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Protein

DBIRD complex subunit ZNF326

Gene

Znf326

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (By similarity). May also play a role in neuronal differentiation. Able to bind DNA and activate expression in vitro.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri312 – 33625C2H2 AKAP95-type 1Add
BLAST
Zinc fingeri405 – 43026C2H2 AKAP95-type 2Add
BLAST

GO - Molecular functioni

  • DNA binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • RNA polymerase II core binding Source: UniProtKB
  • zinc ion binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DBIRD complex subunit ZNF326
Alternative name(s):
Zinc finger protein 326
Zinc finger protein interacting with mRNPs
Zinc finger protein-associated with nuclear matrix of 75 kDa
Gene namesi
Name:Znf326
Synonyms:Zan75, Zfp326, Zird
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1927246. Zfp326.

Subcellular locationi

GO - Cellular componenti

  • DBIRD complex Source: UniProtKB
  • intracellular membrane-bounded organelle Source: MGI
  • nuclear matrix Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580DBIRD complex subunit ZNF326PRO_0000075387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineBy similarity
Modified residuei69 – 691PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei247 – 2471N6-acetyllysineBy similarity
Modified residuei270 – 2701PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO88291.
MaxQBiO88291.
PaxDbiO88291.
PRIDEiO88291.

PTM databases

iPTMnetiO88291.
PhosphoSiteiO88291.

Expressioni

Tissue specificityi

Ubiquitously expressed in adult tissues. Highly expressed in neuronal tissues such as brain and neural tube.2 Publications

Developmental stagei

Weakly expressed during E9.5 and E10.5, expressed at highest level in E11.5 and gradually decreases thereafter. During the cell cycle, it is weakly expressed in G0 and G1 phases. It increases during G1, S, G2 and M phases.2 Publications

Inductioni

Upon retinoic acid treatment.1 Publication

Gene expression databases

BgeeiO88291.
CleanExiMM_ZFP326.

Interactioni

Subunit structurei

Component of the DBIRD complex. Interacts with CCAR2; the interaction is direct (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207624. 3 interactions.
DIPiDIP-58947N.
IntActiO88291. 2 interactions.
MINTiMINT-4105453.
STRINGi10090.ENSMUSP00000031227.

Structurei

3D structure databases

ProteinModelPortaliO88291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 124124Mediates transcriptional activationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi238 – 26023Bipartite nuclear localization signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 211185Gly-richAdd
BLAST
Compositional biasi484 – 56481Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the AKAP95 family.Curated
Contains 2 C2H2 AKAP95-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri312 – 33625C2H2 AKAP95-type 1Add
BLAST
Zinc fingeri405 – 43026C2H2 AKAP95-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGVY. Eukaryota.
ENOG4111H5U. LUCA.
HOGENOMiHOG000234349.
HOVERGENiHBG080752.
InParanoidiO88291.
KOiK13204.
OrthoDBiEOG7DC247.
PhylomeDBiO88291.
TreeFamiTF105407.

Family and domain databases

InterProiIPR007071. AKAP95.
[Graphical view]
PANTHERiPTHR12190. PTHR12190. 1 hit.
PfamiPF04988. AKAP95. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O88291-1) [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
MDFEDDYVHS TCRGAYQDFN GMDRDYGPGS YGGLDRDYGH GSYGGQRSMD
60 70 80 90 100
SYLNQSYGMD NHSGGGGGSR FGPYESYDSR SSLGGRDLYR SGYGFNEPEQ
110 120 130 140 150
TRFGGSYGGR FESSYRNSLD SFGGRNQGGS SWEAPYSRSK LRPGFMEDRG
160 170 180 190 200
RENYSSYSSF SSPHMKPAPV GSRGRGTPAY PESTFGSRSY DAFGGPSTGR
210 220 230 240 250
GRGRGHMGDF GSFHRPGIIV DYQNKPANVT IATARGIKRK MMQIFIKPGG
260 270 280 290 300
AFIKKPKLAK PMDKMNLSKS PTKTDPKNEE EEKRRIEARR EKQRRRREKN
310 320 330 340 350
SEKYGDGYRM AFTCSFCKFR TFEEKDIELH LESSSHQETL DHIQKQTKFD
360 370 380 390 400
KVVMEFLHEC MVNKFKKASI RKQQTLNHPE AYKIIEKDIM EGVTADDHMM
410 420 430 440 450
KVETVHCSAC SVYIPALHSS VQLHLKSPDH SKGKQAYKEQ IKRESVLTAT
460 470 480 490 500
SILNNPIVKA RYERFVKGEN PFEIQDHPQD QQIEGDEEDE EKIDEPIEEE
510 520 530 540 550
EEEEEEEEEE GEEAGSVEEE GDVEGEEGTA EAAAAGEADA VGEAEGAGEA
560 570 580
EEAEEEEEEE GTQEFAAQAC ATEQCEHRQM
Length:580
Mass (Da):65,225
Last modified:November 1, 1998 - v1
Checksum:iEF9672513D0FFC70
GO
Isoform 2 (identifier: O88291-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.

Note: No experimental confirmation available.
Show »
Length:374
Mass (Da):42,704
Checksum:i53B54BA03C1153AF
GO
Isoform 3 (identifier: O88291-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-67: DRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGG → AFKDIYLKILLLSASKGEQHLIFFFLNSYRAGS
     68-580: Missing.

Note: No experimental confirmation available.
Show »
Length:67
Mass (Da):7,613
Checksum:i9CD968EC81C96109
GO

Sequence cautioni

The sequence AAH05567.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551Q → R in BAE27172 (PubMed:16141072).Curated
Sequence conflicti494 – 4941D → G in BAB30878 (PubMed:16141072).Curated
Sequence conflicti494 – 4941D → G in BAE37040 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 206206Missing in isoform 2. 1 PublicationVSP_014957Add
BLAST
Alternative sequencei35 – 6733DRDYG…SGGGG → AFKDIYLKILLLSASKGEQH LIFFFLNSYRAGS in isoform 3. 1 PublicationVSP_014958Add
BLAST
Alternative sequencei68 – 580513Missing in isoform 3. 1 PublicationVSP_014959Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012725 mRNA. Translation: BAA31522.1.
AK017693 mRNA. Translation: BAB30878.1.
AK032801 mRNA. Translation: BAC28029.1.
AK146438 mRNA. Translation: BAE27172.1.
AK162729 mRNA. Translation: BAE37040.1.
BC037055 mRNA. Translation: AAH37055.1.
BC005567 mRNA. Translation: AAH05567.1. Sequence problems.
CCDSiCCDS19496.1. [O88291-1]
RefSeqiNP_061229.2. NM_018759.2.
UniGeneiMm.248876.

Genome annotation databases

GeneIDi54367.
KEGGimmu:54367.
UCSCiuc008ylj.3. mouse. [O88291-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012725 mRNA. Translation: BAA31522.1.
AK017693 mRNA. Translation: BAB30878.1.
AK032801 mRNA. Translation: BAC28029.1.
AK146438 mRNA. Translation: BAE27172.1.
AK162729 mRNA. Translation: BAE37040.1.
BC037055 mRNA. Translation: AAH37055.1.
BC005567 mRNA. Translation: AAH05567.1. Sequence problems.
CCDSiCCDS19496.1. [O88291-1]
RefSeqiNP_061229.2. NM_018759.2.
UniGeneiMm.248876.

3D structure databases

ProteinModelPortaliO88291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207624. 3 interactions.
DIPiDIP-58947N.
IntActiO88291. 2 interactions.
MINTiMINT-4105453.
STRINGi10090.ENSMUSP00000031227.

PTM databases

iPTMnetiO88291.
PhosphoSiteiO88291.

Proteomic databases

EPDiO88291.
MaxQBiO88291.
PaxDbiO88291.
PRIDEiO88291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi54367.
KEGGimmu:54367.
UCSCiuc008ylj.3. mouse. [O88291-1]

Organism-specific databases

CTDi54367.
MGIiMGI:1927246. Zfp326.

Phylogenomic databases

eggNOGiENOG410IGVY. Eukaryota.
ENOG4111H5U. LUCA.
HOGENOMiHOG000234349.
HOVERGENiHBG080752.
InParanoidiO88291.
KOiK13204.
OrthoDBiEOG7DC247.
PhylomeDBiO88291.
TreeFamiTF105407.

Miscellaneous databases

PROiO88291.
SOURCEiSearch...

Gene expression databases

BgeeiO88291.
CleanExiMM_ZFP326.

Family and domain databases

InterProiIPR007071. AKAP95.
[Graphical view]
PANTHERiPTHR12190. PTHR12190. 1 hit.
PfamiPF04988. AKAP95. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel zinc finger protein that associates with nuclear matrix."
    Lee J.-Y., Kambe M., Hayashi M., Takenaga K.
    DNA Cell Biol. 17:849-858(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Thymus and Wolffian duct.
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-277 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Characterization of a zinc finger protein ZAN75: nuclear localization signal, transcriptional activator activity, and expression during neuronal differentiation of P19 cells."
    Lee J.-Y., Nakane Y., Koshikawa N., Nakayama K., Hayashi M., Takenaga K.
    DNA Cell Biol. 19:227-234(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIPARTITE NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Kidney.

Entry informationi

Entry nameiZN326_MOUSE
AccessioniPrimary (citable) accession number: O88291
Secondary accession number(s): Q05DP5
, Q3TRI9, Q3UJI3, Q8BSJ5, Q8K1X9, Q9CYG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.