Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9CXE0 (PRDM5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PR domain zinc finger protein 5

EC=2.1.1.-
Alternative name(s):
PR domain-containing protein 5
Gene names
Name:Prdm5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes By similarity. May regulate the expression of proteins involved in extracellular matrix development and maintenance, connective tissue components and molecules regulating cell migration and adhesion. May caused G2/M arrest and apoptosis in cancer cells By similarity.

Subunit structure

Interacts with EHMT2/G9A, GFI1 and HDAC1 By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

Contains 15 C2H2-type zinc fingers.

Contains 1 SET domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionActivator
Chromatin regulator
Methyltransferase
Repressor
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H3-K9 methylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

repressing transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 599599PR domain zinc finger protein 5
PRO_0000230794

Regions

Domain8 – 124117SET
Zinc finger167 – 19024C2H2-type 1
Zinc finger199 – 22123C2H2-type 2
Zinc finger231 – 25626C2H2-type 3
Zinc finger264 – 28623C2H2-type 4
Zinc finger289 – 31123C2H2-type 5
Zinc finger317 – 33923C2H2-type 6
Zinc finger345 – 36723C2H2-type 7
Zinc finger373 – 39523C2H2-type 8
Zinc finger401 – 42424C2H2-type 9
Zinc finger430 – 45223C2H2-type 10
Zinc finger458 – 48023C2H2-type 11
Zinc finger486 – 50823C2H2-type 12
Zinc finger514 – 53623C2H2-type 13; degenerate
Zinc finger542 – 56423C2H2-type 14
Zinc finger571 – 59424C2H2-type 15
Compositional bias129 – 1346Poly-Glu

Experimental info

Sequence conflict531 – 5322EH → AT in BAB29400. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CXE0 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 545824C2A54DAAF6

FASTA59969,550
        10         20         30         40         50         60 
MLGMYVPDRF ALKSSRVQDG MGLYTARRVR KGEKFGPFAG EKRMPEDLDE NMDYRLMWEV 

        70         80         90        100        110        120 
RGSKGEVLYI LDATNPRHSN WLRFVHEAPS QERKNLAAIQ EGENIFYLAV DDIETDTELL 

       130        140        150        160        170        180 
IGYLDSDVEA EEEEQQALTM TKEGKVDHSK GQLAAGSKGH LGCEEDFACP QCESSFPSEE 

       190        200        210        220        230        240 
VLTEHLQSLH QKPTGEKEFK CENCGKKFPV RQALQRHFEQ HRKACRGEAR FVCKADSCGK 

       250        260        270        280        290        300 
RLKSKDALRR HQENVHTGDP KRKLICSVCN RKCTSVSSLQ EHRKIHEIFD CQECMKKFIS 

       310        320        330        340        350        360 
ANQLKRHMIT HSEKRPYNCE ICNKSFKRLD QVGAHKVIHS EDKPYQCKLC GKGFAHRNVY 

       370        380        390        400        410        420 
KNHKKTHSEE RPFQCDACKA LFRTPFSLQR HLLIHNSERT FKCHHCDATF KRKDTLNVHV 

       430        440        450        460        470        480 
QVVHERHKKY RCELCNKAFV TPSVLRSHKK THTGEKEKVC PYCGQKFASS GTLRVHIRSH 

       490        500        510        520        530        540 
TGERPYQCPY CEKGFSKNDG LKMHIRTHTR EKPYQCSECS KAFSQKRGLD EHKRTHTGEK 

       550        560        570        580        590 
PFQCDVCDLA FSLKKMLIRH KMTHNPNRPM AECHFCHKKF TRNDYLKVHM DNIHGVADS 

« Hide

References

[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. expand/collapse author list , 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: Liver.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK014501 mRNA. Translation: BAB29400.1.
CH466523 Genomic DNA. Translation: EDK98780.1.
BC138901 mRNA. Translation: AAI38902.1.
BC138902 mRNA. Translation: AAI38903.1.
RefSeqNP_081823.2. NM_027547.2.
UniGeneMm.263355.

3D structure databases

ProteinModelPortalQ9CXE0.
SMRQ9CXE0. Positions 9-594.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid214249. 1 interaction.

PTM databases

PhosphoSiteQ9CXE0.

Proteomic databases

PRIDEQ9CXE0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031976; ENSMUSP00000031976; ENSMUSG00000029913.
GeneID70779.
KEGGmmu:70779.
UCSCuc009cek.1. mouse.

Organism-specific databases

CTD11107.
MGIMGI:1918029. Prdm5.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00390000014166.
HOGENOMHOG000234617.
HOVERGENHBG098380.
InParanoidB2RSK8.
OMALGCKEDY.
OrthoDBEOG7KSX7Q.
PhylomeDBQ9CXE0.
TreeFamTF106478.

Gene expression databases

BgeeQ9CXE0.
CleanExMM_PRDM5.
GenevestigatorQ9CXE0.

Family and domain databases

Gene3D3.30.160.60. 14 hits.
InterProIPR001214. SET_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR017125. Znf_PRDM5.
[Graphical view]
PfamPF00096. zf-C2H2. 3 hits.
[Graphical view]
PIRSFPIRSF037162. PRDM. 1 hit.
SMARTSM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 15 hits.
[Graphical view]
PROSITEPS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 15 hits.
PS50157. ZINC_FINGER_C2H2_2. 15 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio332236.
PROQ9CXE0.
SOURCESearch...

Entry information

Entry namePRDM5_MOUSE
AccessionPrimary (citable) accession number: Q9CXE0
Secondary accession number(s): B2RSK8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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