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Protein

Zinc finger protein 268

Gene

ZNF268

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Zinc fingeri276 – 298C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri304 – 326C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri332 – 354C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri360 – 382C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri388 – 410C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri416 – 438C2H2-type 6PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri444 – 466C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri472 – 494C2H2-type 8PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri500 – 522C2H2-type 9PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri528 – 550C2H2-type 10PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri556 – 578C2H2-type 11PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri584 – 606C2H2-type 12PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri612 – 634C2H2-type 13PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri640 – 662C2H2-type 14PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri668 – 690C2H2-type 15PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri696 – 718C2H2-type 16PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri724 – 746C2H2-type 17PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri752 – 774C2H2-type 18PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri780 – 802C2H2-type 19PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri808 – 830C2H2-type 20PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri836 – 858C2H2-type 21PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri864 – 886C2H2-type 22PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri892 – 914C2H2-type 23PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri920 – 942C2H2-type 24PROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • cellular response to tumor necrosis factor Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell cycle arrest Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cell differentiation Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of protein catabolic process Source: UniProtKB
  • positive regulation of protein homodimerization activity Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter during mitosis Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of protein heterodimerization activity Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • release of cytoplasmic sequestered NF-kappaB Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000151963-MONOMER.
ReactomeiR-HSA-212436. Generic Transcription Pathway.
SIGNORiQ14587.

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
Proteomesi
  • UP000005640 Componenti: 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

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi85D → A: Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-86. 1 Publication1
Mutagenesisi86V → A: Reduces nuclear localization. Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-85. 1 Publication1
Mutagenesisi88V → A: Reduces nuclear localization. 1 Publication1
Mutagenesisi90F → A: Reduces nuclear localization. 1 Publication1
Mutagenesisi93E → A: Reduces nuclear localization. Strongly reduces nuclear localization; when associated with A-94 and A-95. 1 Publication1
Mutagenesisi94E → A: Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-95. 1 Publication1
Mutagenesisi95W → A: Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-94. 1 Publication1

Organism-specific databases

DisGeNETi10795.
OpenTargetsiENSG00000090612.
PharmGKBiPA37639.

Polymorphism and mutation databases

BioMutaiZNF268.
DMDMi19863363.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000474951 – 947Zinc finger protein 268Add BLAST947

Proteomic databases

EPDiQ14587.
MaxQBiQ14587.
PaxDbiQ14587.
PeptideAtlasiQ14587.
PRIDEiQ14587.

PTM databases

iPTMnetiQ14587.
PhosphoSitePlusiQ14587.

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

BgeeiENSG00000090612.
CleanExiHS_ZNF268.
ExpressionAtlasiQ14587. baseline and differential.
GenevisibleiQ14587. HS.

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. 3 interactors.
IntActiQ14587. 1 interactor.
STRINGi9606.ENSP00000228289.

Structurei

Secondary structure

1947
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi279 – 282Combined sources4
Beta strandi284 – 287Combined sources4
Helixi288 – 298Combined sources11
Beta strandi304 – 306Combined sources3
Turni307 – 310Combined sources4
Beta strandi311 – 315Combined sources5
Helixi316 – 323Combined sources8
Turni324 – 326Combined sources3
Beta strandi335 – 337Combined sources3
Beta strandi340 – 343Combined sources4
Helixi344 – 354Combined sources11
Turni363 – 366Combined sources4
Helixi372 – 379Combined sources8
Beta strandi382 – 385Combined sources4
Beta strandi391 – 393Combined sources3
Beta strandi396 – 399Combined sources4
Helixi400 – 411Combined sources12
Beta strandi415 – 417Combined sources3
Turni419 – 421Combined sources3
Beta strandi424 – 426Combined sources3
Helixi428 – 437Combined sources10
Turni438 – 440Combined sources3
Beta strandi443 – 445Combined sources3
Beta strandi447 – 449Combined sources3
Beta strandi452 – 455Combined sources4
Helixi456 – 465Combined sources10
Turni466 – 468Combined sources3
Beta strandi495 – 500Combined sources6
Turni503 – 505Combined sources3
Helixi512 – 519Combined sources8
Turni520 – 522Combined sources3
Beta strandi527 – 529Combined sources3
Beta strandi531 – 533Combined sources3
Beta strandi536 – 539Combined sources4
Helixi540 – 547Combined sources8
Turni548 – 550Combined sources3
Beta strandi559 – 561Combined sources3
Beta strandi564 – 567Combined sources4
Helixi568 – 578Combined sources11
Turni587 – 589Combined sources3
Beta strandi592 – 596Combined sources5
Helixi597 – 606Combined sources10
Beta strandi611 – 613Combined sources3
Beta strandi615 – 617Combined sources3
Beta strandi620 – 623Combined sources4
Helixi624 – 632Combined sources9
Beta strandi639 – 642Combined sources4
Turni643 – 646Combined sources4
Beta strandi647 – 651Combined sources5
Helixi652 – 659Combined sources8
Turni660 – 662Combined sources3
Beta strandi667 – 669Combined sources3
Beta strandi671 – 674Combined sources4
Beta strandi676 – 679Combined sources4
Helixi680 – 686Combined sources7
Helixi687 – 689Combined sources3
Beta strandi690 – 692Combined sources3
Beta strandi699 – 701Combined sources3
Helixi708 – 719Combined sources12
Turni727 – 729Combined sources3
Helixi736 – 743Combined sources8
Turni744 – 748Combined sources5
Beta strandi751 – 753Combined sources3
Beta strandi755 – 757Combined sources3
Beta strandi760 – 763Combined sources4
Helixi764 – 771Combined sources8
Helixi772 – 774Combined sources3
Beta strandi783 – 785Combined sources3
Helixi792 – 799Combined sources8
Turni800 – 802Combined sources3
Beta strandi807 – 809Combined sources3
Beta strandi811 – 813Combined sources3
Beta strandi816 – 819Combined sources4
Helixi820 – 827Combined sources8
Helixi828 – 830Combined sources3
Beta strandi835 – 837Combined sources3
Beta strandi839 – 842Combined sources4
Beta strandi844 – 847Combined sources4
Helixi848 – 855Combined sources8
Helixi856 – 858Combined sources3
Beta strandi862 – 865Combined sources4
Beta strandi867 – 869Combined sources3
Beta strandi872 – 875Combined sources4
Helixi876 – 886Combined sources11
Turni895 – 897Combined sources3
Beta strandi900 – 903Combined sources4
Helixi904 – 914Combined sources11
Beta strandi919 – 921Combined sources3
Beta strandi923 – 925Combined sources3
Beta strandi928 – 932Combined sources5
Helixi933 – 941Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14587.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 152KRABPROSITE-ProRule annotationAdd BLAST72

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)DescriptionActionsGraphical viewLength
Zinc fingeri276 – 298C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri304 – 326C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri332 – 354C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri360 – 382C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri388 – 410C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri416 – 438C2H2-type 6PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri444 – 466C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri472 – 494C2H2-type 8PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri500 – 522C2H2-type 9PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri528 – 550C2H2-type 10PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri556 – 578C2H2-type 11PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri584 – 606C2H2-type 12PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri612 – 634C2H2-type 13PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri640 – 662C2H2-type 14PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri668 – 690C2H2-type 15PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri696 – 718C2H2-type 16PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri724 – 746C2H2-type 17PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri752 – 774C2H2-type 18PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri780 – 802C2H2-type 19PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri808 – 830C2H2-type 20PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri836 – 858C2H2-type 21PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri864 – 886C2H2-type 22PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri892 – 914C2H2-type 23PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri920 – 942C2H2-type 24PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00850000132243.
HOGENOMiHOG000234617.
HOVERGENiHBG018163.
InParanoidiQ14587.
KOiK09228.
OMAiMKPYVCN.
OrthoDBiEOG091G02KC.
PhylomeDBiQ14587.

Family and domain databases

CDDicd07765. KRAB_A-box. 1 hit.
Gene3Di3.30.160.60. 24 hits.
InterProiIPR001909. KRAB.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 9 hits.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti323Q → P in AAL99923 (PubMed:12200376).Curated1
Sequence conflicti335 – 336SE → IN in AAL99923 (PubMed:12200376).Curated2
Sequence conflicti340T → A in AAL99923 (PubMed:12200376).Curated1
Sequence conflicti344H → Q in AAL99923 (PubMed:12200376).Curated1
Sequence conflicti363C → D in AAL99923 (PubMed:12200376).Curated1
Sequence conflicti409I → T in AAL99923 (PubMed:12200376).Curated1
Sequence conflicti860R → T in AAL99923 (PubMed:12200376).Curated1
Sequence conflicti860R → T in CAA55526 (PubMed:7865130).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033562175T → M.Corresponds to variant rs7975069dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0069091 – 161Missing in isoform 2. 2 PublicationsAdd BLAST161
Alternative sequenceiVSP_0534611 – 140Missing in isoform 3. 2 PublicationsAdd BLAST140
Alternative sequenceiVSP_05346212 – 99VPPLQ…WQLLD → GTNTPNLISSSSWNKEKSCV WCRPKFQIRPVQTQSGKLMI LWIGIRKIKTSWEVWQKALN ALHLENYVFLVQSIFQDKNL INVARMERV in isoform 4. 2 PublicationsAdd BLAST88
Alternative sequenceiVSP_05346312 – 78Missing in isoform 7. 2 PublicationsAdd BLAST67
Alternative sequenceiVSP_05346412 – 44VPPLQ…PGLQP → GTNTPNLISSSSWNKEKSCV WCRPKFQIRPVQF in isoform 6. 2 PublicationsAdd BLAST33
Alternative sequenceiVSP_05346545 – 947Missing in isoform 6. 2 PublicationsAdd BLAST903
Alternative sequenceiVSP_05346679 – 135GPLSF…FKLEQ → TQSGKLMILWIGIRKIKTSW EVRQKALNALHLENYVFLVQ SIFQDKNLINVARMERV in isoform 5. 2 PublicationsAdd BLAST57
Alternative sequenceiVSP_053467100 – 947Missing in isoform 4. 2 PublicationsAdd BLAST848
Alternative sequenceiVSP_053468136 – 947Missing in isoform 5. 2 PublicationsAdd BLAST812
Alternative sequenceiVSP_053469153 – 183NTVWK…FECTT → ILKAGKSKAKVLAGLVSGEG PLCASKMTPCC in isoform 7. 2 PublicationsAdd BLAST31
Alternative sequenceiVSP_053470184 – 947Missing in isoform 7. 2 PublicationsAdd BLAST764
Alternative sequenceiVSP_053471222 – 947Missing in isoform 3. 2 PublicationsAdd BLAST726

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.
UCSCiuc010tbw.3. human. [Q14587-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116010. 3 interactors.
IntActiQ14587. 1 interactor.
STRINGi9606.ENSP00000228289.

PTM databases

iPTMnetiQ14587.
PhosphoSitePlusiQ14587.

Polymorphism and mutation databases

BioMutaiZNF268.
DMDMi19863363.

Proteomic databases

EPDiQ14587.
MaxQBiQ14587.
PaxDbiQ14587.
PeptideAtlasiQ14587.
PRIDEiQ14587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
UCSCiuc010tbw.3. human. [Q14587-1]

Organism-specific databases

CTDi10795.
DisGeNETi10795.
GeneCardsiZNF268.
HGNCiHGNC:13061. ZNF268.
HPAiHPA001794.
MIMi604753. gene.
neXtProtiNX_Q14587.
OpenTargetsiENSG00000090612.
PharmGKBiPA37639.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00850000132243.
HOGENOMiHOG000234617.
HOVERGENiHBG018163.
InParanoidiQ14587.
KOiK09228.
OMAiMKPYVCN.
OrthoDBiEOG091G02KC.
PhylomeDBiQ14587.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000151963-MONOMER.
ReactomeiR-HSA-212436. Generic Transcription Pathway.
SIGNORiQ14587.

Miscellaneous databases

ChiTaRSiZNF268. human.
EvolutionaryTraceiQ14587.
GeneWikiiZNF268.
GenomeRNAii10795.
PROiQ14587.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090612.
CleanExiHS_ZNF268.
ExpressionAtlasiQ14587. baseline and differential.
GenevisibleiQ14587. HS.

Family and domain databases

CDDicd07765. KRAB_A-box. 1 hit.
Gene3Di3.30.160.60. 24 hits.
InterProiIPR001909. KRAB.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 9 hits.
[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]
ProtoNetiSearch...

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 30, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.