» ]
2KWO NMR - A 261-372 [» ]
ProteinModelPortali Q92784.
SMRi Q92784. Positions 192-223, 260-372.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113779. 26 interactions.
DIPi DIP-59245N.
STRINGi 9606.ENSP00000381791.

PTM databases

PhosphoSitei Q92784.

Polymorphism databases

DMDMi 215274167.

Proteomic databases

MaxQBi Q92784.
PaxDbi Q92784.
PRIDEi Q92784.

Protocols and materials databases

DNASUi 8110.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381216 ; ENSP00000370614 ; ENSG00000205683 . [Q92784-2 ]
ENST00000541685 ; ENSP00000441640 ; ENSG00000205683 . [Q92784-2 ]
ENST00000546183 ; ENSP00000444662 ; ENSG00000205683 . [Q92784-5 ]
ENST00000556509 ; ENSP00000450518 ; ENSG00000205683 . [Q92784-1 ]
ENST00000614862 ; ENSP00000481992 ; ENSG00000205683 . [Q92784-5 ]
GeneIDi 8110.
KEGGi hsa:8110.
UCSCi uc001xnc.2. human. [Q92784-1 ]
uc010ari.1. human. [Q92784-2 ]

Organism-specific databases

CTDi 8110.
GeneCardsi GC14M073086.
HGNCi HGNC:17427. DPF3.
MIMi 601672. gene.
neXtProti NX_Q92784.
PharmGKBi PA134888535.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271547.
GeneTreei ENSGT00530000063194.
HOGENOMi HOG000217918.
HOVERGENi HBG004475.
InParanoidi Q92784.
OMAi CLQFTTN.
PhylomeDBi Q92784.
TreeFami TF318971.

Miscellaneous databases

EvolutionaryTracei Q92784.
GenomeRNAii 8110.
NextBioi 30759.
PROi Q92784.
SOURCEi Search...

Gene expression databases

Bgeei Q92784.
CleanExi HS_DPF3.
ExpressionAtlasi Q92784. baseline and differential.
Genevestigatori Q92784.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi IPR025750. Requiem/DPF_N_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00628. PHD. 1 hit.
PF14051. Requiem_N. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 2 hits.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
    Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
    Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, INTERACTION WITH HISTONES, MUTAGENESIS OF TRP-358; CYS-360 AND CYS-363.
    Tissue: Heart.
  2. "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 3; 4 AND 5).
    Tissue: Brain and Embryo.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2), VARIANT HIS-177.
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-64.
  6. "Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b."
    Zeng L., Zhang Q., Li S., Plotnikov A.N., Walsh M.J., Zhou M.M.
    Nature 466:258-262(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 261-372, DOMAIN PHD.

Entry informationi

Entry nameiDPF3_HUMAN
AccessioniPrimary (citable) accession number: Q92784
Secondary accession number(s): A8MSI3
, B7Z276, F5H575, Q32UJ0, Q6P9E6, Q6ZT41, Q9H7Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 112 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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