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(-) Description

Title :  SOLUTION STRUCTURE OF THE 18TH ZF-C2H2 DOMAIN FROM HUMAN ZINC FINGER PROTEIN 268
 
Authors :  C. Kurosaki, M. Yoshida, F. Hayashi, S. Yokoyama, Riken Structural Genomics/Proteomics Initiative (Rsgi)
Date :  26 Mar 07  (Deposition) - 02 Oct 07  (Release) - 24 Feb 09  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  A  (20x)
Keywords :  Alternative Splicing, Dna-Binding, Metal-Binding, Nuclear Protein, Repeat, Transcription, Transcription Regulation, Zinc, Zinc-Finger, Structural Genomics, Nppsfa, National Project On Protein Structural And Functional Analyses, Riken Structural Genomics/Proteomics Initiative, Rsgi (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  C. Kurosaki, M. Yoshida, F. Hayashi, S. Yokoyama
Solution Structure Of The 18Th Zf-C2H2 Domain From Human Zinc Finger Protein 268
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - ZINC FINGER PROTEIN 268
    ChainsA
    EngineeredYES
    Expression System PlasmidP061218-18
    Expression System Vector TypePLASMID
    FragmentZF-C2H2 DOMAIN
    GeneZNF268
    Organism CommonHUMAN
    Organism ScientificHOMO SAPIENS
    Organism Taxid9606
    Other DetailsCELL FREE PROTEIN SYNTHESIS
    SynonymZINC FINGER PROTEIN HZF3

 Structural Features

(-) Chains, Units

  
NMR Structure (20x)

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 1)

NMR Structure (1, 1)
No.NameCountTypeFull Name
1ZN1Ligand/IonZINC ION

(-) Sites  (0, 0)

(no "Site" information available for 2EL5)

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2EL5)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 2EL5)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2EL5)

(-) PROSITE Motifs  (1, 2)

NMR Structure (1, 2)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1ZINC_FINGER_C2H2_1PS00028 Zinc finger C2H2 type domain signature.ZN268_HUMAN278-298
306-326
334-354
362-382
390-410
418-438
446-466
474-494
502-522
530-550
558-578
586-606
614-634
642-662
670-690
698-718
726-746
754-774
782-802
810-830
838-858
866-886
894-914
920-942
  2-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
A:13-33
A:37-40
-
-
-
-
-

(-) Exons   (1, 1)

NMR Structure (1, 1)
 ENSEMBLUniProtKBPDB
No.Transcript IDExonExon IDGenome LocationLengthIDLocationLengthCountLocationLength
1.8ENST000002282898ENSE00001002664chr12:133757995-133758272278ZN268_HUMAN-00--
1.9ENST000002282899ENSE00001751235chr12:133758532-13375861685ZN268_HUMAN1-11110--
1.10ENST0000022828910ENSE00000874422chr12:133764458-133764658201ZN268_HUMAN12-78670--
1.11ENST0000022828911ENSE00001805079chr12:133768075-133768201127ZN268_HUMAN79-121430--
1.12ENST0000022828912ENSE00001002662chr12:133768494-13376858996ZN268_HUMAN121-153330--
1.14bENST0000022828914bENSE00001002661chr12:133778730-1337817303001ZN268_HUMAN153-9477951A:1-42 (gaps)75

(-) Sequences/Alignments

NMR Structure
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:42
 aligned with ZN268_HUMAN | Q14587 from UniProtKB/Swiss-Prot  Length:947

    Alignment length:75
                                   739       749       759       769       779       789       799     
          ZN268_HUMAN   730 GKSFSFNSQLIVHQRIHTGENPYECSECGKAFNRKDQLISHQRTHAGEKPYGCSECGKAFSSKSYLIIHMRTHSG 804
               SCOP domains -----------------d2el5a1 A:6-33              ------------------------------ SCOP domains
               CATH domains --------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .....------------.....ee......ee.hhhhhhhhhhhhh..------------....---------.. Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ZINC_FINGER_C2H2_-------ZINC_FINGER_C2H2_1   -------ZINC_FINGER_C2H2_1   -- PROSITE
               Transcript 1 Exon 1.14b  PDB: A:1-42 (gaps) UniProt: 153-947 [INCOMPLETE]                Transcript 1
                 2el5 A   1 GSSGS------------SGENPYECSECGKAFNRKDQLISHQRTHAGE------------SGPS---------SG  42
                                |    -       | 8        18        28       | -         -|  |     -   | 
                                5            6                            36           37 40        41 

   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (1, 1)

NMR Structure

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2EL5)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2EL5)

(-) Gene Ontology  (29, 29)

NMR Structure(hide GO term definitions)
Chain A   (ZN268_HUMAN | Q14587)
molecular function
    GO:0003677    DNA binding    Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
    GO:0046872    metal ion binding    Interacting selectively and non-covalently with any metal ion.
    GO:0003676    nucleic acid binding    Interacting selectively and non-covalently with any nucleic acid.
    GO:0005515    protein binding    Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
    GO:0003700    transcription factor activity, sequence-specific DNA binding    Interacting selectively and non-covalently with a specific DNA sequence in order to modulate transcription. The transcription factor may or may not also interact selectively with a protein or macromolecular complex.
biological process
    GO:0030154    cell differentiation    The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
    GO:0071356    cellular response to tumor necrosis factor    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus.
    GO:0043066    negative regulation of apoptotic process    Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
    GO:0071157    negative regulation of cell cycle arrest    Any process that decreases the rate, frequency, or extent of cell cycle arrest, the process in which the cell cycle is halted during one of the normal phases.
    GO:0008285    negative regulation of cell proliferation    Any process that stops, prevents or reduces the rate or extent of cell proliferation.
    GO:0000122    negative regulation of transcription from RNA polymerase II promoter    Any process that stops, prevents, or reduces the frequency, rate or extent of transcription from an RNA polymerase II promoter.
    GO:0043065    positive regulation of apoptotic process    Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
    GO:0045597    positive regulation of cell differentiation    Any process that activates or increases the frequency, rate or extent of cell differentiation.
    GO:0030335    positive regulation of cell migration    Any process that activates or increases the frequency, rate or extent of cell migration.
    GO:0008284    positive regulation of cell proliferation    Any process that activates or increases the rate or extent of cell proliferation.
    GO:0045732    positive regulation of protein catabolic process    Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
    GO:0090073    positive regulation of protein homodimerization activity    Any process that increases the frequency, rate or extent of protein homodimerization, interacting selectively with an identical protein to form a homodimer.
    GO:0001934    positive regulation of protein phosphorylation    Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
    GO:0045944    positive regulation of transcription from RNA polymerase II promoter    Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
    GO:0046022    positive regulation of transcription from RNA polymerase II promoter during mitotic cell cycle    Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter that occurs during the mitotic cell cycle.
    GO:0007346    regulation of mitotic cell cycle    Any process that modulates the rate or extent of progress through the mitotic cell cycle.
    GO:0043497    regulation of protein heterodimerization activity    Any process that modulates the frequency, rate or extent of protein heterodimerization, interacting selectively with a nonidentical protein to form a heterodimer.
    GO:0006355    regulation of transcription, DNA-templated    Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
    GO:0008588    release of cytoplasmic sequestered NF-kappaB    The release of NF-kappaB from specific molecules in the cytoplasm to which it was bound, thereby allowing its translocation into the nucleus.
    GO:0006351    transcription, DNA-templated    The cellular synthesis of RNA on a template of DNA.
cellular component
    GO:0015629    actin cytoskeleton    The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
    GO:0005737    cytoplasm    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
    GO:0005622    intracellular    The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm.
    GO:0005634    nucleus    A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        ZN268_HUMAN | Q145872el4 2el6 2em1 2emv 2emw 2emx 2emy 2en0 2en6 2en7 2eof 2eog 2eoi 2eoj 2eok 2eol 2eop 2epv 2epw 2epy 2ytf 2ytq

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