UniProt Accession

 ZN326_HUMAN; Q5BKZ1; A8MYX1; B4DLN0; B4E179; Q5VW93; Q5VW94; Q5VW96; Q5VW97; Q6NSA2; Q7Z638; Q7Z6C2 

Genbank Protein ID

 AK297073; AK303707; AL161797; AL391497; AL161797; AL391497; AL391497; AL161797; AL391497; AL161797; AL391497; CH471097; CH471097; BC052645; BC053888; BC070341; BC090866 

Genbank Nucleotide ID

 BAG59592.1; BAG64691.1; CAI23073.1; CAI23073.1; CAI23074.1; CAI23074.1; CAH72228.1; CAH72228.1; CAH72229.1; CAH72229.1; CAH72230.1; EAW73125.1; EAW73128.1; AAH52645.1; AAH53888.1; AAH70341.1; AAH90866.1 

Protein Name

 DBIRD complex subunit ZNF326 

Protein Synonyms/Alias

 Zinc finger protein 326; Zinc finger protein interacting with mRNPs and DBC1 

Gene Name

 ZNF326 

Gene Synonyms/Alias

 ZIRD 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
140	EAPYSRSKLRPGFME	ubiquitination	[1, 2]
238	VAAARGIKRKMMQPF	methylation	[3]
247	KMMQPFNKPSGTFIK	acetylation	[4, 5]
383	NNQTEVVKIIEKDVM	acetylation	[4, 5, 6]
383	NNQTEVVKIIEKDVM	ubiquitination	[7, 8, 9]
459	ILNNPIVKARYERFV	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 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. May play a role in neuronal differentiation and is able to bind DNA and activate expression in vitro. 

Sequence Annotation

 ZN_FING 312 336 C2H2 AKAP95-type 1.
 ZN_FING 405 430 C2H2 AKAP95-type 2.
 REGION 1 124 Mediates transcriptional activation (By
 MOTIF 238 260 Bipartite nuclear localization signal (By
 MOD_RES 106 106 Phosphoserine.
 MOD_RES 121 121 Phosphoserine.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 190 190 Phosphotyrosine (By similarity).
 MOD_RES 247 247 N6-acetyllysine.
 MOD_RES 270 270 Phosphoserine.  

Keyword

 Acetylation; Activator; Alternative splicing; Complete proteome; DNA-binding; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 582 AA 

Protein Sequence

Gene Ontology

 GO:0044609; C:DBIRD complex; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0032784; P:regulation of DNA-dependent transcription, elongation; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR007071; AKAP95.
 IPR015880; Znf_C2H2-like. 

Pfam

 PF04988; AKAP95 

SMART

 SM00355; ZnF_C2H2 

PROSITE

  

PRINTS