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Q14587

- ZN268_HUMAN

UniProt

Q14587 - ZN268_HUMAN

Protein

Zinc finger protein 268

Gene

ZNF268

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (29 Aug 2001)
      Previous versions | rss
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    Functioni

    Isoform 1: Acts as a transcriptional repressor. Inhibits erythroid differentiation and tumor cell proliferation. Plays a role during ovarian cancer development and progression.
    Isoform 2: Contributes to cervical carcinogenesis in part through the TNF-alpha-induced NF-kappa-B signaling pathway by interacting with the I-kappa-B-kinase (IKK) core complex.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri276 – 29823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri304 – 32623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri332 – 35423C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri360 – 38223C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri388 – 41023C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri416 – 43823C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri444 – 46623C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri472 – 49423C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri500 – 52223C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri528 – 55023C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri556 – 57823C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri584 – 60623C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri612 – 63423C2H2-type 13PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri640 – 66223C2H2-type 14PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri668 – 69023C2H2-type 15PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri696 – 71823C2H2-type 16PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri724 – 74623C2H2-type 17PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri752 – 77423C2H2-type 18PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri780 – 80223C2H2-type 19PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri808 – 83023C2H2-type 20PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri836 – 85823C2H2-type 21PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri864 – 88623C2H2-type 22PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri892 – 91423C2H2-type 23PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri920 – 94223C2H2-type 24PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cellular response to tumor necrosis factor Source: UniProtKB
    3. negative regulation of apoptotic process Source: UniProtKB
    4. negative regulation of cell cycle arrest Source: UniProtKB
    5. negative regulation of cell proliferation Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. positive regulation of apoptotic process Source: UniProtKB
    8. positive regulation of cell differentiation Source: UniProtKB
    9. positive regulation of cell migration Source: UniProtKB
    10. positive regulation of cell proliferation Source: UniProtKB
    11. positive regulation of protein catabolic process Source: UniProtKB
    12. positive regulation of protein homodimerization activity Source: UniProtKB
    13. positive regulation of protein phosphorylation Source: UniProtKB
    14. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    15. positive regulation of transcription from RNA polymerase II promoter during mitosis Source: UniProtKB
    16. regulation of mitotic cell cycle Source: UniProtKB
    17. regulation of protein heterodimerization activity Source: UniProtKB
    18. regulation of transcription, DNA-templated Source: UniProtKB
    19. release of cytoplasmic sequestered NF-kappaB Source: UniProtKB
    20. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_12627. Generic Transcription Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein 268
    Alternative name(s):
    Zinc finger protein HZF3
    Gene namesi
    Name:ZNF268
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:13061. ZNF268.

    Subcellular locationi

    Isoform 1 : Nucleus 1 Publication
    Isoform 2 : Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851D → A: Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-86. 1 Publication
    Mutagenesisi86 – 861V → A: Reduces nuclear localization. Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-85. 1 Publication
    Mutagenesisi88 – 881V → A: Reduces nuclear localization. 1 Publication
    Mutagenesisi90 – 901F → A: Reduces nuclear localization. 1 Publication
    Mutagenesisi93 – 931E → A: Reduces nuclear localization. Strongly reduces nuclear localization; when associated with A-94 and A-95. 1 Publication
    Mutagenesisi94 – 941E → A: Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-95. 1 Publication
    Mutagenesisi95 – 951W → A: Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-94. 1 Publication

    Organism-specific databases

    PharmGKBiPA37639.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 947947Zinc finger protein 268PRO_0000047495Add
    BLAST

    Proteomic databases

    MaxQBiQ14587.
    PaxDbiQ14587.
    PRIDEiQ14587.

    PTM databases

    PhosphoSiteiQ14587.

    Expressioni

    Tissue specificityi

    Overexpressed in ovarian cancer tissues compared to normal ovarian tissues. Isoform 1 and isoform 2 are expressed in squamous epithelium tissues. Isoform 2 is overexpressed in squamous cervical cancer (at protein level). Expressed in blood cells. Isoform 1 is expressed in pancreas, lung, skeletal muscle, heart, placenta, liver, kidney and brain. Isoform 2 expressed in chronic lymphocytic leukemia (CLL) and several tumor cell lines. Isoform 3 is expressed in several tumor cells. Isoform 5 is expressed in fetal liver and several tumor cells. Isoform 6 is weakly expressed in brain, lung amd small intestin and in several tumor cells. Isoform 7 is expressed in fetal liver and several tumor cells.6 Publications

    Developmental stagei

    Expressed in fetal liver from 5 weeks until 4 months but drastically reduced by 6 months and became non-detectible by 7 months. Expressed in hematopoietic stem cells in 3 weeks and 5 weeks (at protein level). Expressed in fetal liver.2 Publications

    Inductioni

    Down-regulated during erythroid differentiation by GATA1. Down-regulated by HTLV-1 Tax through the CREB/ATF pathway. Up-regulated by the regulator of nonsense transcript UPF1. Up-regulated by the cyclic AMP-dependent transcription factor ATF4.4 Publications

    Gene expression databases

    ArrayExpressiQ14587.
    BgeeiQ14587.
    CleanExiHS_ZNF268.
    GenevestigatoriQ14587.

    Organism-specific databases

    HPAiHPA001794.

    Interactioni

    Subunit structurei

    Interacts (via the KRAB domain) with TRIM28 (via the RBCC domain); the interaction increases ZNF268 nuclear localization activity. Isoform 2 interacts with CHUK and IKBKB; the interaction is further increased in a TNF-alpha-dependent manner.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000228289.

    Structurei

    Secondary structure

    1
    947
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi279 – 2824
    Beta strandi284 – 2874
    Helixi288 – 29811
    Beta strandi304 – 3063
    Turni307 – 3104
    Beta strandi311 – 3155
    Helixi316 – 3238
    Turni324 – 3263
    Beta strandi335 – 3373
    Beta strandi340 – 3434
    Helixi344 – 35411
    Turni363 – 3664
    Helixi372 – 3798
    Beta strandi382 – 3854
    Beta strandi391 – 3933
    Beta strandi396 – 3994
    Helixi400 – 41112
    Beta strandi415 – 4173
    Turni419 – 4213
    Beta strandi424 – 4263
    Helixi428 – 43710
    Turni438 – 4403
    Beta strandi443 – 4453
    Beta strandi447 – 4493
    Beta strandi452 – 4554
    Helixi456 – 46510
    Turni466 – 4683
    Beta strandi495 – 5006
    Turni503 – 5053
    Helixi512 – 5198
    Turni520 – 5223
    Beta strandi527 – 5293
    Beta strandi531 – 5333
    Beta strandi536 – 5394
    Helixi540 – 5478
    Turni548 – 5503
    Beta strandi559 – 5613
    Beta strandi564 – 5674
    Helixi568 – 57811
    Turni587 – 5893
    Beta strandi592 – 5965
    Helixi597 – 60610
    Beta strandi611 – 6133
    Beta strandi615 – 6173
    Beta strandi620 – 6234
    Helixi624 – 6329
    Beta strandi639 – 6424
    Turni643 – 6464
    Beta strandi647 – 6515
    Helixi652 – 6598
    Turni660 – 6623
    Beta strandi667 – 6693
    Beta strandi671 – 6744
    Beta strandi676 – 6794
    Helixi680 – 6867
    Helixi687 – 6893
    Beta strandi690 – 6923
    Beta strandi699 – 7013
    Helixi708 – 71912
    Turni727 – 7293
    Helixi736 – 7438
    Turni744 – 7485
    Beta strandi751 – 7533
    Beta strandi755 – 7573
    Beta strandi760 – 7634
    Helixi764 – 7718
    Helixi772 – 7743
    Beta strandi783 – 7853
    Helixi792 – 7998
    Turni800 – 8023
    Beta strandi807 – 8093
    Beta strandi811 – 8133
    Beta strandi816 – 8194
    Helixi820 – 8278
    Helixi828 – 8303
    Beta strandi835 – 8373
    Beta strandi839 – 8424
    Beta strandi844 – 8474
    Helixi848 – 8558
    Helixi856 – 8583
    Beta strandi862 – 8654
    Beta strandi867 – 8693
    Beta strandi872 – 8754
    Helixi876 – 88611
    Turni895 – 8973
    Beta strandi900 – 9034
    Helixi904 – 91411
    Beta strandi919 – 9213
    Beta strandi923 – 9253
    Beta strandi928 – 9325
    Helixi933 – 9419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EL4NMR-A663-695[»]
    2EL5NMR-A749-777[»]
    2EL6NMR-A831-863[»]
    2EM1NMR-A637-667[»]
    2EMVNMR-A859-889[»]
    2EMWNMR-A301-331[»]
    2EMXNMR-A273-303[»]
    2EMYNMR-A551-583[»]
    2EN0NMR-A385-413[»]
    2EN6NMR-A887-919[»]
    2EN7NMR-A495-525[»]
    2EOFNMR-A411-441[»]
    2EOGNMR-A693-723[»]
    2EOINMR-A329-359[»]
    2EOJNMR-A355-385[»]
    2EOKNMR-A441-469[»]
    2EOLNMR-A581-609[»]
    2EOPNMR-A719-751[»]
    2EPVNMR-A803-833[»]
    2EPWNMR-A915-947[»]
    2EPYNMR-A525-553[»]
    2YTFNMR-A607-639[»]
    2YTQNMR-A775-807[»]
    ProteinModelPortaliQ14587.
    SMRiQ14587. Positions 81-122, 199-947.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14587.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 15272KRABPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The KRAB domain functions to reinforce the nuclear localization of isoform 1 in addition to its transcription repression activity.

    Sequence similaritiesi

    Contains 24 C2H2-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 KRAB domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri276 – 29823C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri304 – 32623C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri332 – 35423C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri360 – 38223C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri388 – 41023C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri416 – 43823C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri444 – 46623C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri472 – 49423C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri500 – 52223C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri528 – 55023C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri556 – 57823C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri584 – 60623C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri612 – 63423C2H2-type 13PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri640 – 66223C2H2-type 14PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri668 – 69023C2H2-type 15PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri696 – 71823C2H2-type 16PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri724 – 74623C2H2-type 17PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri752 – 77423C2H2-type 18PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri780 – 80223C2H2-type 19PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri808 – 83023C2H2-type 20PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri836 – 85823C2H2-type 21PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri864 – 88623C2H2-type 22PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri892 – 91423C2H2-type 23PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri920 – 94223C2H2-type 24PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000234617.
    HOVERGENiHBG018163.
    InParanoidiQ14587.
    KOiK09228.
    OMAiLIVHQGA.
    OrthoDBiEOG7KSX7Q.
    PhylomeDBiQ14587.

    Family and domain databases

    Gene3Di3.30.160.60. 24 hits.
    InterProiIPR001909. Krueppel-associated_box.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF01352. KRAB. 1 hit.
    PF00096. zf-C2H2. 1 hit.
    [Graphical view]
    SMARTiSM00349. KRAB. 1 hit.
    SM00355. ZnF_C2H2. 24 hits.
    [Graphical view]
    SUPFAMiSSF109640. SSF109640. 1 hit.
    PROSITEiPS50805. KRAB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 24 hits.
    PS50157. ZINC_FINGER_C2H2_2. 24 hits.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14587-1) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268a, KW-4 variant-1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATRVRTASI WVPPLQERNS SWDRIRKLQG QESILGQGTP GLQPLPGTPR    50
    QKQKSRRIEK VLEWLFISQE QPKITKSWGP LSFMDVFVDF TWEEWQLLDP 100
    AQKCLYRSVM LENYSNLVSL GYQHTKPDII FKLEQGEELC MVQAQVPNQT 150
    CPNTVWKIDD LMDWHQENKD KLGSTAKSFE CTTFGKLCLL STKYLSRQKP 200
    HKCGTHGKSL KYIDFTSDYA RNNPNGFQVH GKSFFHSKHE QTVIGIKYCE 250
    SIESGKTVNK KSQLMCQQMY MGEKPFGCSC CEKAFSSKSY LLVHQQTHAE 300
    EKPYGCNECG KDFSSKSYLI VHQRIHTGEK LHECSECRKT FSFHSQLVIH 350
    QRIHTGENPY ECCECGKVFS RKDQLVSHQK THSGQKPYVC NECGKAFGLK 400
    SQLIIHERIH TGEKPYECNE CQKAFNTKSN LMVHQRTHTG EKPYVCSDCG 450
    KAFTFKSQLI VHQGIHTGVK PYGCIQCGKG FSLKSQLIVH QRSHTGMKPY 500
    VCNECGKAFR SKSYLIIHTR THTGEKLHEC NNCGKAFSFK SQLIIHQRIH 550
    TGENPYECHE CGKAFSRKYQ LISHQRTHAG EKPYECTDCG KAFGLKSQLI 600
    IHQRTHTGEK PFECSECQKA FNTKSNLIVH QRTHTGEKPY SCNECGKAFT 650
    FKSQLIVHKG VHTGVKPYGC SQCAKTFSLK SQLIVHQRSH TGVKPYGCSE 700
    CGKAFRSKSY LIIHMRTHTG EKPHECRECG KSFSFNSQLI VHQRIHTGEN 750
    PYECSECGKA FNRKDQLISH QRTHAGEKPY GCSECGKAFS SKSYLIIHMR 800
    THSGEKPYEC NECGKAFIWK SLLIVHERTH AGVNPYKCSQ CEKSFSGKLR 850
    LLVHQRMHTR EKPYECSECG KAFIRNSQLI VHQRTHSGEK PYGCNECGKT 900
    FSQKSILSAH QRTHTGEKPC KCTECGKAFC WKSQLIMHQR THVDDKH 947
    Length:947
    Mass (Da):108,374
    Last modified:August 29, 2001 - v2
    Checksum:iAC78F4824F4BE1A0
    GO
    Isoform 2 (identifier: Q14587-2) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268s, KW-4 variant-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-161: Missing.

    Show »
    Length:786
    Mass (Da):89,632
    Checksum:i95F58663B2FEE18E
    GO
    Isoform 3 (identifier: Q14587-3) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-140: Missing.
         222-947: Missing.

    Show »
    Length:81
    Mass (Da):9,314
    Checksum:iA48BA28E62F0BD17
    GO
    Isoform 4 (identifier: Q14587-4) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268d

    The sequence of this isoform differs from the canonical sequence as follows:
         12-99: VPPLQERNSS...FTWEEWQLLD → GTNTPNLISS...LINVARMERV
         100-947: Missing.

    Show »
    Length:100
    Mass (Da):11,720
    Checksum:i74B1E1A3DE23D260
    GO
    Isoform 5 (identifier: Q14587-6) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268e

    The sequence of this isoform differs from the canonical sequence as follows:
         79-135: GPLSFMDVFV...KPDIIFKLEQ → TQSGKLMILW...LINVARMERV
         136-947: Missing.

    Show »
    Length:135
    Mass (Da):15,803
    Checksum:iA3BD7C64C37509C4
    GO
    Isoform 6 (identifier: Q14587-7) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268f

    The sequence of this isoform differs from the canonical sequence as follows:
         12-44: VPPLQERNSSWDRIRKLQGQESILGQGTPGLQP → GTNTPNLISSSSWNKEKSCVWCRPKFQIRPVQF
         45-947: Missing.

    Show »
    Length:44
    Mass (Da):5,113
    Checksum:i7B18E69B3EBB9DC7
    GO
    Isoform 7 (identifier: Q14587-8) [UniParc]FASTAAdd to Basket

    Also known as: ZNF268g

    The sequence of this isoform differs from the canonical sequence as follows:
         12-78: Missing.
         153-183: NTVWKIDDLMDWHQENKDKLGSTAKSFECTT → ILKAGKSKAKVLAGLVSGEGPLCASKMTPCC
         184-947: Missing.

    Show »
    Length:116
    Mass (Da):12,931
    Checksum:i107B06FCECC69F64
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti323 – 3231Q → P in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti335 – 3362SE → IN in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti340 – 3401T → A in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti344 – 3441H → Q in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti363 – 3631C → D in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti409 – 4091I → T in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti860 – 8601R → T in AAL99923. (PubMed:12200376)Curated
    Sequence conflicti860 – 8601R → T in CAA55526. (PubMed:7865130)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751T → M.
    Corresponds to variant rs7975069 [ dbSNP | Ensembl ].
    VAR_033562

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 161161Missing in isoform 2. 2 PublicationsVSP_006909Add
    BLAST
    Alternative sequencei1 – 140140Missing in isoform 3. 2 PublicationsVSP_053461Add
    BLAST
    Alternative sequencei12 – 9988VPPLQ…WQLLD → GTNTPNLISSSSWNKEKSCV WCRPKFQIRPVQTQSGKLMI LWIGIRKIKTSWEVWQKALN ALHLENYVFLVQSIFQDKNL INVARMERV in isoform 4. 2 PublicationsVSP_053462Add
    BLAST
    Alternative sequencei12 – 7867Missing in isoform 7. 2 PublicationsVSP_053463Add
    BLAST
    Alternative sequencei12 – 4433VPPLQ…PGLQP → GTNTPNLISSSSWNKEKSCV WCRPKFQIRPVQF in isoform 6. 2 PublicationsVSP_053464Add
    BLAST
    Alternative sequencei45 – 947903Missing in isoform 6. 2 PublicationsVSP_053465Add
    BLAST
    Alternative sequencei79 – 13557GPLSF…FKLEQ → TQSGKLMILWIGIRKIKTSW EVRQKALNALHLENYVFLVQ SIFQDKNLINVARMERV in isoform 5. 2 PublicationsVSP_053466Add
    BLAST
    Alternative sequencei100 – 947848Missing in isoform 4. 2 PublicationsVSP_053467Add
    BLAST
    Alternative sequencei136 – 947812Missing in isoform 5. 2 PublicationsVSP_053468Add
    BLAST
    Alternative sequencei153 – 18331NTVWK…FECTT → ILKAGKSKAKVLAGLVSGEG PLCASKMTPCC in isoform 7. 2 PublicationsVSP_053469Add
    BLAST
    Alternative sequencei184 – 947764Missing in isoform 7. 2 PublicationsVSP_053470Add
    BLAST
    Alternative sequencei222 – 947726Missing in isoform 3. 2 PublicationsVSP_053471Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF317549 mRNA. Translation: AAG59817.1.
    AF385187 mRNA. Translation: AAK69307.1.
    AF432217 mRNA. Translation: AAL99923.1.
    AC026785 Genomic DNA. No translation available.
    DQ057356 mRNA. No translation available.
    DQ057357 mRNA. No translation available.
    DQ057358 mRNA. No translation available.
    DQ057359 mRNA. No translation available.
    DQ057360 mRNA. No translation available.
    X78926 mRNA. Translation: CAA55526.1.
    CCDSiCCDS45012.1. [Q14587-1]
    CCDS53853.1. [Q14587-4]
    CCDS59240.1. [Q14587-6]
    PIRiS47071.
    RefSeqiNP_001159353.1. NM_001165881.2. [Q14587-1]
    NP_001159355.1. NM_001165883.1. [Q14587-6]
    NP_001159356.2. NM_001165884.2.
    NP_001159357.1. NM_001165885.1.
    NP_001159358.1. NM_001165886.1.
    NP_001159359.1. NM_001165887.1.
    NP_003406.1. NM_003415.2. [Q14587-1]
    NP_694422.2. NM_152943.2.
    UniGeneiHs.124047.

    Genome annotation databases

    EnsembliENST00000228289; ENSP00000228289; ENSG00000090612. [Q14587-1]
    ENST00000536435; ENSP00000444412; ENSG00000090612. [Q14587-1]
    ENST00000539248; ENSP00000467781; ENSG00000090612. [Q14587-6]
    ENST00000588312; ENSP00000466622; ENSG00000090612. [Q14587-7]
    GeneIDi10795.
    KEGGihsa:10795.
    UCSCiuc010tbv.1. human. [Q14587-1]

    Polymorphism databases

    DMDMi19863363.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF317549 mRNA. Translation: AAG59817.1 .
    AF385187 mRNA. Translation: AAK69307.1 .
    AF432217 mRNA. Translation: AAL99923.1 .
    AC026785 Genomic DNA. No translation available.
    DQ057356 mRNA. No translation available.
    DQ057357 mRNA. No translation available.
    DQ057358 mRNA. No translation available.
    DQ057359 mRNA. No translation available.
    DQ057360 mRNA. No translation available.
    X78926 mRNA. Translation: CAA55526.1 .
    CCDSi CCDS45012.1. [Q14587-1 ]
    CCDS53853.1. [Q14587-4 ]
    CCDS59240.1. [Q14587-6 ]
    PIRi S47071.
    RefSeqi NP_001159353.1. NM_001165881.2. [Q14587-1 ]
    NP_001159355.1. NM_001165883.1. [Q14587-6 ]
    NP_001159356.2. NM_001165884.2.
    NP_001159357.1. NM_001165885.1.
    NP_001159358.1. NM_001165886.1.
    NP_001159359.1. NM_001165887.1.
    NP_003406.1. NM_003415.2. [Q14587-1 ]
    NP_694422.2. NM_152943.2.
    UniGenei Hs.124047.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EL4 NMR - A 663-695 [» ]
    2EL5 NMR - A 749-777 [» ]
    2EL6 NMR - A 831-863 [» ]
    2EM1 NMR - A 637-667 [» ]
    2EMV NMR - A 859-889 [» ]
    2EMW NMR - A 301-331 [» ]
    2EMX NMR - A 273-303 [» ]
    2EMY NMR - A 551-583 [» ]
    2EN0 NMR - A 385-413 [» ]
    2EN6 NMR - A 887-919 [» ]
    2EN7 NMR - A 495-525 [» ]
    2EOF NMR - A 411-441 [» ]
    2EOG NMR - A 693-723 [» ]
    2EOI NMR - A 329-359 [» ]
    2EOJ NMR - A 355-385 [» ]
    2EOK NMR - A 441-469 [» ]
    2EOL NMR - A 581-609 [» ]
    2EOP NMR - A 719-751 [» ]
    2EPV NMR - A 803-833 [» ]
    2EPW NMR - A 915-947 [» ]
    2EPY NMR - A 525-553 [» ]
    2YTF NMR - A 607-639 [» ]
    2YTQ NMR - A 775-807 [» ]
    ProteinModelPortali Q14587.
    SMRi Q14587. Positions 81-122, 199-947.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000228289.

    PTM databases

    PhosphoSitei Q14587.

    Polymorphism databases

    DMDMi 19863363.

    Proteomic databases

    MaxQBi Q14587.
    PaxDbi Q14587.
    PRIDEi Q14587.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228289 ; ENSP00000228289 ; ENSG00000090612 . [Q14587-1 ]
    ENST00000536435 ; ENSP00000444412 ; ENSG00000090612 . [Q14587-1 ]
    ENST00000539248 ; ENSP00000467781 ; ENSG00000090612 . [Q14587-6 ]
    ENST00000588312 ; ENSP00000466622 ; ENSG00000090612 . [Q14587-7 ]
    GeneIDi 10795.
    KEGGi hsa:10795.
    UCSCi uc010tbv.1. human. [Q14587-1 ]

    Organism-specific databases

    CTDi 10795.
    GeneCardsi GC12P133757.
    HGNCi HGNC:13061. ZNF268.
    HPAi HPA001794.
    MIMi 604753. gene.
    neXtProti NX_Q14587.
    PharmGKBi PA37639.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000234617.
    HOVERGENi HBG018163.
    InParanoidi Q14587.
    KOi K09228.
    OMAi LIVHQGA.
    OrthoDBi EOG7KSX7Q.
    PhylomeDBi Q14587.

    Enzyme and pathway databases

    Reactomei REACT_12627. Generic Transcription Pathway.

    Miscellaneous databases

    EvolutionaryTracei Q14587.
    GeneWikii ZNF268.
    GenomeRNAii 10795.
    NextBioi 40999.
    PROi Q14587.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14587.
    Bgeei Q14587.
    CleanExi HS_ZNF268.
    Genevestigatori Q14587.

    Family and domain databases

    Gene3Di 3.30.160.60. 24 hits.
    InterProi IPR001909. Krueppel-associated_box.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF01352. KRAB. 1 hit.
    PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    SMARTi SM00349. KRAB. 1 hit.
    SM00355. ZnF_C2H2. 24 hits.
    [Graphical view ]
    SUPFAMi SSF109640. SSF109640. 1 hit.
    PROSITEi PS50805. KRAB. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 24 hits.
    PS50157. ZINC_FINGER_C2H2_2. 24 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel Kruppel-like zinc finger gene, ZNF268, expressed in early human embryo."
      Gou D.M., Sun Y., Gao L., Chow L.M.C., Huang J., Feng Y.D., Jiang D.H., Li W.X.
      Biochim. Biophys. Acta 1518:306-310(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Embryo.
    2. "Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX."
      Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
      Blood 100:2123-2131(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    3. "KRAB-containing zinc finger gene ZNF268 encodes multiple alternatively spliced isoforms that contain transcription regulatory domains."
      Shao H., Zhu C., Zhao Z., Guo M., Qiu H., Liu H., Wang D., Xue L., Gao L., Sun C., Li W.
      Int. J. Mol. Med. 18:457-463(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), TISSUE SPECIFICITY.
    4. "Aberrant alternative splicing of human zinc finger gene ZNF268 in human hematological malignancy."
      Zhao Z., Wang D., Zhu C., Shao H., Sun C., Qiu H., Xue L., Xu J., Guo M., Li W.
      Oncol. Rep. 20:1243-1248(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), TISSUE SPECIFICITY.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Isolation of cDNA clones for 42 different Kruppel-related zinc finger proteins expressed in the human monoblast cell line U-937."
      Abrink M., Aveskogh M., Hellman L.
      DNA Cell Biol. 14:125-136(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 549-947.
    7. "The KRAB domain of zinc finger gene ZNF268: a potential transcriptional repressor."
      Sun Y., Gou D.M., Liu H., Peng X., Li W.X.
      IUBMB Life 55:127-131(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION.
    8. "ZNF268, a novel kruppel-like zinc finger protein, is implicated in early human liver development."
      Sun Y., Shao H., Li Z., Liu J., Gao L., Peng X., Meng Y., Li W.
      Int. J. Mol. Med. 14:971-975(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    9. "Transcription of human zinc finger ZNF268 gene requires an intragenic promoter element."
      Guo M.X., Wang D., Shao H.J., Qiu H.L., Xue L., Zhao Z.Z., Zhu C.G., Shi Y.B., Li W.X.
      J. Biol. Chem. 281:24623-24636(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ATF4.
    10. "Cloning and characterization of two novel alternatively spliced transcripts of ZNF268."
      Sun C., Zhao Z.Z., Gao L., Sun Y., Shao H.J., Li W.X.
      Yi Chuan 28:513-517(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    11. Cited for: INDUCTION BY UPF1.
    12. "Human T-cell leukemia virus type 1 oncoprotein tax represses ZNF268 expression through the cAMP-responsive element-binding protein/activating transcription factor pathway."
      Wang D., Guo M.X., Hu H.M., Zhao Z.Z., Qiu H.L., Shao H.J., Zhu C.G., Xue L., Shi Y.B., Li W.X.
      J. Biol. Chem. 283:16299-16308(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HTLV-1 TAX.
    13. "A splice variant of the C(2)H(2)-type zinc finger protein, ZNF268s, regulates NF-kappaB activation by TNF-alpha."
      Chun J.N., Song I.S., Kang D.H., Song H.J., Kim H.I., Seo J., Suh J.W., Lee K.J., Lee K.J., Kim J., Kang S.W.
      Mol. Cells 26:175-180(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "The zinc finger protein ZNF268 is overexpressed in human cervical cancer and contributes to tumorigenesis via enhancing NF-kappaB signaling."
      Wang W., Guo M., Hu L., Cai J., Zeng Y., Luo J., Shu Z., Li W., Huang Z.
      J. Biol. Chem. 287:42856-42866(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORMS 1 AND 2), INTERACTION WITH CHUK AND IKBKB, TISSUE SPECIFICITY.
    15. "Knockdown of ZNF268, which is transcriptionally downregulated by GATA-1, promotes proliferation of K562 cells."
      Zeng Y., Wang W., Ma J., Wang X., Guo M., Li W.
      PLoS ONE 7:E29518-E29518(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    16. "Novel activity of KRAB domain that functions to reinforce nuclear localization of KRAB-containing zinc finger proteins by interacting with KAP1."
      Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M., Huang Z.
      Cell. Mol. Life Sci. 70:3947-3958(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM28, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), MUTAGENESIS OF ASP-85; VAL-86; VAL-88; PHE-90; GLU-93; GLU-94 AND TRP-95.
    17. "Aberrant expression of ZNF268 alters the growth and migration of ovarian cancer cells."
      Hu L., Wang W., Cai J., Luo J., Huang Y., Xiong S., Li W., Guo M.
      Oncol. Lett. 6:49-54(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    18. "Solution structure of the C2H2 type zinc finger region of human zinc finger protein 268."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 272-947.

    Entry informationi

    Entry nameiZN268_HUMAN
    AccessioniPrimary (citable) accession number: Q14587
    Secondary accession number(s): Q8TDG8, Q96RH4, Q9BZJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3