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Protein

Krueppel-like factor 16

Gene

Klf16

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

Functioni

Transcription factor that binds GC and GT boxes in the D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from these sequences. It modulates dopaminergic transmission in the brain by repressing or activating transcription from several different promoters depending on cellular context.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri126 – 15025C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri156 – 18025C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri186 – 20823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: MGI

GO - Biological processi

  • dopamine receptor signaling pathway Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • 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:
Krueppel-like factor 16
Alternative name(s):
Basic transcription element-binding protein 4
Short name:
BTE-binding protein 4
Dopamine receptor-regulating factor
Transcription factor BTEB4
Gene namesi
Name:Klf16
Synonyms:Bteb4, Drrf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2153049. Klf16.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Krueppel-like factor 16PRO_0000047159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei151 – 1511PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP58334.
MaxQBiP58334.
PaxDbiP58334.
PRIDEiP58334.

PTM databases

PhosphoSiteiP58334.

Expressioni

Tissue specificityi

High expression in brain; olfactory tubercle, olfactory bulb, nucleus accumbens, striatum, hippocampal CA1 region, amygdala, dentate gyrus and frontal cortex. Moderate expression in hippocampal CA2-3 regions, piriform cortex, septum, and distinct thalamic nuclei. Low expression in the cerebellum.

Gene expression databases

BgeeiP58334.
CleanExiMM_KLF16.
ExpressionAtlasiP58334. baseline and differential.
GenevisibleiP58334. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048825.

Structurei

3D structure databases

ProteinModelPortaliP58334.
SMRiP58334. Positions 124-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 136134Ala/Pro-richAdd
BLAST
Compositional biasi103 – 11614Ser-richAdd
BLAST
Compositional biasi223 – 24826Pro/Ser-richAdd
BLAST

Domaini

The Ala/Pro-rich domain may contain discrete activation and repression subdomains and also can mediate protein-protein interactions.

Sequence similaritiesi

Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri126 – 15025C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri156 – 18025C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri186 – 20823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118984.
HOGENOMiHOG000233575.
HOVERGENiHBG050746.
InParanoidiP58334.
KOiK09208.
OMAiFPCPLCT.
OrthoDBiEOG7FJH0Q.
PhylomeDBiP58334.
TreeFamiTF351003.

Family and domain databases

Gene3Di3.30.160.60. 3 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. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P58334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAVACVDY FAADVLMAIS SGAVVHRGRP GPEGAGPAAG LDVRATRREA
60 70 80 90 100
TPPGTPGAPP PPATAPGPGG ATAAPHLLAA SILADLRGGP VVATAASTAG
110 120 130 140 150
GTSPVSSSSA ASSPSSGRAP GAAKSHRCPF HGCAKAYYKS SHLKSHLRTH
160 170 180 190 200
TGERPFACDW PGCDKKFARS DELARHHRTH TGEKRFPCPL CTKRFTRSDH
210 220 230 240 250
LTKHARRHPG FRPELLRRPG ARSVSPSDSL PCSLAGSPTP SPVPSPAPAG

L
Length:251
Mass (Da):25,652
Last modified:August 16, 2004 - v2
Checksum:i3F0D7739BF7B1FA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283891 mRNA. Translation: AAK66968.1.
AK044577 mRNA. Translation: BAC31987.1.
AK154524 mRNA. Translation: BAE32651.1.
CCDSiCCDS24026.1.
RefSeqiNP_510962.2. NM_078477.2.
UniGeneiMm.41513.

Genome annotation databases

EnsembliENSMUST00000038558; ENSMUSP00000048825; ENSMUSG00000035397.
GeneIDi118445.
KEGGimmu:118445.
UCSCiuc007gdt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF283891 mRNA. Translation: AAK66968.1.
AK044577 mRNA. Translation: BAC31987.1.
AK154524 mRNA. Translation: BAE32651.1.
CCDSiCCDS24026.1.
RefSeqiNP_510962.2. NM_078477.2.
UniGeneiMm.41513.

3D structure databases

ProteinModelPortaliP58334.
SMRiP58334. Positions 124-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048825.

PTM databases

PhosphoSiteiP58334.

Proteomic databases

EPDiP58334.
MaxQBiP58334.
PaxDbiP58334.
PRIDEiP58334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038558; ENSMUSP00000048825; ENSMUSG00000035397.
GeneIDi118445.
KEGGimmu:118445.
UCSCiuc007gdt.1. mouse.

Organism-specific databases

CTDi83855.
MGIiMGI:2153049. Klf16.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118984.
HOGENOMiHOG000233575.
HOVERGENiHBG050746.
InParanoidiP58334.
KOiK09208.
OMAiFPCPLCT.
OrthoDBiEOG7FJH0Q.
PhylomeDBiP58334.
TreeFamiTF351003.

Miscellaneous databases

NextBioi369718.
PROiP58334.
SOURCEiSearch...

Gene expression databases

BgeeiP58334.
CleanExiMM_KLF16.
ExpressionAtlasiP58334. baseline and differential.
GenevisibleiP58334. MM.

Family and domain databases

Gene3Di3.30.160.60. 3 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. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Neuroblastoma.
  2. "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 and NOD.
    Tissue: Retina.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung, Spleen and Testis.

Entry informationi

Entry nameiKLF16_MOUSE
AccessioniPrimary (citable) accession number: P58334
Secondary accession number(s): Q3U3Y4, Q8C8S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: August 16, 2004
Last modified: March 16, 2016
This is version 119 of the entry and version 2 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.