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O75152

- ZC11A_HUMAN

UniProt

O75152 - ZC11A_HUMAN

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Protein
Zinc finger CCCH domain-containing protein 11A
Gene
ZC3H11A, KIAA0663, ZC3HDC11A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2 – 2928C3H1-type 1
Add
BLAST
Zinc fingeri31 – 5727C3H1-type 2
Add
BLAST
Zinc fingeri60 – 8627C3H1-type 3
Add
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. poly(A)+ mRNA export from nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger CCCH domain-containing protein 11A
Gene namesi
Name:ZC3H11A
Synonyms:KIAA0663, ZC3HDC11A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29093. ZC3H11A.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 810810Zinc finger CCCH domain-containing protein 11A
PRO_0000213905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Phosphoserine5 Publications
Modified residuei132 – 1321Phosphoserine2 Publications
Modified residuei171 – 1711Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine1 Publication
Modified residuei321 – 3211Phosphothreonine1 Publication
Modified residuei738 – 7381Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine2 Publications
Modified residuei764 – 7641N6-acetyllysine1 Publication
Modified residuei768 – 7681Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75152.
PaxDbiO75152.
PRIDEiO75152.

PTM databases

PhosphoSiteiO75152.

Expressioni

Gene expression databases

ArrayExpressiO75152.
BgeeiO75152.
CleanExiHS_ZC3H11A.
GenevestigatoriO75152.

Organism-specific databases

HPAiHPA026439.
HPA028490.
HPA028526.

Interactioni

Subunit structurei

Interacts with THOC2, DDX39 and POLDIP3; the interactions are ATP-dependent and indicative for an association with the TREX complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MLH1P406923EBI-748480,EBI-744248

Protein-protein interaction databases

BioGridi115208. 29 interactions.
IntActiO75152. 6 interactions.
MINTiMINT-1444822.
STRINGi9606.ENSP00000333253.

Structurei

3D structure databases

ProteinModelPortaliO75152.
SMRiO75152. Positions 6-89.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili362 – 42362 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi161 – 1688Poly-Asp

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG306637.
HOVERGENiHBG082979.
InParanoidiO75152.
OMAiITRHLTK.
OrthoDBiEOG72G19F.
PhylomeDBiO75152.
TreeFamiTF335608.

Family and domain databases

InterProiIPR000571. Znf_CCCH.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 3 hits.
[Graphical view]
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75152-1 [UniParc]FASTAAdd to Basket

« Hide

MPNQGEDCYF FFYSTCTKGD SCPFRHCEAA IGNETVCTLW QEGRCFRQVC    50
RFRHMEIDKK RSEIPCYWEN QPTGCQKLNC AFHHNRGRYV DGLFLPPSKT 100
VLPTVPESPE EEVKASQLSV QQNKLSVQSN PSPQLRSVMK VESSENVPSP 150
THPPVVINAA DDDEDDDDQF SEEGDETKTP TLQPTPEVHN GLRVTSVRKP 200
AVNIKQGECL NFGIKTLEEI KSKKMKEKSK KQGEGSSGVS SLLLHPEPVP 250
GPEKENVRTV VRTVTLSTKQ GEEPLVRLSL TERLGKRKFS AGGDSDPPLK 300
RSLAQRLGKK VEAPETNIDK TPKKAQVSKS LKERLGMSAD PDNEDATDKV 350
NKVGEIHVKT LEEILLERAS QKRGELQTKL KTEGPSKTDD STSGARSSST 400
IRIKTFSEVL AEKKHRQQEA ERQKSKKDTT CIKLKIDSEI KKTVVLPPIV 450
ASRGQSEEPA GKTKSMQEVH IKTLEEIKLE KALRVQQSSE SSTSSPSQHE 500
ATPGARRLLR ITKRTGMKEE KNLQEGNEVD SQSSIRTEAK EASGETTGVD 550
ITKIQVKRCE TMREKHMQKQ QEREKSVLTP LRGDVASCNT QVAEKPVLTA 600
VPGITRHLTK RLPTKSSQKV EVETSGIGDS LLNVKCAAQT LEKRGKAKPK 650
VNVKPSVVKV VSSPKLAPKR KAVEMHAAVI AAVKPLSSSS VLQEPPAKKA 700
AVAVVPLVSE DKSVTVPEAE NPRDSLVLPP TQSSSDSSPP EVSGPSSSQM 750
SMKTRRLSSA STGKPPLSVE DDFEKLIWEI SGGKLEAEID LDPGKDEDDL 800
LLELSEMIDS 810
Length:810
Mass (Da):89,131
Last modified:August 16, 2005 - v3
Checksum:i9048ABC7F4A372FB
GO

Sequence cautioni

The sequence CAH10553.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAA31638.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti640 – 6401T → N.
Corresponds to variant rs11240604 [ dbSNP | Ensembl ].
VAR_052967

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801C → Y in CAH10553. 1 Publication
Sequence conflicti246 – 2461P → L in CAH10530. 1 Publication
Sequence conflicti266 – 2661L → P in CAH10525. 1 Publication
Sequence conflicti277 – 2771R → G in CAH10530. 1 Publication
Sequence conflicti409 – 4091V → G in CAH10525. 1 Publication
Sequence conflicti412 – 4121E → K in CAH10525. 1 Publication
Sequence conflicti616 – 6161S → P in CAH10566. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30978.1.
PIRiT00368.
RefSeqiNP_055642.3. NM_014827.4.
XP_005245700.1. XM_005245643.1.
XP_005245701.1. XM_005245644.2.
XP_006711736.1. XM_006711673.1.
UniGeneiHs.532399.

Genome annotation databases

EnsembliENST00000332127; ENSP00000333253; ENSG00000058673.
ENST00000367210; ENSP00000356179; ENSG00000058673.
ENST00000367212; ENSP00000356181; ENSG00000058673.
ENST00000367214; ENSP00000356183; ENSG00000058673.
ENST00000545588; ENSP00000438527; ENSG00000058673.
GeneIDi9877.
KEGGihsa:9877.
UCSCiuc001hac.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30978.1.
PIRi T00368.
RefSeqi NP_055642.3. NM_014827.4.
XP_005245700.1. XM_005245643.1.
XP_005245701.1. XM_005245644.2.
XP_006711736.1. XM_006711673.1.
UniGenei Hs.532399.

3D structure databases

ProteinModelPortali O75152.
SMRi O75152. Positions 6-89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115208. 29 interactions.
IntActi O75152. 6 interactions.
MINTi MINT-1444822.
STRINGi 9606.ENSP00000333253.

PTM databases

PhosphoSitei O75152.

Proteomic databases

MaxQBi O75152.
PaxDbi O75152.
PRIDEi O75152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332127 ; ENSP00000333253 ; ENSG00000058673 .
ENST00000367210 ; ENSP00000356179 ; ENSG00000058673 .
ENST00000367212 ; ENSP00000356181 ; ENSG00000058673 .
ENST00000367214 ; ENSP00000356183 ; ENSG00000058673 .
ENST00000545588 ; ENSP00000438527 ; ENSG00000058673 .
GeneIDi 9877.
KEGGi hsa:9877.
UCSCi uc001hac.3. human.

Organism-specific databases

CTDi 9877.
GeneCardsi GC01P203765.
H-InvDB HIX0123107.
HGNCi HGNC:29093. ZC3H11A.
HPAi HPA026439.
HPA028490.
HPA028526.
MIMi 613513. gene.
neXtProti NX_O75152.
PharmGKBi PA142670535.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306637.
HOVERGENi HBG082979.
InParanoidi O75152.
OMAi ITRHLTK.
OrthoDBi EOG72G19F.
PhylomeDBi O75152.
TreeFami TF335608.

Miscellaneous databases

ChiTaRSi ZC3H11A. human.
GeneWikii ZC3H11A.
GenomeRNAii 9877.
NextBioi 37225.
PROi O75152.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75152.
Bgeei O75152.
CleanExi HS_ZC3H11A.
Genevestigatori O75152.

Family and domain databases

InterProi IPR000571. Znf_CCCH.
[Graphical view ]
SMARTi SM00356. ZnF_C3H1. 3 hits.
[Graphical view ]
PROSITEi PS50103. ZF_C3H1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiZC11A_HUMAN
AccessioniPrimary (citable) accession number: O75152
Secondary accession number(s): Q6AHY4
, Q6AHY9, Q6AW79, Q6AWA1, Q6PJK4, Q86XZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: September 3, 2014
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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