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Protein

Zinc finger protein with KRAB and SCAN domains 3

Gene

ZKSCAN3

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

Functioni

Transcriptional factor that binds to the consensus sequence 5'-[GT][AG][AGT]GGGG-3' and acts as a repressor of autophagy. Specifically represses expression of genes involved in autophagy and lysosome biogenesis/function such as MAP1LC3B, ULK1 or WIPI2. Associates with chromatin at the ITGB4 and VEGF promoters. Also acts as a transcription activator and promotes cancer cell progression and/or migation in various tumors and myelomas.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri314 – 33623C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri342 – 36423C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri370 – 39223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri398 – 42023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri426 – 44823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri480 – 50223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri508 – 53023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. DNA binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  6. sequence-specific DNA binding Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. lysosome organization Source: UniProtKB
  3. negative regulation of autophagy Source: UniProtKB
  4. negative regulation of cellular senescence Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Autophagy, 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 with KRAB and SCAN domains 3
Alternative name(s):
Zinc finger and SCAN domain-containing protein 13
Zinc finger protein 306
Zinc finger protein 309
Zinc finger protein 47 homolog
Short name:
Zf47
Short name:
Zfp-47
Gene namesi
Name:ZKSCAN3
Synonyms:ZFP47, ZNF306, ZNF309, ZSCAN13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13853. ZKSCAN3.

Subcellular locationi

Nucleus. Cytoplasm
Note: Mainly localizes in the nucleus. Under starvation conditions translocates to the cytoplasm, allowing expression of target genes involved in autophagy and lysosome biogenesis/function.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Zinc finger protein with KRAB and SCAN domains 3PRO_0000047524Add
BLAST

Proteomic databases

MaxQBiQ9BRR0.
PaxDbiQ9BRR0.
PRIDEiQ9BRR0.

PTM databases

PhosphoSiteiQ9BRR0.

Expressioni

Inductioni

Overexpressed in various tumors, such as multiple myeloma, colorectal and prostate cancers (at protein level).3 Publications

Gene expression databases

BgeeiQ9BRR0.
CleanExiHS_ZKSCAN3.
GenevestigatoriQ9BRR0.

Organism-specific databases

HPAiHPA009637.

Interactioni

Protein-protein interaction databases

BioGridi123230. 6 interactions.
IntActiQ9BRR0. 1 interaction.
STRINGi9606.ENSP00000252211.

Structurei

3D structure databases

ProteinModelPortaliQ9BRR0.
SMRiQ9BRR0. Positions 37-129, 289-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 12883SCAN boxPROSITE-ProRule annotationAdd
BLAST
Domaini214 – 27461KRABAdd
BLAST

Sequence similaritiesi

Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 KRAB domain.Curated
Contains 1 SCAN box domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri314 – 33623C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri342 – 36423C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri370 – 39223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri398 – 42023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri426 – 44823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri480 – 50223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri508 – 53023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118881.
HOGENOMiHOG000234619.
HOVERGENiHBG018163.
InParanoidiQ9BRR0.
KOiK09229.
OMAiCCREDAV.
OrthoDBiEOG79GT5W.
PhylomeDBiQ9BRR0.
TreeFamiTF350830.

Family and domain databases

Gene3Di3.30.160.60. 7 hits.
InterProiIPR001909. Krueppel-associated_box.
IPR008916. Retrov_capsid_C.
IPR003309. Tscrpt_reg_SCAN.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF02023. SCAN. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00431. SCAN. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
SSF47353. SSF47353. 1 hit.
PROSITEiPS50804. SCAN_BOX. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BRR0-1) [UniParc]FASTAAdd to basket

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
MARELSESTA LDAQSTEDQM ELLVIKVEEE EAGFPSSPDL GSEGSRERFR
60 70 80 90 100
GFRYPEAAGP REALSRLREL CRQWLQPEMH SKEQILELLV LEQFLTILPG
110 120 130 140 150
NLQSWVREQH PESGEEVVVL LEYLERQLDE PAPQVSGVDQ GQELLCCKMA
160 170 180 190 200
LLTPAPGSQS SQFQLMKALL KHESVGSQPL QDRVLQVPVL AHGGCCREDK
210 220 230 240 250
VVASRLTPES QGLLKVEDVA LTLTPEWTQQ DSSQGNLCRD EKQENHGSLV
260 270 280 290 300
SLGDEKQTKS RDLPPAEELP EKEHGKISCH LREDIAQIPT CAEAGEQEGR
310 320 330 340 350
LQRKQKNATG GRRHICHECG KSFAQSSGLS KHRRIHTGEK PYECEECGKA
360 370 380 390 400
FIGSSALVIH QRVHTGEKPY ECEECGKAFS HSSDLIKHQR THTGEKPYEC
410 420 430 440 450
DDCGKTFSQS CSLLEHHRIH TGEKPYQCSM CGKAFRRSSH LLRHQRIHTG
460 470 480 490 500
DKNVQEPEQG EAWKSRMESQ LENVETPMSY KCNECERSFT QNTGLIEHQK
510 520 530
IHTGEKPYQC NACGKGFTRI SYLVQHQRSH VGKNILSQ
Length:538
Mass (Da):60,641
Last modified:October 17, 2006 - v2
Checksum:i0D8F706F1B2F888F
GO
Isoform 2 (identifier: Q9BRR0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.

Note: No experimental confirmation available.

Show »
Length:390
Mass (Da):43,793
Checksum:iBE2B599E4BE6A684
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2072LT → IP in AAB16813 (PubMed:10520746).Curated
Sequence conflicti348 – 3503GKA → AKP in AAB16813 (PubMed:10520746).Curated
Sequence conflicti437 – 4371R → D in AAB16813 (PubMed:10520746).Curated
Sequence conflicti459 – 47921QGEAW…ETPMS → TGRGWKVGWKASWKMLKLPC P in AAB16813 (PubMed:10520746).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31R → T.
Corresponds to variant rs733743 [ dbSNP | Ensembl ].
VAR_024208
Natural varianti33 – 331G → V.
Corresponds to variant rs3857554 [ dbSNP | Ensembl ].
VAR_028313
Natural varianti34 – 341F → L.
Corresponds to variant rs3857555 [ dbSNP | Ensembl ].
VAR_028314
Natural varianti189 – 1891V → M.1 Publication
Corresponds to variant rs17856167 [ dbSNP | Ensembl ].
VAR_028315
Natural varianti200 – 2001K → A Requires 2 nucleotide substitutions. 3 Publications
Corresponds to variant rs13201752 [ dbSNP | Ensembl ].
VAR_059950
Natural varianti200 – 2001K → E.1 Publication
Corresponds to variant rs45505399 [ dbSNP | Ensembl ].
VAR_028316
Natural varianti200 – 2001K → T.
Corresponds to variant rs13201753 [ dbSNP | Ensembl ].
VAR_028317
Natural varianti246 – 2461H → Q.
Corresponds to variant rs213227 [ dbSNP | Ensembl ].
VAR_028318

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 148148Missing in isoform 2. 1 PublicationVSP_045908Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT007427 mRNA. Translation: AAP36095.1.
AK122790 mRNA. Translation: BAG53732.1.
AK313532 mRNA. Translation: BAG36309.1.
AL358785, AL021997 Genomic DNA. Translation: CAH71668.1.
AL021997, AL358785 Genomic DNA. Translation: CAI23088.1.
CH471081 Genomic DNA. Translation: EAX03157.1.
BC006118 mRNA. Translation: AAH06118.1.
U71601 mRNA. Translation: AAB16813.1.
CCDSiCCDS4650.1. [Q9BRR0-1]
CCDS56408.1. [Q9BRR0-2]
RefSeqiNP_001229823.1. NM_001242894.1. [Q9BRR0-1]
NP_001229824.1. NM_001242895.1. [Q9BRR0-2]
NP_077819.2. NM_024493.3. [Q9BRR0-1]
XP_005249481.1. XM_005249424.1. [Q9BRR0-2]
XP_006715278.1. XM_006715215.1. [Q9BRR0-1]
XP_006715281.1. XM_006715218.1. [Q9BRR0-2]
XP_006715282.1. XM_006715219.1. [Q9BRR0-2]
UniGeneiHs.380930.
Hs.485004.

Genome annotation databases

EnsembliENST00000252211; ENSP00000252211; ENSG00000189298. [Q9BRR0-1]
ENST00000341464; ENSP00000341883; ENSG00000189298. [Q9BRR0-2]
ENST00000377255; ENSP00000366465; ENSG00000189298. [Q9BRR0-1]
GeneIDi80317.
KEGGihsa:80317.
UCSCiuc003nle.4. human. [Q9BRR0-1]

Polymorphism databases

DMDMi116242859.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT007427 mRNA. Translation: AAP36095.1.
AK122790 mRNA. Translation: BAG53732.1.
AK313532 mRNA. Translation: BAG36309.1.
AL358785, AL021997 Genomic DNA. Translation: CAH71668.1.
AL021997, AL358785 Genomic DNA. Translation: CAI23088.1.
CH471081 Genomic DNA. Translation: EAX03157.1.
BC006118 mRNA. Translation: AAH06118.1.
U71601 mRNA. Translation: AAB16813.1.
CCDSiCCDS4650.1. [Q9BRR0-1]
CCDS56408.1. [Q9BRR0-2]
RefSeqiNP_001229823.1. NM_001242894.1. [Q9BRR0-1]
NP_001229824.1. NM_001242895.1. [Q9BRR0-2]
NP_077819.2. NM_024493.3. [Q9BRR0-1]
XP_005249481.1. XM_005249424.1. [Q9BRR0-2]
XP_006715278.1. XM_006715215.1. [Q9BRR0-1]
XP_006715281.1. XM_006715218.1. [Q9BRR0-2]
XP_006715282.1. XM_006715219.1. [Q9BRR0-2]
UniGeneiHs.380930.
Hs.485004.

3D structure databases

ProteinModelPortaliQ9BRR0.
SMRiQ9BRR0. Positions 37-129, 289-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123230. 6 interactions.
IntActiQ9BRR0. 1 interaction.
STRINGi9606.ENSP00000252211.

PTM databases

PhosphoSiteiQ9BRR0.

Polymorphism databases

DMDMi116242859.

Proteomic databases

MaxQBiQ9BRR0.
PaxDbiQ9BRR0.
PRIDEiQ9BRR0.

Protocols and materials databases

DNASUi80317.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252211; ENSP00000252211; ENSG00000189298. [Q9BRR0-1]
ENST00000341464; ENSP00000341883; ENSG00000189298. [Q9BRR0-2]
ENST00000377255; ENSP00000366465; ENSG00000189298. [Q9BRR0-1]
GeneIDi80317.
KEGGihsa:80317.
UCSCiuc003nle.4. human. [Q9BRR0-1]

Organism-specific databases

CTDi80317.
GeneCardsiGC06P028317.
HGNCiHGNC:13853. ZKSCAN3.
HPAiHPA009637.
MIMi612791. gene.
neXtProtiNX_Q9BRR0.
PharmGKBiPA37821.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118881.
HOGENOMiHOG000234619.
HOVERGENiHBG018163.
InParanoidiQ9BRR0.
KOiK09229.
OMAiCCREDAV.
OrthoDBiEOG79GT5W.
PhylomeDBiQ9BRR0.
TreeFamiTF350830.

Enzyme and pathway databases

ReactomeiREACT_12627. Generic Transcription Pathway.

Miscellaneous databases

ChiTaRSiZKSCAN3. human.
GenomeRNAii80317.
NextBioi70823.
PROiQ9BRR0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BRR0.
CleanExiHS_ZKSCAN3.
GenevestigatoriQ9BRR0.

Family and domain databases

Gene3Di3.30.160.60. 7 hits.
InterProiIPR001909. Krueppel-associated_box.
IPR008916. Retrov_capsid_C.
IPR003309. Tscrpt_reg_SCAN.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF02023. SCAN. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00431. SCAN. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
SSF47353. SSF47353. 1 hit.
PROSITEiPS50804. SCAN_BOX. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS MET-189 AND ALA-200.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ALA-200 AND GLU-200.
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-200.
    Tissue: Placenta.
  6. "Computer sequence analysis of human highly conserved zinc finger modules."
    Petroni D., Bartolini E., Chiaramonte R., Ottolenghi S., Comi P.
    DNA Seq. 9:163-169(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 206-538 (ISOFORM 1/2).
  7. "The previously undescribed ZKSCAN3 (ZNF306) is a novel 'driver' of colorectal cancer progression."
    Yang L., Hamilton S.R., Sood A., Kuwai T., Ellis L., Sanguino A., Lopez-Berestein G., Boyd D.D.
    Cancer Res. 68:4321-4330(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Unbiased screening for transcriptional targets of ZKSCAN3 identifies integrin beta 4 and vascular endothelial growth factor as downstream targets."
    Yang L., Zhang L., Wu Q., Boyd D.D.
    J. Biol. Chem. 283:35295-35304(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INDUCTION.
  9. "Evidence of a role for the novel zinc-finger transcription factor ZKSCAN3 in modulating Cyclin D2 expression in multiple myeloma."
    Yang L., Wang H., Kornblau S.M., Graber D.A., Zhang N., Matthews J.A., Wang M., Weber D.M., Thomas S.K., Shah J.J., Zhang L., Lu G., Zhao M., Muddasani R., Yoo S.Y., Baggerly K.A., Orlowski R.Z.
    Oncogene 30:1329-1340(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  10. "The zinc finger transcription factor ZKSCAN3 promotes prostate cancer cell migration."
    Zhang X., Jing Y., Qin Y., Hunsucker S., Meng H., Sui J., Jiang Y., Gao L., An G., Yang N., Orlowski R.Z., Yang L.
    Int. J. Biochem. Cell Biol. 44:1166-1173(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  11. "ZKSCAN3 is a master transcriptional repressor of autophagy."
    Chauhan S., Goodwin J.G., Chauhan S., Manyam G., Wang J., Kamat A.M., Boyd D.D.
    Mol. Cell 50:16-28(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiZKSC3_HUMAN
AccessioniPrimary (citable) accession number: Q9BRR0
Secondary accession number(s): B2R8W2
, B3KVC0, H7BXX1, Q5VXH3, Q92972, Q9H4T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.