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Q14587 (ZN268_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein 268
Alternative name(s):
Zinc finger protein HZF3
Gene names
Name:ZNF268
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length947 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1:Acts as a transcriptional repressor. Inhibits erythroid differentiation and tumor cell proliferation. Plays a role during ovarian cancer development and progression. Ref.7 Ref.8 Ref.13 Ref.14 Ref.15 Ref.17

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. Ref.7 Ref.8 Ref.13 Ref.14 Ref.15 Ref.17

Subunit structure

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. Ref.14 Ref.16

Subcellular location

Isoform 1: Nucleus Ref.7 Ref.8 Ref.13 Ref.16.

Isoform 2: Nucleus. Cytoplasm Ref.7 Ref.8 Ref.13 Ref.16.

Tissue specificity

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. Ref.2 Ref.3 Ref.4 Ref.10 Ref.14 Ref.17

Developmental stage

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. Ref.8 Ref.10

Induction

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. Ref.9 Ref.11 Ref.12 Ref.15

Domain

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

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 24 C2H2-type zinc fingers.

Contains 1 KRAB domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to tumor necrosis factor

Inferred from direct assay Ref.14. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of cell cycle arrest

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.15Ref.17. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of cell differentiation

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of protein catabolic process

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of protein homodimerization activity

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter during mitosis

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of protein heterodimerization activity

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

release of cytoplasmic sequestered NF-kappaB

Inferred from direct assay Ref.14. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8Ref.16. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7Ref.16. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.16Ref.14. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14587-1)

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.
Isoform 2 (identifier: Q14587-2)

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

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
Isoform 3 (identifier: Q14587-3)

Also known as: ZNF268c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: Missing.
     222-947: Missing.
Isoform 4 (identifier: Q14587-4)

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.
Isoform 5 (identifier: Q14587-6)

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.
Isoform 6 (identifier: Q14587-7)

Also known as: ZNF268f;

The sequence of this isoform differs from the canonical sequence as follows:
     12-44: VPPLQERNSSWDRIRKLQGQESILGQGTPGLQP → GTNTPNLISSSSWNKEKSCVWCRPKFQIRPVQF
     45-947: Missing.
Isoform 7 (identifier: Q14587-8)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 947947Zinc finger protein 268
PRO_0000047495

Regions

Domain81 – 15272KRAB
Zinc finger276 – 29823C2H2-type 1
Zinc finger304 – 32623C2H2-type 2
Zinc finger332 – 35423C2H2-type 3
Zinc finger360 – 38223C2H2-type 4
Zinc finger388 – 41023C2H2-type 5
Zinc finger416 – 43823C2H2-type 6
Zinc finger444 – 46623C2H2-type 7
Zinc finger472 – 49423C2H2-type 8
Zinc finger500 – 52223C2H2-type 9
Zinc finger528 – 55023C2H2-type 10
Zinc finger556 – 57823C2H2-type 11
Zinc finger584 – 60623C2H2-type 12
Zinc finger612 – 63423C2H2-type 13
Zinc finger640 – 66223C2H2-type 14
Zinc finger668 – 69023C2H2-type 15
Zinc finger696 – 71823C2H2-type 16
Zinc finger724 – 74623C2H2-type 17
Zinc finger752 – 77423C2H2-type 18
Zinc finger780 – 80223C2H2-type 19
Zinc finger808 – 83023C2H2-type 20
Zinc finger836 – 85823C2H2-type 21
Zinc finger864 – 88623C2H2-type 22
Zinc finger892 – 91423C2H2-type 23
Zinc finger920 – 94223C2H2-type 24

Natural variations

Alternative sequence1 – 161161Missing in isoform 2.
VSP_006909
Alternative sequence1 – 140140Missing in isoform 3.
VSP_053461
Alternative sequence12 – 9988VPPLQ…WQLLD → GTNTPNLISSSSWNKEKSCV WCRPKFQIRPVQTQSGKLMI LWIGIRKIKTSWEVWQKALN ALHLENYVFLVQSIFQDKNL INVARMERV in isoform 4.
VSP_053462
Alternative sequence12 – 7867Missing in isoform 7.
VSP_053463
Alternative sequence12 – 4433VPPLQ…PGLQP → GTNTPNLISSSSWNKEKSCV WCRPKFQIRPVQF in isoform 6.
VSP_053464
Alternative sequence45 – 947903Missing in isoform 6.
VSP_053465
Alternative sequence79 – 13557GPLSF…FKLEQ → TQSGKLMILWIGIRKIKTSW EVRQKALNALHLENYVFLVQ SIFQDKNLINVARMERV in isoform 5.
VSP_053466
Alternative sequence100 – 947848Missing in isoform 4.
VSP_053467
Alternative sequence136 – 947812Missing in isoform 5.
VSP_053468
Alternative sequence153 – 18331NTVWK…FECTT → ILKAGKSKAKVLAGLVSGEG PLCASKMTPCC in isoform 7.
VSP_053469
Alternative sequence184 – 947764Missing in isoform 7.
VSP_053470
Alternative sequence222 – 947726Missing in isoform 3.
VSP_053471
Natural variant1751T → M.
Corresponds to variant rs7975069 [ dbSNP | Ensembl ].
VAR_033562

Experimental info

Mutagenesis851D → A: Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-86. Ref.16
Mutagenesis861V → A: Reduces nuclear localization. Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-85. Ref.16
Mutagenesis881V → A: Reduces nuclear localization. Ref.16
Mutagenesis901F → A: Reduces nuclear localization. Ref.16
Mutagenesis931E → A: Reduces nuclear localization. Strongly reduces nuclear localization; when associated with A-94 and A-95. Ref.16
Mutagenesis941E → A: Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-95. Ref.16
Mutagenesis951W → A: Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-94. Ref.16
Sequence conflict3231Q → P in AAL99923. Ref.2
Sequence conflict335 – 3362SE → IN in AAL99923. Ref.2
Sequence conflict3401T → A in AAL99923. Ref.2
Sequence conflict3441H → Q in AAL99923. Ref.2
Sequence conflict3631C → D in AAL99923. Ref.2
Sequence conflict4091I → T in AAL99923. Ref.2
Sequence conflict8601R → T in AAL99923. Ref.2
Sequence conflict8601R → T in CAA55526. Ref.6

Secondary structure

..................................................................................................................................................... 947
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ZNF268a) (KW-4 variant-1) [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: AC78F4824F4BE1A0

FASTA947108,374
        10         20         30         40         50         60 
MATRVRTASI WVPPLQERNS SWDRIRKLQG QESILGQGTP GLQPLPGTPR QKQKSRRIEK 

        70         80         90        100        110        120 
VLEWLFISQE QPKITKSWGP LSFMDVFVDF TWEEWQLLDP AQKCLYRSVM LENYSNLVSL 

       130        140        150        160        170        180 
GYQHTKPDII FKLEQGEELC MVQAQVPNQT CPNTVWKIDD LMDWHQENKD KLGSTAKSFE 

       190        200        210        220        230        240 
CTTFGKLCLL STKYLSRQKP HKCGTHGKSL KYIDFTSDYA RNNPNGFQVH GKSFFHSKHE 

       250        260        270        280        290        300 
QTVIGIKYCE SIESGKTVNK KSQLMCQQMY MGEKPFGCSC CEKAFSSKSY LLVHQQTHAE 

       310        320        330        340        350        360 
EKPYGCNECG KDFSSKSYLI VHQRIHTGEK LHECSECRKT FSFHSQLVIH QRIHTGENPY 

       370        380        390        400        410        420 
ECCECGKVFS RKDQLVSHQK THSGQKPYVC NECGKAFGLK SQLIIHERIH TGEKPYECNE 

       430        440        450        460        470        480 
CQKAFNTKSN LMVHQRTHTG EKPYVCSDCG KAFTFKSQLI VHQGIHTGVK PYGCIQCGKG 

       490        500        510        520        530        540 
FSLKSQLIVH QRSHTGMKPY VCNECGKAFR SKSYLIIHTR THTGEKLHEC NNCGKAFSFK 

       550        560        570        580        590        600 
SQLIIHQRIH TGENPYECHE CGKAFSRKYQ LISHQRTHAG EKPYECTDCG KAFGLKSQLI 

       610        620        630        640        650        660 
IHQRTHTGEK PFECSECQKA FNTKSNLIVH QRTHTGEKPY SCNECGKAFT FKSQLIVHKG 

       670        680        690        700        710        720 
VHTGVKPYGC SQCAKTFSLK SQLIVHQRSH TGVKPYGCSE CGKAFRSKSY LIIHMRTHTG 

       730        740        750        760        770        780 
EKPHECRECG KSFSFNSQLI VHQRIHTGEN PYECSECGKA FNRKDQLISH QRTHAGEKPY 

       790        800        810        820        830        840 
GCSECGKAFS SKSYLIIHMR THSGEKPYEC NECGKAFIWK SLLIVHERTH AGVNPYKCSQ 

       850        860        870        880        890        900 
CEKSFSGKLR LLVHQRMHTR EKPYECSECG KAFIRNSQLI VHQRTHSGEK PYGCNECGKT 

       910        920        930        940 
FSQKSILSAH QRTHTGEKPC KCTECGKAFC WKSQLIMHQR THVDDKH 

« Hide

Isoform 2 (ZNF268s) (KW-4 variant-2) [UniParc].

Checksum: 95F58663B2FEE18E
Show »

FASTA78689,632
Isoform 3 (ZNF268c) [UniParc].

Checksum: A48BA28E62F0BD17
Show »

FASTA819,314
Isoform 4 (ZNF268d) [UniParc].

Checksum: 74B1E1A3DE23D260
Show »

FASTA10011,720
Isoform 5 (ZNF268e) [UniParc].

Checksum: A3BD7C64C37509C4
Show »

FASTA13515,803
Isoform 6 (ZNF268f) [UniParc].

Checksum: 7B18E69B3EBB9DC7
Show »

FASTA445,113
Isoform 7 (ZNF268g) [UniParc].

Checksum: 107B06FCECC69F64
Show »

FASTA11612,931

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The mammalian gene ZNF268 is regulated by hUpf1."
Zhu C., Zhao Z., Guo M., Shao H., Qiu H., Wang D., Xu J., Xue L., Li W.
Biochemistry (Mosc.) 73:881-885(2008) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45012.1. [Q14587-1]
CCDS53853.1. [Q14587-4]
CCDS59240.1. [Q14587-6]
PIRS47071.
RefSeqNP_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.
UniGeneHs.124047.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ14587.
SMRQ14587. Positions 81-122, 199-947.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000228289.

PTM databases

PhosphoSiteQ14587.

Polymorphism databases

DMDM19863363.

Proteomic databases

MaxQBQ14587.
PaxDbQ14587.
PRIDEQ14587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228289; ENSP00000228289; ENSG00000090612. [Q14587-1]
ENST00000536435; ENSP00000444412; ENSG00000090612. [Q14587-1]
ENST00000537565; ENSP00000445713; ENSG00000090612. [Q14587-2]
ENST00000539248; ENSP00000467781; ENSG00000090612. [Q14587-6]
ENST00000588312; ENSP00000466622; ENSG00000090612. [Q14587-7]
GeneID10795.
KEGGhsa:10795.
UCSCuc010tbv.1. human. [Q14587-1]

Organism-specific databases

CTD10795.
GeneCardsGC12P133757.
HGNCHGNC:13061. ZNF268.
HPAHPA001794.
MIM604753. gene.
neXtProtNX_Q14587.
PharmGKBPA37639.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000234617.
HOVERGENHBG018163.
InParanoidQ14587.
KOK09228.
OMALIVHQGA.
OrthoDBEOG7KSX7Q.
PhylomeDBQ14587.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14587.
BgeeQ14587.
CleanExHS_ZNF268.
GenevestigatorQ14587.

Family and domain databases

Gene3D3.30.160.60. 24 hits.
InterProIPR001909. Krueppel-associated_box.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 24 hits.
[Graphical view]
SUPFAMSSF109640. SSF109640. 1 hit.
PROSITEPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 24 hits.
PS50157. ZINC_FINGER_C2H2_2. 24 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14587.
GeneWikiZNF268.
GenomeRNAi10795.
NextBio40999.
PROQ14587.
SOURCESearch...

Entry information

Entry nameZN268_HUMAN
AccessionPrimary (citable) accession number: Q14587
Secondary accession number(s): Q8TDG8, Q96RH4, Q9BZJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 29, 2001
Last modified: July 9, 2014
This is version 142 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 12

Human chromosome 12: entries, gene names and cross-references to MIM