ZC3H11A | ENSG00000058673 | NCBI 9877

Details for: ZC3H11A

Gene ID: 9877

Symbol: ZC3H11A

Ensembl ID: ENSG00000058673

Description: zinc finger CCCH-type containing 11A

Associated with

Gene expression (transcription)
(R-HSA-74160)
Metabolism of rna
(R-HSA-8953854)
Mrna 3'-end processing
(R-HSA-72187)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Rna polymerase ii transcription
(R-HSA-73857)
Rna polymerase ii transcription termination
(R-HSA-73856)
Transport of mature mrna derived from an intron-containing transcript
(R-HSA-159236)
Transport of mature transcript to cytoplasm
(R-HSA-72202)
Metal ion binding
(GO:0046872)
Nucleoplasm
(GO:0005654)
Poly(a)+ mrna export from nucleus
(GO:0016973)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)
Transcription export complex
(GO:0000346)

Other Information

Proteins

Zinc finger CCCH domain-containing protein 11A

Genular Protein ID: 3540147823

Symbol: ZC11A_HUMAN

Name: Zinc finger CCCH domain-containing protein 11A

UniProtKB Accession Codes:

O75152 Q6AHY4 Q6AHY9 Q6AW79 Q6AWA1 Q6PJK4 Q86XZ7

Database IDs:

Citations:

PubMed ID: 9734811

Title: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.

PubMed ID: 9734811

DOI: 10.1093/dnares/5.3.169

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20844015

Title: ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex.

PubMed ID: 20844015

DOI: 10.1101/gad.1898610

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22928037

Title: The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export.

PubMed ID: 22928037

DOI: 10.1371/journal.pone.0043804

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29610341

Title: Multiple nuclear-replicating viruses require the stress-induced protein ZC3H11A for efficient growth.

PubMed ID: 29610341

DOI: 10.1073/pnas.1722333115

Sequence Information:

Length: 810
Mass: 89131
Checksum: 9048ABC7F4A372FB
Sequence:

MPNQGEDCYF FFYSTCTKGD SCPFRHCEAA IGNETVCTLW QEGRCFRQVC RFRHMEIDKK 
RSEIPCYWEN QPTGCQKLNC AFHHNRGRYV DGLFLPPSKT VLPTVPESPE EEVKASQLSV 
QQNKLSVQSN PSPQLRSVMK VESSENVPSP THPPVVINAA DDDEDDDDQF SEEGDETKTP 
TLQPTPEVHN GLRVTSVRKP AVNIKQGECL NFGIKTLEEI KSKKMKEKSK KQGEGSSGVS 
SLLLHPEPVP GPEKENVRTV VRTVTLSTKQ GEEPLVRLSL TERLGKRKFS AGGDSDPPLK 
RSLAQRLGKK VEAPETNIDK TPKKAQVSKS LKERLGMSAD PDNEDATDKV NKVGEIHVKT 
LEEILLERAS QKRGELQTKL KTEGPSKTDD STSGARSSST IRIKTFSEVL AEKKHRQQEA 
ERQKSKKDTT CIKLKIDSEI KKTVVLPPIV ASRGQSEEPA GKTKSMQEVH IKTLEEIKLE 
KALRVQQSSE SSTSSPSQHE ATPGARRLLR ITKRTGMKEE KNLQEGNEVD SQSSIRTEAK 
EASGETTGVD ITKIQVKRCE TMREKHMQKQ QEREKSVLTP LRGDVASCNT QVAEKPVLTA 
VPGITRHLTK RLPTKSSQKV EVETSGIGDS LLNVKCAAQT LEKRGKAKPK VNVKPSVVKV 
VSSPKLAPKR KAVEMHAAVI AAVKPLSSSS VLQEPPAKKA AVAVVPLVSE DKSVTVPEAE 
NPRDSLVLPP TQSSSDSSPP EVSGPSSSQM SMKTRRLSSA STGKPPLSVE DDFEKLIWEI 
SGGKLEAEID LDPGKDEDDL LLELSEMIDS

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: ZC3H11A

Associated with

Other Information

Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. PubMed ID: 9734811

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex. PubMed ID: 20844015

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export. PubMed ID: 22928037

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Multiple nuclear-replicating viruses require the stress-induced protein ZC3H11A for efficient growth. PubMed ID: 29610341