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Protein

Zinc finger protein 800

Gene

ZNF800

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri69 – 9123C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri230 – 25324C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri287 – 31024C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri357 – 38226C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri486 – 50823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri519 – 54224C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri618 – 64023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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 800
Gene namesi
Name:ZNF800
ORF Names:PP902
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:27267. ZNF800.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162410582.

Polymorphism and mutation databases

BioMutaiZNF800.
DMDMi121941799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 664664Zinc finger protein 800PRO_0000304410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki132 – 132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei319 – 3191PhosphothreonineCombined sources
Modified residuei336 – 3361PhosphoserineCombined sources
Cross-linki409 – 409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki409 – 409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei422 – 4221PhosphoserineBy similarity
Modified residuei426 – 4261PhosphoserineCombined sources
Modified residuei455 – 4551PhosphoserineCombined sources
Modified residuei457 – 4571PhosphoserineCombined sources
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ2TB10.
MaxQBiQ2TB10.
PaxDbiQ2TB10.
PeptideAtlasiQ2TB10.
PRIDEiQ2TB10.

PTM databases

iPTMnetiQ2TB10.
PhosphoSiteiQ2TB10.

Expressioni

Gene expression databases

BgeeiQ2TB10.
CleanExiHS_ZNF800.
ExpressionAtlasiQ2TB10. baseline and differential.
GenevisibleiQ2TB10. HS.

Organism-specific databases

HPAiHPA023090.
HPA052194.

Interactioni

Protein-protein interaction databases

BioGridi127973. 16 interactions.
IntActiQ2TB10. 4 interactions.
STRINGi9606.ENSP00000265827.

Structurei

3D structure databases

ProteinModelPortaliQ2TB10.
SMRiQ2TB10. Positions 62-97, 228-257, 278-318, 348-389, 479-511, 517-548, 612-644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 154Poly-His

Sequence similaritiesi

Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri69 – 9123C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri230 – 25324C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri287 – 31024C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri357 – 38226C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri486 – 50823C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri519 – 54224C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri618 – 64023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00390000008140.
HOGENOMiHOG000168334.
HOVERGENiHBG106061.
InParanoidiQ2TB10.
OMAiRDKCCQT.
OrthoDBiEOG7F7W80.
PhylomeDBiQ2TB10.
TreeFamiTF333197.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF16622. zf-C2H2_11. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 7 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2TB10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLRDKYCQT DHHHHGCCEP VYILEPGDPP LLQQPLQTSK SGIQQIIECF
60 70 80 90 100
RSGTKQLKHI LLKDVDTIFE CKLCRSLFRG LPNLITHKKF YCPPSLQMDD
110 120 130 140 150
NLPDVNDKQS QAINDLLEAI YPSVDKREYI IKLEPIETNQ NAVFQYISRT
160 170 180 190 200
DNPIEVTESS STPEQTEVQI QETSTEQSKT VPVTDTEVET VEPPPVEIVT
210 220 230 240 250
DEVAPTSDEQ PQESQADLET SDNSDFGHQL ICCLCRKEFN SRRGVRRHIR
260 270 280 290 300
KVHKKKMEEL KKYIETRKNP NQSSKGRSKN VLVPLSRSCP VCCKSFATKA
310 320 330 340 350
NVRRHFDEVH RGLRRDSITP DIATKPGQPL FLDSISPKKS FKTRKQKSSS
360 370 380 390 400
KAEYNLTACK CLLCKRKYSS QIMLKRHMQI VHKITLSGTN SKREKGPNNT
410 420 430 440 450
ANSSEIKVKV EPADSVESSP PSITHSPQNE LKGTNHSNEK KNTPAAQKNK
460 470 480 490 500
VKQDSESPKS TSPSAAGGQQ KTRKPKLSAG FDFKQLYCKL CKRQFTSKQN
510 520 530 540 550
LTKHIELHTD GNNIYVKFYK CPLCTYETRR KRDVIRHITV VHKKSSRYLG
560 570 580 590 600
KITASLEIRA IKKPIDFVLN KVAKRGPSRD EAKHSDSKHD GTSNSPSKKY
610 620 630 640 650
EVADVGIEVK VTKNFSLHRC NKCGKAFAKK TYLEHHKKTH KANASNSPEG
660
NKTKGRSTRS KALV
Length:664
Mass (Da):75,236
Last modified:January 24, 2006 - v1
Checksum:iF0F0DA1214AC6F2E
GO

Sequence cautioni

The sequence AAG17274.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAG17274.1 differs from that shown. Reason: Frameshift at position 335. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021L → V.
Corresponds to variant rs17865569 [ dbSNP | Ensembl ].
VAR_052904

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH471070 Genomic DNA. Translation: EAW83626.1.
BC110623 mRNA. Translation: AAI10624.1.
BC110624 mRNA. Translation: AAI10625.1.
AF218032 mRNA. Translation: AAG17274.1. Sequence problems.
CCDSiCCDS5795.1.
RefSeqiNP_789784.2. NM_176814.4.
XP_005250238.1. XM_005250181.2.
UniGeneiHs.159006.
Hs.667035.

Genome annotation databases

EnsembliENST00000265827; ENSP00000265827; ENSG00000048405.
ENST00000393312; ENSP00000376988; ENSG00000048405.
ENST00000393313; ENSP00000376989; ENSG00000048405.
GeneIDi168850.
KEGGihsa:168850.
UCSCiuc003vly.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH471070 Genomic DNA. Translation: EAW83626.1.
BC110623 mRNA. Translation: AAI10624.1.
BC110624 mRNA. Translation: AAI10625.1.
AF218032 mRNA. Translation: AAG17274.1. Sequence problems.
CCDSiCCDS5795.1.
RefSeqiNP_789784.2. NM_176814.4.
XP_005250238.1. XM_005250181.2.
UniGeneiHs.159006.
Hs.667035.

3D structure databases

ProteinModelPortaliQ2TB10.
SMRiQ2TB10. Positions 62-97, 228-257, 278-318, 348-389, 479-511, 517-548, 612-644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127973. 16 interactions.
IntActiQ2TB10. 4 interactions.
STRINGi9606.ENSP00000265827.

PTM databases

iPTMnetiQ2TB10.
PhosphoSiteiQ2TB10.

Polymorphism and mutation databases

BioMutaiZNF800.
DMDMi121941799.

Proteomic databases

EPDiQ2TB10.
MaxQBiQ2TB10.
PaxDbiQ2TB10.
PeptideAtlasiQ2TB10.
PRIDEiQ2TB10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265827; ENSP00000265827; ENSG00000048405.
ENST00000393312; ENSP00000376988; ENSG00000048405.
ENST00000393313; ENSP00000376989; ENSG00000048405.
GeneIDi168850.
KEGGihsa:168850.
UCSCiuc003vly.2. human.

Organism-specific databases

CTDi168850.
GeneCardsiZNF800.
HGNCiHGNC:27267. ZNF800.
HPAiHPA023090.
HPA052194.
neXtProtiNX_Q2TB10.
PharmGKBiPA162410582.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00390000008140.
HOGENOMiHOG000168334.
HOVERGENiHBG106061.
InParanoidiQ2TB10.
OMAiRDKCCQT.
OrthoDBiEOG7F7W80.
PhylomeDBiQ2TB10.
TreeFamiTF333197.

Miscellaneous databases

ChiTaRSiZNF800. human.
GenomeRNAii168850.
PROiQ2TB10.

Gene expression databases

BgeeiQ2TB10.
CleanExiHS_ZNF800.
ExpressionAtlasiQ2TB10. baseline and differential.
GenevisibleiQ2TB10. HS.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF16622. zf-C2H2_11. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 7 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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].
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-471.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; THR-319; SER-336; SER-455 AND SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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.
  6. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZN800_HUMAN
AccessioniPrimary (citable) accession number: Q2TB10
Secondary accession number(s): Q9HBN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 24, 2006
Last modified: July 6, 2016
This is version 101 of the entry and version 1 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 7
    Human chromosome 7: 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. 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.