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O00488

- ZN593_HUMAN

UniProt

O00488 - ZN593_HUMAN

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Protein
Zinc finger protein 593
Gene
ZNF593
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity. Could act either by binding to DNA octamer or by interacting with Oct-2. May also be a modulator of other octamer-binding proteins.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri61 – 8525C2H2-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. transcription corepressor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 593
Alternative name(s):
Zinc finger protein T86
Gene namesi
Name:ZNF593
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30943. ZNF593.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134962156.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 134134Zinc finger protein 593
PRO_0000047684Add
BLAST

Proteomic databases

MaxQBiO00488.
PaxDbiO00488.
PRIDEiO00488.

2D gel databases

SWISS-2DPAGEO00488.

PTM databases

PhosphoSiteiO00488.

Expressioni

Tissue specificityi

Ubiquitous. Detected in spleen, prostate, testis, small intestine, colon and to a minor level in thymus and peripheral blood leukocytes.

Gene expression databases

ArrayExpressiO00488.
BgeeiO00488.
CleanExiHS_ZNF593.
GenevestigatoriO00488.

Organism-specific databases

HPAiHPA054363.
HPA059387.

Interactioni

Protein-protein interaction databases

BioGridi119241. 18 interactions.
IntActiO00488. 5 interactions.
MINTiMINT-1387753.
STRINGi9606.ENSP00000363384.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 553
Helixi56 – 594
Turni64 – 663
Helixi73 – 797
Helixi83 – 9210
Turni99 – 1013

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZR9NMR-A20-134[»]
DisProtiDP00549.
ProteinModelPortaliO00488.
SMRiO00488. Positions 46-112.

Miscellaneous databases

EvolutionaryTraceiO00488.

Family & Domainsi

Domaini

The protein is largely disordered, with the exception of the zinc finger domain.1 Publication

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5112.
HOGENOMiHOG000216641.
HOVERGENiHBG058255.
KOiK14821.
OrthoDBiEOG7KSXBJ.
PhylomeDBiO00488.
TreeFamiTF315114.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR022755. Znf_C2H2_jaz.
[Graphical view]
PfamiPF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00488-1 [UniParc]FASTAAdd to Basket

« Hide

MGRSRRTGAH RAHSLARQMK AKRRRPDLDE IHRELRPQGS ARPQPDPNAE    50
FDPDLPGGGL HRCLACARYF IDSTNLKTHF RSKDHKKRLK QLSVEPYSQE 100
EAERAAGMGS YVPPRRLAVP TEVSTEVPEM DTST 134
Length:134
Mass (Da):15,199
Last modified:July 28, 2009 - v2
Checksum:i883BCE4F72459818
GO

Sequence cautioni

The sequence AAH02580.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH19267.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA20369.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAG34867.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61R → Q.
Corresponds to variant rs2232649 [ dbSNP | Ensembl ].
VAR_059924

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK311926 mRNA. Translation: BAG34867.1. Different initiation.
AL391650 Genomic DNA. Translation: CAI17137.1.
CH471059 Genomic DNA. Translation: EAX07843.1.
BC002580 mRNA. Translation: AAH02580.1. Different initiation.
BC019267 mRNA. Translation: AAH19267.1. Different initiation.
D45213 mRNA. Translation: BAA20369.1. Different initiation.
CCDSiCCDS275.2.
RefSeqiNP_056955.2. NM_015871.4.
UniGeneiHs.477273.

Genome annotation databases

EnsembliENST00000374266; ENSP00000363384; ENSG00000142684.
GeneIDi51042.
KEGGihsa:51042.
UCSCiuc001bll.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK311926 mRNA. Translation: BAG34867.1 . Different initiation.
AL391650 Genomic DNA. Translation: CAI17137.1 .
CH471059 Genomic DNA. Translation: EAX07843.1 .
BC002580 mRNA. Translation: AAH02580.1 . Different initiation.
BC019267 mRNA. Translation: AAH19267.1 . Different initiation.
D45213 mRNA. Translation: BAA20369.1 . Different initiation.
CCDSi CCDS275.2.
RefSeqi NP_056955.2. NM_015871.4.
UniGenei Hs.477273.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZR9 NMR - A 20-134 [» ]
DisProti DP00549.
ProteinModelPortali O00488.
SMRi O00488. Positions 46-112.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119241. 18 interactions.
IntActi O00488. 5 interactions.
MINTi MINT-1387753.
STRINGi 9606.ENSP00000363384.

PTM databases

PhosphoSitei O00488.

2D gel databases

SWISS-2DPAGE O00488.

Proteomic databases

MaxQBi O00488.
PaxDbi O00488.
PRIDEi O00488.

Protocols and materials databases

DNASUi 51042.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374266 ; ENSP00000363384 ; ENSG00000142684 .
GeneIDi 51042.
KEGGi hsa:51042.
UCSCi uc001bll.4. human.

Organism-specific databases

CTDi 51042.
GeneCardsi GC01P026496.
HGNCi HGNC:30943. ZNF593.
HPAi HPA054363.
HPA059387.
neXtProti NX_O00488.
PharmGKBi PA134962156.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5112.
HOGENOMi HOG000216641.
HOVERGENi HBG058255.
KOi K14821.
OrthoDBi EOG7KSXBJ.
PhylomeDBi O00488.
TreeFami TF315114.

Miscellaneous databases

EvolutionaryTracei O00488.
GeneWikii ZNF593.
GenomeRNAii 51042.
NextBioi 53596.
PROi O00488.

Gene expression databases

ArrayExpressi O00488.
Bgeei O00488.
CleanExi HS_ZNF593.
Genevestigatori O00488.

Family and domain databases

InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR022755. Znf_C2H2_jaz.
[Graphical view ]
Pfami PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Lymph.
  5. "A novel genetic system to isolate a dominant negative effector on DNA-binding activity of Oct-2."
    Terunuma A., Shiba K., Noda T.
    Nucleic Acids Res. 25:1984-1990(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-134.
    Tissue: T-cell lymphoma.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein."
    Hayes P.L., Lytle B.L., Volkman B.F., Peterson F.C.
    Protein Sci. 17:571-576(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 20-134 IN COMPLEX WITH ZINC IONS, DOMAIN.

Entry informationi

Entry nameiZN593_HUMAN
AccessioniPrimary (citable) accession number: O00488
Secondary accession number(s): B2R4S0, Q5T2H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 121 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 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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