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Q14587

- ZN268_HUMAN

UniProt

Q14587 - ZN268_HUMAN

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Protein

Zinc finger protein 268

Gene

ZNF268

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ14587.
CleanExiHS_ZNF268.
ExpressionAtlasiQ14587. baseline and differential.
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

BioGridi116010. 1 interaction.
STRINGi9606.ENSP00000228289.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120469.
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

        10         20         30         40         50
MATRVRTASI WVPPLQERNS SWDRIRKLQG QESILGQGTP GLQPLPGTPR
60 70 80 90 100
QKQKSRRIEK VLEWLFISQE QPKITKSWGP LSFMDVFVDF TWEEWQLLDP
110 120 130 140 150
AQKCLYRSVM LENYSNLVSL GYQHTKPDII FKLEQGEELC MVQAQVPNQT
160 170 180 190 200
CPNTVWKIDD LMDWHQENKD KLGSTAKSFE CTTFGKLCLL STKYLSRQKP
210 220 230 240 250
HKCGTHGKSL KYIDFTSDYA RNNPNGFQVH GKSFFHSKHE QTVIGIKYCE
260 270 280 290 300
SIESGKTVNK KSQLMCQQMY MGEKPFGCSC CEKAFSSKSY LLVHQQTHAE
310 320 330 340 350
EKPYGCNECG KDFSSKSYLI VHQRIHTGEK LHECSECRKT FSFHSQLVIH
360 370 380 390 400
QRIHTGENPY ECCECGKVFS RKDQLVSHQK THSGQKPYVC NECGKAFGLK
410 420 430 440 450
SQLIIHERIH TGEKPYECNE CQKAFNTKSN LMVHQRTHTG EKPYVCSDCG
460 470 480 490 500
KAFTFKSQLI VHQGIHTGVK PYGCIQCGKG FSLKSQLIVH QRSHTGMKPY
510 520 530 540 550
VCNECGKAFR SKSYLIIHTR THTGEKLHEC NNCGKAFSFK SQLIIHQRIH
560 570 580 590 600
TGENPYECHE CGKAFSRKYQ LISHQRTHAG EKPYECTDCG KAFGLKSQLI
610 620 630 640 650
IHQRTHTGEK PFECSECQKA FNTKSNLIVH QRTHTGEKPY SCNECGKAFT
660 670 680 690 700
FKSQLIVHKG VHTGVKPYGC SQCAKTFSLK SQLIVHQRSH TGVKPYGCSE
710 720 730 740 750
CGKAFRSKSY LIIHMRTHTG EKPHECRECG KSFSFNSQLI VHQRIHTGEN
760 770 780 790 800
PYECSECGKA FNRKDQLISH QRTHAGEKPY GCSECGKAFS SKSYLIIHMR
810 820 830 840 850
THSGEKPYEC NECGKAFIWK SLLIVHERTH AGVNPYKCSQ CEKSFSGKLR
860 870 880 890 900
LLVHQRMHTR EKPYECSECG KAFIRNSQLI VHQRTHSGEK PYGCNECGKT
910 920 930 940
FSQKSILSAH QRTHTGEKPC KCTECGKAFC WKSQLIMHQR THVDDKH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BioGridi 116010. 1 interaction.
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.
GeneTreei ENSGT00770000120469.
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

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

Gene expression databases

Bgeei Q14587.
CleanExi HS_ZNF268.
ExpressionAtlasi Q14587. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 146 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