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O75152 (ZC11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger CCCH domain-containing protein 11A
Gene names
Name:ZC3H11A
Synonyms:KIAA0663, ZC3HDC11A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex. Ref.15

Subunit structure

Interacts with THOC2, DDX39 and POLDIP3; the interactions are ATP-dependent and indicative for an association with the TREX complex. Ref.15

Sequence similarities

Contains 3 C3H1-type zinc fingers.

Sequence caution

The sequence BAA31638.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAH10553.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processmRNA transport
Transport
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpoly(A)+ mRNA export from nucleus

Inferred from mutant phenotype Ref.15. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLH1P406923EBI-748480,EBI-744248

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810Zinc finger CCCH domain-containing protein 11A
PRO_0000213905

Regions

Zinc finger2 – 2928C3H1-type 1
Zinc finger31 – 5727C3H1-type 2
Zinc finger60 – 8627C3H1-type 3
Coiled coil362 – 42362 Potential
Compositional bias161 – 1688Poly-Asp

Amino acid modifications

Modified residue1081Phosphoserine Ref.6 Ref.7 Ref.9 Ref.12 Ref.14
Modified residue1321Phosphoserine Ref.7 Ref.12
Modified residue1711Phosphoserine Ref.7
Modified residue2901Phosphoserine Ref.7
Modified residue3211Phosphothreonine Ref.7
Modified residue7381Phosphoserine Ref.9
Modified residue7581Phosphoserine Ref.7 Ref.12
Modified residue7641N6-acetyllysine Ref.10
Modified residue7681Phosphoserine Ref.7

Natural variations

Natural variant6401T → N.
Corresponds to variant rs11240604 [ dbSNP | Ensembl ].
VAR_052967

Experimental info

Sequence conflict801C → Y in CAH10553. Ref.3
Sequence conflict2461P → L in CAH10530. Ref.3
Sequence conflict2661L → P in CAH10525. Ref.3
Sequence conflict2771R → G in CAH10530. Ref.3
Sequence conflict4091V → G in CAH10525. Ref.3
Sequence conflict4121E → K in CAH10525. Ref.3
Sequence conflict6161S → P in CAH10566. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O75152 [UniParc].

Last modified August 16, 2005. Version 3.
Checksum: 9048ABC7F4A372FB

FASTA81089,131
        10         20         30         40         50         60 
MPNQGEDCYF FFYSTCTKGD SCPFRHCEAA IGNETVCTLW QEGRCFRQVC RFRHMEIDKK 

        70         80         90        100        110        120 
RSEIPCYWEN QPTGCQKLNC AFHHNRGRYV DGLFLPPSKT VLPTVPESPE EEVKASQLSV 

       130        140        150        160        170        180 
QQNKLSVQSN PSPQLRSVMK VESSENVPSP THPPVVINAA DDDEDDDDQF SEEGDETKTP 

       190        200        210        220        230        240 
TLQPTPEVHN GLRVTSVRKP AVNIKQGECL NFGIKTLEEI KSKKMKEKSK KQGEGSSGVS 

       250        260        270        280        290        300 
SLLLHPEPVP GPEKENVRTV VRTVTLSTKQ GEEPLVRLSL TERLGKRKFS AGGDSDPPLK 

       310        320        330        340        350        360 
RSLAQRLGKK VEAPETNIDK TPKKAQVSKS LKERLGMSAD PDNEDATDKV NKVGEIHVKT 

       370        380        390        400        410        420 
LEEILLERAS QKRGELQTKL KTEGPSKTDD STSGARSSST IRIKTFSEVL AEKKHRQQEA 

       430        440        450        460        470        480 
ERQKSKKDTT CIKLKIDSEI KKTVVLPPIV ASRGQSEEPA GKTKSMQEVH IKTLEEIKLE 

       490        500        510        520        530        540 
KALRVQQSSE SSTSSPSQHE ATPGARRLLR ITKRTGMKEE KNLQEGNEVD SQSSIRTEAK 

       550        560        570        580        590        600 
EASGETTGVD ITKIQVKRCE TMREKHMQKQ QEREKSVLTP LRGDVASCNT QVAEKPVLTA 

       610        620        630        640        650        660 
VPGITRHLTK RLPTKSSQKV EVETSGIGDS LLNVKCAAQT LEKRGKAKPK VNVKPSVVKV 

       670        680        690        700        710        720 
VSSPKLAPKR KAVEMHAAVI AAVKPLSSSS VLQEPPAKKA AVAVVPLVSE DKSVTVPEAE 

       730        740        750        760        770        780 
NPRDSLVLPP TQSSSDSSPP EVSGPSSSQM SMKTRRLSSA STGKPPLSVE DDFEKLIWEI 

       790        800        810 
SGGKLEAEID LDPGKDEDDL LLELSEMIDS 

« Hide

References

« Hide 'large scale' references
[1]"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."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]Ohara O., Suyama M., Nagase T., Ishikawa K.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal kidney and Retina.
[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].
Tissue: Kidney and Placenta.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-132; SER-171; SER-290; THR-321; SER-758 AND SER-768, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-764, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex."
Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.
Genes Dev. 24:2043-2053(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE TREX COMPLEX.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-132 AND SER-758, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export."
Folco E.G., Lee C.S., Dufu K., Yamazaki T., Reed R.
PLoS ONE 7:E43804-E43804(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THOC2; DDX39B AND POLDIP3, ASSOCIATION WITH THE TREX COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014563 mRNA. Translation: BAA31638.2. Different initiation.
CR627439 mRNA. Translation: CAH10525.1.
CR627446 mRNA. Translation: CAH10530.1.
BX648271 mRNA. Translation: CAH10553.1. Sequence problems.
BX649148 mRNA. Translation: CAH10566.1.
BC014268 mRNA. Translation: AAH14268.1.
PIRT00368.
RefSeqNP_055642.3. NM_014827.4.
XP_005245700.1. XM_005245643.1.
XP_005245701.1. XM_005245644.2.
UniGeneHs.532399.

3D structure databases

ProteinModelPortalO75152.
SMRO75152. Positions 6-89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115208. 27 interactions.
IntActO75152. 6 interactions.
MINTMINT-1444822.
STRING9606.ENSP00000333253.

PTM databases

PhosphoSiteO75152.

Proteomic databases

PaxDbO75152.
PRIDEO75152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332127; ENSP00000333253; ENSG00000058673.
ENST00000367210; ENSP00000356179; ENSG00000058673.
ENST00000367212; ENSP00000356181; ENSG00000058673.
ENST00000367214; ENSP00000356183; ENSG00000058673.
ENST00000545588; ENSP00000438527; ENSG00000058673.
GeneID9877.
KEGGhsa:9877.
UCSCuc001hac.3. human.

Organism-specific databases

CTD9877.
GeneCardsGC01P203765.
H-InvDBHIX0123107.
HGNCHGNC:29093. ZC3H11A.
HPAHPA026439.
HPA028490.
HPA028526.
MIM613513. gene.
neXtProtNX_O75152.
PharmGKBPA142670535.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306637.
HOVERGENHBG082979.
InParanoidO75152.
OMAARKPGVN.
OrthoDBEOG72G19F.
PhylomeDBO75152.
TreeFamTF335608.

Gene expression databases

ArrayExpressO75152.
BgeeO75152.
CleanExHS_ZC3H11A.
GenevestigatorO75152.

Family and domain databases

InterProIPR000571. Znf_CCCH.
[Graphical view]
SMARTSM00356. ZnF_C3H1. 3 hits.
[Graphical view]
PROSITEPS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZC3H11A. human.
GeneWikiZC3H11A.
GenomeRNAi9877.
NextBio37225.
PROO75152.
SOURCESearch...

Entry information

Entry nameZC11A_HUMAN
AccessionPrimary (citable) accession number: O75152
Secondary accession number(s): Q6AHY4 expand/collapse secondary AC list , Q6AHY9, Q6AW79, Q6AWA1, Q6PJK4, Q86XZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM