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Protein

Homeobox protein PKNOX2

Gene

Pknox2

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi291 – 35060HomeoboxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • actin filament binding Source: MGI
  • actin monomer binding Source: MGI
  • DNA binding Source: MGI
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • sequence-specific DNA binding Source: MGI

GO - Biological processi

  • regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Homeobox protein PKNOX2
Alternative name(s):
Homeobox protein PREP-2
PBX/knotted homeobox 2
Gene namesi
Name:Pknox2
Synonyms:Prep2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2445415. Pknox2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • microtubule cytoskeleton Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Homeobox protein PKNOX2PRO_0000249880Add
BLAST

Proteomic databases

MaxQBiQ8BG99.
PaxDbiQ8BG99.
PRIDEiQ8BG99.

PTM databases

PhosphoSiteiQ8BG99.

Expressioni

Gene expression databases

BgeeiQ8BG99.
CleanExiMM_PKNOX2.
ExpressionAtlasiQ8BG99. baseline and differential.
GenevisibleiQ8BG99. MM.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: MGI
  • actin monomer binding Source: MGI

Protein-protein interaction databases

BioGridi228942. 6 interactions.
IntActiQ8BG99. 1 interaction.
MINTiMINT-4110211.
STRINGi10090.ENSMUSP00000035806.

Structurei

3D structure databases

ProteinModelPortaliQ8BG99.
SMRiQ8BG99. Positions 289-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 234Poly-Pro
Compositional biasi426 – 45631Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the TALE/MEIS homeobox family.Curated
Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Homeobox

Phylogenomic databases

eggNOGiKOG0773. Eukaryota.
ENOG410XPMQ. LUCA.
GeneTreeiENSGT00550000074260.
HOGENOMiHOG000253922.
HOVERGENiHBG055193.
InParanoidiQ8BG99.
OMAiTMMATQS.
OrthoDBiEOG71CFNK.
PhylomeDBiQ8BG99.
TreeFamiTF318093.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR001356. Homeobox_dom.
IPR008422. Homeobox_KN_domain.
IPR009057. Homeodomain-like.
IPR032453. PKNOX/Meis_N.
[Graphical view]
PfamiPF05920. Homeobox_KN. 1 hit.
PF16493. Meis_PKNOX_N. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BG99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQHASPAPA LTMMATQNVP PPPYQDSPQM TATAQPPSKA QAVHISAPSA
60 70 80 90 100
TASTPVPSAP IDPQAQLEAD KRAVYRHPLF PLLTLLFEKC EQATQGSECI
110 120 130 140 150
TSASFDVDIE NFVHQQEQEH KPFFSDDPEL DNLMVKAIQV LRIHLLELEK
160 170 180 190 200
VNELCKDFCN RYITCLKTKM HSDNLLRNDL GGPYSPNQPS INLHSQDLLQ
210 220 230 240 250
NSPNSMSGVS NNPQGIVVPA SALQQGNIAM TTVNSQVVSG GALYQPVTMV
260 270 280 290 300
TSQGQVVTQA IPQGAIQIQN TQVNLDLTSL LDNEDKKSKN KRGVLPKHAT
310 320 330 340 350
NIMRSWLFQH LMHPYPTEDE KRQIAAQTNL TLLQVNNWFI NARRRILQPM
360 370 380 390 400
LDASNPDPAP KAKKIKSQHR PTQRFWPNSI AAGVLQQQGG TPGTNPDGSI
410 420 430 440 450
NLDNLQSLSS DNATMAMQQA MMAAHDDSLD GTEEEDEDDM EEEEEEEEEL
460 470
EEEADELQTT NVSDLGLEHS DSLE
Length:474
Mass (Da):52,331
Last modified:March 1, 2003 - v1
Checksum:iB2B160A7D13E7579
GO

Sequence cautioni

The sequence AAM18702.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF487460 mRNA. Translation: AAM18702.1. Different initiation.
AB086817 mRNA. Translation: BAC20215.1.
AK082952 mRNA. Translation: BAC38705.1.
BC050865 mRNA. Translation: AAH50865.2.
CCDSiCCDS22974.1.
RefSeqiNP_001025009.1. NM_001029838.2.
NP_683752.2. NM_148950.3.
XP_006510187.1. XM_006510124.2.
XP_006510188.1. XM_006510125.2.
XP_006510189.1. XM_006510126.2.
XP_006510190.1. XM_006510127.2.
UniGeneiMm.260335.

Genome annotation databases

EnsembliENSMUST00000039674; ENSMUSP00000035806; ENSMUSG00000035934.
ENSMUST00000080754; ENSMUSP00000079578; ENSMUSG00000035934.
ENSMUST00000177218; ENSMUSP00000135581; ENSMUSG00000035934.
GeneIDi208076.
KEGGimmu:208076.
UCSCiuc009oue.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF487460 mRNA. Translation: AAM18702.1. Different initiation.
AB086817 mRNA. Translation: BAC20215.1.
AK082952 mRNA. Translation: BAC38705.1.
BC050865 mRNA. Translation: AAH50865.2.
CCDSiCCDS22974.1.
RefSeqiNP_001025009.1. NM_001029838.2.
NP_683752.2. NM_148950.3.
XP_006510187.1. XM_006510124.2.
XP_006510188.1. XM_006510125.2.
XP_006510189.1. XM_006510126.2.
XP_006510190.1. XM_006510127.2.
UniGeneiMm.260335.

3D structure databases

ProteinModelPortaliQ8BG99.
SMRiQ8BG99. Positions 289-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228942. 6 interactions.
IntActiQ8BG99. 1 interaction.
MINTiMINT-4110211.
STRINGi10090.ENSMUSP00000035806.

PTM databases

PhosphoSiteiQ8BG99.

Proteomic databases

MaxQBiQ8BG99.
PaxDbiQ8BG99.
PRIDEiQ8BG99.

Protocols and materials databases

DNASUi208076.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039674; ENSMUSP00000035806; ENSMUSG00000035934.
ENSMUST00000080754; ENSMUSP00000079578; ENSMUSG00000035934.
ENSMUST00000177218; ENSMUSP00000135581; ENSMUSG00000035934.
GeneIDi208076.
KEGGimmu:208076.
UCSCiuc009oue.3. mouse.

Organism-specific databases

CTDi63876.
MGIiMGI:2445415. Pknox2.

Phylogenomic databases

eggNOGiKOG0773. Eukaryota.
ENOG410XPMQ. LUCA.
GeneTreeiENSGT00550000074260.
HOGENOMiHOG000253922.
HOVERGENiHBG055193.
InParanoidiQ8BG99.
OMAiTMMATQS.
OrthoDBiEOG71CFNK.
PhylomeDBiQ8BG99.
TreeFamiTF318093.

Miscellaneous databases

PROiQ8BG99.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BG99.
CleanExiMM_PKNOX2.
ExpressionAtlasiQ8BG99. baseline and differential.
GenevisibleiQ8BG99. MM.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR001356. Homeobox_dom.
IPR008422. Homeobox_KN_domain.
IPR009057. Homeodomain-like.
IPR032453. PKNOX/Meis_N.
[Graphical view]
PfamiPF05920. Homeobox_KN. 1 hit.
PF16493. Meis_PKNOX_N. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prep2: cloning and expression of a new prep family member."
    Haller K., Rambaldi I., Kovacs E.N., Daniels E., Featherstone M.
    Dev. Dyn. 225:358-364(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/N.
  2. "Prep2, a novel Pbx partner expressed in the distinctive domains during vertebrate embryogenesis."
    Yamagishi A., Shinya M., Takeda H., Kuroiwa A.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Spinal cord.
  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: Embryo.

Entry informationi

Entry nameiPKNX2_MOUSE
AccessioniPrimary (citable) accession number: Q8BG99
Secondary accession number(s): Q8R4B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 102 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.