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Protein

Zinc finger protein 575

Gene

Znf575

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 7923C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri85 – 10723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 13523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri141 – 16323C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri171 – 19323C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri207 – 23024C2H2-type 6PROSITE-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 575
Gene namesi
Name:Znf575
Synonyms:Zfp575
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2141921. Zfp575.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Zinc finger protein 575PRO_0000047666Add
BLAST

Proteomic databases

PaxDbiQ3TXZ1.
PRIDEiQ3TXZ1.

PTM databases

iPTMnetiQ3TXZ1.
PhosphoSiteiQ3TXZ1.

Expressioni

Gene expression databases

BgeeiQ3TXZ1.
CleanExiMM_ZFP575.
ExpressionAtlasiQ3TXZ1. baseline and differential.
GenevisibleiQ3TXZ1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092294.

Structurei

3D structure databases

ProteinModelPortaliQ3TXZ1.
SMRiQ3TXZ1. Positions 55-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 6 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 7923C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri85 – 10723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 13523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri141 – 16323C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri171 – 19323C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri207 – 23024C2H2-type 6PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129960.
HOGENOMiHOG000060290.
HOVERGENiHBG018163.
InParanoidiQ3TXZ1.
OMAiHRCSSCN.
OrthoDBiEOG7VQJF1.
PhylomeDBiQ3TXZ1.
TreeFamiTF338022.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3TXZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGGSVKSEV RASEPSPTCQ DPETKAPHQD LPRPNQPAAS GSVPSRPRRR
60 70 80 90 100
PPPQRPHRCP DCPKAFSYPS KLATHRLAHG GTRPHPCPDC PKAFSYPSKL
110 120 130 140 150
AAHRLTHSGA RPHSCPHCPK AFGHRSKLAA HLWTHAPARP YPCPDCPKSF
160 170 180 190 200
CYPSKLAAHR HTHHATDARP YPCPHCPKAF SFPSKLAAHR LCHDPPTAPS
210 220 230
SQATGSHRCS SCNQAFGQRR LLLVHQRSHH QSEGQGERE
Length:239
Mass (Da):26,282
Last modified:October 11, 2005 - v1
Checksum:i7606F7DDFC24616A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159025 mRNA. Translation: BAE34773.1.
CCDSiCCDS20956.1.
RefSeqiNP_001028377.1. NM_001033205.3.
XP_006539509.1. XM_006539446.2.
UniGeneiMm.20117.

Genome annotation databases

EnsembliENSMUST00000094705; ENSMUSP00000092294; ENSMUSG00000066721.
GeneIDi101544.
KEGGimmu:101544.
UCSCiuc009fqa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159025 mRNA. Translation: BAE34773.1.
CCDSiCCDS20956.1.
RefSeqiNP_001028377.1. NM_001033205.3.
XP_006539509.1. XM_006539446.2.
UniGeneiMm.20117.

3D structure databases

ProteinModelPortaliQ3TXZ1.
SMRiQ3TXZ1. Positions 55-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000092294.

PTM databases

iPTMnetiQ3TXZ1.
PhosphoSiteiQ3TXZ1.

Proteomic databases

PaxDbiQ3TXZ1.
PRIDEiQ3TXZ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094705; ENSMUSP00000092294; ENSMUSG00000066721.
GeneIDi101544.
KEGGimmu:101544.
UCSCiuc009fqa.1. mouse.

Organism-specific databases

CTDi101544.
MGIiMGI:2141921. Zfp575.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129960.
HOGENOMiHOG000060290.
HOVERGENiHBG018163.
InParanoidiQ3TXZ1.
OMAiHRCSSCN.
OrthoDBiEOG7VQJF1.
PhylomeDBiQ3TXZ1.
TreeFamiTF338022.

Miscellaneous databases

PROiQ3TXZ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TXZ1.
CleanExiMM_ZFP575.
ExpressionAtlasiQ3TXZ1. baseline and differential.
GenevisibleiQ3TXZ1. MM.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Visual cortex.

Entry informationi

Entry nameiZN575_MOUSE
AccessioniPrimary (citable) accession number: Q3TXZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.